메뉴 건너뛰기




Volumn 1752, Issue 2, 2005, Pages 202-204

Crystallization and preliminary X-ray crystallographic studies of Protac®, a commercial protein C activator isolated from Agkistrodon contortrix contortrix venom

Author keywords

Agkistrodon contortrix contortrix venom; Protein C activator; Serine proteinase; X ray diffraction analysis

Indexed keywords

ACTIVATED PROTEIN C; AMMONIUM SULFATE; ENZYME PRECURSOR; PROTAC; SERINE PROTEINASE; SNAKE VENOM; THROMBOMODULIN;

EID: 25144503261     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.08.003     Document Type: Article
Times cited : (2)

References (27)
  • 1
    • 0029381847 scopus 로고
    • Cellular regulation of the protein C pathway
    • C.T. Esmon, and K. Fukudome Cellular regulation of the protein C pathway Semin. Cell Biol. 6 1995 259 268
    • (1995) Semin. Cell Biol. , vol.6 , pp. 259-268
    • Esmon, C.T.1    Fukudome, K.2
  • 2
    • 0035869411 scopus 로고    scopus 로고
    • Endothelial cell protein C receptor plays an important role in protein C activation in vivo
    • F.B. Taylor, G.T. Peer, M.S. Lockhart, G. Ferrell, and C.T. Esmon Endothelial cell protein C receptor plays an important role in protein C activation in vivo Blood 97 2001 1685 1688
    • (2001) Blood , vol.97 , pp. 1685-1688
    • Taylor, F.B.1    Peer, G.T.2    Lockhart, M.S.3    Ferrell, G.4    Esmon, C.T.5
  • 3
    • 0018715761 scopus 로고
    • The inhibition of blood coagulation by activated Protein C through the selective inactivation of activated Factor V
    • F.J. Walker, P.W. Sexton, and C.T. Esmon The inhibition of blood coagulation by activated Protein C through the selective inactivation of activated Factor V Biochim. Biophys. Acta 571 1979 333 342
    • (1979) Biochim. Biophys. Acta , vol.571 , pp. 333-342
    • Walker, F.J.1    Sexton, P.W.2    Esmon, C.T.3
  • 4
    • 0021344553 scopus 로고
    • Proteolytic inactivation of human factor VIII procoagulant protein by activated human protein C and its analogy with factor V
    • C.A. Fulcher, J.E. Gardiner, J.H. Griffin, and T.S. Zimmerman Proteolytic inactivation of human factor VIII procoagulant protein by activated human protein C and its analogy with factor V Blood 63 1984 486 489
    • (1984) Blood , vol.63 , pp. 486-489
    • Fulcher, C.A.1    Gardiner, J.E.2    Griffin, J.H.3    Zimmerman, T.S.4
  • 6
    • 0035992710 scopus 로고    scopus 로고
    • Activated protein C: Potential therapy for severe sepsis, thrombosis, and stroke
    • J.H. Griffin, B. Zlokovic, and J.A. Fernandez Activated protein C: potential therapy for severe sepsis, thrombosis, and stroke Semin. Hematol. 39 2002 197 205
    • (2002) Semin. Hematol. , vol.39 , pp. 197-205
    • Griffin, J.H.1    Zlokovic, B.2    Fernandez, J.A.3
  • 8
    • 0009562026 scopus 로고    scopus 로고
    • Proteinases activating protein C
    • G.S. Bailey Fort Collins Alaken
    • J. Meier Proteinases activating protein C G.S. Bailey The Enzymology of Snake Venoms 1998 Fort Collins Alaken 253 285
    • (1998) The Enzymology of Snake Venoms , pp. 253-285
    • Meier, J.1
  • 10
    • 0027208127 scopus 로고
    • Protein C activator from the venom of Agkistrodon blomhoffi ussuriensis retards thrombus formation in the arterio-venous shunt in rats
    • A.E. Kogan, G.V. Bashkov, I.D. Bobruskin, E.P. Romanova, V.A. Makarov, and S.M. Strukova Protein C activator from the venom of Agkistrodon blomhoffi ussuriensis retards thrombus formation in the arterio-venous shunt in rats Thromb. Res. 70 1993 385 393
    • (1993) Thromb. Res. , vol.70 , pp. 385-393
    • Kogan, A.E.1    Bashkov, G.V.2    Bobruskin, I.D.3    Romanova, E.P.4    Makarov, V.A.5    Strukova, S.M.6
  • 11
    • 0025860283 scopus 로고
    • Comparative study of protein C activators from the Agkistrodon snake venoms
    • A.E. Kogan, A.N. Makarov, I.D. Bobruskin, and S.M. Strukova Comparative study of protein C activators from the Agkistrodon snake venoms Thromb. Res. 62 1991 775 780
    • (1991) Thromb. Res. , vol.62 , pp. 775-780
    • Kogan, A.E.1    Makarov, A.N.2    Bobruskin, I.D.3    Strukova, S.M.4
  • 12
    • 0009562306 scopus 로고    scopus 로고
    • Identification of protein C activator from nine species of Chinese snake venoms
    • L. Sun, J. Guang, S. Huang, and Q. Yu Identification of protein C activator from nine species of Chinese snake venoms Zhongguo Bingli Shengli Zazhi 17 2001 241 244
    • (2001) Zhongguo Bingli Shengli Zazhi , vol.17 , pp. 241-244
    • Sun, L.1    Guang, J.2    Huang, S.3    Yu, Q.4
  • 14
    • 0023946074 scopus 로고
    • The simultaneous measurement of total and free protein S by ELISA
    • B.J. Woodhams The simultaneous measurement of total and free protein S by ELISA Thromb. Res. 50 1988 213 220
    • (1988) Thromb. Res. , vol.50 , pp. 213-220
    • Woodhams, B.J.1
  • 15
    • 0025346255 scopus 로고
    • Laboratory diagnosis of inherited protein S deficiency
    • J.R. Edson, J.M. Vogt, and D.A. Huesman Laboratory diagnosis of inherited protein S deficiency Am. J. Clin. Pathol. 94 1990 176 186
    • (1990) Am. J. Clin. Pathol. , vol.94 , pp. 176-186
    • Edson, J.R.1    Vogt, J.M.2    Huesman, D.A.3
  • 16
    • 0023830885 scopus 로고
    • Plasma protein S activity measured using Protac®, a snake venom derived activator of protein C
    • K. Suzuki, and J. Nishioka Plasma protein S activity measured using Protac®, a snake venom derived activator of protein C Thromb. Res. 49 1988 241 251
    • (1988) Thromb. Res. , vol.49 , pp. 241-251
    • Suzuki, K.1    Nishioka, J.2
  • 18
    • 0024328912 scopus 로고
    • Functional activity of protein S determined with use of protein C activated by venom activator
    • I. Kobayashi, N. Amemiya, T. Endo, K. Okuyama, K. Tamura, and S. Kume Functional activity of protein S determined with use of protein C activated by venom activator Clin. Chem. 35 1989 1644 1648
    • (1989) Clin. Chem. , vol.35 , pp. 1644-1648
    • Kobayashi, I.1    Amemiya, N.2    Endo, T.3    Okuyama, K.4    Tamura, K.5    Kume, S.6
  • 19
    • 0022506820 scopus 로고
    • Fast functional protein C assay using Protac®, a novel protein C activator
    • J.L. Martinoli, and K. Stocker Fast functional protein C assay using Protac®, a novel protein C activator Thromb. Res. 43 1986 253 264
    • (1986) Thromb. Res. , vol.43 , pp. 253-264
    • Martinoli, J.L.1    Stocker, K.2
  • 20
    • 0023115106 scopus 로고
    • Characterization of the protein C activator Protac® from the venom of the southern copperhead (Agkistrodon contortrix) snake
    • K. Stocker, H. Fischer, J. Meier, M. Brogli, and L. Svendsen Characterization of the protein C activator Protac® from the venom of the southern copperhead (Agkistrodon contortrix) snake Toxicon 25 1987 239 252
    • (1987) Toxicon , vol.25 , pp. 239-252
    • Stocker, K.1    Fischer, H.2    Meier, J.3    Brogli, M.4    Svendsen, L.5
  • 21
    • 0024256689 scopus 로고
    • Practical application of the protein C activator Protac® from Agkistrodon contortrix venom
    • K. Stocker, H. Fischer, and J. Meier Practical application of the protein C activator Protac® from Agkistrodon contortrix venom Folia Haematol. 115 1988 260 264
    • (1988) Folia Haematol. , vol.115 , pp. 260-264
    • Stocker, K.1    Fischer, H.2    Meier, J.3
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 23
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 24
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • J. Navaza AmoRe: an automated package for molecular replacement Acta Crystallogr. A50 1994 157 163
    • (1994) Acta Crystallogr. , vol.50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 0032530323 scopus 로고    scopus 로고
    • The crystal structure of the novel snake venom plasminogen activator TSV-PA: A prototype structure for snake venom serine proteinases
    • M.A Parry, U. Jacob, R. Huber, A. Wisner, C. Bon, and W. Bode The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases Structure 6 1998 195 206
    • (1998) Structure , vol.6 , pp. 195-206
    • Parry, M.A.1    Jacob, U.2    Huber, R.3    Wisner, A.4    Bon, C.5    Bode, W.6
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structure by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structure by the maximum-likelihood method Acta Crystallogr. D53 1997 240 255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 27
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
    • T.A. Jones Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO Methods Enzymol. 115 1985 157 171
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.