메뉴 건너뛰기




Volumn 405, Issue 3, 2007, Pages 489-494

Molecular characterization of centerin, a germinal centre cell serpin

Author keywords

Centerin; Germinal centre B cell expressed transcript 1 (GCET1); Lymphoma; Protease; Serine protease inhibitor (serpin); Trypsin

Indexed keywords

CENTERIN; GERMINAL CENTRE B-CELL-EXPRESSED TRANSCRIPT 1 (GCET1); LYMPHOMA; PROTEASE; SERINE PROTEASE INHIBITOR (SERPIN); TRYPSIN;

EID: 34547492843     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070174     Document Type: Article
Times cited : (13)

References (17)
  • 2
    • 0037631625 scopus 로고    scopus 로고
    • Two newly characterised germinal centre B-cell-associated genes, GCET1 and GCET2, have differential expression in normal and neoplastic B cells
    • Pan, Z., Shen, Y., Du, C., Zhou, G., Rosenwald, A., Staudt, L., Greiner, T., McKeithan, T. and Chan, W. (2003) Two newly characterised germinal centre B-cell-associated genes, GCET1 and GCET2, have differential expression in normal and neoplastic B cells. Am. J. Pathol. 163, 135-144
    • (2003) Am. J. Pathol , vol.163 , pp. 135-144
    • Pan, Z.1    Shen, Y.2    Du, C.3    Zhou, G.4    Rosenwald, A.5    Staudt, L.6    Greiner, T.7    McKeithan, T.8    Chan, W.9
  • 3
    • 0037142053 scopus 로고    scopus 로고
    • The use of molecular profiling to predict survival after chemotherapy for diffuse large-B-cell lymphoma
    • Rosenwald, A., Wright, G., Chan, W., Connors, J., Campo, E. and Fisher, R. (2002) The use of molecular profiling to predict survival after chemotherapy for diffuse large-B-cell lymphoma. N. Eng. J. Med. 346, 1937-1947
    • (2002) N. Eng. J. Med , vol.346 , pp. 1937-1947
    • Rosenwald, A.1    Wright, G.2    Chan, W.3    Connors, J.4    Campo, E.5    Fisher, R.6
  • 4
    • 0037343426 scopus 로고    scopus 로고
    • A review and comparison of the murine alpha(1)-antitrypsin and alpha(1)-antichymotrypsin multigene clusters with the human clade A serpins
    • Forsyth, S., Horvath, A. and Coughlin, P. (2003) A review and comparison of the murine alpha(1)-antitrypsin and alpha(1)-antichymotrypsin multigene clusters with the human clade A serpins. Genomics 81, 336-345
    • (2003) Genomics , vol.81 , pp. 336-345
    • Forsyth, S.1    Horvath, A.2    Coughlin, P.3
  • 6
    • 0037066736 scopus 로고    scopus 로고
    • Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation
    • Irving, J. A., Shushanov, S. S., Pike, R. N., Popova, E. Y., Bromme, D., Coetzer, T. H., Bottomley, S. P., Boulynko, I. A., Grigoryev, S. A. and Whisstock, J. C. (2002) Inhibitory activity of a heterochromatin-associated serpin (MENT) against papain-like cysteine proteinases affects chromatin structure and blocks cell proliferation. J. Biol. Chem. 277, 13192-13201
    • (2002) J. Biol. Chem , vol.277 , pp. 13192-13201
    • Irving, J.A.1    Shushanov, S.S.2    Pike, R.N.3    Popova, E.Y.4    Bromme, D.5    Coetzer, T.H.6    Bottomley, S.P.7    Boulynko, I.A.8    Grigoryev, S.A.9    Whisstock, J.C.10
  • 7
    • 0027498670 scopus 로고
    • Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin
    • Bjork, I., Olson, S. T. and Shore, J. D. (1993) Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Methods Enzymol. 222, 525-559
    • (1993) Methods Enzymol , vol.222 , pp. 525-559
    • Bjork, I.1    Olson, S.T.2    Shore, J.D.3
  • 8
    • 0034602778 scopus 로고    scopus 로고
    • Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational disease
    • Gooptu, B., Hazes, B., Chang, W. S., Dafforn, T. R., Carrell, R. W., Read, R. J. and Lomas, D. A. (2000) Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease. Proc. Natl. Acad. Sci. U.S.A. 97, 67-72
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 67-72
    • Gooptu, B.1    Hazes, B.2    Chang, W.S.3    Dafforn, T.R.4    Carrell, R.W.5    Read, R.J.6    Lomas, D.A.7
  • 9
    • 0034695402 scopus 로고    scopus 로고
    • Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin
    • Whisstock, J. C., Skinner, R., Carrell, R. W. and Lesk, A. M. (2000) Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin. J. Mol. Biol. 295, 651-665
    • (2000) J. Mol. Biol , vol.295 , pp. 651-665
    • Whisstock, J.C.1    Skinner, R.2    Carrell, R.W.3    Lesk, A.M.4
  • 10
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding supertamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman, G. A., Bird, P. I., Carrell, R. W., Church, F. C., Coughlin, P. B., Gettins, P. G., Irving, J. A., Lomas, D. A., Luke, C. J., Moyer, R. W. et al. (2001) The serpins are an expanding supertamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J. Biol. Chem. 276, 33293-33296
    • (2001) J. Biol. Chem , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.6    Irving, J.A.7    Lomas, D.A.8    Luke, C.J.9    Moyer, R.W.10
  • 11
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. G. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804
    • (2002) Chem. Rev , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 12
    • 0345829928 scopus 로고    scopus 로고
    • Acyl-enzyme complexes between tissue-type plasminogen activator and neuroserpin are short-lived in vitro
    • Barker-Carlson, K., Lawrence, D. A. and Schwartz, B. S. (2002) Acyl-enzyme complexes between tissue-type plasminogen activator and neuroserpin are short-lived in vitro. J. Biol. Chem. 277, 46852-46857
    • (2002) J. Biol. Chem , vol.277 , pp. 46852-46857
    • Barker-Carlson, K.1    Lawrence, D.A.2    Schwartz, B.S.3
  • 13
    • 0024308381 scopus 로고
    • The use of α2-antiplasmin as a model for the demonstration of complex reversibility in serpins
    • Shieh, B. H., Potempa, J. and Travis, J. (1989) The use of α2-antiplasmin as a model for the demonstration of complex reversibility in serpins. J. Biol. Chem. 264, 13420-13423
    • (1989) J. Biol. Chem , vol.264 , pp. 13420-13423
    • Shieh, B.H.1    Potempa, J.2    Travis, J.3
  • 14
    • 13244270050 scopus 로고    scopus 로고
    • Crystal structure of thrombin bound to heparin
    • Carter, W. J., Cama, E. and Huntington, J. A. (2005) Crystal structure of thrombin bound to heparin. J. Biol. Chem. 280, 2745-2749
    • (2005) J. Biol. Chem , vol.280 , pp. 2745-2749
    • Carter, W.J.1    Cama, E.2    Huntington, J.A.3
  • 15
    • 0033605391 scopus 로고    scopus 로고
    • MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member
    • Grigoryev, S. A., Bednar, J. and Woodcock, C. L. (1999) MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. J. Biol. Chem. 274, 5626-5636
    • (1999) J. Biol. Chem , vol.274 , pp. 5626-5636
    • Grigoryev, S.A.1    Bednar, J.2    Woodcock, C.L.3
  • 16
    • 0031859661 scopus 로고    scopus 로고
    • Germinal centres: Form and function
    • Tarlinton, D. (1998) Germinal centres: form and function. Curr. Opin. Immunol. 10, 245-251
    • (1998) Curr. Opin. Immunol , vol.10 , pp. 245-251
    • Tarlinton, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.