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Volumn 45, Issue 24, 2006, Pages 7429-7433

Allosteric disulfide bonds

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; CONFORMATIONS; PROTEINS; X RAY ANALYSIS;

EID: 33745161382     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0603064     Document Type: Article
Times cited : (277)

References (28)
  • 1
    • 0037397499 scopus 로고    scopus 로고
    • Disulfide bonds as switches for protein function
    • Hogg, P. J. (2003) Disulfide bonds as switches for protein function, Trends Biochem. Sci. 28, 210-214.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 210-214
    • Hogg, P.J.1
  • 2
    • 0346374729 scopus 로고    scopus 로고
    • Cross-strand disulphides in cell entry proteins: Poised to act
    • Wouters, M. A., Lau, K. K., and Hogg, P. J. (2004) Cross-strand disulphides in cell entry proteins: Poised to act, Bioessays 26, 73-79.
    • (2004) Bioessays , vol.26 , pp. 73-79
    • Wouters, M.A.1    Lau, K.K.2    Hogg, P.J.3
  • 3
    • 17644395645 scopus 로고    scopus 로고
    • Thioredoxin and its related molecules: Update 2005
    • Nakamura, H. (2005) Thioredoxin and its related molecules: Update 2005, Antioxid. Redox Signal. 7, 823-828.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 823-828
    • Nakamura, H.1
  • 5
    • 0023034995 scopus 로고
    • The crystallographically determined structures of atypical strained disulfides engineered into subtilisin
    • Katz, B. A., and Kossiakoff, A. (1986) The crystallographically determined structures of atypical strained disulfides engineered into subtilisin, J. Biol. Chem. 261, 15480-15485.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15480-15485
    • Katz, B.A.1    Kossiakoff, A.2
  • 6
    • 0022998684 scopus 로고
    • In vivo formation and stability of engineered disulfide bonds in subtilisin
    • Wells, J. A., and Powers, D. B. (1986) In vivo formation and stability of engineered disulfide bonds in subtilisin, J. Biol. Chem. 261, 6564-6570.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6564-6570
    • Wells, J.A.1    Powers, D.B.2
  • 7
    • 0025182227 scopus 로고
    • Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond
    • Kuwajima, K., Ikeguchi, M., Sugawara, T., Hiraoka, Y., and Sugai, S. (1990) Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6-Cys120 disulfide bond, Biochemistry 29, 8240-8249.
    • (1990) Biochemistry , vol.29 , pp. 8240-8249
    • Kuwajima, K.1    Ikeguchi, M.2    Sugawara, T.3    Hiraoka, Y.4    Sugai, S.5
  • 9
    • 0025319751 scopus 로고
    • Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein
    • Pjura, P. E., Matsumura, M., Wozniak, J. A., and Matthews, B. W. (1990) Structure of a thermostable disulfide-bridge mutant of phage T4 lysozyme shows that an engineered cross-link in a flexible region does not increase the rigidity of the folded protein, Biochemistry 29, 2592-2598.
    • (1990) Biochemistry , vol.29 , pp. 2592-2598
    • Pjura, P.E.1    Matsumura, M.2    Wozniak, J.A.3    Matthews, B.W.4
  • 11
    • 0030573025 scopus 로고    scopus 로고
    • The disulphide β-cross: From cystine geometry and clustering to classification of small disulphide-rich protein folds
    • Harrison, P. M., and Sternberg, M. J. (1996) The disulphide β-cross: From cystine geometry and clustering to classification of small disulphide-rich protein folds, J. Mol. Biol. 264, 603-623.
    • (1996) J. Mol. Biol. , vol.264 , pp. 603-623
    • Harrison, P.M.1    Sternberg, M.J.2
  • 12
    • 0037112164 scopus 로고    scopus 로고
    • Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation
    • Sauer, F. G., Pinkner, J. S., Waksman, G., and Hultgren, S. J. (2002) Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation, Cell 111, 543-551.
    • (2002) Cell , vol.111 , pp. 543-551
    • Sauer, F.G.1    Pinkner, J.S.2    Waksman, G.3    Hultgren, S.J.4
  • 13
    • 0037119945 scopus 로고    scopus 로고
    • The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDα complex
    • Haebel, P. W., Goldstone, D., Katzen, F., Beckwith, J., and Metcalf, P. (2002) The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDα complex. EMBO J. 21, 4774-4784.
    • (2002) EMBO J. , vol.21 , pp. 4774-4784
    • Haebel, P.W.1    Goldstone, D.2    Katzen, F.3    Beckwith, J.4    Metcalf, P.5
  • 14
    • 0029058159 scopus 로고
    • An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters, M. A., and Curmi, P. M. (1995) An analysis of side chain interactions and pair correlations within antiparallel β-sheets: The differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs, Proteins 22, 119-131.
    • (1995) Proteins , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.2
  • 17
    • 33745178673 scopus 로고    scopus 로고
    • Evidence for a domain-swapped CD4 dimer as the co-receptor for binding to class II major histocompatibility complex
    • in press
    • Maekawa, A., Schmidt, B., Fazekas de St. Groth, B., Sanejouand, Y.-H., and Hogg, P. J. (2006) Evidence for a domain-swapped CD4 dimer as the co-receptor for binding to class II major histocompatibility complex, J. Immunol., in press.
    • (2006) J. Immunol.
    • Maekawa, A.1    Schmidt, B.2    Fazekas De St. Groth, B.3    Sanejouand, Y.-H.4    Hogg, P.J.5
  • 18
    • 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, T. M., Mandel, R., Trahey, M., Broder, C. C., Viglianti, G. A., and Ryser, H. J. (2002) 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) 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
  • 19
    • 0037474328 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion
    • Barbouche, R., Miquelis, R., Jones, I. M., and Fenouillet, E. (2003) Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion, J. Biol. Chem. 278, 3131-3136.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3131-3136
    • Barbouche, R.1    Miquelis, R.2    Jones, I.M.3    Fenouillet, E.4
  • 21
    • 0031015826 scopus 로고    scopus 로고
    • Functional consequences of disulfide bond formation in gelsolin
    • Allen, P. G. (1997) Functional consequences of disulfide bond formation in gelsolin, FEBS Lett. 401, 89-94.
    • (1997) FEBS Lett. , vol.401 , pp. 89-94
    • Allen, P.G.1
  • 24
    • 33644557719 scopus 로고    scopus 로고
    • Emerging insights in tissue factor-dependent signaling events
    • Versteeg, H. H., and Ruf, W. (2006) Emerging insights in tissue factor-dependent signaling events. Semin. Thromb. Hemostasis 32, 24-32.
    • (2006) Semin. Thromb. Hemostasis , vol.32 , pp. 24-32
    • Versteeg, H.H.1    Ruf, W.2
  • 25
    • 0026650453 scopus 로고
    • Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces
    • Le, D. T., Rapaport, S. I., and Rao, L. V. (1992) Relations between factor VIIa binding and expression of factor VIIa/tissue factor catalytic activity on cell surfaces, J. Biol. Chem. 267, 15447-15454.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15447-15454
    • Le, D.T.1    Rapaport, S.I.2    Rao, L.V.3
  • 26
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. (1989) Thioredoxin and glutaredoxin systems, J. Biol. Chem. 264, 13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 27
    • 0031442195 scopus 로고    scopus 로고
    • General acid/base catalysis in the active site of Escherichia coli thioredoxin
    • Chivers, P. T., and Raines, R. T. (1997) General acid/base catalysis in the active site of Escherichia coli thioredoxin, Biochemistry 36, 15810-15816.
    • (1997) Biochemistry , vol.36 , pp. 15810-15816
    • Chivers, P.T.1    Raines, R.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.