메뉴 건너뛰기




Volumn 15, Issue 9, 1997, Pages 891-895

Site-specific dissection of substrate recognition by Thrombin

Author keywords

Drug design; Plasmin; Serine proteases; Trypsin

Indexed keywords

THROMBIN;

EID: 0030848495     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0997-891     Document Type: Article
Times cited : (65)

References (27)
  • 1
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J A. 1990. Additivity of mutational effects in proteins. Biochemistry 29:8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 2
    • 0029826905 scopus 로고    scopus 로고
    • Hormone mimicry
    • Wells, J.A. 1996. Hormone mimicry. Science 273:449-450.
    • (1996) Science , vol.273 , pp. 449-450
    • Wells, J.A.1
  • 3
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson, T. and Wells, J.A. 1995. A hot spot of binding energy in a hormone-receptor interface. Science 267:383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 5
    • 0029992658 scopus 로고    scopus 로고
    • Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor Vila
    • Dickinson, C.D., Kelly, C.R., and Ruf, W. 1996. Identification of surface residues mediating tissue factor binding and catalytic function of the serine protease factor Vila. Proc. Wail. Acad. Sci. USA 93:14379-14384.
    • (1996) Proc. Wail. Acad. Sci. USA , vol.93 , pp. 14379-14384
    • Dickinson, C.D.1    Kelly, C.R.2    Ruf, W.3
  • 6
    • 0024280501 scopus 로고
    • Dissecting the catalytic triad of a serine protease
    • Carter, P. and Wells, J.A. 1988. Dissecting the catalytic triad of a serine protease. Nature 332:564-568.
    • (1988) Nature , vol.332 , pp. 564-568
    • Carter, P.1    Wells, J.A.2
  • 7
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in serine proteinases
    • Perona, J.J. and Craik, C.S. 1995. Structural basis of substrate specificity in serine proteinases. Protein Sci. 4:337-360.
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 9
    • 0025004285 scopus 로고
    • Random peptide libraries: A source of specific protein binding molecules
    • Devlin, J.J., Panganiban, L.C., and Devlin, P.E. 1990. Random peptide libraries: a source of specific protein binding molecules. Science 249:404-406.
    • (1990) Science , vol.249 , pp. 404-406
    • Devlin, J.J.1    Panganiban, L.C.2    Devlin, P.E.3
  • 12
    • 0031052393 scopus 로고    scopus 로고
    • Rational engineering of activity and specificity in a serine protease
    • Dang, Q.D., Guinto, E.R., and Di Cera, E. 1997. Rational engineering of activity and specificity in a serine protease. Nature Biotechnology 15:146-149.
    • (1997) Nature Biotechnology , vol.15 , pp. 146-149
    • Dang, Q.D.1    Guinto, E.R.2    Di Cera, E.3
  • 13
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg-chloromethylketone-inhibited human a-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode, W., Turk, D., and Karshikov, A. 1992. The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg-chloromethylketone-inhibited human a-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci. 1:426-471.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 15
  • 16
    • 0029785840 scopus 로고    scopus 로고
    • +-induced allosteric regulation of catalytic activity in serine proteases
    • +-induced allosteric regulation of catalytic activity in serine proteases. Proc. Natl. Acad. Sci. USA 93:10653-10656.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10653-10656
    • Dang, Q.D.1    Di Cera, E.2
  • 17
    • 0024791521 scopus 로고
    • Crystal structure of bovine B-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density
    • Bartunik, H.D., Summers, L.J., and Bartsch, H.H. 1989. Crystal structure of bovine B-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. J. Mol. Biol. 210:813-828.
    • (1989) J. Mol. Biol , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3
  • 18
    • 0025060964 scopus 로고
    • The chemical synthesis of the chro-mogenic substrates, H-D-Val-Leu-Lys-p-nitroanilide (S2251) and H-D-lle-Pro-Arg-p-nltroanilide (S2288)
    • Sharma, S.K. and Castellino, F.J. 1990. The chemical synthesis of the chro-mogenic substrates, H-D-Val-Leu-Lys-p-nitroanilide (S2251) and H-D-lle-Pro-Arg-p-nltroanilide (S2288). Thromb. Res. 57:127-138.
    • (1990) Thromb. Res , vol.57 , pp. 127-138
    • Sharma, S.K.1    Castellino, F.J.2
  • 19
    • 0030933791 scopus 로고    scopus 로고
    • Critical role of W60d in thrombin allostery
    • Guinto, E.R. and Di Cera, E. 1997. Critical role of W60d in thrombin allostery. Biophys. Chem. 64:103-109.
    • (1997) Biophys. Chem , vol.64 , pp. 103-109
    • Guinto, E.R.1    Di Cera, E.2
  • 21
    • 0026606829 scopus 로고
    • Partial characterization of vertebrate prothrombin cDNAs: Amplification and sequence analysis of the B chain of thrombin from nine different species
    • Banfield, D.K. and MacGillivray, R.T.A. 1992. Partial characterization of vertebrate prothrombin cDNAs: amplification and sequence analysis of the B chain of thrombin from nine different species. Proc. Natl. Acad. Sci. USA 89:2779-2783.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2779-2783
    • Banfield, D.K.1    Macgillivray, R.T.A.2
  • 22
    • 0030895222 scopus 로고    scopus 로고
    • Design of highly potent noncovalent thrombin inhibitors that utilize a novel lipophilic binding pocket in the thrombin active site
    • Tucker, T.J., Lumma, W.C., Naylor-Olsen, A.M., Lewis, S.D., Lucas, R., Freidinger, R.M., et al. 1997. Design of highly potent noncovalent thrombin inhibitors that utilize a novel lipophilic binding pocket in the thrombin active site. J. Med. Chem. 40:830-832.
    • (1997) J. Med. Chem , vol.40 , pp. 830-832
    • Tucker, T.J.1    Lumma, W.C.2    Naylor-Olsen, A.M.3    Lewis, S.D.4    Lucas, R.5    Freidinger, R.M.6
  • 23
  • 24
    • 0028236301 scopus 로고
    • Synthetic peptides and peptidomimetics as substrates and inhibitors of thrombin and other proteases in the blood coagulation system
    • Claeson, G. 1994. Synthetic peptides and peptidomimetics as substrates and inhibitors of thrombin and other proteases in the blood coagulation system. Blood Coagul. Fibrin. 5:411-436.
    • (1994) Blood Coagul. Fibrin , vol.5 , pp. 411-436
    • Claeson, G.1
  • 25
    • 0029147003 scopus 로고
    • Core domain of hirudin from the leech Hirudinaria manillensis: Chemical synthesis, purification, and characterization of a Trp3 analog of fragment 1-47
    • De Filippis, V, Vindigni, A., Altichieri, L., and Fontana, A. 1995. Core domain of hirudin from the leech Hirudinaria manillensis: chemical synthesis, purification, and characterization of a Trp3 analog of fragment 1-47. Biochemistry 34:9552-9564.
    • (1995) Biochemistry , vol.34 , pp. 9552-9564
    • De Filippis, V.1    Vindigni, A.2    Altichieri, L.3    Fontana, A.4
  • 26
    • 0030948651 scopus 로고    scopus 로고
    • Energetics of thrombin-thrombomodulin interaction
    • Vindigni, A., White, C.E., Komives, E.A., and Di Cera, E. 1997. Energetics of thrombin-thrombomodulin interaction. Biochemistry 36:6674-6681.
    • (1997) Biochemistry , vol.36 , pp. 6674-6681
    • Vindigni, A.1    White, C.E.2    Komives, E.A.3    Di Cera, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.