메뉴 건너뛰기




Volumn 17, Issue 1-4, 2003, Pages 241-248

Disulfide exchange in CD4

Author keywords

[No Author keywords available]

Indexed keywords

CD4 ANTIGEN; DISULFIDE; THIOREDOXIN;

EID: 0142075880     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520170123     Document Type: Conference Paper
Times cited : (8)

References (33)
  • 1
    • 0028369997 scopus 로고
    • Enzymatic catalysis of disulfide formation
    • R. Noiva, Enzymatic catalysis of disulfide formation, Protein Expr. Purif. 5 (1994), 1-13.
    • (1994) Protein Expr. Purif. , vol.5 , pp. 1-13
    • Noiva, R.1
  • 2
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonucelase T1 with zero, one, and two intact disulfide-bonds
    • C.N. Pace, G.R. Grimsley, J.A. Thomson and B.J. Barnett, Conformational stability and activity of ribonucelase T1 with zero, one, and two intact disulfide-bonds, J. Biol. Chem. 263 (1988), 11820-11825.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thomson, J.A.3    Barnett, B.J.4
  • 3
    • 0001227472 scopus 로고
    • Harnessing disulfide-bonds using protein engineering
    • R. Wetzel, Harnessing disulfide-bonds using protein engineering, Trends Biochem. Sci. 12 (1987), 478-482.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 478-482
    • Wetzel, R.1
  • 5
    • 0023034995 scopus 로고
    • The crystallographically determined structures of atypical strained disulfides engineered into subtilisin
    • B.A. Katz and A. Kossiakoff, The crystallographically determined structures of atypical strained disulfides engineered into subtilisin, J. Biol. Chem. 261 (1986), 15480-15485.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15480-15485
    • Katz, B.A.1    Kossiakoff, A.2
  • 6
    • 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
    • P.E. Pjura, M. Matsumura, J.A. Wozniak and B.W. Matthews, 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 (1990), 2592-2598.
    • (1990) Biochemistry , vol.29 , pp. 2592-2598
    • Pjura, P.E.1    Matsumura, M.2    Wozniak, J.A.3    Matthews, B.W.4
  • 7
    • 0022998684 scopus 로고
    • In vivo formation and stability of engineered disulfide-bonds in subtilisin
    • J.A. Wells and D.B. Power, In vivo formation and stability of engineered disulfide-bonds in subtilisin, J. Biol. Chem. 261 (1986), 6564-6570.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6564-6570
    • Wells, J.A.1    Power, D.B.2
  • 8
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • J.M. Thornton, Disulphide bridges in globular proteins, J. Mol. Biol. 151 (1981), 261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 9
  • 10
    • 0035908117 scopus 로고    scopus 로고
    • Control of von Willebrand factor multimer size by thrombospondin-1
    • L. Xie, C.N. Chesterman and P.J. Hogg, Control of von Willebrand factor multimer size by thrombospondin-1, J. Exp. Med. 193 (2001), 1341-1349.
    • (2001) J. Exp. Med. , vol.193 , pp. 1341-1349
    • Xie, L.1    Chesterman, C.N.2    Hogg, P.J.3
  • 14
    • 0027219115 scopus 로고
    • Crystal structure of domains 3 and 4 of rat CD4: Relation to the NH2-terminal domains
    • R.L. Brady, E.J. Dodson, G. Lange, S.J. Davis, A.F. Williams and A.N. Barclay, Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains, Science 260 (1993), 979-983.
    • (1993) Science , vol.260 , pp. 979-983
    • Brady, R.L.1    Dodson, E.J.2    Lange, G.3    Davis, S.J.4    Williams, A.F.5    Barclay, A.N.6
  • 17
    • 0032784589 scopus 로고    scopus 로고
    • Direct evidence for native CD4 oligomers in lymphoid and monocytoid cells
    • G.W. Lynch, A.J. Sloane, V. Rasco, A. Lai and A.L. Cunningham, Direct evidence for native CD4 oligomers in lymphoid and monocytoid cells, Eur. J. Immunol. 29 (1999), 2590-2602.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2590-2602
    • Lynch, G.W.1    Sloane, A.J.2    Rasco, V.3    Lai, A.4    Cunningham, A.L.5
  • 18
    • 0028257964 scopus 로고
    • Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction
    • H.J.-P. Ryser, E.M. Levy, R. Mandel and G.J. DiSciullo, Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction, Proc. Natl. Acad. Sci. USA 91 (1994), 45459-4563.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 45459-54563
    • Ryser, H.J.-P.1    Levy, E.M.2    Mandel, R.3    DiSciullo, G.J.4
  • 19
    • 0022741831 scopus 로고
    • Junctional plasma membrane domains isolated from aggregating Dictyostelium discoideum amebae
    • H.M. Ingalls, C.M. Goodloe-Holland and E.J. Luna, Junctional plasma membrane domains isolated from aggregating Dictyostelium discoideum amebae, Proc. Natl. Acad. Sci. USA 83 (1986), 4779-4783.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4779-4783
    • Ingalls, H.M.1    Goodloe-Holland, C.M.2    Luna, E.J.3
  • 20
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • X.-M. Jiang, M. Fitzgerald, C.M. Grant and P.J. Hogg, Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase, J. Biol. Chem. 274 (1999), 2416-2423.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2416-2423
    • Jiang, X.-M.1    Fitzgerald, M.2    Grant, C.M.3    Hogg, P.J.4
  • 24
    • 0023835296 scopus 로고
    • Cyclic cystine peptides. Antiparallel β-sheet conformation for the 20-membered ring in Boc-Cys-Val-Aib-Ala-Leu-Cys-NHMe
    • I.L. Karle, R. Kishore, S. Raghothama and P. Balaram, Cyclic cystine peptides. Antiparallel β-sheet conformation for the 20-membered ring in Boc-Cys-Val-Aib-Ala-Leu-Cys-NHMe, J. Am. Chem. Soc. 110 (1988), 1958-1963.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1958-1963
    • Karle, I.L.1    Kishore, R.2    Raghothama, S.3    Balaram, P.4
  • 27
    • 0024347437 scopus 로고
    • The alpha-chain of murine CD8 lacks an invariant Ig-like disulfide-bond but contains a unique intrachain loop instead
    • L. Kirszbaum, J.A. Sharpe, N. Goss, J. Lahnstein and I.D. Walker, The alpha-chain of murine CD8 lacks an invariant Ig-like disulfide-bond but contains a unique intrachain loop instead, J. Immunol. 142 (1989), 3931-3936.
    • (1989) J. Immunol. , vol.142 , pp. 3931-3936
    • Kirszbaum, L.1    Sharpe, J.A.2    Goss, N.3    Lahnstein, J.4    Walker, I.D.5
  • 29
    • 0024461420 scopus 로고
    • ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin: Possible involvement of a dithiol-reduction in the IL-2 receptor induction
    • Y. Tagaya, Y. Maeda, A. Mitsui, N. Kondo, H. Matsui, J. Hamuro, N. Brown, K. Arai, T. Yokota, H. Wakasugi and J. Yodoi, ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin: possible involvement of a dithiol-reduction in the IL-2 receptor induction, EMBO J. 8 (1989), 757-764.
    • (1989) EMBO J. , vol.8 , pp. 757-764
    • Tagaya, Y.1    Maeda, Y.2    Mitsui, A.3    Kondo, N.4    Matsui, H.5    Hamuro, J.6    Brown, N.7    Arai, K.8    Yokota, T.9    Wakasugi, H.10    Yodoi, J.11
  • 30
    • 0026084915 scopus 로고
    • Identification of a thioredoxin-related protein associated with plasma membranes
    • H. Martin and M. Dean, Identification of a thioredoxin-related protein associated with plasma membranes, Biochem. Biophys. Res. Commun. 175 (1991), 123-128.
    • (1991) Biochem. Biophys. Res. Commun. , vol.175 , pp. 123-128
    • Martin, H.1    Dean, M.2
  • 31
    • 0026443077 scopus 로고
    • Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway
    • A. Rubartelli, A. Bajetto, G. Allavena, E. Wollman and R. Sitia, Secretion of thioredoxin by normal and neoplastic cells through a leaderless secretory pathway, J. Biol. Chem. 267 (1992), 24161-24164.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24161-24164
    • Rubartelli, A.1    Bajetto, A.2    Allavena, G.3    Wollman, E.4    Sitia, R.5
  • 32
    • 0031584072 scopus 로고    scopus 로고
    • Detection of membrane associated thioredoxin on human cell lines
    • E.E. Woolman, A. Kahan and D. Fradelizi, Detection of membrane associated thioredoxin on human cell lines, Biochem. Biophys. Res. Commun. 230 (1997), 602-606.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 602-606
    • Woolman, E.E.1    Kahan, A.2    Fradelizi, D.3
  • 33
    • 0242501629 scopus 로고    scopus 로고
    • Thioredoxin reductase, a redox-active selenoprotein, is secreted by normal and neoplastic cells: Presence in human plasma
    • A. Soderberg, B. Sahaf and A. Rosen, Thioredoxin reductase, a redox-active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma, Cancer Res. 60 (2000), 2281-2289.
    • (2000) Cancer Res. , vol.60 , pp. 2281-2289
    • Soderberg, A.1    Sahaf, B.2    Rosen, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.