Binding and uptake of ligands by scavenger receptors (Homo sapiens)

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1. Nishikawa K, Arai H, Inoue K.; ''Scavenger receptor-mediated uptake and metabolism of lipid vesicles containing acidic phospholipids by mouse peritoneal macrophages.''; PubMed Europe PMC Scholia
2. Haberland ME, Olch CL, Folgelman AM.; ''Role of lysines in mediating interaction of modified low density lipoproteins with the scavenger receptor of human monocyte macrophages.''; PubMed Europe PMC Scholia
3. Nieland TJ, Ehrlich M, Krieger M, Kirchhausen T.; ''Endocytosis is not required for the selective lipid uptake mediated by murine SR-BI.''; PubMed Europe PMC Scholia
4. Sun B, Boyanovsky BB, Connelly MA, Shridas P, van der Westhuyzen DR, Webb NR.; ''Distinct mechanisms for OxLDL uptake and cellular trafficking by class B scavenger receptors CD36 and SR-BI.''; PubMed Europe PMC Scholia
5. Prevo R, Banerji S, Ni J, Jackson DG.; ''Rapid plasma membrane-endosomal trafficking of the lymph node sinus and high endothelial venule scavenger receptor/homing receptor stabilin-1 (FEEL-1/CLEVER-1).''; PubMed Europe PMC Scholia
6. Potter D, Chroneos ZC, Baynes JW, Sinclair PR, Gorman N, Liem HH, Muller-Eberhard U, Thorpe SR.; ''In vivo fate of hemopexin and heme-hemopexin complexes in the rat.''; PubMed Europe PMC Scholia
7. Babitt J, Trigatti B, Rigotti A, Smart EJ, Anderson RG, Xu S, Krieger M.; ''Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae.''; PubMed Europe PMC Scholia
8. Rechner C, Kühlewein C, Müller A, Schild H, Rudel T.; ''Host glycoprotein Gp96 and scavenger receptor SREC interact with PorB of disseminating Neisseria gonorrhoeae in an epithelial invasion pathway.''; PubMed Europe PMC Scholia
9. Boucher P, Herz J.; ''Signaling through LRP1: Protection from atherosclerosis and beyond.''; PubMed Europe PMC Scholia
10. Hamaguchi H, Isomoto A, Miyake Y, Nakajima H.; ''Some spectral properties of the human hemoglobin-haptoglobin complex.''; PubMed Europe PMC Scholia
11. Tolosano E, Fagoonee S, Morello N, Vinchi F, Fiorito V.; ''Heme scavenging and the other facets of hemopexin.''; PubMed Europe PMC Scholia
12. Baranova IN, Vishnyakova TG, Bocharov AV, Kurlander R, Chen Z, Kimelman ML, Remaley AT, Csako G, Thomas F, Eggerman TL, Patterson AP.; ''Serum amyloid A binding to CLA-1 (CD36 and LIMPII analogous-1) mediates serum amyloid A protein-induced activation of ERK1/2 and p38 mitogen-activated protein kinases.''; PubMed Europe PMC Scholia
13. Shakhov YA, Oram JF, Perova NV, Alexandri AL, Kolpakova GV, Marcovina S, Oganov RG, Bierman EL.; ''Comparative study of the activity and composition of HDL3 in Russian and American men.''; PubMed Europe PMC Scholia
14. Harris EN, Weigel PH.; ''The ligand-binding profile of HARE: hyaluronan and chondroitin sulfates A, C, and D bind to overlapping sites distinct from the sites for heparin, acetylated low-density lipoprotein, dermatan sulfate, and CS-E.''; PubMed Europe PMC Scholia
15. Gough PJ, Greaves DR, Gordon S.; ''A naturally occurring isoform of the human macrophage scavenger receptor (SR-A) gene generated by alternative splicing blocks modified LDL uptake.''; PubMed Europe PMC Scholia
16. Yang H, Chen SC, Tang YQ, Dai YL.; ''Effect of overexpression of human SR-AI on oxLDL uptake and apoptosis in 293T cells.''; PubMed Europe PMC Scholia
17. Boullier A, Gillotte KL, Hörkkö S, Green SR, Friedman P, Dennis EA, Witztum JL, Steinberg D, Quehenberger O.; ''The binding of oxidized low density lipoprotein to mouse CD36 is mediated in part by oxidized phospholipids that are associated with both the lipid and protein moieties of the lipoprotein.''; PubMed Europe PMC Scholia
18. Haisma HJ, Boesjes M, Beerens AM, van der Strate BW, Curiel DT, Plüddemann A, Gordon S, Bellu AR.; ''Scavenger receptor A: a new route for adenovirus 5.''; PubMed Europe PMC Scholia
19. Mielewczyk SS, Breslauer KJ, Anachi RB, Brodsky B.; ''Binding studies of a triple-helical peptide model of macrophage scavenger receptor to tetraplex nucleic acids.''; PubMed Europe PMC Scholia
20. Xu S, Laccotripe M, Huang X, Rigotti A, Zannis VI, Krieger M.; ''Apolipoproteins of HDL can directly mediate binding to the scavenger receptor SR-BI, an HDL receptor that mediates selective lipid uptake.''; PubMed Europe PMC Scholia
21. Tamura Y, Adachi H, Osuga J, Ohashi K, Yahagi N, Sekiya M, Okazaki H, Tomita S, Iizuka Y, Shimano H, Nagai R, Kimura S, Tsujimoto M, Ishibashi S.; ''FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end products.''; PubMed Europe PMC Scholia
22. Solar I, Muller-Eberhard U, Shaklai N.; ''Serum proteins as mediators of hemin efflux from red cell membranes: specificity of hemopexin.''; PubMed Europe PMC Scholia
23. Greer J, Liao WD, Brown WE.; ''Haptoglobin-hemoglobin complex. Subunit interaction probed by cross-linking.''; PubMed Europe PMC Scholia
24. Harris EN, Baggenstoss BA, Weigel PH.; ''Rat and human HARE/stabilin-2 are clearance receptors for high- and low-molecular-weight heparins.''; PubMed Europe PMC Scholia
25. Bultel-Brienne S, Lestavel S, Pilon A, Laffont I, Tailleux A, Fruchart JC, Siest G, Clavey V.; ''Lipid free apolipoprotein E binds to the class B Type I scavenger receptor I (SR-BI) and enhances cholesteryl ester uptake from lipoproteins.''; PubMed Europe PMC Scholia
26. Limmon GV, Arredouani M, McCann KL, Corn Minor RA, Kobzik L, Imani F.; ''Scavenger receptor class-A is a novel cell surface receptor for double-stranded RNA.''; PubMed Europe PMC Scholia
27. Peiser L, Gough PJ, Kodama T, Gordon S.; ''Macrophage class A scavenger receptor-mediated phagocytosis of Escherichia coli: role of cell heterogeneity, microbial strain, and culture conditions in vitro.''; PubMed Europe PMC Scholia
28. ALLISON AC, REES WA.; ''The binding of haemoglobin by plasma proteins (haptoglobins); its bearing on the renal threshold for haemoglobin and the aetiology of haemoglobinuria.''; PubMed Europe PMC Scholia
29. El Khoury J, Hickman SE, Thomas CA, Cao L, Silverstein SC, Loike JD.; ''Scavenger receptor-mediated adhesion of microglia to beta-amyloid fibrils.''; PubMed Europe PMC Scholia
30. Jang S, Ohtani K, Fukuoh A, Yoshizaki T, Fukuda M, Motomura W, Mori K, Fukuzawa J, Kitamoto N, Yoshida I, Suzuki Y, Wakamiya N.; ''Scavenger receptor collectin placenta 1 (CL-P1) predominantly mediates zymosan phagocytosis by human vascular endothelial cells.''; PubMed Europe PMC Scholia
31. Bodart V, Febbraio M, Demers A, McNicoll N, Pohankova P, Perreault A, Sejlitz T, Escher E, Silverstein RL, Lamontagne D, Ong H.; ''CD36 mediates the cardiovascular action of growth hormone-releasing peptides in the heart.''; PubMed Europe PMC Scholia
32. Araki N, Higashi T, Mori T, Shibayama R, Kawabe Y, Kodama T, Takahashi K, Shichiri M, Horiuchi S.; ''Macrophage scavenger receptor mediates the endocytic uptake and degradation of advanced glycation end products of the Maillard reaction.''; PubMed Europe PMC Scholia
33. Schaer DJ, Schaer CA, Buehler PW, Boykins RA, Schoedon G, Alayash AI, Schaffner A.; ''CD163 is the macrophage scavenger receptor for native and chemically modified hemoglobins in the absence of haptoglobin.''; PubMed Europe PMC Scholia
34. Hamilton RF, Thakur SA, Mayfair JK, Holian A.; ''MARCO mediates silica uptake and toxicity in alveolar macrophages from C57BL/6 mice.''; PubMed Europe PMC Scholia
35. Chakraborty S, Cai Y, Tarr MA.; ''Mapping oxidations of apolipoprotein B-100 in human low-density lipoprotein by liquid chromatography-tandem mass spectrometry.''; PubMed Europe PMC Scholia
36. Kzhyshkowska J, Workman G, Cardó-Vila M, Arap W, Pasqualini R, Gratchev A, Krusell L, Goerdt S, Sage EH.; ''Novel function of alternatively activated macrophages: stabilin-1-mediated clearance of SPARC.''; PubMed Europe PMC Scholia
37. Yoshida T, Tsuruta Y, Iwasaki M, Yamane S, Ochi T, Suzuki R.; ''SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn antigen.''; PubMed Europe PMC Scholia
38. Kazim AL, Atassi MZ.; ''Haemoglobin binding with haptoglobin. Unequivocal demonstration that the beta-chains of human haemoglobin bind to haptoglobin.''; PubMed Europe PMC Scholia
39. Peiser L, Makepeace K, Plüddemann A, Savino S, Wright JC, Pizza M, Rappuoli R, Moxon ER, Gordon S.; ''Identification of Neisseria meningitidis nonlipopolysaccharide ligands for class A macrophage scavenger receptor by using a novel assay.''; PubMed Europe PMC Scholia
40. Rigotti A, Acton SL, Krieger M.; ''The class B scavenger receptors SR-BI and CD36 are receptors for anionic phospholipids.''; PubMed Europe PMC Scholia
41. Neyen C, Plüddemann A, Roversi P, Thomas B, Cai L, van der Westhuyzen DR, Sim RB, Gordon S.; ''Macrophage scavenger receptor A mediates adhesion to apolipoproteins A-I and E.''; PubMed Europe PMC Scholia
42. Coombs PJ, Graham SA, Drickamer K, Taylor ME.; ''Selective binding of the scavenger receptor C-type lectin to Lewisx trisaccharide and related glycan ligands.''; PubMed Europe PMC Scholia
43. Allhorn M, Berggård T, Nordberg J, Olsson ML, Akerström B.; ''Processing of the lipocalin alpha(1)-microglobulin by hemoglobin induces heme-binding and heme-degradation properties.''; PubMed Europe PMC Scholia
44. Vinchi F, Gastaldi S, Silengo L, Altruda F, Tolosano E.; ''Hemopexin prevents endothelial damage and liver congestion in a mouse model of heme overload.''; PubMed Europe PMC Scholia
45. Selman L, Hansen S.; ''Structure and function of collectin liver 1 (CL-L1) and collectin 11 (CL-11, CL-K1).''; PubMed Europe PMC Scholia
46. Matsumoto A, Naito M, Itakura H, Ikemoto S, Asaoka H, Hayakawa I, Kanamori H, Aburatani H, Takaku F, Suzuki H.; ''Human macrophage scavenger receptors: primary structure, expression, and localization in atherosclerotic lesions.''; PubMed Europe PMC Scholia
47. Laugerette F, Passilly-Degrace P, Patris B, Niot I, Febbraio M, Montmayeur JP, Besnard P.; ''CD36 involvement in orosensory detection of dietary lipids, spontaneous fat preference, and digestive secretions.''; PubMed Europe PMC Scholia
48. Larsson J, Allhorn M, Kerström B.; ''The lipocalin alpha(1)-microglobulin binds heme in different species.''; PubMed Europe PMC Scholia
49. Collins RF, Touret N, Kuwata H, Tandon NN, Grinstein S, Trimble WS.; ''Uptake of oxidized low density lipoprotein by CD36 occurs by an actin-dependent pathway distinct from macropinocytosis.''; PubMed Europe PMC Scholia
50. Smith A, Morgan WT.; ''Hemopexin-mediated heme uptake by liver. Characterization of the interaction of heme-hemopexin with isolated rabbit liver plasma membranes.''; PubMed Europe PMC Scholia
51. Nielsen MJ, Petersen SV, Jacobsen C, Oxvig C, Rees D, Møller HJ, Moestrup SK.; ''Haptoglobin-related protein is a high-affinity hemoglobin-binding plasma protein.''; PubMed Europe PMC Scholia
52. Harris EN, Weigel JA, Weigel PH.; ''The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin.''; PubMed Europe PMC Scholia
53. Miller YI, Shaklai N.; ''Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation.''; PubMed Europe PMC Scholia
54. Murshid A, Gong J, Calderwood SK.; ''Heat shock protein 90 mediates efficient antigen cross presentation through the scavenger receptor expressed by endothelial cells-I.''; PubMed Europe PMC Scholia
55. Nielsen MJ, Møller HJ, Moestrup SK.; ''Hemoglobin and heme scavenger receptors.''; PubMed Europe PMC Scholia
56. Eckhardt ER, Cai L, Sun B, Webb NR, van der Westhuyzen DR.; ''High density lipoprotein uptake by scavenger receptor SR-BII.''; PubMed Europe PMC Scholia
57. Elshourbagy NA, Li X, Terrett J, Vanhorn S, Gross MS, Adamou JE, Anderson KM, Webb CL, Lysko PG.; ''Molecular characterization of a human scavenger receptor, human MARCO.''; PubMed Europe PMC Scholia
58. Schaer CA, Schoedon G, Imhof A, Kurrer MO, Schaer DJ.; ''Constitutive endocytosis of CD163 mediates hemoglobin-heme uptake and determines the noninflammatory and protective transcriptional response of macrophages to hemoglobin.''; PubMed Europe PMC Scholia
59. Fadok VA, Warner ML, Bratton DL, Henson PM.; ''CD36 is required for phagocytosis of apoptotic cells by human macrophages that use either a phosphatidylserine receptor or the vitronectin receptor (alpha v beta 3).''; PubMed Europe PMC Scholia
60. Harris EN, Weigel JA, Weigel PH.; ''Endocytic function, glycosaminoglycan specificity, and antibody sensitivity of the recombinant human 190-kDa hyaluronan receptor for endocytosis (HARE).''; PubMed Europe PMC Scholia
61. Abumrad NA, el-Maghrabi MR, Amri EZ, Lopez E, Grimaldi PA.; ''Cloning of a rat adipocyte membrane protein implicated in binding or transport of long-chain fatty acids that is induced during preadipocyte differentiation. Homology with human CD36.''; PubMed Europe PMC Scholia
62. Madsen M, Møller HJ, Nielsen MJ, Jacobsen C, Graversen JH, Graversen JH, van den Berg T, Moestrup SK.; ''Molecular characterization of the haptoglobin.hemoglobin receptor CD163. Ligand binding properties of the scavenger receptor cysteine-rich domain region.''; PubMed Europe PMC Scholia
63. Brännström A, Sankala M, Tryggvason K, Pikkarainen T.; ''Arginine residues in domain V have a central role for bacteria-binding activity of macrophage scavenger receptor MARCO.''; PubMed Europe PMC Scholia
64. Kristiansen M, Graversen JH, Graversen JH, Jacobsen C, Sonne O, Hoffman HJ, Law SK, Moestrup SK.; ''Identification of the haemoglobin scavenger receptor.''; PubMed Europe PMC Scholia
65. Li R, Oteiza A, Sørensen KK, McCourt P, Olsen R, Smedsrød B, Svistounov D.; ''Role of liver sinusoidal endothelial cells and stabilins in elimination of oxidized low-density lipoproteins.''; PubMed Europe PMC Scholia
66. Orr GA, Chrisler WB, Cassens KJ, Tan R, Tarasevich BJ, Markillie LM, Zangar RC, Thrall BD.; ''Cellular recognition and trafficking of amorphous silica nanoparticles by macrophage scavenger receptor A.''; PubMed Europe PMC Scholia
67. Bin LH, Nielson LD, Liu X, Mason RJ, Shu HB.; ''Identification of uteroglobin-related protein 1 and macrophage scavenger receptor with collagenous structure as a lung-specific ligand-receptor pair.''; PubMed Europe PMC Scholia
68. Elomaa O, Sankala M, Pikkarainen T, Bergmann U, Tuuttila A, Raatikainen-Ahokas A, Sariola H, Tryggvason K.; ''Structure of the human macrophage MARCO receptor and characterization of its bacteria-binding region.''; PubMed Europe PMC Scholia
69. Ohtani K, Suzuki Y, Eda S, Kawai T, Kase T, Keshi H, Sakai Y, Fukuoh A, Sakamoto T, Itabe H, Suzutani T, Ogasawara M, Yoshida I, Wakamiya N.; ''The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells.''; PubMed Europe PMC Scholia
70. Ohtani K, Suzuki Y, Wakamiya N.; ''Biological functions of the novel collectins CL-L1, CL-K1, and CL-P1.''; PubMed Europe PMC Scholia
71. Palecanda A, Paulauskis J, Al-Mutairi E, Imrich A, Qin G, Suzuki H, Kodama T, Tryggvason K, Koziel H, Kobzik L.; ''Role of the scavenger receptor MARCO in alveolar macrophage binding of unopsonized environmental particles.''; PubMed Europe PMC Scholia
72. Areschoug T, Gordon S.; ''Scavenger receptors: role in innate immunity and microbial pathogenesis.''; PubMed Europe PMC Scholia
73. Ip SH, Johnson ML, Ackers GK.; ''Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates.''; PubMed Europe PMC Scholia
74. Hoebe K, Georgel P, Rutschmann S, Du X, Mudd S, Crozat K, Sovath S, Shamel L, Hartung T, Zähringer U, Beutler B.; ''CD36 is a sensor of diacylglycerides.''; PubMed Europe PMC Scholia
75. Hansen S, Selman L, Palaniyar N, Ziegler K, Brandt J, Kliem A, Jonasson M, Skjoedt MO, Nielsen O, Hartshorn K, Jørgensen TJ, Skjødt K, Skjødt K, Holmskov U.; ''Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity.''; PubMed Europe PMC Scholia
76. Calero M, Escribano J, Grubb A, Méndez E.; ''Location of a novel type of interpolypeptide chain linkage in the human protein HC-IgA complex (HC-IgA) and identification of a heterogeneous chromophore associated with the complex.''; PubMed Europe PMC Scholia
77. Krieger M, Abrams JM, Lux A, Steller H.; ''Molecular flypaper, atherosclerosis, and host defense: structure and function of the macrophage scavenger receptor.''; PubMed Europe PMC Scholia
78. Adachi H, Tsujimoto M, Arai H, Inoue K.; ''Expression cloning of a novel scavenger receptor from human endothelial cells.''; PubMed Europe PMC Scholia
79. Rhainds D, Falstrault L, Tremblay C, Brissette L.; ''Uptake and fate of class B scavenger receptor ligands in HepG2 cells.''; PubMed Europe PMC Scholia
80. Waks M, Kahn PC, Beychok S.; ''Studies on the structures of haptoglobin 1-1 and hemoglobin in the haptoglobin-hemoglobin complex.''; PubMed Europe PMC Scholia
81. Miller YI, Smith A, Morgan WT, Shaklai N.; ''Role of hemopexin in protection of low-density lipoprotein against hemoglobin-induced oxidation.''; PubMed Europe PMC Scholia
82. Greenberg ME, Sun M, Zhang R, Febbraio M, Silverstein R, Hazen SL.; ''Oxidized phosphatidylserine-CD36 interactions play an essential role in macrophage-dependent phagocytosis of apoptotic cells.''; PubMed Europe PMC Scholia
83. Zeng Y, Tao N, Chung KN, Heuser JE, Lublin DM.; ''Endocytosis of oxidized low density lipoprotein through scavenger receptor CD36 utilizes a lipid raft pathway that does not require caveolin-1.''; PubMed Europe PMC Scholia
84. Thelen T, Hao Y, Medeiros AI, Curtis JL, Serezani CH, Kobzik L, Harris LH, Aronoff DM.; ''The class A scavenger receptor, macrophage receptor with collagenous structure, is the major phagocytic receptor for Clostridium sordellii expressed by human decidual macrophages.''; PubMed Europe PMC Scholia
85. Ascenzi P, Bocedi A, Visca P, Altruda F, Tolosano E, Beringhelli T, Fasano M.; ''Hemoglobin and heme scavenging.''; PubMed Europe PMC Scholia
86. Murao K, Terpstra V, Green SR, Kondratenko N, Steinberg D, Quehenberger O.; ''Characterization of CLA-1, a human homologue of rodent scavenger receptor BI, as a receptor for high density lipoprotein and apoptotic thymocytes.''; PubMed Europe PMC Scholia
87. JAYLE MF, BOUSSIER G, TONNELAT J.; ''[Isolation of the haptoglobin-hemoglobin complex in human blood in homogenous state. II].''; PubMed Europe PMC Scholia
88. DeWitte-Orr SJ, Collins SE, Bauer CM, Bowdish DM, Mossman KL.; ''An accessory to the 'Trinity': SR-As are essential pathogen sensors of extracellular dsRNA, mediating entry and leading to subsequent type I IFN responses.''; PubMed Europe PMC Scholia
89. Terpstra V, Bird DA, Steinberg D.; ''Evidence that the lipid moiety of oxidized low density lipoprotein plays a role in its interaction with macrophage receptors.''; PubMed Europe PMC Scholia
90. Wang R, Chandawarkar RY.; ''Phagocytosis of fungal agents and yeast via macrophage cell surface scavenger receptors.''; PubMed Europe PMC Scholia
91. Pasternack RF, Gibbs EJ, Mauk AG, Reid LS, Wong NM, Kurokawa K, Hashim M, Muller-Eberhard U.; ''Kinetics of hemoprotein reduction and interprotein heme transfer.''; PubMed Europe PMC Scholia
92. Zhou B, McGary CT, Weigel JA, Saxena A, Weigel PH.; ''Purification and molecular identification of the human hyaluronan receptor for endocytosis.''; PubMed Europe PMC Scholia
93. Zhang Y, Ahmed AM, Tran TL, Lin J, McFarlane N, Boreham DR, Igdoura SA, Truant R, Trigatti BL.; ''The inhibition of endocytosis affects HDL-lipid uptake mediated by the human scavenger receptor class B type I.''; PubMed Europe PMC Scholia
94. Józefowski S, Sulahian TH, Arredouani M, Kobzik L.; ''Role of scavenger receptor MARCO in macrophage responses to CpG oligodeoxynucleotides.''; PubMed Europe PMC Scholia
95. Bessa Pereira C, Bocková M, Santos RF, Santos AM, Martins de Araújo M, Oliveira L, Homola J, Carmo AM.; ''The Scavenger Receptor SSc5D Physically Interacts with Bacteria through the SRCR-Containing N-Terminal Domain.''; PubMed Europe PMC Scholia
96. Siebel JF, Kosinsky RL, Åkerström B, Knipp M.; ''Insertion of heme b into the structure of the Cys34-carbamidomethylated human lipocalin α(1)-microglobulin: formation of a [(heme)(2) (α(1)-Microglobulin)](3) complex.''; PubMed Europe PMC Scholia
97. Means TK, Mylonakis E, Tampakakis E, Colvin RA, Seung E, Puckett L, Tai MF, Stewart CR, Pukkila-Worley R, Hickman SE, Moore KJ, Calderwood SB, Hacohen N, Luster AD, El Khoury J.; ''Evolutionarily conserved recognition and innate immunity to fungal pathogens by the scavenger receptors SCARF1 and CD36.''; PubMed Europe PMC Scholia
98. Calvo D, Gómez-Coronado D, Lasunción MA, Vega MA.; ''CLA-1 is an 85-kD plasma membrane glycoprotein that acts as a high-affinity receptor for both native (HDL, LDL, and VLDL) and modified (OxLDL and AcLDL) lipoproteins.''; PubMed Europe PMC Scholia
99. Smith A, Morgan WT.; ''Hemopexin-mediated heme transport to the liver. Evidence for a heme-binding protein in liver plasma membranes.''; PubMed Europe PMC Scholia
100. Andersen CB, Torvund-Jensen M, Nielsen MJ, de Oliveira CL, Hersleth HP, Andersen NH, Pedersen JS, Andersen GR, Moestrup SK.; ''Structure of the haptoglobin-haemoglobin complex.''; PubMed Europe PMC Scholia
101. Smith A, Tatum FM, Muster P, Burch MK, Morgan WT.; ''Importance of ligand-induced conformational changes in hemopexin for receptor-mediated heme transport.''; PubMed Europe PMC Scholia
102. Dorrington MG, Roche AM, Chauvin SE, Tu Z, Mossman KL, Weiser JN, Bowdish DM.; ''MARCO is required for TLR2- and Nod2-mediated responses to Streptococcus pneumoniae and clearance of pneumococcal colonization in the murine nasopharynx.''; PubMed Europe PMC Scholia
103. Brown MS, Basu SK, Falck JR, Ho YK, Goldstein JL.; ''The scavenger cell pathway for lipoprotein degradation: specificity of the binding site that mediates the uptake of negatively-charged LDL by macrophages.''; PubMed Europe PMC Scholia
104. Harrington JM, Howell S, Hajduk SL.; ''Membrane permeabilization by trypanosome lytic factor, a cytolytic human high density lipoprotein.''; PubMed Europe PMC Scholia
105. Aguilar-Gaytan R, Mas-Oliva J.; ''Oxidative stress impairs endocytosis of the scavenger receptor class A.''; PubMed Europe PMC Scholia
106. Hvidberg V, Maniecki MB, Jacobsen C, Højrup P, Møller HJ, Moestrup SK.; ''Identification of the receptor scavenging hemopexin-heme complexes.''; PubMed Europe PMC Scholia
107. Mauk MR, Mauk AG.; ''Metal ions and electrolytes regulate the dissociation of heme from human hemopexin at physiological pH.''; PubMed Europe PMC Scholia
108. Adachi H, Tsujimoto M.; ''FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and angiogenesis-modulating activities.''; PubMed Europe PMC Scholia
109. Nakamura K, Funakoshi H, Miyamoto K, Tokunaga F, Nakamura T.; ''Molecular cloning and functional characterization of a human scavenger receptor with C-type lectin (SRCL), a novel member of a scavenger receptor family.''; PubMed Europe PMC Scholia
110. Eckhardt ER, Cai L, Shetty S, Zhao Z, Szanto A, Webb NR, Van der Westhuyzen DR.; ''High density lipoprotein endocytosis by scavenger receptor SR-BII is clathrin-dependent and requires a carboxyl-terminal dileucine motif.''; PubMed Europe PMC Scholia
111. Rosell FI, Mauk MR, Mauk AG.; ''pH- and metal ion-linked stability of the hemopexin-heme complex.''; PubMed Europe PMC Scholia
112. Pagler TA, Rhode S, Neuhofer A, Laggner H, Strobl W, Hinterndorfer C, Volf I, Pavelka M, Eckhardt ER, van der Westhuyzen DR, Schütz GJ, Stangl H.; ''SR-BI-mediated high density lipoprotein (HDL) endocytosis leads to HDL resecretion facilitating cholesterol efflux.''; PubMed Europe PMC Scholia
113. Mukhopadhyay S, Chen Y, Sankala M, Peiser L, Pikkarainen T, Kraal G, Tryggvason K, Gordon S.; ''MARCO, an innate activation marker of macrophages, is a class A scavenger receptor for Neisseria meningitidis.''; PubMed Europe PMC Scholia
114. Kzhyshkowska J, Gratchev A, Martens JH, Pervushina O, Mamidi S, Johansson S, Schledzewski K, Hansen B, He X, Tang J, Nakayama K, Goerdt S.; ''Stabilin-1 localizes to endosomes and the trans-Golgi network in human macrophages and interacts with GGA adaptors.''; PubMed Europe PMC Scholia
115. Kzhyshkowska J, Gratchev A, Brundiers H, Mamidi S, Krusell L, Goerdt S.; ''Phosphatidylinositide 3-kinase activity is required for stabilin-1-mediated endosomal transport of acLDL.''; PubMed Europe PMC Scholia
116. Hampton RY, Golenbock DT, Penman M, Krieger M, Raetz CR.; ''Recognition and plasma clearance of endotoxin by scavenger receptors.''; PubMed Europe PMC Scholia
117. Park SY, Jung MY, Kim HJ, Lee SJ, Kim SY, Lee BH, Kwon TH, Park RW, Kim IS.; ''Rapid cell corpse clearance by stabilin-2, a membrane phosphatidylserine receptor.''; PubMed Europe PMC Scholia
118. Ren Y, Silverstein RL, Allen J, Savill J.; ''CD36 gene transfer confers capacity for phagocytosis of cells undergoing apoptosis.''; PubMed Europe PMC Scholia
119. Goldstein JL, Ho YK, Basu SK, Brown MS.; ''Binding site on macrophages that mediates uptake and degradation of acetylated low density lipoprotein, producing massive cholesterol deposition.''; PubMed Europe PMC Scholia
120. Wardell M, Wang Z, Ho JX, Robert J, Ruker F, Ruble J, Carter DC.; ''The atomic structure of human methemalbumin at 1.9 A.''; PubMed Europe PMC Scholia
121. Harris EN, Kyosseva SV, Weigel JA, Weigel PH.; ''Expression, processing, and glycosaminoglycan binding activity of the recombinant human 315-kDa hyaluronic acid receptor for endocytosis (HARE).''; PubMed Europe PMC Scholia
122. Berwin B, Delneste Y, Lovingood RV, Post SR, Pizzo SV.; ''SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin.''; PubMed Europe PMC Scholia
123. Pearson AM, Rich A, Krieger M.; ''Polynucleotide binding to macrophage scavenger receptors depends on the formation of base-quartet-stabilized four-stranded helices.''; PubMed Europe PMC Scholia
124. Nilsen NJ, Deininger S, Nonstad U, Skjeldal F, Husebye H, Rodionov D, von Aulock S, Hartung T, Lien E, Bakke O, Espevik T.; ''Cellular trafficking of lipoteichoic acid and Toll-like receptor 2 in relation to signaling: role of CD14 and CD36.''; PubMed Europe PMC Scholia
125. Pasternack RF, Gibbs EJ, Hoeflin E, Kosar WP, Kubera G, Skowronek CA, Wong NM, Muller-Eberhard U.; ''Hemin binding to serum proteins and the catalysis of interprotein transfer.''; PubMed Europe PMC Scholia
126. Calvo D, Gómez-Coronado D, Suárez Y, Lasunción MA, Vega MA.; ''Human CD36 is a high affinity receptor for the native lipoproteins HDL, LDL, and VLDL.''; PubMed Europe PMC Scholia
127. McDermott-Roe C, Martin J, Collot-Teixeira S, McGregor JL.; ''CD36 N-terminal cytoplasmic domain is not required for the internalization of oxidized low-density lipoprotein.''; PubMed Europe PMC Scholia
128. Podrez EA, Febbraio M, Sheibani N, Schmitt D, Silverstein RL, Hajjar DP, Cohen PA, Frazier WA, Hoff HF, Hazen SL.; ''Macrophage scavenger receptor CD36 is the major receptor for LDL modified by monocyte-generated reactive nitrogen species.''; PubMed Europe PMC Scholia
129. Murphy JE, Tedbury PR, Homer-Vanniasinkam S, Walker JH, Ponnambalam S.; ''Biochemistry and cell biology of mammalian scavenger receptors.''; PubMed Europe PMC Scholia
130. Parthasarathy S, Fong LG, Otero D, Steinberg D.; ''Recognition of solubilized apoproteins from delipidated, oxidized low density lipoprotein (LDL) by the acetyl-LDL receptor.''; PubMed Europe PMC Scholia
131. Li X, Kan HY, Lavrentiadou S, Krieger M, Zannis V.; ''Reconstituted discoidal ApoE-phospholipid particles are ligands for the scavenger receptor BI. The amino-terminal 1-165 domain of ApoE suffices for receptor binding.''; PubMed Europe PMC Scholia
132. Smith A, Morgan WT.; ''Hemopexin-mediated transport of heme into isolated rat hepatocytes.''; PubMed Europe PMC Scholia
133. Apostolov EO, Shah SV, Ray D, Basnakian AG.; ''Scavenger receptors of endothelial cells mediate the uptake and cellular proatherogenic effects of carbamylated LDL.''; PubMed Europe PMC Scholia
134. Facciponte JG, Wang XY, Subjeck JR.; ''Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cells-I.''; PubMed Europe PMC Scholia
135. Sakai M, Miyazaki A, Hakamata H, Kobori S, Shichiri M, Horiuchi S.; ''Endocytic uptake of lysophosphatidylcholine mediated by macrophage scavenger receptor plays a major role in oxidized low density lipoprotein-induced macrophage growth.''; PubMed Europe PMC Scholia
136. Adams PA, Berman MC.; ''Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin.''; PubMed Europe PMC Scholia
137. Smith A, Farooqui SM, Morgan WT.; ''The murine haemopexin receptor. Evidence that the haemopexin-binding site resides on a 20 kDa subunit and that receptor recycling is regulated by protein kinase C.''; PubMed Europe PMC Scholia
138. Morgan WT, Liem HH, Sutor RP, Muller-Ebergard U.; ''Transfer of heme from heme-albumin to hemopexin.''; PubMed Europe PMC Scholia
139. Santiago-García J, Kodama T, Pitas RE.; ''The class A scavenger receptor binds to proteoglycans and mediates adhesion of macrophages to the extracellular matrix.''; PubMed Europe PMC Scholia
140. Widener J, Nielsen MJ, Shiflett A, Moestrup SK, Hajduk S.; ''Hemoglobin is a co-factor of human trypanosome lytic factor.''; PubMed Europe PMC Scholia
141. Resnick D, Chatterton JE, Schwartz K, Slayter H, Krieger M.; ''Structures of class A macrophage scavenger receptors. Electron microscopic study of flexible, multidomain, fibrous proteins and determination of the disulfide bond pattern of the scavenger receptor cysteine-rich domain.''; PubMed Europe PMC Scholia
142. Dunne DW, Resnick D, Greenberg J, Krieger M, Joiner KA.; ''The type I macrophage scavenger receptor binds to gram-positive bacteria and recognizes lipoteichoic acid.''; PubMed Europe PMC Scholia
143. Shiflett AM, Bishop JR, Pahwa A, Hajduk SL.; ''Human high density lipoproteins are platforms for the assembly of multi-component innate immune complexes.''; PubMed Europe PMC Scholia
144. Keshi H, Sakamoto T, Kawai T, Ohtani K, Katoh T, Jang SJ, Motomura W, Yoshizaki T, Fukuda M, Koyama S, Fukuzawa J, Fukuoh A, Yoshida I, Suzuki Y, Wakamiya N.; ''Identification and characterization of a novel human collectin CL-K1.''; PubMed Europe PMC Scholia
145. Berwin B, Hart JP, Rice S, Gass C, Pizzo SV, Post SR, Nicchitta CV.; ''Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells.''; PubMed Europe PMC Scholia
146. Dahl M, Bauer AK, Arredouani M, Soininen R, Tryggvason K, Kleeberger SR, Kobzik L.; ''Protection against inhaled oxidants through scavenging of oxidized lipids by macrophage receptors MARCO and SR-AI/II.''; PubMed Europe PMC Scholia
147. Janabi M, Yamashita S, Hirano K, Sakai N, Hiraoka H, Matsumoto K, Zhang Z, Nozaki S, Matsuzawa Y.; ''Oxidized LDL-induced NF-kappa B activation and subsequent expression of proinflammatory genes are defective in monocyte-derived macrophages from CD36-deficient patients.''; PubMed Europe PMC Scholia
148. Podrez EA, Poliakov E, Shen Z, Zhang R, Deng Y, Sun M, Finton PJ, Shan L, Gugiu B, Fox PL, Hoff HF, Salomon RG, Hazen SL.; ''Identification of a novel family of oxidized phospholipids that serve as ligands for the macrophage scavenger receptor CD36.''; PubMed Europe PMC Scholia
149. Park SY, Jung MY, Lee SJ, Kang KB, Gratchev A, Riabov V, Kzhyshkowska J, Kim IS.; ''Stabilin-1 mediates phosphatidylserine-dependent clearance of cell corpses in alternatively activated macrophages.''; PubMed Europe PMC Scholia
150. Yokota T, Ehlin-Henriksson B, Hansson GK.; ''Scavenger receptors mediate adhesion of activated B lymphocytes.''; PubMed Europe PMC Scholia
151. Tao N, Wagner SJ, Lublin DM.; ''CD36 is palmitoylated on both N- and C-terminal cytoplasmic tails.''; PubMed Europe PMC Scholia
152. Arredouani MS, Palecanda A, Koziel H, Huang YC, Imrich A, Sulahian TH, Ning YY, Yang Z, Pikkarainen T, Sankala M, Vargas SO, Takeya M, Tryggvason K, Kobzik L.; ''MARCO is the major binding receptor for unopsonized particles and bacteria on human alveolar macrophages.''; PubMed Europe PMC Scholia
153. Nielsen MJ, Petersen SV, Jacobsen C, Thirup S, Enghild JJ, Graversen JH, Graversen JH, Moestrup SK.; ''A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex.''; PubMed Europe PMC Scholia
154. Hansen B, Longati P, Elvevold K, Nedredal GI, Schledzewski K, Olsen R, Falkowski M, Kzhyshkowska J, Carlsson F, Johansson S, Smedsrød B, Goerdt S, Johansson S, McCourt P.; ''Stabilin-1 and stabilin-2 are both directed into the early endocytic pathway in hepatic sinusoidal endothelium via interactions with clathrin/AP-2, independent of ligand binding.''; PubMed Europe PMC Scholia
155. Vishnyakova TG, Bocharov AV, Baranova IN, Chen Z, Remaley AT, Csako G, Eggerman TL, Patterson AP.; ''Binding and internalization of lipopolysaccharide by Cla-1, a human orthologue of rodent scavenger receptor B1.''; PubMed Europe PMC Scholia
156. Smith A, Morgan WT.; ''Haem transport to the liver by haemopexin. Receptor-mediated uptake with recycling of the protein.''; PubMed Europe PMC Scholia
157. Gowen BB, Borg TK, Ghaffar A, Mayer EP.; ''Selective adhesion of macrophages to denatured forms of type I collagen is mediated by scavenger receptors.''; PubMed Europe PMC Scholia
158. Morgan WT.; ''The binding and transport of heme by hemopexin.''; PubMed Europe PMC Scholia
159. Palani S, Maksimow M, Miiluniemi M, Auvinen K, Jalkanen S, Salmi M.; ''Stabilin-1/CLEVER-1, a type 2 macrophage marker, is an adhesion and scavenging molecule on human placental macrophages.''; PubMed Europe PMC Scholia
160. Endemann G, Stanton LW, Madden KS, Bryant CM, White RT, Protter AA.; ''CD36 is a receptor for oxidized low density lipoprotein.''; PubMed Europe PMC Scholia

History

View all...

Compare	Revision	Action	Time	User	Comment
	117864	view	10:15, 23 May 2021	Eweitz	Modified title
	114786	view	16:28, 25 January 2021	ReactomeTeam	Reactome version 75
	113231	view	11:29, 2 November 2020	ReactomeTeam	Reactome version 74
	112452	view	15:40, 9 October 2020	ReactomeTeam	Reactome version 73
	101359	view	11:25, 1 November 2018	ReactomeTeam	reactome version 66
	100897	view	20:59, 31 October 2018	ReactomeTeam	reactome version 65
	100438	view	19:34, 31 October 2018	ReactomeTeam	reactome version 64
	99987	view	16:18, 31 October 2018	ReactomeTeam	reactome version 63
	99541	view	14:52, 31 October 2018	ReactomeTeam	reactome version 62 (2nd attempt)
	99175	view	12:42, 31 October 2018	ReactomeTeam	reactome version 62
	93792	view	13:36, 16 August 2017	ReactomeTeam	reactome version 61
	93328	view	11:20, 9 August 2017	ReactomeTeam	reactome version 61
	87094	view	14:28, 18 July 2016	Mkutmon	Ontology Term : 'transport pathway' added !
	86413	view	09:17, 11 July 2016	ReactomeTeam	reactome version 56
	83217	view	10:25, 18 November 2015	ReactomeTeam	Version54
	81607	view	13:09, 21 August 2015	ReactomeTeam	Version53
	77068	view	08:36, 17 July 2014	ReactomeTeam	Fixed remaining interactions
	76773	view	12:13, 16 July 2014	ReactomeTeam	Fixed remaining interactions
	76096	view	10:16, 11 June 2014	ReactomeTeam	Re-fixing comment source
	75808	view	11:35, 10 June 2014	ReactomeTeam	Reactome 48 Update
	75158	view	14:10, 8 May 2014	Anwesha	Fixing comment source for displaying WikiPathways description
	74805	view	08:54, 30 April 2014	ReactomeTeam	New pathway

External references

DataNodes

View all...

Name	Type	Database reference	Comment
1,3-beta-D-glucan [endocytic vesicle lumen]	Metabolite	CHEBI:37671 (ChEBI)
1,3-beta-D-glucan [extracellular region]	Metabolite	CHEBI:37671 (ChEBI)
10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) [endocytic vesicle lumen]	Protein	P04114 (Uniprot-TrEMBL)
10xdHF-10xglutamyl semialdehyde (Pro)-6xL-tyrosine residue-3xOxoH-2xmodified L-lysine residue-N'-formyl-L-kynurenine-APOB(28-4563) [extracellular region]	Protein	P04114 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-5Hyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-5Hyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-5Hyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GalHyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GalHyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GalHyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GlcGalHyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GlcGalHyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-3Hyp-GlcGalHyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-5Hyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-5Hyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-5Hyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-GalHyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-GalHyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-GalHyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
3x4Hyp-GlcGalHyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
3x4Hyp-GlcGalHyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
3x4Hyp-GlcGalHyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
4xPalmC-CD36 [endocytic vesicle membrane]	Protein	P16671 (Uniprot-TrEMBL)
4xPalmC-CD36 [plasma membrane]	Protein	P16671 (Uniprot-TrEMBL)
4xPalmC-CD36	Protein	P16671 (Uniprot-TrEMBL)
5,6beta-epoxy-cholesterol [endocytic vesicle lumen]	Metabolite	CHEBI:28164 (ChEBI)
5,6beta-epoxy-cholesterol [extracellular region]	Metabolite	CHEBI:28164 (ChEBI)
5Hyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
5Hyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
5Hyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
5xHC-HP(162-406) [endocytic vesicle lumen]	Protein	P00738 (Uniprot-TrEMBL)
5xHC-HP(162-406) [extracellular region]	Protein	P00738 (Uniprot-TrEMBL)
6xHC-MARCO [endocytic vesicle membrane]	Protein	Q9UEW3 (Uniprot-TrEMBL)
6xHC-MARCO [plasma membrane]	Protein	Q9UEW3 (Uniprot-TrEMBL)
6xHC-MSR1 [endocytic vesicle membrane]	Protein	P21757 (Uniprot-TrEMBL)
6xHC-MSR1 [plasma membrane]	Protein	P21757 (Uniprot-TrEMBL)
7-ketocholesterol [endocytic vesicle lumen]	Metabolite	CHEBI:64294 (ChEBI)
7-ketocholesterol [extracellular region]	Metabolite	CHEBI:64294 (ChEBI)
7xHC-HP(19-160) [endocytic vesicle lumen]	Protein	P00738 (Uniprot-TrEMBL)
7xHC-HP(19-160) [extracellular region]	Protein	P00738 (Uniprot-TrEMBL)
ALB [extracellular region]	Protein	P02768 (Uniprot-TrEMBL)
ALB	Protein	P02768 (Uniprot-TrEMBL)
AMBP(20-198) [extracellular region]	Protein	P02760 (Uniprot-TrEMBL)
AMBP(20-198)	Protein	P02760 (Uniprot-TrEMBL)
AMBP(20-202) [extracellular region]	Protein	P02760 (Uniprot-TrEMBL)
AMBP(20-202)	Protein	P02760 (Uniprot-TrEMBL)
APOA1(25-266) [endocytic vesicle lumen]	Protein	P02647 (Uniprot-TrEMBL)
APOA1(25-266) [extracellular region]	Protein	P02647 (Uniprot-TrEMBL)
APOB(28-4563) [endocytic vesicle lumen]	Protein	P04114 (Uniprot-TrEMBL)
APOB(28-4563) [extracellular region]	Protein	P04114 (Uniprot-TrEMBL)
APOE [endocytic vesicle lumen]	Protein	P02649 (Uniprot-TrEMBL)
APOE [extracellular region]	Protein	P02649 (Uniprot-TrEMBL)
APOL1 [extracellular region]	Protein	O14791 (Uniprot-TrEMBL)
AcK-APOB(28-4563) [endocytic vesicle lumen]	Protein	P04114 (Uniprot-TrEMBL)
AcK-APOB(28-4563) [extracellular region]	Protein	P04114 (Uniprot-TrEMBL)
Albumin:ferriheme	Complex	REACT_160718 (Reactome)
Alpha1-Microglobulin:heme trimer	Complex	REACT_161267 (Reactome)
Apohemoglobin	Complex	REACT_161051 (Reactome)
CALR [endocytic vesicle lumen]	Protein	P27797 (Uniprot-TrEMBL)
CALR [extracellular region]	Protein	P27797 (Uniprot-TrEMBL)
CD163 [endocytic vesicle membrane]	Protein	Q86VB7 (Uniprot-TrEMBL)
CD163 [plasma membrane]	Protein	Q86VB7 (Uniprot-TrEMBL)
CD163	Protein	Q86VB7 (Uniprot-TrEMBL)
CHEST [extracellular region]	Metabolite	CHEBI:17002 (ChEBI)
CHOL [extracellular region]	Metabolite	CHEBI:16113 (ChEBI)
CHS [endocytic vesicle lumen]	Metabolite	CHEBI:37397 (ChEBI)
CHS [extracellular region]	Metabolite	CHEBI:37397 (ChEBI)
COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
COL4A1(173-1669) [extracellular region]	Protein	P02462 (Uniprot-TrEMBL)
COL4A2(184-?) [extracellular region]	Protein	P08572 (Uniprot-TrEMBL)
COLEC11 [extracellular region]	Protein	Q9BWP8 (Uniprot-TrEMBL)
COLEC11:Ligand	Complex	REACT_164610 (Reactome)
COLEC11:MASP1	Complex	REACT_165089 (Reactome)
COLEC12 [endocytic vesicle membrane]	Protein	Q5KU26 (Uniprot-TrEMBL)
COLEC12 [plasma membrane]	Protein	Q5KU26 (Uniprot-TrEMBL)
COLEC12 trimer	Complex	REACT_164280 (Reactome)
COLEC12:Ligand	Complex	REACT_164817 (Reactome)
COLEC12:Ligand	Complex	REACT_164862 (Reactome)
Denatured Collagen I,III, Collagen IV	Complex	REACT_164920 (Reactome)
FTH1(2-183) [endocytic vesicle lumen]	Protein	P02794 (Uniprot-TrEMBL)
FTH1(2-183) [extracellular region]	Protein	P02794 (Uniprot-TrEMBL)
FTL [endocytic vesicle lumen]	Protein	P02792 (Uniprot-TrEMBL)
FTL [extracellular region]	Protein	P02792 (Uniprot-TrEMBL)
Fe3+ [endocytic vesicle lumen]	Metabolite	CHEBI:29034 (ChEBI)
Fe3+ [extracellular region]	Metabolite	CHEBI:29034 (ChEBI)
GalHyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
GalHyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
GalHyl-COL3A1 [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
GalNAc [extracellular region]	Metabolite	CHEBI:28037 (ChEBI)
GalNAc [endocytic vesicle lumen]	Metabolite	CHEBI:28037 (ChEBI)
GlcGalHyl-COL1A1 [extracellular region]	Protein	P02452 (Uniprot-TrEMBL)
GlcGalHyl-COL1A2 [extracellular region]	Protein	P08123 (Uniprot-TrEMBL)
GlcGalHyl-COL3A1(154-1241) [extracellular region]	Protein	P02461 (Uniprot-TrEMBL)
GlcNAc [extracellular region]	Metabolite	CHEBI:17411 (ChEBI)
HBA1 [endocytic vesicle lumen]	Protein	P69905 (Uniprot-TrEMBL)
HBA1 [extracellular region]	Protein	P69905 (Uniprot-TrEMBL)
HBB [endocytic vesicle lumen]	Protein	P68871 (Uniprot-TrEMBL)
HBB [extracellular region]	Protein	P68871 (Uniprot-TrEMBL)
HPR [extracellular region]	Protein	P00739 (Uniprot-TrEMBL)
HPR:APOL1:APOA1:HDL3	Complex	REACT_160983 (Reactome)
HPX [endocytic vesicle lumen]	Protein	P02790 (Uniprot-TrEMBL)
HPX [extracellular region]	Protein	P02790 (Uniprot-TrEMBL)
HPX:ferriheme b	Complex	REACT_161270 (Reactome)
HPX:heme b	Complex	REACT_160999 (Reactome)
HPX	Protein	P02790 (Uniprot-TrEMBL)
HSP90AA1 [extracellular region]	Protein	P07900 (Uniprot-TrEMBL)
HSP90AA1 [endocytic vesicle lumen]	Protein	P07900 (Uniprot-TrEMBL)
HSP90B1 [extracellular region]	Protein	P14625 (Uniprot-TrEMBL)
HSP90B1 [endocytic vesicle lumen]	Protein	P14625 (Uniprot-TrEMBL)
HSPH1 [endocytic vesicle lumen]	Protein	Q92598 (Uniprot-TrEMBL)
HSPH1 [extracellular region]	Protein	Q92598 (Uniprot-TrEMBL)
HUA [endocytic vesicle lumen]	Metabolite	CHEBI:16336 (ChEBI)
HUA [extracellular region]	Metabolite	CHEBI:16336 (ChEBI)
HYOU1 [endocytic vesicle lumen]	Protein	Q9Y4L1 (Uniprot-TrEMBL)
HYOU1 [extracellular region]	Protein	Q9Y4L1 (Uniprot-TrEMBL)
Haptoglobin Dimer	Complex	REACT_161554 (Reactome)
Hemoglobin Dimer	Complex	REACT_161542 (Reactome)
Hemoglobin:HPR:APOL1:APOA1:HDL3	Complex	REACT_160920 (Reactome)
Hemoglobin:Haptoglobin:CD163	Complex	REACT_161113 (Reactome)
Hemoglobin:Haptoglobin:CD163	Complex	REACT_161221 (Reactome)
Hemoglobin:Haptoglobin	Complex	REACT_160524 (Reactome)
Heparins [extracellular region]	Metabolite	CHEBI:24505 (ChEBI)
Heparins [endocytic vesicle lumen]	Metabolite	CHEBI:24505 (ChEBI)
IGHA1(1-353) [extracellular region]	Protein	P01876 (Uniprot-TrEMBL)
IGHA2(1-340) [extracellular region]	Protein	P01877 (Uniprot-TrEMBL)
IGHV(1-?) [extracellular region]	Protein	A2KUC3 (Uniprot-TrEMBL)
IGHV7-81(1-?) [extracellular region]	Protein	Q6PIL0 (Uniprot-TrEMBL)
IGKC(1-106) [extracellular region]	Protein	P01834 (Uniprot-TrEMBL)
IGKV1-5(23-?) [extracellular region]	Protein	P01602 (Uniprot-TrEMBL)
IGKV4-1(21-?) [extracellular region]	Protein	P06312 (Uniprot-TrEMBL)
IGKVA18(21-?) [extracellular region]	Protein	A2NJV5 (Uniprot-TrEMBL)
IGLC1(1-105) [extracellular region]	Protein	P0CG04 (Uniprot-TrEMBL)
IGLC2(?-106) [extracellular region]	Protein	P0CG05 (Uniprot-TrEMBL)
IGLC3(?-106) [extracellular region]	Protein	P0CG06 (Uniprot-TrEMBL)
IGLC6(?-106) [extracellular region]	Protein	P0CF74 (Uniprot-TrEMBL)
IGLC7(?-106) [extracellular region]	Protein	A0M8Q6 (Uniprot-TrEMBL)
IGLV(23-?) [extracellular region]	Protein	A2NXD2 (Uniprot-TrEMBL)
IGLV1-36(1-?) [extracellular region]	Protein	Q5NV67 (Uniprot-TrEMBL)
IGLV1-40(1-?) [extracellular region]	Protein	Q5NV69 (Uniprot-TrEMBL)
IGLV1-44(1-?) [extracellular region]	Protein	Q5NV81 (Uniprot-TrEMBL)
IGLV10-54(1-?) [extracellular region]	Protein	Q5NV86 (Uniprot-TrEMBL)
IGLV11-55(1-?) [extracellular region]	Protein	Q5NV87 (Uniprot-TrEMBL)
IGLV2-11(1-?) [extracellular region]	Protein	Q5NV84 (Uniprot-TrEMBL)
IGLV2-18(1-?) [extracellular region]	Protein	Q5NV65 (Uniprot-TrEMBL)
IGLV2-23(1-?) [extracellular region]	Protein	Q5NV89 (Uniprot-TrEMBL)
IGLV2-33(1-?) [extracellular region]	Protein	Q5NV66 (Uniprot-TrEMBL)
IGLV3-12(1-?) [extracellular region]	Protein	Q5NV85 (Uniprot-TrEMBL)
IGLV3-16(1-?) [extracellular region]	Protein	Q5NV64 (Uniprot-TrEMBL)
IGLV3-22(1-?) [extracellular region]	Protein	Q5NV75 (Uniprot-TrEMBL)
IGLV3-25(1-?) [extracellular region]	Protein	Q5NV90 (Uniprot-TrEMBL)
IGLV3-27(1-?) [extracellular region]	Protein	Q5NV91 (Uniprot-TrEMBL)
IGLV4-3(1-?) [extracellular region]	Protein	Q5NV61 (Uniprot-TrEMBL)
IGLV4-60(1-?) [extracellular region]	Protein	Q5NV79 (Uniprot-TrEMBL)
IGLV4-69(1-?) [extracellular region]	Protein	Q5NV92 (Uniprot-TrEMBL)
IGLV5-37(1-?) [extracellular region]	Protein	Q5NV68 (Uniprot-TrEMBL)
IGLV5-45(1-?) [extracellular region]	Protein	Q5NV82 (Uniprot-TrEMBL)
IGLV7-43(1-?) [extracellular region]	Protein	Q5NV80 (Uniprot-TrEMBL)
IGLV7-46(1-?) [extracellular region]	Protein	Q5NV83 (Uniprot-TrEMBL)
IGLV8-61(1-?) [extracellular region]	Protein	Q5NV62 (Uniprot-TrEMBL)
Ig heavy chain V-I region EU [extracellular region]	Protein	P01742 (Uniprot-TrEMBL)
Ig heavy chain V-I region HG3 [extracellular region]	Protein	P01743 (Uniprot-TrEMBL)
Ig heavy chain V-I region Mot [extracellular region]	Protein	P06326 (Uniprot-TrEMBL)
Ig heavy chain V-I region ND [extracellular region]	Protein	P01744 (Uniprot-TrEMBL)
Ig heavy chain V-I region SIE [extracellular region]	Protein	P01761 (Uniprot-TrEMBL)
Ig heavy chain V-I region WOL [extracellular region]	Protein	P01760 (Uniprot-TrEMBL)
Ig heavy chain V-II region ARH-77 [extracellular region]	Protein	P06331 (Uniprot-TrEMBL)
Ig heavy chain V-II region COR [extracellular region]	Protein	P01815 (Uniprot-TrEMBL)
Ig heavy chain V-II region DAW [extracellular region]	Protein	P01816 (Uniprot-TrEMBL)
Ig heavy chain V-II region HE [extracellular region]	Protein	P01818 (Uniprot-TrEMBL)
Ig heavy chain V-II region MCE [extracellular region]	Protein	P01817 (Uniprot-TrEMBL)
Ig heavy chain V-II region NEWM [extracellular region]	Protein	P01825 (Uniprot-TrEMBL)
Ig heavy chain V-II region OU [extracellular region]	Protein	P01814 (Uniprot-TrEMBL)
Ig heavy chain V-II region SESS [extracellular region]	Protein	P04438 (Uniprot-TrEMBL)
Ig heavy chain V-II region WAH [extracellular region]	Protein	P01824 (Uniprot-TrEMBL)
Ig heavy chain V-III region BRO [extracellular region]	Protein	P01766 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUR [extracellular region]	Protein	P01773 (Uniprot-TrEMBL)
Ig heavy chain V-III region BUT [extracellular region]	Protein	P01767 (Uniprot-TrEMBL)
Ig heavy chain V-III region CAM [extracellular region]	Protein	P01768 (Uniprot-TrEMBL)
Ig heavy chain V-III region DOB [extracellular region]	Protein	P01782 (Uniprot-TrEMBL)
Ig heavy chain V-III region GA [extracellular region]	Protein	P01769 (Uniprot-TrEMBL)
Ig heavy chain V-III region GAL [extracellular region]	Protein	P01781 (Uniprot-TrEMBL)
Ig heavy chain V-III region HIL [extracellular region]	Protein	P01771 (Uniprot-TrEMBL)
Ig heavy chain V-III region JON [extracellular region]	Protein	P01780 (Uniprot-TrEMBL)
Ig heavy chain V-III region KOL [extracellular region]	Protein	P01772 (Uniprot-TrEMBL)
Ig heavy chain V-III region LAY [extracellular region]	Protein	P01775 (Uniprot-TrEMBL)
Ig heavy chain V-III region NIE [extracellular region]	Protein	P01770 (Uniprot-TrEMBL)
Ig heavy chain V-III region POM [extracellular region]	Protein	P01774 (Uniprot-TrEMBL)
Ig heavy chain V-III region TEI [extracellular region]	Protein	P01777 (Uniprot-TrEMBL)
Ig heavy chain V-III region TIL [extracellular region]	Protein	P01765 (Uniprot-TrEMBL)
Ig heavy chain V-III region TRO [extracellular region]	Protein	P01762 (Uniprot-TrEMBL)
Ig heavy chain V-III region TUR [extracellular region]	Protein	P01779 (Uniprot-TrEMBL)
Ig heavy chain V-III region WAS [extracellular region]	Protein	P01776 (Uniprot-TrEMBL)
Ig heavy chain V-III region WEA [extracellular region]	Protein	P01763 (Uniprot-TrEMBL)
Ig heavy chain V-III region ZAP [extracellular region]	Protein	P01778 (Uniprot-TrEMBL)
Ig kappa chain V region EV15 [extracellular region]	Protein	P06315 (Uniprot-TrEMBL)
Ig kappa chain V-I region AG [extracellular region]	Protein	P01593 (Uniprot-TrEMBL)
Ig kappa chain V-I region AU [extracellular region]	Protein	P01594 (Uniprot-TrEMBL)
Ig kappa chain V-I region BAN [extracellular region]	Protein	P04430 (Uniprot-TrEMBL)
Ig kappa chain V-I region Bi [extracellular region]	Protein	P01595 (Uniprot-TrEMBL)
Ig kappa chain V-I region CAR [extracellular region]	Protein	P01596 (Uniprot-TrEMBL)
Ig kappa chain V-I region DEE [extracellular region]	Protein	P01597 (Uniprot-TrEMBL)
Ig kappa chain V-I region Daudi [extracellular region]	Protein	P04432 (Uniprot-TrEMBL)
Ig kappa chain V-I region EU [extracellular region]	Protein	P01598 (Uniprot-TrEMBL)
Ig kappa chain V-I region Gal [extracellular region]	Protein	P01599 (Uniprot-TrEMBL)
Ig kappa chain V-I region HK101 [extracellular region]	Protein	P01601 (Uniprot-TrEMBL)
Ig kappa chain V-I region Hau [extracellular region]	Protein	P01600 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ka [extracellular region]	Protein	P01603 (Uniprot-TrEMBL)
Ig kappa chain V-I region Kue [extracellular region]	Protein	P01604 (Uniprot-TrEMBL)
Ig kappa chain V-I region Lay [extracellular region]	Protein	P01605 (Uniprot-TrEMBL)
Ig kappa chain V-I region Mev [extracellular region]	Protein	P01612 (Uniprot-TrEMBL)
Ig kappa chain V-I region Ni [extracellular region]	Protein	P01613 (Uniprot-TrEMBL)
Ig kappa chain V-I region OU [extracellular region]	Protein	P01606 (Uniprot-TrEMBL)
Ig kappa chain V-I region Rei [extracellular region]	Protein	P01607 (Uniprot-TrEMBL)
Ig kappa chain V-I region Roy [extracellular region]	Protein	P01608 (Uniprot-TrEMBL)
Ig kappa chain V-I region Scw [extracellular region]	Protein	P01609 (Uniprot-TrEMBL)
Ig kappa chain V-I region WAT [extracellular region]	Protein	P80362 (Uniprot-TrEMBL)
Ig kappa chain V-I region WEA [extracellular region]	Protein	P01610 (Uniprot-TrEMBL)
Ig kappa chain V-I region Walker [extracellular region]	Protein	P04431 (Uniprot-TrEMBL)
Ig kappa chain V-I region Wes [extracellular region]	Protein	P01611 (Uniprot-TrEMBL)
Ig kappa chain V-II region Cum [extracellular region]	Protein	P01614 (Uniprot-TrEMBL)
Ig kappa chain V-II region FR [extracellular region]	Protein	P01615 (Uniprot-TrEMBL)
Ig kappa chain V-II region GM607 [extracellular region]	Protein	P06309 (Uniprot-TrEMBL)
Ig kappa chain V-II region MIL [extracellular region]	Protein	P01616 (Uniprot-TrEMBL)
Ig kappa chain V-II region RPMI 6410 [extracellular region]	Protein	P06310 (Uniprot-TrEMBL)
Ig kappa chain V-II region TEW [extracellular region]	Protein	P01617 (Uniprot-TrEMBL)
Ig kappa chain V-III region B6 [extracellular region]	Protein	P01619 (Uniprot-TrEMBL)
Ig kappa chain V-III region CLL [extracellular region]	Protein	P04207 (Uniprot-TrEMBL)
Ig kappa chain V-III region GOL [extracellular region]	Protein	P04206 (Uniprot-TrEMBL)
Ig kappa chain V-III region HAH [extracellular region]	Protein	P18135 (Uniprot-TrEMBL)
Ig kappa chain V-III region HIC [extracellular region]	Protein	P18136 (Uniprot-TrEMBL)
Ig kappa chain V-III region IARC/BL41 [extracellular region]	Protein	P06311 (Uniprot-TrEMBL)
Ig kappa chain V-III region NG9 [extracellular region]	Protein	P01621 (Uniprot-TrEMBL)
Ig kappa chain V-III region POM [extracellular region]	Protein	P01624 (Uniprot-TrEMBL)
Ig kappa chain V-III region SIE [extracellular region]	Protein	P01620 (Uniprot-TrEMBL)
Ig kappa chain V-III region Ti [extracellular region]	Protein	P01622 (Uniprot-TrEMBL)
Ig kappa chain V-III region VG [extracellular region]	Protein	P04433 (Uniprot-TrEMBL)
Ig kappa chain V-III region VH [extracellular region]	Protein	P04434 (Uniprot-TrEMBL)
Ig kappa chain V-III region WOL [extracellular region]	Protein	P01623 (Uniprot-TrEMBL)
Ig kappa chain V-IV region B17 [extracellular region]	Protein	P06314 (Uniprot-TrEMBL)
Ig kappa chain V-IV region JI [extracellular region]	Protein	P06313 (Uniprot-TrEMBL)
Ig kappa chain V-IV region Len [extracellular region]	Protein	P01625 (Uniprot-TrEMBL)
Ig kappa chain V-IV region STH [extracellular region]	Protein	P83593 (Uniprot-TrEMBL)
Ig lambda chain V-III region LOI [extracellular region]	Protein	P80748 (Uniprot-TrEMBL)
Ig lambda chain V-III region SH [extracellular region]	Protein	P01714 (Uniprot-TrEMBL)
Ig lambda chain V-VII region MOT [extracellular region]	Protein	P01720 (Uniprot-TrEMBL)
Ig lambda chain V region 4A [extracellular region]	Protein	P04211 (Uniprot-TrEMBL)
Ig lambda chain V-I region BL2 [extracellular region]	Protein	P06316 (Uniprot-TrEMBL)
Ig lambda chain V-I region EPS [extracellular region]	Protein	P06888 (Uniprot-TrEMBL)
Ig lambda chain V-I region HA [extracellular region]	Protein	P01700 (Uniprot-TrEMBL)
Ig lambda chain V-I region MEM [extracellular region]	Protein	P06887 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEW [extracellular region]	Protein	P01701 (Uniprot-TrEMBL)
Ig lambda chain V-I region NEWM [extracellular region]	Protein	P01703 (Uniprot-TrEMBL)
Ig lambda chain V-I region NIG-64 [extracellular region]	Protein	P01702 (Uniprot-TrEMBL)
Ig lambda chain V-I region VOR [extracellular region]	Protein	P01699 (Uniprot-TrEMBL)
Ig lambda chain V-I region WAH [extracellular region]	Protein	P04208 (Uniprot-TrEMBL)
Ig lambda chain V-II region BO [extracellular region]	Protein	P01710 (Uniprot-TrEMBL)
Ig lambda chain V-II region BOH [extracellular region]	Protein	P01706 (Uniprot-TrEMBL)
Ig lambda chain V-II region BUR [extracellular region]	Protein	P01708 (Uniprot-TrEMBL)
Ig lambda chain V-II region MGC [extracellular region]	Protein	P01709 (Uniprot-TrEMBL)
Ig lambda chain V-II region NEI [extracellular region]	Protein	P01705 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-58 [extracellular region]	Protein	P01713 (Uniprot-TrEMBL)
Ig lambda chain V-II region NIG-84 [extracellular region]	Protein	P04209 (Uniprot-TrEMBL)
Ig lambda chain V-II region TOG [extracellular region]	Protein	P01704 (Uniprot-TrEMBL)
Ig lambda chain V-II region TRO [extracellular region]	Protein	P01707 (Uniprot-TrEMBL)
Ig lambda chain V-II region VIL [extracellular region]	Protein	P01711 (Uniprot-TrEMBL)
Ig lambda chain V-II region WIN [extracellular region]	Protein	P01712 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Bau [extracellular region]	Protein	P01715 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Hil [extracellular region]	Protein	P01717 (Uniprot-TrEMBL)
Ig lambda chain V-IV region Kern [extracellular region]	Protein	P01718 (Uniprot-TrEMBL)
Ig lambda chain V-IV region MOL [extracellular region]	Protein	P06889 (Uniprot-TrEMBL)
Ig lambda chain V-IV region X [extracellular region]	Protein	P01716 (Uniprot-TrEMBL)
Ig lambda chain V-V region DEL [extracellular region]	Protein	P01719 (Uniprot-TrEMBL)
Ig lambda chain V-VI region AR [extracellular region]	Protein	P01721 (Uniprot-TrEMBL)
Ig lambda chain V-VI region EB4 [extracellular region]	Protein	P06319 (Uniprot-TrEMBL)
Ig lambda chain V-VI region NIG-48 [extracellular region]	Protein	P01722 (Uniprot-TrEMBL)
Ig lambda chain V-VI region SUT [extracellular region]	Protein	P06317 (Uniprot-TrEMBL)
Ig lambda chain V-VI region WLT [extracellular region]	Protein	P06318 (Uniprot-TrEMBL)
IgA:Alpha-1-Microglobulin	Complex	REACT_161115 (Reactome)
IgA	Complex	REACT_160552 (Reactome)
IgH heavy chain V-III region VH26 precursor [extracellular region]	Protein	P01764 (Uniprot-TrEMBL)
L-fucose [extracellular region]	Metabolite	CHEBI:2181 (ChEBI)
LCFAs [endocytic vesicle lumen]	Metabolite	CHEBI:15904 (ChEBI)
LCFAs [extracellular region]	Metabolite	CHEBI:15904 (ChEBI)
LPS [endocytic vesicle lumen]	Metabolite	CHEBI:16412 (ChEBI)
LPS [extracellular region]	Metabolite	CHEBI:16412 (ChEBI)
LRP1 [endocytic vesicle membrane]	Protein	Q07954 (Uniprot-TrEMBL)
LRP1 [plasma membrane]	Protein	Q07954 (Uniprot-TrEMBL)
LRP1:Hemopexin:heme	Complex	REACT_160657 (Reactome)
LRP1:Hemopexin:heme	Complex	REACT_161454 (Reactome)
LRP1	Protein	Q07954 (Uniprot-TrEMBL)
Ligands of CD36	Complex	REACT_164594 (Reactome)
Ligands of COLEC11	Metabolite	REACT_164682 (Reactome)
Ligands of COLEC12		REACT_164668 (Reactome)
Ligands of MARCO	Metabolite	REACT_164133 (Reactome)
Ligands of MSR1	Metabolite	REACT_164161 (Reactome)
Ligands of SCARA5		REACT_165390 (Reactome)
Ligands of SCARB1	Complex	REACT_165375 (Reactome)
Ligands of SCARF1	Metabolite	REACT_165072 (Reactome)
Ligands of STAB1	Complex	REACT_165287 (Reactome)
Ligands of STAB2	Metabolite	REACT_165222 (Reactome)
Lipoteichoic acid [endocytic vesicle lumen]	Metabolite	CHEBI:28640 (ChEBI)
Lipoteichoic acid [extracellular region]	Metabolite	CHEBI:28640 (ChEBI)
MARCO trimer	Complex	REACT_165245 (Reactome)
MARCO:Ligand	Complex	REACT_164163 (Reactome)
MARCO:Ligand	Complex	REACT_164178 (Reactome)
MASP1(20-699) [extracellular region]	Protein	P48740 (Uniprot-TrEMBL)
MSR1 (SCARA1) trimer	Complex	REACT_164470 (Reactome)
MSR1:Collagen I,III,IV	Complex	REACT_165150 (Reactome)
MSR1:Ligand	Complex	REACT_164371 (Reactome)
MSR1:Ligand	Complex	REACT_165339 (Reactome)
Man [extracellular region]	Metabolite	CHEBI:4208 (ChEBI)
Methemoglobin	Complex	REACT_160621 (Reactome)
N-epsilon-(1-(1-carboxy)ethyl)lysine [endocytic vesicle lumen]	Metabolite	CHEBI:60125 (ChEBI)
N-epsilon-(1-(1-carboxy)ethyl)lysine [extracellular region]	Metabolite	CHEBI:60125 (ChEBI)
NECML [endocytic vesicle lumen]	Metabolite	CHEBI:53014 (ChEBI)
NECML [extracellular region]	Metabolite	CHEBI:53014 (ChEBI)
O2 [endocytic vesicle lumen]	Metabolite	CHEBI:15379 (ChEBI)
O2 [extracellular region]	Metabolite	CHEBI:15379 (ChEBI)
PL [endocytic vesicle lumen]	Metabolite	CHEBI:16247 (ChEBI)
PL [extracellular region]	Metabolite	CHEBI:16247 (ChEBI)
Peptide [extracellular region]	Metabolite	CHEBI:16670 (ChEBI)
Peptide [endocytic vesicle lumen]	Metabolite	CHEBI:16670 (ChEBI)
Phosphatidylserine [endocytic vesicle lumen]	Metabolite	CHEBI:18303 (ChEBI)
Phosphatidylserine [extracellular region]	Metabolite	CHEBI:18303 (ChEBI)
Platelet glycoprotein IV:Ligand	Complex	REACT_165052 (Reactome)
Platelet glycoprotein IV:Ligand	Complex	REACT_165582 (Reactome)
SAA1(19-122) [endocytic vesicle lumen]	Protein	P0DJI8 (Uniprot-TrEMBL)
SAA1(19-122) [extracellular region]	Protein	P0DJI8 (Uniprot-TrEMBL)
SCARA5 [endocytic vesicle membrane]	Protein	Q6ZMJ2 (Uniprot-TrEMBL)
SCARA5 [plasma membrane]	Protein	Q6ZMJ2 (Uniprot-TrEMBL)
SCARA5 trimer	Complex	REACT_164905 (Reactome)
SCARA5:Ligand	Complex	REACT_164504 (Reactome)
SCARA5:Ligand	Complex	REACT_164789 (Reactome)
SCARB1-2 [endocytic vesicle membrane]	Protein	Q8WTV0-2 (Uniprot-TrEMBL)
SCARB1-2 [plasma membrane]	Protein	Q8WTV0-2 (Uniprot-TrEMBL)
SCARB1-2	Protein	Q8WTV0-2 (Uniprot-TrEMBL)
SCARB1:Endocytosed Ligand	Complex	REACT_164502 (Reactome)
SCARB1:Endocytosed Ligand	Complex	REACT_164891 (Reactome)
SCARB1:Ligand	Complex	REACT_164882 (Reactome)
SCARF1 [endocytic vesicle membrane]	Protein	Q14162 (Uniprot-TrEMBL)
SCARF1 [plasma membrane]	Protein	Q14162 (Uniprot-TrEMBL)
SCARF1:Ligand	Complex	REACT_165139 (Reactome)
SCARF1:Ligand	Complex	REACT_165478 (Reactome)
SCARF1	Protein	Q14162 (Uniprot-TrEMBL)
SCGB3A2 [extracellular region]	Protein	Q96PL1 (Uniprot-TrEMBL)
SCGB3A2 [endocytic vesicle lumen]	Protein	Q96PL1 (Uniprot-TrEMBL)
SPARC [endocytic vesicle lumen]	Protein	P09486 (Uniprot-TrEMBL)
SPARC [extracellular region]	Protein	P09486 (Uniprot-TrEMBL)
STAB1 [endocytic vesicle membrane]	Protein	Q9NY15 (Uniprot-TrEMBL)
STAB1 [plasma membrane]	Protein	Q9NY15 (Uniprot-TrEMBL)
STAB1:Ligand	Complex	REACT_164343 (Reactome)
STAB1:Ligand	Complex	REACT_164896 (Reactome)
STAB1	Protein	Q9NY15 (Uniprot-TrEMBL)
STAB2(1136-2551) [endocytic vesicle membrane]	Protein	Q8WWQ8 (Uniprot-TrEMBL)
STAB2(1136-2551) [plasma membrane]	Protein	Q8WWQ8 (Uniprot-TrEMBL)
STAB2(1136-2551)	Protein	Q8WWQ8 (Uniprot-TrEMBL)
STAB2:Ligand	Complex	REACT_164253 (Reactome)
STAB2:Ligand	Complex	REACT_164299 (Reactome)
TAGs [endocytic vesicle lumen]	Metabolite	CHEBI:17855 (ChEBI)
TAGs [extracellular region]	Metabolite	CHEBI:17855 (ChEBI)
Truncated Alpha1-Microglobulin:heme trimer	Complex	REACT_161123 (Reactome)
carrageenan [endocytic vesicle lumen]	Metabolite	CHEBI:3435 (ChEBI)
carrageenan [extracellular region]	Metabolite	CHEBI:3435 (ChEBI)
cholesterol [endocytic vesicle lumen]	Metabolite	CHEBI:16113 (ChEBI)
cholesterol esters [endocytic vesicle lumen]	Metabolite	CHEBI:17002 (ChEBI)
dextran sulfate [endocytic vesicle lumen]	Metabolite	CHEBI:34674 (ChEBI)
dextran sulfate [extracellular region]	Metabolite	CHEBI:34674 (ChEBI)
ferriheme b [endocytic vesicle lumen]	Metabolite	CHEBI:36144 (ChEBI)
ferriheme b [extracellular region]	Metabolite	CHEBI:36144 (ChEBI)
ferroheme b [endocytic vesicle lumen]	Metabolite	CHEBI:17627 (ChEBI)
ferroheme b [extracellular region]	Metabolite	CHEBI:17627 (ChEBI)
hematite nanoparticle [endocytic vesicle lumen]	Metabolite	CHEBI:50824 (ChEBI)
hematite nanoparticle [extracellular region]	Metabolite	CHEBI:50824 (ChEBI)
heme b [extracellular region]	Metabolite	CHEBI:26355 (ChEBI)
heme b	Metabolite	CHEBI:26355 (ChEBI)
heme b	Metabolite	REACT_161398 (Reactome)
hydroperoxy fatty acid [endocytic vesicle lumen]	Metabolite	CHEBI:64009 (ChEBI)
hydroperoxy fatty acid [extracellular region]	Metabolite	CHEBI:64009 (ChEBI)
hydroxy fatty acid [endocytic vesicle lumen]	Metabolite	CHEBI:24654 (ChEBI)
hydroxy fatty acid [extracellular region]	Metabolite	CHEBI:24654 (ChEBI)
lysophosphatidylcholine [endocytic vesicle lumen]	Metabolite	CHEBI:60479 (ChEBI)
lysophosphatidylcholine [extracellular region]	Metabolite	CHEBI:60479 (ChEBI)
oxidized phospholipids [endocytic vesicle lumen]	Metabolite	CHEBI:60156 (ChEBI)
oxidized phospholipids [extracellular region]	Metabolite	CHEBI:60156 (ChEBI)
phosphatidylinositol [endocytic vesicle lumen]	Metabolite	CHEBI:16749 (ChEBI)
phosphatidylinositol [extracellular region]	Metabolite	CHEBI:16749 (ChEBI)
porB [endocytic vesicle lumen]	Protein	P18195 (Uniprot-TrEMBL)
porB [extracellular region]	Protein	P18195 (Uniprot-TrEMBL)
silicon dioxide nanoparticle [endocytic vesicle lumen]	Metabolite	CHEBI:50828 (ChEBI)
silicon dioxide nanoparticle [extracellular region]	Metabolite	CHEBI:50828 (ChEBI)
thioether crosslinked residues-AMBP(20-202) [extracellular region]	Protein	P02760 (Uniprot-TrEMBL)
titanium dioxide nanoparticle [endocytic vesicle lumen]	Metabolite	CHEBI:51050 (ChEBI)
titanium dioxide nanoparticle [extracellular region]	Metabolite	CHEBI:51050 (ChEBI)

Annotated Interactions

View all...

Source	Target	Type	Database reference	Comment
4xPalmC-CD36			REACT_163694 (Reactome)
	ALB	Arrow	REACT_160182 (Reactome)
	AMBP(20-198)	Arrow	REACT_160303 (Reactome)
AMBP(20-198)			REACT_160136 (Reactome)
AMBP(20-202)			REACT_160079 (Reactome)
Albumin:ferriheme			REACT_160182 (Reactome)
	Alpha1-Microglobulin:heme trimer	Arrow	REACT_160079 (Reactome)
	Apohemoglobin	Arrow	REACT_160297 (Reactome)
CD163			REACT_160225 (Reactome)
	COLEC11:Ligand	Arrow	REACT_163764 (Reactome)
COLEC11:MASP1			REACT_163764 (Reactome)
COLEC12 trimer			REACT_163907 (Reactome)
	COLEC12:Ligand	Arrow	REACT_163780 (Reactome)
	COLEC12:Ligand	Arrow	REACT_163907 (Reactome)
COLEC12:Ligand			REACT_163780 (Reactome)
Denatured Collagen I,III, Collagen IV			REACT_163647 (Reactome)
HPR:APOL1:APOA1:HDL3			REACT_160200 (Reactome)
	HPX:ferriheme b	Arrow	REACT_160182 (Reactome)
	HPX:ferriheme b	Arrow	REACT_160297 (Reactome)
	HPX:heme b	Arrow	REACT_160112 (Reactome)
HPX:heme b			REACT_160235 (Reactome)
HPX			REACT_160112 (Reactome)
HPX			REACT_160182 (Reactome)
HPX			REACT_160297 (Reactome)
Haptoglobin Dimer			REACT_160172 (Reactome)
Hemoglobin Dimer			REACT_160172 (Reactome)
Hemoglobin Dimer			REACT_160200 (Reactome)
	Hemoglobin:HPR:APOL1:APOA1:HDL3	Arrow	REACT_160200 (Reactome)
	Hemoglobin:Haptoglobin:CD163	Arrow	REACT_160193 (Reactome)
	Hemoglobin:Haptoglobin:CD163	Arrow	REACT_160225 (Reactome)
Hemoglobin:Haptoglobin:CD163			REACT_160193 (Reactome)
	Hemoglobin:Haptoglobin	Arrow	REACT_160172 (Reactome)
Hemoglobin:Haptoglobin			REACT_160225 (Reactome)
IgA:Alpha-1-Microglobulin			REACT_160303 (Reactome)
	IgA	Arrow	REACT_160303 (Reactome)
	LRP1:Hemopexin:heme	Arrow	REACT_160232 (Reactome)
	LRP1:Hemopexin:heme	Arrow	REACT_160235 (Reactome)
LRP1:Hemopexin:heme			REACT_160232 (Reactome)
LRP1			REACT_160235 (Reactome)
Ligands of CD36			REACT_163694 (Reactome)
Ligands of COLEC11			REACT_163764 (Reactome)
Ligands of COLEC12			REACT_163907 (Reactome)
Ligands of MARCO			REACT_163964 (Reactome)
Ligands of MSR1			REACT_163645 (Reactome)
Ligands of SCARA5			REACT_163819 (Reactome)
Ligands of SCARB1			REACT_163672 (Reactome)
Ligands of SCARF1			REACT_164012 (Reactome)
Ligands of STAB1			REACT_163850 (Reactome)
Ligands of STAB2			REACT_163962 (Reactome)
MARCO trimer			REACT_163964 (Reactome)
	MARCO:Ligand	Arrow	REACT_163964 (Reactome)
	MARCO:Ligand	Arrow	REACT_163998 (Reactome)
MARCO:Ligand			REACT_163998 (Reactome)
MSR1 (SCARA1) trimer			REACT_163645 (Reactome)
MSR1 (SCARA1) trimer			REACT_163647 (Reactome)
	MSR1:Collagen I,III,IV	Arrow	REACT_163647 (Reactome)
	MSR1:Ligand	Arrow	REACT_163645 (Reactome)
	MSR1:Ligand	Arrow	REACT_163711 (Reactome)
MSR1:Ligand			REACT_163711 (Reactome)
Methemoglobin			REACT_160297 (Reactome)
	Platelet glycoprotein IV:Ligand	Arrow	REACT_163694 (Reactome)
	Platelet glycoprotein IV:Ligand	Arrow	REACT_163736 (Reactome)
Platelet glycoprotein IV:Ligand			REACT_163736 (Reactome)
			REACT_160079 (Reactome)	Alpha-1-Microglobulin binds heme b (Allhorn et al. 2002, Larsson et al. 2004). The crystal structure of the complex indicates that each microglobulin molecule binds 2 heme molecules and the microglobulin:heme complex trimerizes (Siebel et al. 2012).
			REACT_160112 (Reactome)	Hemopexin binds either ferriheme b or ferroheme b, however the stability of the complex containing ferriheme b is greater than the stability of the complex containing ferroheme b (Morgan 1976, Pasternack et al. 1983, Solar et al. 1989, Miller and Shaklai 1999, Rosell et al. 2005, Mauk and Mauk 2010).
			REACT_160136 (Reactome)	Truncated Alpha-1-Microglobulin binds heme b and then degrades heme b by an unknown mechanism (Allhorn et al. 2002). The crystal structure of the untruncated Alpha1-Microglobulin:heme complex indicates that each Alpha1-Microglobulin molecule binds 2 heme molecules and the Alpha1-Microglobulin molecules trimerize (Siebel et al. 2012).
			REACT_160172 (Reactome)	Haptoglobin is an acute phase protein. It is produced by the liver and secreted into the plasma where it binds alpha-beta dimers of hemoglobin (Hamaguchi et al. 1971, Nagel and Gibson 1971, Tsapis et al. 1978, reviewed in Chiabrando et al. 2011). Haptoglobin monomers contain alpha and beta chains cleaved from a single proprotein and bonded by cystine disulfide bonds. The monomers further associate into dimers by disulfide-bonding and beta strand swapping (Andersen et al. 2012). Each haptoglobin dimer can bind two hemoglobin dimers, each containing hemoglobin alpha and hemoglobin beta.
			REACT_160182 (Reactome)	Despite the lower affinity of ferriheme for albumin than for hemopexin, ferriheme initially associates with albumin, presumably because the molar concentration of albumin in plasma is considerably greater than that of hemopexin. Ferriheme is transferred directly from serum albumin to hemopexin (Morgan et al. 1976, Pasternack et al. 1983, Pasternack et al. 1985).
			REACT_160193 (Reactome)	The CD163:haptoglobin:hemoglobin complex is endocytosed (Schaer et al. 2006, Kristiansen et al. 2001) by monocytes or macrophages. CD163 is constitutively endocytosed by monocytes independently of ligand binding (Schaer et al. 2006). Upon endocytosis, the receptor–ligand complex enters early endosomes where haptoglobin:hemoglobin complexes are released from CD163. The receptor then recycles to the cell surface while haptoglobin:hemoglobin complexes continue through the endocytic pathway to end up in lysosomes where the protein moieties and the ligand are degraded.
			REACT_160200 (Reactome)	Haptoglobin-related protein (HRP) is present in human serum in a complex known as trypanosome lytic factor-1 (TLF-1) that contains APOL1, APOA1, and HDL3. The HPR subunit of the complex binds hemoglobin with an unknown stoichiometry (Shiflett et al. 2005, Nielsen et al. 2006, Widener et al. 2007, Harrington et al. 2009).
			REACT_160225 (Reactome)	The CD163 receptor binds the haptoglobin:hemoglobin complex (Kristiansen et al. 2001, Madsen et al. 2004, Nielsen et al. 2007). After binding, the CD163:haptoglobin:hemoglobin complex is internalized by endocytosis and is degraded in the lysosome. CD163 is found on the membranes of monocytes and macrophages.
			REACT_160232 (Reactome)	The LRP1:hemopexin:heme complex is endocytosed and the complex is dissociated in lysosomes, leading to heme uptake. Heme is then degraded by heme oxygenases. Whereas LRP1 is subsequently recycled to the plasma membrane, the destiny of hemopexin is controversial. Some studies have suggested that hemopexin can be recycled as an intact molecule to the extracellular milieu (Smith and Morgan, 1979). However, it has also been proposed that following hepatic uptake of heme from hemopexin:heme, varying proportions of the protein are either returned to the circulation or degraded in the liver (Potter et al., 1993). Recently, Hvidberg et al. have shown that most hemopexin is degraded in lysosomes (Hvidberg et al., 2005).
			REACT_160235 (Reactome)	Once formed in the plasma, the hemopexin:heme complex is rapidly cleared from circulation and it is taken up by the liver (Smith and Morgan 1984, Smith and Morgan 1985, Tolosano et al. 2010, Vinchi et al. 2008), where heme is degraded by heme oxygenases. In mouse, rat and rabbit several experimental evidences led to the postulation of a specific receptor on hepatocytes with high affinity for the hemopexin:heme complex (Smith and Morgan 1981, Smith and Morgan 1984, Smith et al, 1988, Smith et al., 1991), but such a receptor has not been identified to date. The only known hemopexin:heme receptor is LRP1 (CD91) that is ubiquitously expressed and has a low affinity for the complex. LRP1 is a multi-ligand scavenger receptor, involved in endocytosis in some cells types, for example macrophages, and in signaling in other cell types (reviewed in Boucher and Herz 2011). LRP1 is known to act in the metabolism of lipoprotein and it is expressed in several cell types including macrophages, hepatocytes and neurons. Among several ligands, LRP1 (CD91) can bind the hemopexin:heme complex (Hvidberg et al. 2005).
			REACT_160297 (Reactome)	When haptoglobin capacity to buffer hemoglobin is overwhelmed, hemoglobin undergoes a rapid conversion to methemoglobin. Ferriheme is transferred directly from methemoglobin to hemopexin (Miller et al. 1996, Mauk and Mauk 2010).
			REACT_160303 (Reactome)	Both hemoglobin and the cytosolic face of erythrocytes are able to catalyze the cleavage of Alpha-1-Microglobulin in the IgA:Alpha-1-Microglobulin complex present in serum (Allhorn et al. 2002). The reaction produces truncated Alpha-1-Microglobulin, which is able to bind and degrade heme. About half of the circulating Alpha-1-Microglobulin is covalently bound to IgA.
			REACT_163645 (Reactome)	MSR1 (SCARA1, SR-A) binds oxidized and acetylated low density lipid (LDL) particles ((Brown et al. 1980), Haberland et al 1984, Gough et al. 1998, Yang et al. 2011), apolipoproteins A-I and E (human and mouse, Neyen et al. 2009), lysophosphatidylcholine from apoptotic cells (mouse, Sakai et al. 1996), phosphatidylinositol and phosphatidylserine (mouse, Nishikawa et al. 1990). MSR1 binds activated B-lymphocytes (human, Yokota et al. 1998), calreticulin and gp96 (mouse, Berwin et al. 2003). MSR1 binds bacterial products (E.coli, Neisseria meningitides, Staphylococcus aureus) (mouse, Peiser et al. 2006), Lipopolysaccharide (LPS) (mouse and bovine, Hampton et al. 1991), Lipoteichoic acid (LTA) and Gram-positive bacteria (bovine, Dunne et al. 1994), Adenovirus 5 (Haisma et al. 2009). MSR1 binds polysaccharides (carrageenan, dextran sulphate, fucoidan) (Brown et al. 1980, Krieger et al. 1992), extracellular matrix proteoglycans, biglycan and decorin (mouse, Santiago-Garcia et al. 2003). MSR1 binds extracellular matrix molecules, including denatured type I and III collagen, as well as glycated collagen IV (human and mouse and bovine, el Khoury et al. 1994, Gowen et al. 2000, Gowen et al. 2001), beta-amyloid fibrils (human and mouse, El Khoury et al. 1996), maleyl-BSA and advanced glycation end-product modified (AGE)-BSA (bovine, Brown et al. 1980, Araki et al. 1995). MSR1 binds polynucleotides (polyI, polyG) (bovine, Brown et al. 1980, Pearson et al. 1993, Mielewczyk et al. 1996), double-stranded RNA (Limmon et al. 2008, DeWitte-Orr et al. 2010). MSR1 interacts with the modified apoB-100 component of LDL (Parthasarathy et al. 1987) and with the lipid part of LDL (Terpstra et al. 1998). MSR1 is expressed most strongly on macrophages and can also be detected on endothelial cells and smooth muscle cells.
			REACT_163647 (Reactome)	As inferred from mouse, MSR1 (SCARA1) binds denatured collagen I, denatured collagen III, and nondenatured or glycated collagen IV.
			REACT_163672 (Reactome)	SCARB1 (SR-BI) binds low density lipoprotein (LDL), acetylated LDL, oxidized LDL, high density lipoprotein (HDL) (Calvo et al. 1997, Murao et al. 1997, Rhainds et al. 1999, inferred from hamster in Acton et al. 1994). SCARB1 binds HDL via its protein moiety, including apolipoproteins A-I, A-II, CII, CIII and E (Bultel-Brienne et al. 2002, inferred from mouse in Xu, Laccotripe et al. 1997, Li et al. 2002). SCARB1 also binds serum amyloid A protein (Baranova et al. 2005), and lipopolysaccharide (LPS) (Vishnyakova et al. 2003). SCARB1 is expressed on the extracellular face of the plasma membrane of several types of polarized epithelial cells.
			REACT_163694 (Reactome)	CD36 (Platelet glycoprotein IV) binds oxidized LDL (Janabi et al. 2000, Endemann et al. 1993) through both the lipid and the protein moieties of LDL (Boullier et al. 2000), oxidized phospholipids (Podrez et al. 2002), long-chain fatty acids (inferred from rat and mouse, Abumrad et al. 1993, Laugerette et al. 2005), hexarelin (a hexapeptide member of the growth hormone-releasing peptide family) (inferred from rat and mouse, Bodart et al. 2002), betaglucan (Means et al. 2009), oxidized and native phosphatidylserine (Greenberg et al. 2006) and apoptotic cells (Ren et al. 1995; Fadok et al. 1998), lipopeptide from Staphylococcus aureus as well as lipoteichoic acid from Gram-positive bacteria, both in cooperation with TLR2 (inferred from mouse, Hoebe et al. 2005). As inferred from mouse, CD36 also binds phosphatidylinositol, and HDL.
			REACT_163711 (Reactome)	The MSR1:ligand complex (SCARA1:ligand, SR-A:ligand) is endocytosed (Matsumoto et al. 1990, Gough et al. 1998, Peiser et al. 2000, Aguilar-Gaytan and Mas-Oliva 2003, Wang and Chandawarkar 2010, Orr et al. 2011). In the cases in which the ligands are located on bacteria or yeast cells the entire cell is phagocytosed (Aguilar-Gaytan and Mas-Oliva 2003, Wang and Chandawarkar 2010). Uptake of modified LDL by macrophages via MSR1 appears to contribute to foam cell formation during atherosclerosis (Matsumoto et al. 1990).
			REACT_163736 (Reactome)	The Platelet glycoprotein IV (CD36):ligand complex is endocytosed (Zeng et al. 2003, McDermott_Roe et al. 2008, Nilsen et al. 2008, Collins et al. 2009). The endocytosis of CD36:oxidized LDL is independent of caveolin (Zeng et al. 2003) and dependent on actin (Collins et al. 2009). As inferred from mouse, endocytosis of CD36:oxidized LDL is independent of caveolae, microtubules, and actin cytoskeleton, but dependent on dynamin (Sun et al. 2007).
			REACT_163764 (Reactome)	COLEC11 (CL-K1) binds D-mannose, L-fucose, N-acetylglucosamine, DNA, lipopolysaccharide (LPS), and lipoteichoic acid (LTA) (Keshi et al. 2006, Hansen et al. 2010).
			REACT_163777 (Reactome)	The STAB2:ligand complex is endocytosed (Tamura et al. 2003, Li et al. 2011). Endocytosis of stabilin-1 or stabilin-2 can occur independently of ligand binding, via clathrin (Hansen et al. 2005).
			REACT_163780 (Reactome)	COLEC12 (CL-P1, SCARA4, SRCL, NSR2) bound to yeast or bacteria is phagocytosed (Jang et al. 2009, Ohtani et al. 2012). Endocytosis of other ligands bound to COLEC12 is inferred.
			REACT_163819 (Reactome)	SCARA5 binds double-stranded RNA (DeWitte-Orr et al. 2010). As inferred from mouse SCARA5 also binds lipopolysaccharide and ferritin. SCARA5 is expressed on epithelial cells.
			REACT_163824 (Reactome)	The SCARB1 (SR-BI, SR-BII):ligand complex is endocytosed (Calvo et al. 1997, Murao et al. 1997, Rhainds et al. 1999, Vishnyakova et al. 2003, Baranova et al. 2005, Eckhardt et al. 2004) but selective lipid uptake from lipoprotein particles does not require SR-BI endocytosis in mouse (Nieland et al. 2005) but is partly dependent on endocytosis in human (Zhang et al. 2007). HDL particles are resecreted after lipid unloading in the endocytic pathway (Pagler et al. 2006; Zhang et al. 2007). SR-BI colocalizes with caveolae (inferred from mouse, Babitt et al. 1997) while SR-BII, an alternatively spliced form of SCARB1, localizes to clathrin-coated pits due to a dileucine motif in the cytosolic tail (inferred from mouse, Eckhardt et al. 2006). Endocytosis of oxidized LDL by SR-BI is independent of caveolae, microtubules, and actin cytoskeleton (inferred from mouse, Sun et al. 2007).
			REACT_163850 (Reactome)	STAB1 (FEEL-1) binds acetylated low density lipoprotein (LDL) (Adachi & Tsujimoto 2002, Palani et al. 2011), phosphatidylserine (exposed when cells are lysed) (Park et al. 2009), advanced glycation end products (AGE) (Tamura et al. 2003, Hansen et al. 2005), and Osteonectin (SPARC) (Kzhyshkowska et al. 2006).
			REACT_163867 (Reactome)	The STAB1:ligand complex is endocytosed (Tamura et al. 2003, Kzhyshkowska et al. 2004, Li et al. 2011, Prevo et al. 2004; Kzhyshkowska et al. 2005). Endocytosis of stabilin-1 or stabilin-2 can occur independently of ligand binding, via clathrin (Hansen et al. 2005).
			REACT_163907 (Reactome)	COLEC12 (SCARA4) binds beta-glucan (Jang et al. 2009), N-acetylgalactosamine (Yoshida et al. 2003), oxidized LDL (Ohtani et al. 2001), and double-stranded RNA (DeWitte-Orr et al. 2010). COLEC12 is expressed on endothelial cells
			REACT_163962 (Reactome)	STAB2 (FEEL-2) binds acetylated low density lipoprotein (LDL) (Adachi & Tsujimoto 2002, Harris & Weigel 2008), advanced glycation end products (AGE) (Tamura et al. 2003), chondroitin sulfate (Harris & Weigel 2008), hyaluronic acid (Zhou et al. 2003, Harris et al. 2004, Harris et al. 2007, Harris & Weigel 2008), heparin (Harris et al. 2008, Harris & Weigel 2008, Harris et al. 2009), and phosphatidylserne (Park et al. 2008).
			REACT_163964 (Reactome)	Unlike MSR1, MARCO uses the SRCR domain and more particularly the arginine-rich region within this domain for binding. (Brannstrom et al. 2002). MARCO binds lipopolysaccharide and lipoteichoic acid, both found on the surfaces of bacteria (Elomaa et al. 1998, Elshourbagy et al. 2000). MARCO binds and phagocytoses Streptococcus pneumoniae (mouse, Dorrington et al. 2013), Escherichia coli and Staphylococcus aureus (Elshourbagy, Li et al. 2000), Neisseria meningitidis (Mukhopadhyay et al. 2006), Clostridium sordellii (Thelen et al. 2010). MARCO binds proinflammatory oxidized lipids (mouse, Dahl et al. 2007). MARCO binds CpG oligonucleotide sequences (CpG-ODN) in microbial DNA (mouse, Jozefowski et al. 2006), uteroglobin-related protein 1 (Bin et al. 2003), unopsonized particles (TiO2, Fe2O3, and latex beads) (Palecanda et al. 1999) and silica particles (Hamilton et al. 2006). MARCO is most strongly expressed on subgroups of macrophages and can also be detected on splenic dendritic cells.
			REACT_163969 (Reactome)	As inferred from mouse, the SCARA5:ligand complex is endocytosed.
			REACT_163998 (Reactome)	The MARCO:ligand complex is endocytosed (Arredouani et al. 2005, Thelen et al. 2010). In cases where the ligand is part of a bacterial cell the entire cell is phagocytosed.
			REACT_164000 (Reactome)	The SCARF1:ligand complex is endocytosed (Adachi et al. 1997, Berwin et al. 2004) and cross-presented on MHC class II (Murshid et al. 2010). SREC-I mediates host cell entry of Neisseria gonorrhoeae (Rechner et al. 2007)
			REACT_164012 (Reactome)	SCARF1 (SREC-I) binds low density lipoprotein (LDL), oxidized LDL, acetylated LDL (Adachi et al. 1997), carbamylated LDL (Apostolov et al. 2009), beta glucan (Means et al. 2009), and calreticulin (Berwin et al. 2004). SREC-I binds Hsp90 and Hsp90-chaperoned peptides (Murshid et al. 2010) as well as Heat shock protein 110 (hsp110) and glucose-regulated protein (grp170) (inferred from mouse, Facciponte, Wang et al. 2007). SREC-I interacts with PorB of Neisseria gonorrhoeae and mediates host cell entry (Rechner et al. 2007).
SCARA5 trimer			REACT_163819 (Reactome)
	SCARA5:Ligand	Arrow	REACT_163819 (Reactome)
	SCARA5:Ligand	Arrow	REACT_163969 (Reactome)
SCARA5:Ligand			REACT_163969 (Reactome)
SCARB1-2			REACT_163672 (Reactome)
	SCARB1:Endocytosed Ligand	Arrow	REACT_163824 (Reactome)
SCARB1:Endocytosed Ligand			REACT_163824 (Reactome)
	SCARB1:Ligand	Arrow	REACT_163672 (Reactome)
	SCARF1:Ligand	Arrow	REACT_164000 (Reactome)
	SCARF1:Ligand	Arrow	REACT_164012 (Reactome)
SCARF1:Ligand			REACT_164000 (Reactome)
SCARF1			REACT_164012 (Reactome)
	STAB1:Ligand	Arrow	REACT_163850 (Reactome)
	STAB1:Ligand	Arrow	REACT_163867 (Reactome)
STAB1:Ligand			REACT_163867 (Reactome)
STAB1			REACT_163850 (Reactome)
STAB2(1136-2551)			REACT_163962 (Reactome)
	STAB2:Ligand	Arrow	REACT_163777 (Reactome)
	STAB2:Ligand	Arrow	REACT_163962 (Reactome)
STAB2:Ligand			REACT_163777 (Reactome)
	Truncated Alpha1-Microglobulin:heme trimer	Arrow	REACT_160136 (Reactome)
heme b			REACT_160079 (Reactome)
heme b			REACT_160112 (Reactome)
heme b			REACT_160136 (Reactome)