메뉴 건너뛰기




Volumn 84, Issue 1, 1996, Pages 33-43

Interaction between Yersinia pestis YopM protein and human α-thrombin

Author keywords

crosslinking; Yersinia pestis; YopM; thrombin

Indexed keywords

BACTERIAL PROTEIN; HIRUDIN; HIRUGEN; THROMBIN;

EID: 0030272453     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/0049-3848(96)00159-4     Document Type: Article
Times cited : (12)

References (28)
  • 2
    • 0000378277 scopus 로고
    • Platelets
    • J. I. Gallin, I. M. Goldstein and R. Snyderman (ed.), Raven Press, New York
    • 2. WEKSLER, B. B. Platelets. In: Inflammation: basic principles and clinical correlates. J. I. Gallin, I. M. Goldstein and R. Snyderman (ed.), pp. 543-557, Raven Press, New York, 1988.
    • (1988) Inflammation: Basic Principles and Clinical Correlates , pp. 543-557
    • Weksler, B.B.1
  • 3
    • 0025006850 scopus 로고
    • YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice
    • 3. LEUNG, K. Y., REISNER, B. S. and STRALEY, S. C. YopM inhibits platelet aggregation and is necessary for virulence of Yersinia pestis in mice. Infect. Immun. 58, 3262-3271, 1990.
    • (1990) Infect. Immun. , vol.58 , pp. 3262-3271
    • Leung, K.Y.1    Reisner, B.S.2    Straley, S.C.3
  • 4
    • 0026443901 scopus 로고
    • Yersinia pestis YopM: Thrombin binding and overexpression
    • 4. REISNER, B.S. and STRALEY, S.C. Yersinia pestis YopM: thrombin binding and overexpression. Infect. Immun. 60, 5242-5252, 1992.
    • (1992) Infect. Immun. , vol.60 , pp. 5242-5252
    • Reisner, B.S.1    Straley, S.C.2
  • 5
    • 0024364388 scopus 로고
    • The yopM gene of Yersinia pestis encodes a released protein having homology with the human platelet surface protein GPIbα
    • 5. LEUNG, K. Y. and STRALEY, S. C. The yopM gene of Yersinia pestis encodes a released protein having homology with the human platelet surface protein GPIbα. J. Bacteriol. 171, 4623-4632, 1989.
    • (1989) J. Bacteriol. , vol.171 , pp. 4623-4632
    • Leung, K.Y.1    Straley, S.C.2
  • 6
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • 6. KOBE, B. and DEISENHOFER, J. The leucine-rich repeat: a versatile binding motif. Trends in Biochem. Sci. 19, 415-421, 1994.
    • (1994) Trends in Biochem. Sci. , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 7
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • 7. KOBE, B. and DEISENHOFER, J. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature (London). 374, 183-186, 1995.
    • (1995) Nature (London) , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 9
    • 0024462894 scopus 로고
    • Thrombin interactions with hirudin
    • 9. FENTON, J. W. Thrombin interactions with hirudin. Sem. Throm. Hem. 15, 265-268, 1989.
    • (1989) Sem. Throm. Hem. , vol.15 , pp. 265-268
    • Fenton, J.W.1
  • 10
    • 0028912561 scopus 로고
    • The clot thickens: Clue provided by thrombin structure
    • 10. STUBBS, M. and BODE, W. The clot thickens: clue provided by thrombin structure. Trends in Biochem. Sci. 1, 23-28, 1995.
    • (1995) Trends in Biochem. Sci. , vol.1 , pp. 23-28
    • Stubbs, M.1    Bode, W.2
  • 11
    • 0027729854 scopus 로고
    • Spatial structure of thrombin as a guide to its multiple sites of interaction
    • 11. BODE, W. and STUBBS, M. T. Spatial structure of thrombin as a guide to its multiple sites of interaction. Sem. Throm. Hem. 19, 321-333, 1993.
    • (1993) Sem. Throm. Hem. , vol.19 , pp. 321-333
    • Bode, W.1    Stubbs, M.T.2
  • 12
    • 0027716416 scopus 로고
    • Electrostatic properties of thrombin: Importance for structural stabilization and ligand binding
    • 12. KARSHKOV, A. and BODE, W. Electrostatic properties of thrombin: Importance for structural stabilization and ligand binding. Sem. Throm. Hem. 19, 334-343, 1993.
    • (1993) Sem. Throm. Hem. , vol.19 , pp. 334-343
    • Karshkov, A.1    Bode, W.2
  • 13
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • 13. RYDEL, T.J. and TULINSKY, A. Refined structure of the hirudin-thrombin complex. J. Mol. Biol. 221, 583-601, 1991.
    • (1991) J. Mol. Biol. , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2
  • 14
    • 0023279803 scopus 로고
    • Identification of regions of α-thrombin involved in its interaction with hirudin
    • 14. STONE, S. R., BRAUN, P. J. and HOFSTEENGE, J. Identification of regions of α-thrombin involved in its interaction with hirudin. Biochemistry. 26, 4617-4624, 1987.
    • (1987) Biochemistry , vol.26 , pp. 4617-4624
    • Stone, S.R.1    Braun, P.J.2    Hofsteenge, J.3
  • 16
    • 0028209977 scopus 로고
    • Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes
    • 16. MATHEWS, I. I., PADMANABHAN, K. P., GANESH, V. and TULINSKY, A. Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes. Biochemistry. 33, 3266-3279, 1994.
    • (1994) Biochemistry , vol.33 , pp. 3266-3279
    • Mathews, I.I.1    Padmanabhan, K.P.2    Ganesh, V.3    Tulinsky, A.4
  • 17
    • 0024462894 scopus 로고
    • Thrombin interactions with hirudin
    • 17. FENTON, J. W. Thrombin interactions with hirudin. Sem. Throm. Hem. 15, 265-268, 1989.
    • (1989) Sem. Throm. Hem. , vol.15 , pp. 265-268
    • Fenton, J.W.1
  • 18
    • 0027467617 scopus 로고
    • Thrombin-binding DNA aptamer forms a unimolecular quadruplex structure in solution
    • 18. MACAYA, R. F., SCHULZE, P., SMITH, F. W., ROE, J. A. and FEIGON, J. Thrombin-binding DNA aptamer forms a unimolecular quadruplex structure in solution. Proc. Natl. Acad. Sci. USA, 90, 3745-3749, 1993
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3745-3749
    • Macaya, R.F.1    Schulze, P.2    Smith, F.W.3    Roe, J.A.4    Feigon, J.5
  • 19
    • 0026464915 scopus 로고
    • Localization of the single stranded DNA binding site in the thrombin anion-binding exosite
    • 19. WU, Q., TSIANG, M. and SADLER, J. E. Localization of the single stranded DNA binding site in the thrombin anion-binding exosite. J. Biol. Chem. 267, 24408-24412, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24408-24412
    • Wu, Q.1    Tsiang, M.2    Sadler, J.E.3
  • 20
    • 0026575221 scopus 로고
    • Selection of single-stranded DNA molecules that bind and inhibit human thrombin
    • 20. BOCK, L. C., GRIFFIN, L. C., LATHAM, J. A., VERMAAS, E. H. and TOOLE, J. J. Selection of single-stranded DNA molecules that bind and inhibit human thrombin. Nature (London). 355, 564-566, 1992.
    • (1992) Nature (London) , vol.355 , pp. 564-566
    • Bock, L.C.1    Griffin, L.C.2    Latham, J.A.3    Vermaas, E.H.4    Toole, J.J.5
  • 21
    • 0022629859 scopus 로고
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins
    • 2+ in Yersinia pestis include structural genes for outer membrane proteins. Infect. Immun. 51, 445-454, 1986.
    • (1986) Infect. Immun. , vol.51 , pp. 445-454
    • Straley, S.C.1    Bowmer, W.S.2
  • 22
    • 85012789457 scopus 로고
    • Plaque formation and isolation of pure lines with polimyelitis viruses
    • 22. DULBECCO, R. and VOGT, M. Plaque formation and isolation of pure lines with polimyelitis viruses. J. Exp. Med. 99, 167-182, 1954.
    • (1954) J. Exp. Med. , vol.99 , pp. 167-182
    • Dulbecco, R.1    Vogt, M.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 23. LAEMMLI, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London). 227, 680-685, 1970.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0025840282 scopus 로고
    • LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response
    • 24. PLANO, G. V., BARVE, S. S. and STRALEY, S. C. LcrD, a membrane-bound regulator of the Yersinia pestis low-calcium response. J. Bacteriol. 173, 7293-7303, 1991.
    • (1991) J. Bacteriol. , vol.173 , pp. 7293-7303
    • Plano, G.V.1    Barve, S.S.2    Straley, S.C.3
  • 25
    • 0027741220 scopus 로고
    • Crystallographic determination of thrombin complexes with small synthetic inhibitors as a starting point for the receptor-based design of antithrombotics
    • 25. BAUER, M., BRANDSTETTER, H., TURK, D., STURZEBECHER, J. and BODE, W. Crystallographic determination of thrombin complexes with small synthetic inhibitors as a starting point for the receptor-based design of antithrombotics. Sem. Throm. Hem. 19, 352-360, 1993.
    • (1993) Sem. Throm. Hem. , vol.19 , pp. 352-360
    • Bauer, M.1    Brandstetter, H.2    Turk, D.3    Sturzebecher, J.4    Bode, W.5
  • 27
    • 0028802323 scopus 로고
    • Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell
    • 27. PERSSON, C., NORDFELTH, R., HOLMSTRÖM, A., HÅKANSSON, S., ROSQVIST, R. and WOLF-WATZ, H. Cell-surface-bound Yersinia translocate the protein tyrosine phosphatase YopH by a polarized mechanism into the target cell. Mol. Microbiol. 18, 135-150, 1995.
    • (1995) Mol. Microbiol. , vol.18 , pp. 135-150
    • Persson, C.1    Nordfelth, R.2    Holmström, A.3    Håkansson, S.4    Rosqvist, R.5    Wolf-Watz, H.6
  • 28
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • 28. HÅKANSSON, S., GALYOV, E. E., ROSQVIST, R. and WOLF-WATZ, H. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20, 593-603, 1996.
    • (1996) Mol. Microbiol. , vol.20 , pp. 593-603
    • Håkansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.