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Volumn 8, Issue 3-4, 2006, Pages 312-324

Extracellular disulfide exchange and the regulation of cellular function

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA1 INTEGRIN; BETA3 INTEGRIN; CD4 ANTIGEN; GLYCOPROTEIN GP 120; ISOMERASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERP5; PROTEIN ERP57; PROTEIN ERP72; THIOL ISOMERASE; UNCLASSIFIED DRUG;

EID: 33646698875     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.312     Document Type: Review
Times cited : (134)

References (108)
  • 3
    • 0031043060 scopus 로고    scopus 로고
    • A collagen-like peptide stimulates tyrosine phosphorylation of syk and phospholipase C gamma2 in platelets independent of the integrin alpha2beta1
    • Asselin J, Gibbins JM, Achison M, Lee YH, Morton LF, Farndale RW, Barnes MJ, and Watson SP. A collagen-like peptide stimulates tyrosine phosphorylation of syk and phospholipase C gamma2 in platelets independent of the integrin alpha2beta1. Blood 89: 1235-1242, 1997.
    • (1997) Blood , vol.89 , pp. 1235-1242
    • Asselin, J.1    Gibbins, J.M.2    Achison, M.3    Lee, Y.H.4    Morton, L.F.5    Farndale, R.W.6    Barnes, M.J.7    Watson, S.P.8
  • 4
    • 0029564658 scopus 로고
    • Interaction of calreticulin with protein disulfide isomerase
    • Baksh S, Burns K, Andrin C, and Michalak M. Interaction of calreticulin with protein disulfide isomerase. J Biol Chem 270: 31338-31344, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 31338-31344
    • Baksh, S.1    Burns, K.2    Andrin, C.3    Michalak, M.4
  • 6
    • 0030610003 scopus 로고    scopus 로고
    • Agonist-activated alphav beta3 on platelets and lymphocytes binds to the matrix protein osteopontin
    • Bennett JS, Chan C, Vilaire G, Mousa SA, and DeGrado WF. Agonist-activated alphav beta3 on platelets and lymphocytes binds to the matrix protein osteopontin. J Biol Chem 272: 8137-8140, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 8137-8140
    • Bennett, J.S.1    Chan, C.2    Vilaire, G.3    Mousa, S.A.4    DeGrado, W.F.5
  • 7
    • 0034655128 scopus 로고    scopus 로고
    • Sulfhydryl regulation of L-selectin shedding: Phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes
    • Bennett TA, Edwards BS, Sklar LA, and Rogelj S. Sulfhydryl regulation of L-selectin shedding: phenylarsine oxide promotes activation-independent L-selectin shedding from leukocytes. J Immunol 164: 4120-4129, 2000.
    • (2000) J Immunol , vol.164 , pp. 4120-4129
    • Bennett, T.A.1    Edwards, B.S.2    Sklar, L.A.3    Rogelj, S.4
  • 8
    • 0034737776 scopus 로고    scopus 로고
    • Physical proximity and functional association of glycoprotein 1ba and protein disulfide isomerase on the platelet plasma membrane
    • Burgess JK, Hotchkiss KA, Suter C, Dudman NPB, Szollosi J, Chesterman CN, Chong BH, and Hogg PJ. Physical proximity and functional association of glycoprotein 1ba and protein disulfide isomerase on the platelet plasma membrane. J Biol Chem 275: 9758-9766, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 9758-9766
    • Burgess, J.K.1    Hotchkiss, K.A.2    Suter, C.3    Dudman, N.P.B.4    Szollosi, J.5    Chesterman, C.N.6    Chong, B.H.7    Hogg, P.J.8
  • 9
    • 0029025521 scopus 로고
    • Characterisation of protein, disulfide isomerase released from activated platelets
    • Chen K, Detwiler TC, and Essex DW. Characterisation of protein, disulfide isomerase released from activated platelets. Br J Haematol 90: 425-431, 1995.
    • (1995) Br J Haematol , vol.90 , pp. 425-431
    • Chen, K.1    Detwiler, T.C.2    Essex, D.W.3
  • 10
    • 0026704930 scopus 로고
    • Protein disulfide isomerase activity is released by activated platelets
    • Chen K, Lin Y, and Detwiler TC. Protein disulfide isomerase activity is released by activated platelets. Blood 79: 2226-2228, 1992.
    • (1992) Blood , vol.79 , pp. 2226-2228
    • Chen, K.1    Lin, Y.2    Detwiler, T.C.3
  • 13
    • 0027139182 scopus 로고
    • Regulation of integrin-mediated myeloid cell adhesion to fibronectin: Influence of disulfide reducing agents, divalent cations and phorbol ester
    • Davis G and Camarillo C. Regulation of integrin-mediated myeloid cell adhesion to fibronectin: influence of disulfide reducing agents, divalent cations and phorbol ester. J Immunol 151: 7138-7150, 1993.
    • (1993) J Immunol , vol.151 , pp. 7138-7150
    • Davis, G.1    Camarillo, C.2
  • 14
    • 0031778169 scopus 로고    scopus 로고
    • Peptide LSAR-LAF activates alpha(IIb)beta3 on resting platelets and causes resting platelet aggregate formation without platelet shape change
    • Derrick JM, Loudon RG, and Gartner TK. Peptide LSAR-LAF activates alpha(IIb)beta3 on resting platelets and causes resting platelet aggregate formation without platelet shape change. Thromb Res 89: 31-40, 1998.
    • (1998) Thromb Res , vol.89 , pp. 31-40
    • Derrick, J.M.1    Loudon, R.G.2    Gartner, T.K.3
  • 15
    • 0030790357 scopus 로고    scopus 로고
    • The peptide LSARLAF causes platelet secretion and aggregation by directly activating the integrin alphaIIbbeta3
    • Derrick JM, Taylor DB, Loudon RG, and Gartner TK. The peptide LSARLAF causes platelet secretion and aggregation by directly activating the integrin alphaIIbbeta3. Biochem J 325 (Pt 2): 309-313, 1997.
    • (1997) Biochem J , vol.325 , Issue.PART 2 , pp. 309-313
    • Derrick, J.M.1    Taylor, D.B.2    Loudon, R.G.3    Gartner, T.K.4
  • 16
    • 0037588974 scopus 로고    scopus 로고
    • Inactivation of the human P2Y12 receptor by thiol reagents requires interaction with both extracellular cysteine residues, Cys17 and Cys270
    • Ding Z, Kimn S, Dorsam RT, Jin J, and Kunapuli SP. Inactivation of the human P2Y12 receptor by thiol reagents requires interaction with both extracellular cysteine residues, Cys17 and Cys270. Blood 101: 3908-3914, 2003.
    • (2003) Blood , vol.101 , pp. 3908-3914
    • Ding, Z.1    Kimn, S.2    Dorsam, R.T.3    Jin, J.4    Kunapuli, S.P.5
  • 17
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson CM. The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci 356: 133-145, 2001.
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 18
    • 0030046449 scopus 로고    scopus 로고
    • Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites
    • Donella-Deana A, James P, Staudenmann W, Cesaro L, Marin O, Brunati AM, Ruzzene M, and Pinna LA. Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites. Eur J Biochem 235: 18-25, 1996.
    • (1996) Eur J Biochem , vol.235 , pp. 18-25
    • Donella-Deana, A.1    James, P.2    Staudenmann, W.3    Cesaro, L.4    Marin, O.5    Brunati, A.M.6    Ruzzene, M.7    Pinna, L.A.8
  • 19
    • 0034495137 scopus 로고    scopus 로고
    • Presence of closely spaced protein thiols on the surface of mammalian cells
    • Donoghue N, Yam PTW, Jiang X-M, and Hogg PJ. Presence of closely spaced protein thiols on the surface of mammalian cells. Protein Sci 9: 2436-2445, 2000.
    • (2000) Protein Sci , vol.9 , pp. 2436-2445
    • Donoghue, N.1    Yam, P.T.W.2    Jiang, X.-M.3    Hogg, P.J.4
  • 20
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert DM and Kim PS. Mechanisms of viral membrane fusion and its inhibition. Annu Rev Biochem 70: 777-810, 2001.
    • (2001) Annu Rev Biochem , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 21
    • 3042824871 scopus 로고    scopus 로고
    • The role of thiols and disulfides in platelet function
    • Essex DW. The role of thiols and disulfides in platelet function. Antioxid Redox Signal 6: 736-746, 2004.
    • (2004) Antioxid Redox Signal , vol.6 , pp. 736-746
    • Essex, D.W.1
  • 22
    • 0029144477 scopus 로고
    • Localisation of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, and Swiatkowska M. Localisation of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 86: 2168-2173, 1995.
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 23
    • 0032985071 scopus 로고    scopus 로고
    • Protein disulfide isomerase mediates platelet aggregation and secretion
    • Essex DW and Li M. Protein disulfide isomerase mediates platelet aggregation and secretion. Br J Haematology 104: 448-454, 1999.
    • (1999) Br J Haematology , vol.104 , pp. 448-454
    • Essex, D.W.1    Li, M.2
  • 24
    • 0037435609 scopus 로고    scopus 로고
    • Redox control of platelet aggregation
    • Essex DW and Li M. Redox control of platelet aggregation. Biochemistry 42: 129-136, 2003.
    • (2003) Biochemistry , vol.42 , pp. 129-136
    • Essex, D.W.1    Li, M.2
  • 25
    • 4444282377 scopus 로고    scopus 로고
    • Platelet surface glutathione reductase-like activity
    • Essex DW, Li M, Feinman RD, and Miller A. Platelet surface glutathione reductase-like activity. Blood 104: 1383-1385, 2004.
    • (2004) Blood , vol.104 , pp. 1383-1385
    • Essex, D.W.1    Li, M.2    Feinman, R.D.3    Miller, A.4
  • 26
    • 0035918587 scopus 로고    scopus 로고
    • Protien disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
    • Essex DW, Li M, Miller A, and Feinman RD. Protien disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry 40: 6070-6075, 2001.
    • (2001) Biochemistry , vol.40 , pp. 6070-6075
    • Essex, D.W.1    Li, M.2    Miller, A.3    Feinman, R.D.4
  • 28
    • 0032146759 scopus 로고    scopus 로고
    • ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif
    • Ferrari DM, Nguyen Van P, Kratzin HD, and Soling HD. ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif. Eur J Biochem 255: 570-579, 1998.
    • (1998) Eur J Biochem , vol.255 , pp. 570-579
    • Ferrari, D.M.1    Van Nguyen, P.2    Kratzin, H.D.3    Soling, H.D.4
  • 29
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulfide isomerase family: Unraveling a string of folds
    • Ferrari DM and Soling H-D. The protein disulfide isomerase family: Unraveling a string of folds. Biochem J 339: 1-10, 1999.
    • (1999) Biochem J , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.-D.2
  • 30
    • 0034918524 scopus 로고    scopus 로고
    • A journey with platelet P-selectin: The molecular basis of granule secretion, signalling and cell adhesion
    • Furie B, Furie BC, and Flaumenhaft R. A journey with platelet P-selectin: the molecular basis of granule secretion, signalling and cell adhesion. Thromb Haemost 86: 214-221, 2001.
    • (2001) Thromb Haemost , vol.86 , pp. 214-221
    • Furie, B.1    Furie, B.C.2    Flaumenhaft, R.3
  • 31
    • 0345772126 scopus 로고    scopus 로고
    • Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry
    • Gallina A, Hanley TM, Mandel R, Trahey M, Broder CC, Viglianti GA, and Ryser HJ. Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry. J Biol Chem 277: 50579-50588, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 50579-50588
    • Gallina, A.1    Hanley, T.M.2    Mandel, R.3    Trahey, M.4    Broder, C.C.5    Viglianti, G.A.6    Ryser, H.J.7
  • 32
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert HF. Molecular and cellular aspects of thiol-disulfide exchange. Adv Enzymol Relat Areas Mol Biol 63: 69-172, 1990.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 33
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU and Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858, 2002.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 34
    • 0025904916 scopus 로고
    • Comparison of the activities of protein disulfide-isomerase and thioredoxin in catalysing disulfide isomerization in a protein substrate
    • Hawkins HC, Blackburn EC, and Freedman RB. Comparison of the activities of protein disulfide-isomerase and thioredoxin in catalysing disulfide isomerization in a protein substrate. Biochem J 275 (Pt 2): 349-353, 1991.
    • (1991) Biochem J , vol.275 , Issue.PART 2 , pp. 349-353
    • Hawkins, H.C.1    Blackburn, E.C.2    Freedman, R.B.3
  • 35
    • 0028846534 scopus 로고
    • Cloning and sequencing of the cDNA encoding human P5
    • Hayano T and Kikuchi M. Cloning and sequencing of the cDNA encoding human P5. Gene 164: 377-378, 1995.
    • (1995) Gene , vol.164 , pp. 377-378
    • Hayano, T.1    Kikuchi, M.2
  • 36
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg PJ. Disulfide bonds as switches for protein function. Trends Biochem Sci 28: 210-214, 2003.
    • (2003) Trends Biochem Sci , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 37
    • 0029780967 scopus 로고    scopus 로고
    • Catalysis of disulfide isomerization in thrombospondin 1 by protein disulfide isomerase
    • Hotchkiss KA, Chesterman CN, and Hogg PJ. Catalysis of disulfide isomerization in thrombospondin 1 by protein disulfide isomerase. Biochemistry 35: 9761-9767, 1996.
    • (1996) Biochemistry , vol.35 , pp. 9761-9767
    • Hotchkiss, K.A.1    Chesterman, C.N.2    Hogg, P.J.3
  • 38
    • 0032506098 scopus 로고    scopus 로고
    • Exposure of the cryptic Arg-Gly-Asp sequence in thrombospondin-1 by protein disulfide isomerase
    • Hotchkiss KA, Matthias LJ, and Hogg PJ. Exposure of the cryptic Arg-Gly-Asp sequence in thrombospondin-1 by protein disulfide isomerase. Biochim Biophys Acta 1388: 478-488, 1998.
    • (1998) Biochim Biophys Acta , vol.1388 , pp. 478-488
    • Hotchkiss, K.A.1    Matthias, L.J.2    Hogg, P.J.3
  • 39
    • 0032714092 scopus 로고    scopus 로고
    • Secretion of the galectin family of mammalian carbohydrate-binding proteins
    • Hughes RC. Secretion of the galectin family of mammalian carbohydrate-binding proteins. Biochim Biophys Acta 1473: 172-185, 1999.
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 172-185
    • Hughes, R.C.1
  • 40
    • 0142244518 scopus 로고    scopus 로고
    • Profiling of the cell surface proteome
    • Jang JH and Hanash S. Profiling of the cell surface proteome. Proteomics 3: 1947-1954, 2003.
    • (2003) Proteomics , vol.3 , pp. 1947-1954
    • Jang, J.H.1    Hanash, S.2
  • 41
    • 0031032915 scopus 로고    scopus 로고
    • Phosphorylation of CaBP1 and CaBP2 by protein kinase CK2
    • Janson IM, Ek B, and Ek P. Phosphorylation of CaBP1 and CaBP2 by protein kinase CK2. J Biochem (Tokyo) 121: 112-117, 1997.
    • (1997) J Biochem (Tokyo) , vol.121 , pp. 112-117
    • Janson, I.M.1    Ek, B.2    Ek, P.3
  • 42
    • 0032543397 scopus 로고    scopus 로고
    • KDEL motif interacts with a specific sequence in mammalian erd2 receptor
    • Janson IM, Tomik R, O'Farrell F, and Elk P. KDEL motif interacts with a specific sequence in mammalian erd2 receptor. Biochem Biophys. Res Comm 247: 447-451, 1998.
    • (1998) Biochem Biophys Res Comm , vol.247 , pp. 447-451
    • Janson, I.M.1    Tomik, R.2    O'Farrell, F.3    Elk, P.4
  • 43
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disuflide isomerase
    • Jiang X-M, Fitzgerald M, Grant CM, and Hogg PJ. Redox control of exofacial protein thiols/disulfides by protein disuflide isomerase. J Biol Chem 274: 2416-2423, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 2416-2423
    • Jiang, X.-M.1    Fitzgerald, M.2    Grant, C.M.3    Hogg, P.J.4
  • 45
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink J, Darby NJ, Dijkstra K, Nilges M, and Creighton TE. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr Biol 7: 239-245, 1997.
    • (1997) Curr Biol , vol.7 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstra, K.3    Nilges, M.4    Creighton, T.E.5
  • 46
    • 0036737949 scopus 로고    scopus 로고
    • Functional analysis of human P5, a protein disulfide isomerase homologue
    • Kikuchi M, Doi E, Tsujimoto I, Horibe T and Tsujimoto Y. Functional analysis of human P5, a protein disulfide isomerase homologue. J Biochem (Tokyo) 132: 451-455, 2002.
    • (2002) J Biochem (Tokyo) , vol.132 , pp. 451-455
    • Kikuchi, M.1    Doi, E.2    Tsujimoto, I.3    Horibe, T.4    Tsujimoto, Y.5
  • 47
    • 0034614620 scopus 로고    scopus 로고
    • The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens
    • Knight CG, Morton LF, Peachey AR, Tuckwell DS, Farndale RW, and Barnes MJ. The collagen-binding A-domains of integrins alpha(1)beta(1) and alpha(2)beta(1) recognize the same specific amino acid sequence, GFOGER, in native (triple-helical) collagens. J Biol Chem 275: 35-40, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35-40
    • Knight, C.G.1    Morton, L.F.2    Peachey, A.R.3    Tuckwell, D.S.4    Farndale, R.W.5    Barnes, M.J.6
  • 48
    • 0023654667 scopus 로고
    • A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase
    • Koivu J, Myllyla R, Helaakoski T, Pihlajaniemi T, Tasanen K, and Kivirikko KI. A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. J Biol Chem 262: 6447-6449, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 6447-6449
    • Koivu, J.1    Myllyla, R.2    Helaakoski, T.3    Pihlajaniemi, T.4    Tasanen, K.5    Kivirikko, K.I.6
  • 49
    • 0035396642 scopus 로고    scopus 로고
    • Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding
    • Kramer B, Ferrari DM, Klappa P, Pohlmann N, and Soling H-D. Functional roles and efficiencies of the thioredoxin boxes of calcium-binding proteins 1 and 2 in protein folding. Biochem J 357: 83-95, 2001.
    • (2001) Biochem J , vol.357 , pp. 83-95
    • Kramer, B.1    Ferrari, D.M.2    Klappa, P.3    Pohlmann, N.4    Soling, H.-D.5
  • 50
    • 0028292443 scopus 로고
    • Thiol-proteindisulfide-oxidoreductase (protein disulfide isomerase): A new plasma membrane constituent of mature human B lymphocytes
    • Kroning H, Kahne T, Ittenson A, Franke A, and Ansorge S. Thiol-proteindisulfide-oxidoreductase (protein disulfide isomerase): A new plasma membrane constituent of mature human B lymphocytes. Scand J immunol 39: 346-350, 1994.
    • (1994) Scand J Immunol , vol.39 , pp. 346-350
    • Kroning, H.1    Kahne, T.2    Ittenson, A.3    Franke, A.4    Ansorge, S.5
  • 51
    • 0034674762 scopus 로고    scopus 로고
    • Protein disulfide isomerase mediates, integrin-dependent adhesion
    • Lahav J, Gofer-Dadosh N, Luboshitz J, Hess O, and Shaklai M. Protein disulfide isomerase mediates, integrin-dependent adhesion. FEBS Lett 475: 89-92, 2000.
    • (2000) FEBS Lett , vol.475 , pp. 89-92
    • Lahav, J.1    Gofer-Dadosh, N.2    Luboshitz, J.3    Hess, O.4    Shaklai, M.5
  • 52
    • 0036786353 scopus 로고    scopus 로고
    • Sustained integrin ligation involves extracellular free sulfhdryls and enzymatically catalyzed disulfide exchange
    • Lahav J, Jurk K, Hess O, Barnes MJ, Farndale RW, Luboshitz J, and Kehrel BE. Sustained integrin ligation involves extracellular free sulfhdryls and enzymatically catalyzed disulfide exchange. Blood 100: 2472-2478, 2002.
    • (2002) Blood , vol.100 , pp. 2472-2478
    • Lahav, J.1    Jurk, K.2    Hess, O.3    Barnes, M.J.4    Farndale, R.W.5    Luboshitz, J.6    Kehrel, B.E.7
  • 54
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia ML and Lennarz WJ. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell 74: 899-908, 1993.
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 55
    • 0033548441 scopus 로고    scopus 로고
    • Identification of protein-disulfide isomerase activity in fibronectin
    • Langenbach KJ and Sottile J. Identification of protein-disulfide isomerase activity in fibronectin. J Biol Chem 274: 7032-7038, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 7032-7038
    • Langenbach, K.J.1    Sottile, J.2
  • 56
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • Liddington RC and Ginsberg MH. Integrin activation takes shape. J Cell Biol 158: 833-839, 2002.
    • (2002) J Cell Biol , vol.158 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2
  • 57
    • 0033601739 scopus 로고    scopus 로고
    • An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins
    • Locker JK and Griffiths G. An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins. J Cell Biol 144: 267-279, 1999.
    • (1999) J Cell Biol , vol.144 , pp. 267-279
    • Locker, J.K.1    Griffiths, G.2
  • 59
    • 0016350060 scopus 로고
    • Evidence for two populations of disulfide bonds on blood platelets
    • MacIntyre DE and Gordon JL. Evidence for two populations of disulfide bonds on blood platelets. Biochem Soc Trans 2: 873-875, 1974.
    • (1974) Biochem Soc Trans , vol.2 , pp. 873-875
    • MacIntyre, D.E.1    Gordon, J.L.2
  • 60
    • 0016318471 scopus 로고
    • Prostaglandin receptor on blood platelets: Effects of thiol reagents on inhibition of platelet aggregation by prostaglandin E1
    • MacIntyre DE and Gordon JL. Prostaglandin receptor on blood platelets: effects of thiol reagents on inhibition of platelet aggregation by prostaglandin E1. Biochem Soc Trans 2: 1265-1269, 1974.
    • (1974) Biochem Soc Trans , vol.2 , pp. 1265-1269
    • MacIntyre, D.E.1    Gordon, J.L.2
  • 61
    • 0017355938 scopus 로고
    • Effect of thiol reagents on platelet transport processes and responses to stimuli
    • MacIntyre DE, Grainge CA, Drummond AH, and Gordon JL. Effect of thiol reagents on platelet transport processes and responses to stimuli. Biochem Pharmacol 26: 319-323, 1977.
    • (1977) Biochem Pharmacol , vol.26 , pp. 319-323
    • MacIntyre, D.E.1    Grainge, C.A.2    Drummond, A.H.3    Gordon, J.L.4
  • 62
    • 0027312063 scopus 로고
    • Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide isomerase
    • Mandel R, Ryser HJ-P, Ghani F, Wu M, and Peak D. Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide isomerase. Proc Natl Acad Sci USA 90: 4112-4116, 1993.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 4112-4116
    • Mandel, R.1    Ryser, H.J.-P.2    Ghani, F.3    Wu, M.4    Peak, D.5
  • 63
    • 0032583172 scopus 로고    scopus 로고
    • Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates
    • Markovic I, Pulyaeva H, Sokoloff A, and Chernomordik LV. Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates. J Cell Biol 143: 1155-1166, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 1155-1166
    • Markovic, I.1    Pulyaeva, H.2    Sokoloff, A.3    Chernomordik, L.V.4
  • 66
    • 0037296312 scopus 로고    scopus 로고
    • Redox control on the cell surface: Implications for HIV-1 entry
    • Matthias LJ and Hogg PJ. Redox control on the cell surface: Implications for HIV-1 entry. Antioxid Redox Signal 5: 133-138, 2003.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 133-138
    • Matthias, L.J.1    Hogg, P.J.2
  • 68
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella RA, Srinivasan M, Haugejorden SM, and Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 265: 1094-1101, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 69
    • 0033574156 scopus 로고    scopus 로고
    • Endogenous substrates of sphingosine-dependent kinases (SDKs) are chaperone proteins: Heat shock proteins, glucose-regulated proteins, protein disulfide isomerase, and calreticulin
    • Megidish T, Takio K, Titani K, Iwabuchi K, Hamaguchi A, Igarashi Y, and Hakomori S. Endogenous substrates of sphingosine-dependent kinases (SDKs) are chaperone proteins: heat shock proteins, glucose-regulated proteins, protein disulfide isomerase, and calreticulin. Biochemistry 38: 3369-3378, 1999.
    • (1999) Biochemistry , vol.38 , pp. 3369-3378
    • Megidish, T.1    Takio, K.2    Titani, K.3    Iwabuchi, K.4    Hamaguchi, A.5    Igarashi, Y.6    Hakomori, S.7
  • 70
    • 0032874303 scopus 로고    scopus 로고
    • Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III
    • Milev Y and Essex DW. Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III. Arch Biochem Biophys 361: 120-126, 1999.
    • (1999) Arch Biochem Biophys , vol.361 , pp. 120-126
    • Milev, Y.1    Essex, D.W.2
  • 71
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GP VI the central receptor?
    • Nieswandt B and Watson SP. Platelet-collagen interaction: is GP VI the central receptor? Blood 102: 449-461, 2003.
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 74
    • 0026495238 scopus 로고
    • Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets
    • Palabrica T, Lobb R, Furie BC, Aronovitz M, Benjamin C, Hsu YM, Sajer SA, and Furie B. Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets. Nature 359: 848-851, 1992.
    • (1992) Nature , vol.359 , pp. 848-851
    • Palabrica, T.1    Lobb, R.2    Furie, B.C.3    Aronovitz, M.4    Benjamin, C.5    Hsu, Y.M.6    Sajer, S.A.7    Furie, B.8
  • 75
    • 0023988955 scopus 로고
    • Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment
    • Pelham HR. Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. EMBO J 7: 913-918, 1988.
    • (1988) EMBO J , vol.7 , pp. 913-918
    • Pelham, H.R.1
  • 77
    • 0346101760 scopus 로고    scopus 로고
    • Cell surface expression of GluR5 kainate receptors is regulated by an endoplasmic reticulum retention signal
    • Ren Z, Riley NJ, Needleman LA, Sanders JM, Swanson GT, and Marshall J. Cell surface expression of GluR5 kainate receptors is regulated by an endoplasmic reticulum retention signal. J Biol Chem 278: 52700-52709, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 52700-52709
    • Ren, Z.1    Riley, N.J.2    Needleman, L.A.3    Sanders, J.M.4    Swanson, G.T.5    Marshall, J.6
  • 78
    • 0141498240 scopus 로고    scopus 로고
    • Von Willebrand factor, platelets and endothelial cell interactions
    • Ruggeri ZM. Von Willebrand factor, platelets and endothelial cell interactions. J Thromb Haemost 1: 1335-1342, 2003.
    • (2003) J Thromb Haemost , vol.1 , pp. 1335-1342
    • Ruggeri, Z.M.1
  • 79
    • 0035889152 scopus 로고    scopus 로고
    • A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa (IIb3) integrin receptor locked in a high-affinity state and a Glanzmann thrombasthenia-like phenotype
    • Ruiz C, Liu C-Y, Sun Q-H, Sigaud-Fiks M, Fressinaud E, Muller J-Y, Nurden P, Nurden AT, Newman PJ, and Valentin N. A point mutation in the cysteine-rich domain of glycoprotein (GP) IIIa results in the expression of a GPIIb-IIIa (IIb3) integrin receptor locked in a high-affinity state and a Glanzmann thrombasthenia-like phenotype. Blood 98: 2432-2441, 2001.
    • (2001) Blood , vol.98 , pp. 2432-2441
    • Ruiz, C.1    Liu, C.-Y.2    Sun, Q.-H.3    Sigaud-Fiks, M.4    Fressinaud, E.5    Muller, J.-Y.6    Nurden, P.7    Nurden, A.T.8    Newman, P.J.9    Valentin, N.10
  • 80
    • 0028257964 scopus 로고
    • Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction
    • Ryser HJ, Levy EM, Mandel R, and DiSciullo GJ. Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction. Proc Natl Acad Sci USA 91: 4559-4563, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4559-4563
    • Ryser, H.J.1    Levy, E.M.2    Mandel, R.3    DiSciullo, G.J.4
  • 81
    • 0031978341 scopus 로고    scopus 로고
    • Hsp47 binds to the KDEL receptor and cell surface expression is modulated by cytoplasmic and endosomal pH
    • Sauk JJ, Norris K, Herbert C, Ordonez J, and Reynolds M. Hsp47 binds to the KDEL receptor and cell surface expression is modulated by cytoplasmic and endosomal pH. Connect Tiss Res 37: 105-119, 1998.
    • (1998) Connect Tiss Res , vol.37 , pp. 105-119
    • Sauk, J.J.1    Norris, K.2    Herbert, C.3    Ordonez, J.4    Reynolds, M.5
  • 82
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil SJ, Kashiwagi H, and Pampori N. Integrin signaling: the platelet paradigm. Blood 91: 2645-2657, 1998.
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 83
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: Dynamic scaffolds for adhesion and signaling in platelets
    • Shattil SJ and Newman PJ. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood 104: 1606-1615, 2004.
    • (2004) Blood , vol.104 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 85
    • 0037105364 scopus 로고    scopus 로고
    • Disruption of the long-range GPIIIa Cys(5)-Cys(435) disulfide bond results in the production of constitutively active GPIIb-IIIa (alpha(IIb)beta(3)) integrin complexes
    • Sun QH, Liu CY, Wang R, Paddock C, and Newman PJ. Disruption of the long-range GPIIIa Cys(5)-Cys(435) disulfide bond results in the production of constitutively active GPIIb-IIIa (alpha(IIb)beta(3)) integrin complexes. Blood 100: 2094-2101, 2002.
    • (2002) Blood , vol.100 , pp. 2094-2101
    • Sun, Q.H.1    Liu, C.Y.2    Wang, R.3    Paddock, C.4    Newman, P.J.5
  • 87
    • 0030853923 scopus 로고    scopus 로고
    • Membrane-bound protein disulfide isomerase(PDI) is involved in regulation of surface expression of thiols and drug sensitivity of B-CLL cells
    • Tager M, Kroning H, Thiel U, and Ansorge S. Membrane-bound protein disulfide isomerase(PDI) is involved in regulation of surface expression of thiols and drug sensitivity of B-CLL cells. Exp Hematol 25: 601-607, 1997.
    • (1997) Exp Hematol , vol.25 , pp. 601-607
    • Tager, M.1    Kroning, H.2    Thiel, U.3    Ansorge, S.4
  • 88
    • 0036798783 scopus 로고    scopus 로고
    • Improperly folded green fluorescent protein is secreted via a non-classical pathway
    • Tanudji M, Hevi S, and Chuck SL. Improperly folded green fluorescent protein is secreted via a non-classical pathway. J Cell Sci 115: 3849-3857, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 3849-3857
    • Tanudji, M.1    Hevi, S.2    Chuck, S.L.3
  • 89
    • 0029778556 scopus 로고    scopus 로고
    • Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus
    • Teasdale RD and Jackson MR. Signal-mediated sorting of membrane proteins between the endoplasmic reticulum and the golgi apparatus. Annu Rev Cell Dev Biol 12: 27-54, 1996.
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 27-54
    • Teasdale, R.D.1    Jackson, M.R.2
  • 90
    • 0029095952 scopus 로고
    • The selectins: Vascular adhesion molecules
    • Tedder TF, Steeber DA, Chen A, and Engel P. The selectins: vascular adhesion molecules. FASEB J 9: 866-873, 1995.
    • (1995) FASEB J , vol.9 , pp. 866-873
    • Tedder, T.F.1    Steeber, D.A.2    Chen, A.3    Engel, P.4
  • 91
    • 0029163450 scopus 로고
    • Secretion, surface localisation, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes
    • Terada K, Manchikalapudi P, Noiva R, Jauregui HO, Stocken RJ, and Schilsky ML. Secretion, surface localisation, turnover, and steady state expression of protein disulfide isomerase in rat hepatocytes. J Biol Chem 270: 20410-20416, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 20410-20416
    • Terada, K.1    Manchikalapudi, P.2    Noiva, R.3    Jauregui, H.O.4    Stocken, R.J.5    Schilsky, M.L.6
  • 92
    • 4344697308 scopus 로고    scopus 로고
    • Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide
    • Triantafilou M and Triantafilou K. Heat-shock protein 70 and heat-shock protein 90 associate with Toll-like receptor 4 in response to bacterial lipopolysaccharide. Biochem Soc Trans 32: 636-639, 2004.
    • (2004) Biochem Soc Trans , vol.32 , pp. 636-639
    • Triantafilou, M.1    Triantafilou, K.2
  • 93
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: Unpredicted non-ER locations and functions
    • Turano C, Coppari S, Altieri F, and Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell Physiol 193: 154-163, 2002.
    • (2002) J Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 96
    • 0029763215 scopus 로고    scopus 로고
    • Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets
    • Wagner CL, Mascelli MA, Neblock DS, Weisman HF, Coller BS, and Jordan RE. Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets. Blood 88: 907-914, 1996.
    • (1996) Blood , vol.88 , pp. 907-914
    • Wagner, C.L.1    Mascelli, M.A.2    Neblock, D.S.3    Weisman, H.F.4    Coller, B.S.5    Jordan, R.E.6
  • 97
    • 0346463126 scopus 로고    scopus 로고
    • Redox modulation of integrin alpha IIb beta 3 involves a novel allosteric regulation of its thiol isomerase activity
    • Walsh GM, Sheehan D, Kinsella A, Moran N, and O'Neill S. Redox modulation of integrin alpha IIb beta 3 involves a novel allosteric regulation of its thiol isomerase activity. Biochemistry 43: 473-480, 2004.
    • (2004) Biochemistry , vol.43 , pp. 473-480
    • Walsh, G.M.1    Sheehan, D.2    Kinsella, A.3    Moran, N.4    O'Neill, S.5
  • 98
    • 0030810716 scopus 로고    scopus 로고
    • Disruption of a long-range disulfide bond between residues Cys406 and Cys655 in glycoprotein Ilia does not affect the function of platelet glycoprotein IIb-IIIa
    • Wang R, Peterson J, Aster RH, and Newman PJ. Disruption of a long-range disulfide bond between residues Cys406 and Cys655 in glycoprotein Ilia does not affect the function of platelet glycoprotein IIb-IIIa. Blood 90: 1718-1719, 1997.
    • (1997) Blood , vol.90 , pp. 1718-1719
    • Wang, R.1    Peterson, J.2    Aster, R.H.3    Newman, P.J.4
  • 99
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex
    • Wetterau JR, Combs KA, Spinner SN, and Joiner BJ. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 265: 9801-9807, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 9801-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 101
    • 0033828950 scopus 로고    scopus 로고
    • Reduction of von Willebrand factor by endothelial cells
    • Xie LJ, Chesterman CN, and Hogg PJ. Reduction of von Willebrand factor by endothelial cells. Thromb Haemost 84: 506-513, 2000.
    • (2000) Thromb Haemost , vol.84 , pp. 506-513
    • Xie, L.J.1    Chesterman, C.N.2    Hogg, P.J.3
  • 102
    • 0035908117 scopus 로고    scopus 로고
    • Control of von Willebrand factor multimer size by thrombospondin-1
    • Xie LJ, Chesterman CN, and Hogg PJ. Control of von Willebrand factor multimer size by thrombospondin-1. J Exp Med 193: 1341-1349, 2001.
    • (2001) J Exp Med , vol.193 , pp. 1341-1349
    • Xie, L.J.1    Chesterman, C.N.2    Hogg, P.J.3
  • 104
    • 0042739086 scopus 로고    scopus 로고
    • New insights into the structural basis of integrin activation
    • Xiong JP, Stehle T, Goodman SL, and Arnaout MA. New insights into the structural basis of integrin activation. Blood 102: 1155-1159, 2003.
    • (2003) Blood , vol.102 , pp. 1155-1159
    • Xiong, J.P.1    Stehle, T.2    Goodman, S.L.3    Arnaout, M.A.4
  • 106
    • 0034704162 scopus 로고    scopus 로고
    • A redox site involved in integrin activation
    • Yan B and Smith JW. A redox site involved in integrin activation. J Biol Chem 275: 39964-39972, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 39964-39972
    • Yan, B.1    Smith, J.W.2
  • 107
    • 0035979337 scopus 로고    scopus 로고
    • Mechanism of integrin activation by disulfide bond reduction
    • Yan B and Smith JW. Mechanism of integrin activation by disulfide bond reduction. Biochemistry 40: 8861-8867, 2001.
    • (2001) Biochemistry , vol.40 , pp. 8861-8867
    • Yan, B.1    Smith, J.W.2
  • 108
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyses transnitrosation and regulates intracellular transfer of nitric oxide
    • Zai A, Rudd A, Scribner AW, and Loscalzo J. Cell-surface protein disulfide isomerase catalyses transnitrosation and regulates intracellular transfer of nitric oxide. J Clin Invest 103: 393-399, 1999.
    • (1999) J Clin Invest , vol.103 , pp. 393-399
    • Zai, A.1    Rudd, A.2    Scribner, A.W.3    Loscalzo, J.4


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