메뉴 건너뛰기




Volumn 14, Issue 1, 2011, Pages 113-126

Control of mature protein function by allosteric disulfide bonds

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARYL SULFOTRANSFERASE; BETA2 GLYCOPROTEIN 1; BETA3 INTEGRIN; BOTULINUM TOXIN; CD4 ANTIGEN; CYSTEINE; DISULFIDE; PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; THROMBOPLASTIN; VON WILLEBRAND FACTOR;

EID: 78649484651     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2010.3620     Document Type: Review
Times cited : (42)

References (108)
  • 2
    • 60649102427 scopus 로고    scopus 로고
    • Human glutaredoxin-1 catalyzes the reduction of HIV-1 gp120 and CD4 disulfides and its inhibition reduces HIV-1 replication
    • Auwerx J, Isacsson O, Soderlund J, Balzarini J, Johansson M, and Lundberg M. Human glutaredoxin-1 catalyzes the reduction of HIV-1 gp120 and CD4 disulfides and its inhibition reduces HIV-1 replication. Int J Biochem Cell Biol 41: 1269-1275, 2009.
    • (2009) Int J Biochem Cell Biol , vol.41 , pp. 1269-1275
    • Auwerx, J.1    Isacsson, O.2    Soderlund, J.3    Balzarini, J.4    Johansson, M.5    Lundberg, M.6
  • 3
    • 85102663244 scopus 로고    scopus 로고
    • The disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin
    • In press
    • Azimi I, Matthias LJ, Center RJ, Wong JWH, and Hogg PJ. The disulfide bond that constrains the HIV-1 gp120 V3 domain is cleaved by thioredoxin. J Biol Chem (In press).
    • J Biol Chem
    • Azimi, I.1    Matthias, L.J.2    Center, R.J.3    Jwh, W.4    Hogg, P.J.5
  • 5
    • 0037474328 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of two di-sulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion
    • Barbouche R, Miquelis R, Jones IM, and Fenouillet E. Protein-disulfide isomerase-mediated reduction of two di-sulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion. J Biol Chem 278: 3131-3136, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 3131-3136
    • Barbouche, R.1    Miquelis, R.2    Jones, I.M.3    Fenouillet, E.4
  • 7
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt C, Lillig CH, and Holmgren A. Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783: 641-650, 2008.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 9
    • 33746659382 scopus 로고    scopus 로고
    • Association between disruption of CD4 receptor dimer-ization and increased human immunodeficiency virus type 1 entry
    • Bourgeois R, Mercier J, Paquette-Brooks I, and Cohen EA. Association between disruption of CD4 receptor dimer-ization and increased human immunodeficiency virus type 1 entry. Retrovirology 3: 31, 2006.
    • (2006) Retrovirology , vol.3 , pp. 31
    • Bourgeois, R.1    Mercier, J.2    Paquette-Brooks, I.3    Cohen, E.A.4
  • 10
    • 0036792118 scopus 로고    scopus 로고
    • Evolution of amino acid frequencies in proteins over deep time: Inferred order of introduction of amino acids into the genetic code
    • Brooks DJ, Fresco JR, Lesk AM, and Singh M. Evolution of amino acid frequencies in proteins over deep time: inferred order of introduction of amino acids into the genetic code. Mol Biol Evol 19: 1645-1655, 2002.
    • (2002) Mol Biol Evol , vol.19 , pp. 1645-1655
    • Brooks, D.J.1    Fresco, J.R.2    Lesk, A.M.3    Singh, M.4
  • 11
  • 12
    • 33750985704 scopus 로고    scopus 로고
    • Allosteric disulfide bonds in thrombosis and thrombolysis
    • Chen VM and Hogg PJ. Allosteric disulfide bonds in thrombosis and thrombolysis. J Thromb Haemost 4: 2533-2541, 2006.
    • (2006) J Thromb Haemost , vol.4 , pp. 2533-2541
    • Chen, V.M.1    Hogg, P.J.2
  • 13
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • Cho J, Furie BC, Coughlin SR, and Furie B. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J Clin Invest 118: 1123-1131, 2008.
    • (2008) J Clin Invest , vol.118 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3    Furie, B.4
  • 14
    • 37249000281 scopus 로고    scopus 로고
    • Shear-induced disulfide bond formation regulates adhesion activity of von Willebrand factor
    • Choi H, Aboulfatova K, Pownall HJ, Cook R, and Dong JF. Shear-induced disulfide bond formation regulates adhesion activity of von Willebrand factor. J Biol Chem 282: 35604-35611, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 35604-35611
    • Choi, H.1    Aboulfatova, K.2    Pownall, H.J.3    Cook, R.4    Dong, J.F.5
  • 15
    • 0014961369 scopus 로고
    • Mechanism of the inactivation of guinea pig liver transglutaminase by tetrathionate
    • Chung SI and Folk JE. Mechanism of the inactivation of guinea pig liver transglutaminase by tetrathionate. J Biol Chem 245: 681-689, 1970.
    • (1970) J Biol Chem , vol.245 , pp. 681-689
    • Chung, S.I.1    Folk, J.E.2
  • 16
    • 0037178798 scopus 로고    scopus 로고
    • Recon-stitution of a disulfide isomerization system
    • Collet JF, Riemer J, Bader MW, and Bardwell JC. Recon-stitution of a disulfide isomerization system. J Biol Chem 277: 26886-26892, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 26886-26892
    • Collet, J.F.1    Riemer, J.2    Bader, M.W.3    Bardwell, J.C.4
  • 17
  • 18
    • 0018123566 scopus 로고
    • Disulfide bonds and the quaternary structure of factor VIII=von Willebrand factor
    • Counts RB, Paskell SL, and Elgee SK. Disulfide bonds and the quaternary structure of factor VIII=von Willebrand factor. J Clin Invest 62: 702-709, 1978.
    • (1978) J Clin Invest , vol.62 , pp. 702-709
    • Counts, R.B.1    Paskell, S.L.2    Elgee, S.K.3
  • 19
    • 28344435221 scopus 로고    scopus 로고
    • Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions
    • Dong JF. Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions. J Thromb Haemost 3: 1710-1716, 2005.
    • (2005) J Thromb Haemost , vol.3 , pp. 1710-1716
    • Dong, J.F.1
  • 20
    • 0030407682 scopus 로고    scopus 로고
    • Maturation and assembly of retroviral glyco-proteins
    • Einfeld D. Maturation and assembly of retroviral glyco-proteins. Curr Top Microbiol Immunol 214: 133-176, 1996.
    • (1996) Curr Top Microbiol Immunol , vol.214 , pp. 133-176
    • Einfeld, D.1
  • 21
    • 64549119138 scopus 로고    scopus 로고
    • Redox control of platelet function
    • Essex DW. Redox control of platelet function. Antioxid Re-dox Signal 11: 1191-1225, 2009.
    • (2009) Antioxid Re-dox Signal , vol.11 , pp. 1191-1225
    • Essex, D.W.1
  • 22
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex DW, Chen K, and Swiatkowska M. Localization 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
    • 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
  • 24
    • 0347719283 scopus 로고    scopus 로고
    • Theoretical insights into the mechanism for thiol=disulfide exchange
    • Fernandes PA and Ramos MJ. Theoretical insights into the mechanism for thiol=disulfide exchange. Chemistry 10: 257-266, 2004.
    • (2004) Chemistry , vol.10 , pp. 257-266
    • Fernandes, P.A.1    Ramos, M.J.2
  • 25
    • 35748961106 scopus 로고    scopus 로고
    • Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes
    • Fischer A and Montal M. Crucial role of the disulfide bridge between botulinum neurotoxin light and heavy chains in protease translocation across membranes. J Biol Chem 282: 29604-29611, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 29604-29611
    • Fischer, A.1    Montal, M.2
  • 26
    • 50449098285 scopus 로고    scopus 로고
    • Mechanisms of thrombus formation
    • Furie B and Furie BC. Mechanisms of thrombus formation. N Engl J Med 359: 938-949, 2008.
    • (2008) N Engl J Med , vol.359 , pp. 938-949
    • Furie, B.1    Furie, B.C.2
  • 27
    • 0029907370 scopus 로고    scopus 로고
    • Von Willebrand factor: Molecular size and functional activity
    • Furlan M. Von Willebrand factor: molecular size and functional activity. Ann Hematol 72: 341-348, 1996.
    • (1996) Ann Hematol , vol.72 , pp. 341-348
    • Furlan, M.1
  • 28
    • 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
  • 30
    • 33845532626 scopus 로고    scopus 로고
    • Hypothesis for control of von Willebrand factor multimer size by intra-molecular thiol-disulphide exchange
    • Ganderton T, Berndt MC, Chesterman CN, and Hogg PJ. Hypothesis for control of von Willebrand factor multimer size by intra-molecular thiol-disulphide exchange. J Thromb Haemost 5: 204-206, 2007.
    • (2007) J Thromb Haemost , vol.5 , pp. 204-206
    • Ganderton, T.1    Berndt, M.C.2    Chesterman, C.N.3    Hogg, P.J.4
  • 31
    • 0037012541 scopus 로고    scopus 로고
    • Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems
    • Garcia Abreu J, Coffinier C, Larrain J, Oelgeschlager M, and De Robertis EM. Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems. Gene 287: 39-47, 2002.
    • (2002) Gene , vol.287 , pp. 39-47
    • Garcia Abreu, J.1    Coffinier, C.2    Larrain, J.3    Oelgeschlager, M.4    De Robertis, E.M.5
  • 32
    • 0027135805 scopus 로고
    • Refinement and analysis of the structure of the first two domains of human CD4
    • Garrett TP, Wang J, Yan Y, Liu J, and Harrison SC. Refinement and analysis of the structure of the first two domains of human CD4. J Mol Biol 234: 763-778, 1993.
    • (1993) J Mol Biol , vol.234 , pp. 763-778
    • Garrett, T.P.1    Wang, J.2    Yan, Y.3    Liu, J.4    Harrison, S.C.5
  • 36
    • 0036901574 scopus 로고    scopus 로고
    • Transglutami-nases: Nature's biological glues
    • Griffin M, Casadio R, and Bergamini CM. Transglutami-nases: nature's biological glues. Biochem J 368: 377-396, 2002.
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 37
    • 45549122242 scopus 로고    scopus 로고
    • DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli
    • Grimshaw JP, Stirnimann CU, Brozzo MS, Malojcic G, Grutter MG, Capitani G, and Glockshuber R. DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli. J Mol Biol 380: 667-680, 2008.
    • (2008) J Mol Biol , vol.380 , pp. 667-680
    • Grimshaw, J.P.1    Stirnimann, C.U.2    Brozzo, M.S.3    Malojcic, G.4    Grutter, M.G.5    Capitani, G.6    Glockshuber, R.7
  • 38
    • 0029861713 scopus 로고    scopus 로고
    • Cell stress-regulated human major histo-compatibility complex class i gene expressed in gastrointestinal epithelium
    • Groh V, Bahram S, Bauer S, Herman A, Beauchamp M, and Spies T. Cell stress-regulated human major histo-compatibility complex class I gene expressed in gastrointestinal epithelium. Proc Natl Acad Sci USA 93: 12445-12450, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12445-12450
    • Groh, V.1    Bahram, S.2    Bauer, S.3    Herman, A.4    Beauchamp, M.5    Spies, T.6
  • 39
    • 0033536068 scopus 로고    scopus 로고
    • Broad tumor-associated expression and recognition by tumor-derived gamma delta T cells of MICA and MICB
    • Groh V, Rhinehart R, Secrist H, Bauer S, Grabstein KH, and Spies T. Broad tumor-associated expression and recognition by tumor-derived gamma delta T cells of MICA and MICB. Proc Natl Acad Sci USA 96: 6879-6884, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6879-6884
    • Groh, V.1    Rhinehart, R.2    Secrist, H.3    Bauer, S.4    Grabstein, K.H.5    Spies, T.6
  • 40
    • 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
  • 42
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 110: 673-687, 2002.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 43
    • 77956903176 scopus 로고    scopus 로고
    • Naturally occurring free thiols within ß2-glycoprotein i in vivo: Nitrosylation, redox modification by endothelial cells and regulation of oxidative stress induced cell injury
    • Ioannou Y, Zhang J-Y, Passam FH, Rahgozar S, Qi JC, Giannakopoulos B, Yu MQP, Yu DM, Hogg PJ, and Krilis SA. Naturally occurring free thiols within ß2-glycoprotein I in vivo: nitrosylation, redox modification by endothelial cells and regulation of oxidative stress induced cell injury. Blood 116: 1995-1997, 2010.
    • (2010) Blood , vol.116 , pp. 1995-1997
    • Ioannou, Y.1    Zhang, J.-Y.2    Passam, F.H.3    Rahgozar, S.4    Qi, J.C.5    Giannakopoulos, B.6    Mqp, Y.7    Yu, D.M.8    Hogg, P.J.9    Krilis, S.A.10
  • 45
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols=disulfides by protein disulfide isomerase
    • Jiang XM, Fitzgerald M, Grant CM, and Hogg PJ. Redox control of exofacial protein thiols=disulfides by protein disulfide 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
  • 46
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, and Thornton JM. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8: 275-282, 1992.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 49
    • 0025914427 scopus 로고
    • Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Es-cherichia coli thioredoxin
    • Krause G, Lundstrom J, Barea JL, Pueyo de la Cuesta C, and Holmgren A. Mimicking the active site of protein disulfide-isomerase by substitution of proline 34 in Es-cherichia coli thioredoxin. J Biol Chem 266: 9494-9500, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 9494-9500
    • Krause, G.1    Lundstrom, J.2    Barea, J.L.3    Pueyo De La Cuesta, C.4    Holmgren, A.5
  • 51
    • 0026650453 scopus 로고
    • Relations between factor VIIa binding and expression of factor VIIa=tissue factor catalytic activity on cell surfaces
    • Le DT, Rapaport SI, and Rao LV. Relations between factor VIIa binding and expression of factor VIIa=tissue factor catalytic activity on cell surfaces. J Biol Chem 267: 15447-15454, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 15447-15454
    • Le, D.T.1    Rapaport, S.I.2    Rao, L.V.3
  • 52
    • 0035347169 scopus 로고    scopus 로고
    • Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA
    • Li P, Morris DL, Willcox BE, Steinle A, Spies T, and Strong RK. Complex structure of the activating immunoreceptor NKG2D and its MHC class I-like ligand MICA. Nat Immunol 2: 443-451, 2001.
    • (2001) Nat Immunol , vol.2 , pp. 443-451
    • Li, P.1    Morris, D.L.2    Willcox, B.E.3    Steinle, A.4    Spies, T.5    Strong, R.K.6
  • 53
    • 0033136696 scopus 로고    scopus 로고
    • Crystal structure of the MHC class i homolog MIC-A, a gammadelta T cell ligand
    • Li P, Willie ST, Bauer S, Morris DL, Spies T, and Strong RK. Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand. Immunity 10: 577-584, 1999.
    • (1999) Immunity , vol.10 , pp. 577-584
    • Li, P.1    Willie, S.T.2    Bauer, S.3    Morris, D.L.4    Spies, T.5    Strong, R.K.6
  • 54
  • 55
    • 50949106954 scopus 로고    scopus 로고
    • Critical importance of the cell system when studying tissue factor de-encryption
    • author reply 913
    • Liang HP and Hogg PJ. Critical importance of the cell system when studying tissue factor de-encryption. Blood 112: 912-913; author reply 913, 2008.
    • (2008) Blood , vol.112 , pp. 912-913
    • Liang, H.P.1    Hogg, P.J.2
  • 57
    • 77954695284 scopus 로고    scopus 로고
    • The importance of vicinal cysteines C1669 and C1670 for von Willebrand factor A2 domain function
    • Luken BM, Winn LY, Emsley J, Lane DA, and Crawley JT. The importance of vicinal cysteines, C1669 and C1670, for von Willebrand factor A2 domain function. Blood 115:4910- 4913, 2010.
    • (2010) Blood , vol.115 , pp. 4910-4913
    • Luken, B.M.1    Winn, L.Y.2    Emsley, J.3    Lane, D.A.4    Crawley, J.T.5
  • 58
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glu-tathione and thioredoxin
    • Lundstrom J and Holmgren A. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glu-tathione and thioredoxin. Biochemistry 32: 6649-6655, 1993.
    • (1993) Biochemistry , vol.32 , pp. 6649-6655
    • Lundstrom, J.1    Holmgren, A.2
  • 59
    • 33646859763 scopus 로고    scopus 로고
    • Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC
    • Maekawa A, Schmidt B, Fazekas de St Groth B, Sanejouand YH, and Hogg PJ. Evidence for a domain-swapped CD4 dimer as the coreceptor for binding to class II MHC. J Immunol 176: 6873-6878, 2006.
    • (2006) J Immunol , vol.176 , pp. 6873-6878
    • Maekawa, A.1    Schmidt, B.2    Fazekas De St Groth, B.3    Sanejouand, Y.H.4    Hogg, P.J.5
  • 60
    • 58049194127 scopus 로고    scopus 로고
    • A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sul-fotransferase from uropathogenic Escherichia coli
    • Malojcic G, Owen RL, Grimshaw JP, Brozzo MS, Dreher-Teo H, and Glockshuber R. A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sul-fotransferase from uropathogenic Escherichia coli. Proc Natl Acad Sci USA 105: 19217-19222, 2008.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19217-19222
    • Malojcic, G.1    Owen, R.L.2    Grimshaw, J.P.3    Brozzo, M.S.4    Dreher-Teo, H.5    Glockshuber, R.6
  • 62
    • 78649462789 scopus 로고    scopus 로고
    • Reduced monomeric CD4 is the preferred receptor for HIV
    • Oct 25 [Epub ahead of print]
    • Matthias LJ, Azimi I, Tabrett CA, and Hogg PJ. Reduced monomeric CD4 is the preferred receptor for HIV. J Biol Chem 2010 Oct 25 [Epub ahead of print].
    • (2010) J Biol Chem
    • Matthias, L.J.1    Azimi, I.2    Tabrett, C.A.3    Hogg, P.J.4
  • 64
    • 31744437770 scopus 로고    scopus 로고
    • The physiological function of von Willebrand's factor depends on its tubular storage in endothelial Weibel-Palade bodies
    • Michaux G, Abbitt KB, Collinson LM, Haberichter SL, Norman KE, and Cutler DF. The physiological function of von Willebrand's factor depends on its tubular storage in endothelial Weibel-Palade bodies. Dev Cell 10: 223-232, 2006.
    • (2006) Dev Cell , vol.10 , pp. 223-232
    • Michaux, G.1    Abbitt, K.B.2    Collinson, L.M.3    Haberichter, S.L.4    Norman, K.E.5    Cutler, D.F.6
  • 65
    • 33846008333 scopus 로고    scopus 로고
    • A novel disulfide bond in the SH2 domain of the C-terminal Src kinase controls catalytic activity
    • Mills JE, Whitford PC, Shaffer J, Onuchic JN, Adams JA, and Jennings PA. A novel disulfide bond in the SH2 domain of the C-terminal Src kinase controls catalytic activity. J Mol Biol 365: 1460-1468, 2007.
    • (2007) J Mol Biol , vol.365 , pp. 1460-1468
    • Mills, J.E.1    Whitford, P.C.2    Shaffer, J.3    Onuchic, J.N.4    Adams, J.A.5    Jennings, P.A.6
  • 66
    • 7044240799 scopus 로고    scopus 로고
    • Beta 2 gly-coprotein I-function in health and disease
    • Miyakis S, Giannakopoulos B, and Krilis SA. Beta 2 gly-coprotein I-function in health and disease. Thromb Res 114: 335-346, 2004.
    • (2004) Thromb Res , vol.114 , pp. 335-346
    • Miyakis, S.1    Giannakopoulos, B.2    Krilis, S.A.3
  • 68
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: A marvel of protein design
    • Montal M. Botulinum neurotoxin: a marvel of protein design. Annu Rev Biochem 79: 591-617, 2010.
    • (2010) Annu Rev Biochem , vol.79 , pp. 591-617
    • Montal, M.1
  • 69
    • 50349098094 scopus 로고    scopus 로고
    • Specific cysteines in beta3 are involved in disulfide bond exchange-dependent and -independent activation of alphaIIbbeta3
    • Mor-Cohen R, Rosenberg N, Landau M, Lahav J, and Seligsohn U. Specific cysteines in beta3 are involved in disulfide bond exchange-dependent and -independent activation of alphaIIbbeta3. J Biol Chem 283: 19235-19244, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 19235-19244
    • Mor-Cohen, R.1    Rosenberg, N.2    Landau, M.3    Lahav, J.4    Seligsohn, U.5
  • 71
    • 11144240469 scopus 로고    scopus 로고
    • Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Will-ebrand Factor type C module) from collagen IIA
    • O'Leary JM, Hamilton JM, Deane CM, Valeyev NV, Sandell LJ, and Downing AK. Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Will-ebrand Factor type C module) from collagen IIA. J Biol Chem 279: 53857-53866, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 53857-53866
    • O'Leary, J.M.1    Hamilton, J.M.2    Deane, C.M.3    Valeyev, N.V.4    Sandell, L.J.5    Downing, A.K.6
  • 72
    • 0035502932 scopus 로고    scopus 로고
    • Shedding light on disulfide bond formation: Engineering a redox switch in green fluorescent protein
    • Ostergaard H, Henriksen A, Hansen FG, and Winther JR. Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein. EMBO J 20: 5853-5862, 2001.
    • (2001) EMBO J , vol.20 , pp. 5853-5862
    • Ostergaard, H.1    Henriksen, A.2    Hansen, F.G.3    Winther, J.R.4
  • 73
    • 33745236040 scopus 로고    scopus 로고
    • Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion
    • Ou W and Silver J. Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion. Virology 350: 406-417, 2006.
    • (2006) Virology , vol.350 , pp. 406-417
    • Ou, W.1    Silver, J.2
  • 76
    • 37049001668 scopus 로고    scopus 로고
    • Tissue factor activation: Is disulfide bond switching a regulatory mechanism?
    • Pendurthi UR, Ghosh S, Mandal SK, and Rao LV. Tissue factor activation: is disulfide bond switching a regulatory mechanism? Blood 110: 3900-3908, 2007.
    • (2007) Blood , vol.110 , pp. 3900-3908
    • Pendurthi, U.R.1    Ghosh, S.2    Mandal, S.K.3    Rao, L.V.4
  • 77
    • 54049143232 scopus 로고    scopus 로고
    • Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor
    • Persson E. Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor. Thromb Res 123: 171-176, 2008.
    • (2008) Thromb Res , vol.123 , pp. 171-176
    • Persson, E.1
  • 78
    • 11144281811 scopus 로고    scopus 로고
    • Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: Characterization of DraB-DraE complexes
    • Piatek R, Zalewska B, Kolaj O, Ferens M, Nowicki B, and Kur J. Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: characterization of DraB-DraE complexes. Infect Immun 73: 135-145, 2005.
    • (2005) Infect Immun , vol.73 , pp. 135-145
    • Piatek, R.1    Zalewska, B.2    Kolaj, O.3    Ferens, M.4    Nowicki, B.5    Kur, J.6
  • 79
    • 38549156658 scopus 로고    scopus 로고
    • Trans-glutaminase 2 undergoes a large conformational change upon activation
    • Pinkas DM, Strop P, Brunger AT, and Khosla C. Trans-glutaminase 2 undergoes a large conformational change upon activation. PLoS Biol 5: e327, 2007.
    • (2007) PLoS Biol , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 80
    • 0023185461 scopus 로고
    • Initiation of the extrinsic pathway of coagulation Association of factor VIIa with a cell line expressing tissue factor
    • Ploplis VA, Edgington TS, and Fair DS. Initiation of the extrinsic pathway of coagulation. Association of factor VIIa with a cell line expressing tissue factor, J Biol Chem, 262, 9503-9508, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 9503-9508
    • Ploplis, V.A.1    Edgington, T.S.2    Fair, D.S.3
  • 81
    • 55749091808 scopus 로고    scopus 로고
    • Platelet microparticle-associated protein disulfide isomerase promotes platelet aggregation and inactivates insulin
    • Raturi A, Miersch S, Hudson JW, and Mutus B. Platelet microparticle-associated protein disulfide isomerase promotes platelet aggregation and inactivates insulin. Biochim Biophys Acta 1778: 2790-2796, 2008.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2790-2796
    • Raturi, A.1    Miersch, S.2    Hudson, J.W.3    Mutus, B.4
  • 84
    • 45849134503 scopus 로고    scopus 로고
    • Thermodynamic aspects of DsbD-mediated electron transport
    • Rozhkova A and Glockshuber R. Thermodynamic aspects of DsbD-mediated electron transport. J Mol Biol 380: 783-788, 2008.
    • (2008) J Mol Biol , vol.380 , pp. 783-788
    • Rozhkova, A.1    Glockshuber, R.2
  • 85
    • 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
  • 86
    • 0024345543 scopus 로고
    • Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation
    • Sakai T, Lund-Hansen T, Paborsky L, Pedersen AH, and Kisiel W. Binding of human factors VII and VIIa to a human bladder carcinoma cell line (J82). Implications for the initiation of the extrinsic pathway of blood coagulation. J Biol Chem 264: 9980-9988, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 9980-9988
    • Sakai, T.1    Lund-Hansen, T.2    Paborsky, L.3    Pedersen, A.H.4    Kisiel, W.5
  • 87
    • 4444358269 scopus 로고    scopus 로고
    • Domain swapping of CD4 upon dimer-ization
    • Sanejouand YH. Domain swapping of CD4 upon dimer-ization. Proteins 57: 205-212, 2004.
    • (2004) Proteins , vol.57 , pp. 205-212
    • Sanejouand, Y.H.1
  • 88
    • 0037112164 scopus 로고    scopus 로고
    • Cha-perone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer FG, Pinkner JS, Waksman G, and Hultgren SJ. Cha-perone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 111: 543-551, 2002.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 89
    • 33745161382 scopus 로고    scopus 로고
    • Allosteric disulfide bonds
    • Schmidt B, Ho L, and Hogg PJ. Allosteric disulfide bonds. Biochemistry 45: 7429-7433, 2006.
    • (2006) Biochemistry , vol.45 , pp. 7429-7433
    • Schmidt, B.1    Ho, L.2    Hogg, P.J.3
  • 90
    • 34547891553 scopus 로고    scopus 로고
    • Search for allosteric disulfide bonds in NMR structures
    • Schmidt B and Hogg PJ. Search for allosteric disulfide bonds in NMR structures. BMC Struct Biol 7: 49, 2007.
    • (2007) BMC Struct Biol , vol.7 , pp. 49
    • Schmidt, B.1    Hogg, P.J.2
  • 91
    • 0033570889 scopus 로고    scopus 로고
    • Crystal structure of human beta2-glycoprotein I: Implications for phospholipid binding and the antiphospholipid syndrome
    • Schwarzenbacher R, Zeth K, Diederichs K, Gries A, Kostner GM, Laggner P, and Prassl R. Crystal structure of human beta2-glycoprotein I: implications for phospholipid binding and the antiphospholipid syndrome. EMBO J 18: 6228-6239, 1999.
    • (1999) EMBO J , vol.18 , pp. 6228-6239
    • Schwarzenbacher, R.1    Zeth, K.2    Diederichs, K.3    Gries, A.4    Kostner, G.M.5    Laggner, P.6    Prassl, R.7
  • 93
    • 34447286702 scopus 로고    scopus 로고
    • Transglutaminase 2 inhibitors and their therapeutic role in disease states
    • Siegel M and Khosla C. Transglutaminase 2 inhibitors and their therapeutic role in disease states. Pharmacol Ther 115: 232-245, 2007.
    • (2007) Pharmacol Ther , vol.115 , pp. 232-245
    • Siegel, M.1    Khosla, C.2
  • 94
    • 0033884053 scopus 로고    scopus 로고
    • Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B
    • DOI 10.1038/78005
    • Swaminathan S and Eswaramoorthy S. Structural analysis of the catalytic and binding sites of Clostridium botulinum neurotoxin B. Nat Struct Biol 7: 693-699, 2000. (Pubitemid 30636683)
    • (2000) Nature Structural Biology , vol.7 , Issue.8 , pp. 693-699
    • Swaminathan, S.1    Eswaramoorthy, S.2
  • 95
    • 41549150319 scopus 로고    scopus 로고
    • Interaction and functional association of protein dis-ulfide isomerase with alphaVbeta3 integrin on endothelial cells
    • Swiatkowska M, Szymanski J, Padula G, and Cierniewski CS. Interaction and functional association of protein dis-ulfide isomerase with alphaVbeta3 integrin on endothelial cells. FEBS J 275: 1813-1823, 2008.
    • (2008) FEBS J , vol.275 , pp. 1813-1823
    • Swiatkowska, M.1    Szymanski, J.2    Padula, G.3    Cierniewski, C.S.4
  • 96
    • 0242266981 scopus 로고    scopus 로고
    • Shear stress and von Willebrand factor in health and disease
    • Tsai HM. Shear stress and von Willebrand factor in health and disease. Semin Thromb Hemost 29: 479-488, 2003.
    • (2003) Semin Thromb Hemost , vol.29 , pp. 479-488
    • Tsai, H.M.1
  • 97
    • 34548494139 scopus 로고    scopus 로고
    • Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
    • Versteeg HH and Ruf W. Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity. J Biol Chem 282: 25416-25424, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 25416-25424
    • Versteeg, H.H.1    Ruf, W.2
  • 99
    • 78649480973 scopus 로고    scopus 로고
    • Disulfide bond acquisition through eukaryotic protein evolution
    • Jul 30 [Epub ahead of print]
    • Wong JWH, Ho SYW, and Hogg PJ. Disulfide bond acquisition through eukaryotic protein evolution. Mol Biol Evol 2010 Jul 30 [Epub ahead of print].
    • (2010) Mol Biol Evol
    • Jwh, W.1    Syw, H.2    Hogg, P.J.3
  • 100
    • 0346374729 scopus 로고    scopus 로고
    • Cross-strand dis-ulphides in cell entry proteins: Poised to act
    • Wouters MA, Lau KK, and Hogg PJ. Cross-strand dis-ulphides in cell entry proteins: poised to act. Bioessays 26: 73-79, 2004.
    • (2004) Bioessays , vol.26 , pp. 73-79
    • Wouters, M.A.1    Lau, K.K.2    Hogg, P.J.3
  • 101
    • 0035908117 scopus 로고    scopus 로고
    • Control of von Willebrand factor multimer size by thrombospondin-1
    • Xie L, 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.1    Chesterman, C.N.2    Hogg, P.J.3
  • 104
    • 34547117636 scopus 로고    scopus 로고
    • Willebrand factor type C domain-containing proteins regulate bone morphogenetic protein signaling through different recognition mechanisms
    • Zhang JL, Huang Y, Qiu LY, Nickel J, and Sebald W. von Willebrand factor type C domain-containing proteins regulate bone morphogenetic protein signaling through different recognition mechanisms. J Biol Chem 282: 20002-20014, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 20002-20014
    • Zhang, J.L.1    Huang, Y.2    Qiu, L.Y.3    Nickel, J.4    Von Sebald, W.5
  • 106
    • 67249086879 scopus 로고    scopus 로고
    • Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor
    • Zhang Q, Zhou YF, Zhang CZ, Zhang X, Lu C, and Springer TA. Structural specializations of A2, a force-sensing domain in the ultralarge vascular protein von Willebrand factor. Proc Natl Acad Sci USA 106: 9226-9231, 2009.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9226-9231
    • Zhang, Q.1    Zhou, Y.F.2    Zhang, C.Z.3    Zhang, X.4    Lu, C.5    Springer, T.A.6
  • 107
    • 66749099068 scopus 로고    scopus 로고
    • Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor
    • Zhang X, Halvorsen K, Zhang CZ, Wong WP, and Springer TA. Mechanoenzymatic cleavage of the ultralarge vascular protein von Willebrand factor. Science 324: 1330-1334, 2009.
    • (2009) Science , vol.324 , pp. 1330-1334
    • Zhang, X.1    Halvorsen, K.2    Zhang, C.Z.3    Wong, W.P.4    Springer, T.A.5
  • 108
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu J, Luo BH, Xiao T, Zhang C, Nishida N, and Springer TA. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell 32: 849-861, 2008.
    • (2008) Mol Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.