메뉴 건너뛰기




Volumn 341, Issue 3, 2004, Pages 829-837

Crystal structure of schistatin, a disintegrin homodimer from saw-scaled viper (Echis carinatus) at 2.5 Å resolution

Author keywords

Arg Gly Asp loop; crystal structure; disintegrin; homodimer; schistatin

Indexed keywords

DISINTEGRIN; PROTEIN SUBUNIT; SCHISTATIN; UNCLASSIFIED DRUG; VIPER VENOM;

EID: 4344607978     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.06.048     Document Type: Article
Times cited : (43)

References (61)
  • 2
    • 0024206252 scopus 로고
    • Echistatin: A potent platelet aggregation inhibitor from the venom of the viper Echis carinatus
    • Z.R. Gan, R.J. Gould, J.W. Jacobs, P.A. Freidman, and M.A. Polokof Echistatin: a potent platelet aggregation inhibitor from the venom of the viper Echis carinatus J. Biol. Chem. 263 1988 19827 19832
    • (1988) J. Biol. Chem. , vol.263 , pp. 19827-19832
    • Gan, Z.R.1    Gould, R.J.2    Jacobs, J.W.3    Freidman4    Polokof, M.A.P.A.5
  • 3
    • 0027254333 scopus 로고
    • Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom
    • L.C. Au, J.S. Chou, K.J. Chang, G.W. Teh, and S.B. Lin Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom Biochim. Biophys. Acta 1173 1993 243 245
    • (1993) Biochim. Biophys. Acta , vol.1173 , pp. 243-245
    • Au, L.C.1    Chou, J.S.2    Chang, K.J.3    Teh4    Lin, S.B.G.W.5
  • 4
    • 0035999118 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of cDNA encoding flavoridin, a disintegrin from the venom of Trimeresurus flavoviridis
    • M. Kishimoto, and T. Takahashi Molecular cloning and sequence analysis of cDNA encoding flavoridin, a disintegrin from the venom of Trimeresurus flavoviridis Toxicon 40 2002 1033 1040
    • (2002) Toxicon , vol.40 , pp. 1033-1040
    • Kishimoto1    Takahashi, T.M.2
  • 5
    • 0023639428 scopus 로고
    • Trigramin: A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed glycoprotein IIb-IIIa complex
    • T.F. Huanf, J.C. Holt, H. Lukasiewicz, and S. Niewiarowski Trigramin: a low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed glycoprotein IIb-IIIa complex J. Biol. Chem. 262 1987 16157 16163
    • (1987) J. Biol. Chem. , vol.262 , pp. 16157-16163
    • Huanf, T.F.1    Holt, J.C.2    Lukasiewicz3    Niewiarowski, S.H.4
  • 6
    • 0026099011 scopus 로고
    • Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex
    • T.F. Huang, J.R. Sheu, C.M. Teng, S.W. Chen, and C.S. Liu Triflavin, an antiplatelet Arg-Gly-Asp-containing peptide, is a specific antagonist of platelet membrane glycoprotein IIb-IIIa complex J. Biochem. 109 1991 328 334
    • (1991) J. Biochem. , vol.109 , pp. 328-334
    • Huang, T.F.1    Sheu, J.R.2    Teng, C.M.3    Chen4    Liu, C.S.S.W.5
  • 7
    • 0025267306 scopus 로고
    • Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: Evidence for a family of platelet-aggregation inhibitors
    • M.S. Dennis, W.J. Henzel, R.M. Pitti, M.T. Lipari, M.A., Napier, and T.A. Deisher Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: evidence for a family of platelet-aggregation inhibitors Proc. Natl Acad. Sci. USA 87 1990 2471 2475
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 2471-2475
    • Dennis, M.S.1    Henzel, W.J.2    Pitti, R.M.3    Lipari, M.T.4    Napier5    Deisher, T.A.M.A.6
  • 8
    • 0025887032 scopus 로고
    • Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri
    • R.M. Scarborough, J.W. Rose, M.A. Hsu, D.R. Phillips, V.A. Fried, and A.M. Campbell Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri J. Biol. Chem. 266 1991 9359 9362
    • (1991) J. Biol. Chem. , vol.266 , pp. 9359-9362
    • Scarborough, R.M.1    Rose, J.W.2    Hsu, M.A.3    Phillips, D.R.4    Fried5    Campbell, A.M.V.A.6
  • 9
    • 0030995291 scopus 로고    scopus 로고
    • Isolation and amino acid sequence of flavostatin, a novel disintegrin from the venom of Trimeresurus flavoviridis
    • K. Maruyama, T. Kawasaki, Y. Sakai, Y. Taniuchi, M. Shimizu, H. Kawashima, and T. Takenaka Isolation and amino acid sequence of flavostatin, a novel disintegrin from the venom of Trimeresurus flavoviridis Peptides 18 1997 73 78
    • (1997) Peptides , vol.18 , pp. 73-78
    • Maruyama, K.1    Kawasaki, T.2    Sakai, Y.3    Taniuchi, Y.4    Shimizu, M.5    Kawashima6    Takenaka, T.H.7
  • 10
    • 0025880046 scopus 로고
    • Halysin, an antiplatelet Arg-Gly-Asp-containing snake venom peptide, as fibrinogen receptor antagonist
    • T.F. Huang, C.Z. Liu, C.H. Ouyang, and C.M. Teng Halysin, an antiplatelet Arg-Gly-Asp-containing snake venom peptide, as fibrinogen receptor antagonist Biochem. Pharmacol. 42 1991 1209 1219
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 1209-1219
    • Huang, T.F.1    Liu, C.Z.2    Ouyang3    Teng, C.M.C.H.4
  • 11
    • 0025333470 scopus 로고
    • Elegantin and albolabrin purified peptides from viper venoms: Homologies with the RGDS domain of fibrinogen and von Willebrand factor
    • J. Williams, B. Rucinski, J. Holt, and S. Niewiarowski Elegantin and albolabrin purified peptides from viper venoms: homologies with the RGDS domain of fibrinogen and von Willebrand factor Biochim. Biophys. Acta 1039 1990 81 89
    • (1990) Biochim. Biophys. Acta , vol.1039 , pp. 81-89
    • Williams, J.1    Rucinski, B.2    Holt3    Niewiarowski, S.J.4
  • 13
    • 0033617466 scopus 로고    scopus 로고
    • EC3 a novel MLD dependant disintegrin from Echis carinatus, is a potent antagonist for α4 integrins
    • C. Marcinkiewicz, J.J. Calvete, M.M. Marcinkiewicz, M. Raida, S. Vijay-Kumar, and Z. Huang EC3 a novel MLD dependant disintegrin from Echis carinatus, is a potent antagonist for α4 integrins J. Biol. Chem. 274 1999 12468 12473
    • (1999) J. Biol. Chem. , vol.274 , pp. 12468-12473
    • Marcinkiewicz, C.1    Calvete, J.J.2    Marcinkiewicz, M.M.3    Raida, M.4    Vijay-Kumar5    Huang, Z.S.6
  • 14
    • 0034644725 scopus 로고    scopus 로고
    • Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin alpha 9beta 1 with VCAM-1, tenascin-C and osteopontin
    • C. Marcinkiewicz, Y. Taooka, Y. Yokosaki, J.J. Calvete, M.M. Marcinkiewicz, and R.R. Lobb Inhibitory effects of MLDG-containing heterodimeric disintegrins reveal distinct structural requirements for interaction of the integrin alpha 9beta 1 with VCAM-1, tenascin-C and osteopontin J. Biol. Chem. 275 2000 31930 31937
    • (2000) J. Biol. Chem. , vol.275 , pp. 31930-31937
    • Marcinkiewicz, C.1    Taooka, Y.2    Yokosaki, Y.3    Calvete, J.J.4    Marcinkiewicz5    Lobb, R.R.M.M.6
  • 15
    • 0032884927 scopus 로고    scopus 로고
    • Structural and functional characterization of EMF10, a heterodimeric disintegrin from Eristocophis macmahoni venom that selectively inhibits alpha5 beta1 integrin
    • C. Marcinkiewicz, J.J. Calvete, S. Vijay-Kumar, M.M. Marcinkiewicz, M. Raida, and P. Schick Structural and functional characterization of EMF10, a heterodimeric disintegrin from Eristocophis macmahoni venom that selectively inhibits alpha5 beta1 integrin Biochemistry 38 1999 13302 13309
    • (1999) Biochemistry , vol.38 , pp. 13302-13309
    • Marcinkiewicz, C.1    Calvete, J.J.2    Vijay-Kumar, S.3    Marcinkiewicz, M.M.4    Raida5    Schick, P.M.6
  • 16
    • 0034854834 scopus 로고    scopus 로고
    • Purification and characterization of a new RGD/KGD-containing dimeric disintegrin, piscivostatin, from the venom of Agkistrodon piscivorus piscivorus: The unique effect of piscivostatin on platelet aggregation
    • D. Okuda, and T. Morita Purification and characterization of a new RGD/KGD-containing dimeric disintegrin, piscivostatin, from the venom of Agkistrodon piscivorus piscivorus: the unique effect of piscivostatin on platelet aggregation J. Biochem. 130 2001 407 415
    • (2001) J. Biochem. , vol.130 , pp. 407-415
    • Okuda1    Morita, T.D.2
  • 17
    • 0035810673 scopus 로고    scopus 로고
    • Amino acid structure and characterization of a heterodimeric disintegrin from Vipera lebetina venom
    • A. Gasmi, N. Sriari, S. Guermazi, H. Dkhil, H. Karoui, and M.E. Ayeb Amino acid structure and characterization of a heterodimeric disintegrin from Vipera lebetina venom Biochim. Biophys. Acta 1547 2001 51 56
    • (2001) Biochim. Biophys. Acta , vol.1547 , pp. 51-56
    • Gasmi, A.1    Sriari, N.2    Guermazi, S.3    Dkhil, H.4    Karoui5    Ayeb, M.E.H.6
  • 18
    • 0037016015 scopus 로고    scopus 로고
    • A new gene structure of the disintegrin family: A subunit of dimeric disintegrin has a short coding region
    • D. Okuda, H. Koike, and T. Morita A new gene structure of the disintegrin family: a subunit of dimeric disintegrin has a short coding region Biochemistry 41 2002 14248 14254
    • (2002) Biochemistry , vol.41 , pp. 14248-14254
    • Okuda, D.1    Koike2    Morita, T.H.3
  • 19
    • 0037065736 scopus 로고    scopus 로고
    • The presence of the WGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on alphaII(b)beta3, alpha(v)beta3 and alpha5beta1 integrins
    • J.J. Calvete, J.W. Fow, A. Agelan, S. Niewiarowski, and C. Marcinkiewicz The presence of the WGD motif in CC8 heterodimeric disintegrin increases its inhibitory effect on alphaII(b)beta3, alpha(v)beta3 and alpha5beta1 integrins Biochemistry 41 2002 2014 2021
    • (2002) Biochemistry , vol.41 , pp. 2014-2021
    • Calvete, J.J.1    Fow, J.W.2    Agelan, A.3    Niewiarowski4    Marcinkiewicz, C.S.5
  • 20
    • 0028111866 scopus 로고
    • Contortrostatin a snake venom disintegrin, inhibits β1 integrin mediated human metastatic melanoma cell adhesion and blocks experimental metastasis
    • M. Trikha, Y.A. De Clarke, and F.S. Markland Contortrostatin a snake venom disintegrin, inhibits β1 integrin mediated human metastatic melanoma cell adhesion and blocks experimental metastasis Cancer Res. 54 1994 4993 4998
    • (1994) Cancer Res. , vol.54 , pp. 4993-4998
    • Trikha, M.1    De Clarke2    Markland, F.S.Y.A.3
  • 21
    • 0034653988 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of contortrostatin, a homodimeric disintegrin from southern copperhead snake venom
    • Q. Zhou, P. Hu, M.R. Ritter, S.D. Swenson, S. Argounova, A.L. Epstein, and F.S. Markland Molecular cloning and functional expression of contortrostatin, a homodimeric disintegrin from southern copperhead snake venom Arch. Biochem. Biophys. 375 2000 278 288
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 278-288
    • Zhou, Q.1    Hu, P.2    Ritter, M.R.3    Swenson, S.D.4    Argounova, S.5    Epstein6    Markland, F.S.A.L.7
  • 22
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: A versatile cell recognition signal
    • M.D. Pierschbacher, and E. Rouslahti Arg-Gly-Asp: a versatile cell recognition signal Cell 44 1986 517 518
    • (1986) Cell , vol.44 , pp. 517-518
    • Pierschbacher1    Rouslahti, E.M.D.2
  • 23
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • R. Hynes Integrins: versatility, modulation, and signaling in cell adhesion Cell 69 1992 11 25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.1
  • 24
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • R.O. Hynes Integrins: a family of cell surface receptors Cell 48 1987 549 554
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 25
    • 0034233562 scopus 로고    scopus 로고
    • In vivo functions of integrins: Lessons from null mutations in mice
    • D. Sheppard In vivo functions of integrins: lessons from null mutations in mice Matrix Biol. 9 2000 203 209
    • (2000) Matrix Biol. , vol.9 , pp. 203-209
    • Sheppard, D.1
  • 27
    • 0028362876 scopus 로고
    • Requirement of vascular integrin α5β3 for angiogenesis
    • P.C. Brooks, R.A.F. Clark, and D.A. Cheresh Requirement of vascular integrin α5β3 for angiogenesis Science 264 1994 569 571
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark2    Cheresh, D.A.R.A.F.3
  • 29
    • 0042354203 scopus 로고    scopus 로고
    • Ovarian cancer cell proliferation and motility is induced by engagement of integrin alpha(v)beta3/Vitronectin interaction
    • S. Hapke, H. Kessler, B. Luber, A. Benge, P. Hutzler, and H. Hofler Ovarian cancer cell proliferation and motility is induced by engagement of integrin alpha(v)beta3/Vitronectin interaction Biol. Chem. 384 2003 1073 1083
    • (2003) Biol. Chem. , vol.384 , pp. 1073-1083
    • Hapke, S.1    Kessler, H.2    Luber, B.3    Benge, A.4    Hutzler5    Hofler, H.P.6
  • 30
    • 0042165831 scopus 로고    scopus 로고
    • Alpha v integrin inhibitors and cancer therapy
    • G.C. Tucker Alpha v integrin inhibitors and cancer therapy Curr. Opin. Investig. Drugs 4 2003 722 731
    • (2003) Curr. Opin. Investig. Drugs , vol.4 , pp. 722-731
    • Tucker, G.C.1
  • 31
    • 0041765057 scopus 로고    scopus 로고
    • Integrin-mediated control of cell growth
    • D. Schuppan, and M. Ocker Integrin-mediated control of cell growth Hepatology 38 2003 289 291
    • (2003) Hepatology , vol.38 , pp. 289-291
    • Schuppan1    Ocker, M.D.2
  • 32
    • 0023915420 scopus 로고
    • The platelet membrane glycoprotein IIb-IIIa complex
    • D.R. Philips, I.F. Charo, L.V. Parise, and L.A. Fitzgerald The platelet membrane glycoprotein IIb-IIIa complex Blood 71 1988 831 843
    • (1988) Blood , vol.71 , pp. 831-843
    • Philips, D.R.1    Charo, I.F.2    Parise3    Fitzgerald, L.A.L.V.4
  • 33
    • 0024531099 scopus 로고
    • Cellular adhesion GP IIb-IIIa as prototypic adhesion receptor
    • E.F. Plow, and M.H. Ginsberg Cellular adhesion GP IIb-IIIa as prototypic adhesion receptor Prog. Hemost. Thromb. 9 1989 117 156
    • (1989) Prog. Hemost. Thromb. , vol.9 , pp. 117-156
    • Plow1    Ginsberg, M.H.E.F.2
  • 34
    • 0028037889 scopus 로고
    • Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation
    • E.A. Clark, M. Trikha, F.S. Markland, and J.S. Brugge Structurally distinct disintegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation J. Mol. Biol. 269 1994 21940 21943
    • (1994) J. Mol. Biol. , vol.269 , pp. 21940-21943
    • Clark, E.A.1    Trikha, M.2    Markland3    Brugge, J.S.F.S.4
  • 36
    • 0029916911 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its new supplement TREMBL
    • A. Bairoch, and R. Apweiler The SWISS-PROT protein sequence data bank and its new supplement TREMBL Nucl. Acids Res. 24 1996 21 25
    • (1996) Nucl. Acids Res. , vol.24 , pp. 21-25
    • Bairoch1    Apweiler, R.A.2
  • 37
    • 0030750415 scopus 로고    scopus 로고
    • Significance of RGD loop and C-terminal domain of echistatin for recognition of alphaIIb beta3 and alpha(v) beta3 integrins and expression of ligand-induced binding site
    • C. Marcinkiewicz, S. Vijay-Kumar, M.A. McLane, and S. Niewiarowski Significance of RGD loop and C-terminal domain of echistatin for recognition of alphaIIb beta3 and alpha(v) beta3 integrins and expression of ligand-induced binding site Blood 90 1997 1565 1575
    • (1997) Blood , vol.90 , pp. 1565-1575
    • Marcinkiewicz, C.1    Vijay-Kumar, S.2    McLane3    Niewiarowski, S.M.A.4
  • 39
    • 0027508996 scopus 로고
    • Characterization of the integrin specificities of disintegrin isolated from American pit viper venoms
    • R.M. Scarborough, J.W. Rose, M.A. Naughton, R.D. Phillips, L. Nannizzi, and A. Arfsten Characterization of the integrin specificities of disintegrin isolated from American pit viper venoms J. Biol. Chem. 268 1993 1058 1065
    • (1993) J. Biol. Chem. , vol.268 , pp. 1058-1065
    • Scarborough, R.M.1    Rose, J.W.2    Naughton, M.A.3    Phillips, R.D.4    Nannizzi5    Arfsten, A.L.6
  • 40
    • 0030570733 scopus 로고    scopus 로고
    • Importance of the structure of the RGD containing loop in the disintegrins echistatin and eristostatin for recognition of alpha IIb beta 3 and alpha v beta 3 integrins
    • M.A. McLane, S. Vijay-Kumar, C. Marcinkiewicz, J.J. Calvete, and S. Niewiarowski Importance of the structure of the RGD containing loop in the disintegrins echistatin and eristostatin for recognition of alpha IIb beta 3 and alpha v beta 3 integrins FEBS Letters 391 1996 139 143
    • (1996) FEBS Letters , vol.391 , pp. 139-143
    • McLane, M.A.1    Vijay-Kumar, S.2    Marcinkiewicz, C.3    Calvete4    Niewiarowski, S.J.J.5
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallog. 26 1993 283 291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss3    Thornton, J.M.D.S.4
  • 44
    • 0038385565 scopus 로고    scopus 로고
    • Disulfide-bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin alpha5beta1 antagonist from Eristocophis macmahoni venom
    • J.J. Calvete, M. Jurgens, C. Marcinkiewicz, A. Romero, M. Schrader, and S. Niewiarowski Disulfide-bond pattern and molecular modelling of the dimeric disintegrin EMF-10, a potent and selective integrin alpha5beta1 antagonist from Eristocophis macmahoni venom Biochem. J. 345 2000 573 581
    • (2000) Biochem. J. , vol.345 , pp. 573-581
    • Calvete, J.J.1    Jurgens, M.2    Marcinkiewicz, C.3    Romero, A.4    Schrader5    Niewiarowski, S.M.6
  • 45
    • 0345118115 scopus 로고    scopus 로고
    • Crystal structure of echicetin from Echis carinatus (Indian Saw-scaled Viper) at 2.4 Å resolution
    • J. Jasti, M. Paramasivam, A. Srinivasan, and T.P. Singh Crystal structure of echicetin from Echis carinatus (Indian Saw-scaled Viper) at 2.4 Å resolution J. Mol. Biol. 335 2004 167 176
    • (2004) J. Mol. Biol. , vol.335 , pp. 167-176
    • Jasti, J.1    Paramasivam, M.2    Srinivasan3    Singh, T.P.A.4
  • 46
    • 0026350087 scopus 로고
    • Solution structure of Kistrin, potent platelet aggregation Inhibitor and GP IIb-IIIa antagonist
    • M. Adler, R.A. Lazarus, M.S. Dennis, and G. Wagner Solution structure of Kistrin, potent platelet aggregation Inhibitor and GP IIb-IIIa antagonist Science 253 1991 445 448
    • (1991) Science , vol.253 , pp. 445-448
    • Adler, M.1    Lazarus, R.A.2    Dennis3    Wagner, G.M.S.4
  • 47
    • 0025786742 scopus 로고
    • Three dimensional structure of echistatin, the smallest active RGD protein
    • V. Saudek, R.A. Atkinson, P. Lepage, and J.T. Pelton Three dimensional structure of echistatin, the smallest active RGD protein Biochemistry 30 1991 7369 7372
    • (1991) Biochemistry , vol.30 , pp. 7369-7372
    • Saudek, V.1    Atkinson, R.A.2    Lepage3    Pelton, J.T.P.4
  • 48
    • 0027165368 scopus 로고
    • The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIa-IIIa receptor
    • H. Senn, and W. Klaus The nuclear magnetic resonance solution structure of flavoridin, an antagonist of the platelet GP IIa-IIIa receptor J. Mol. Biol. 232 1993 907 925
    • (1993) J. Mol. Biol. , vol.232 , pp. 907-925
    • Senn1    Klaus, W.H.2
  • 49
    • 0042887427 scopus 로고    scopus 로고
    • Crystal structure of trimestatin, a disintegrin containing cell adhesion recognition motif RGD
    • Y. Fuji, D. Okuda, Z. Fujimoto, K. Horii, T. Morita, and H. Mizuno Crystal structure of trimestatin, a disintegrin containing cell adhesion recognition motif RGD J. Mol. Biol. 332 2003 1115 1122
    • (2003) J. Mol. Biol. , vol.332 , pp. 1115-1122
    • Fuji, Y.1    Okuda, D.2    Fujimoto, Z.3    Horii, K.4    Morita5    Mizuno, H.T.6
  • 50
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha V beta 3, and alpha 5 beta 1 integrins
    • M. Pfaff, K. Tangemann, B. Muller, M. Gurrath, G. Muller, and H. Kessler Selective recognition of cyclic RGD peptides of NMR defined conformation by alpha IIb beta 3, alpha V beta 3, and alpha 5 beta 1 integrins J. Biol. Chem. 269 1994 20233 20238
    • (1994) J. Biol. Chem. , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Muller, B.3    Gurrath, M.4    Muller5    Kessler, H.G.6
  • 51
    • 0034598655 scopus 로고    scopus 로고
    • Differential regulation of tyrosine phosphorylation in tumor cells by contortrostatin, a homodimeric disintegrin and monomeric disintegrins echistatin and flavoridin
    • M.R. Ritter, and F.S. Markland Jr Differential regulation of tyrosine phosphorylation in tumor cells by contortrostatin, a homodimeric disintegrin and monomeric disintegrins echistatin and flavoridin Toxicon 39 2001 283 289
    • (2001) Toxicon , vol.39 , pp. 283-289
    • Markland F.S., Jr.1    Ritter, M.R.2
  • 52
    • 0032578007 scopus 로고    scopus 로고
    • Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin alphaIIb beta3
    • T. Hato, N. Pampori, and S.J. Shattil Complementary roles for receptor clustering and conformational change in the adhesive and signaling functions of integrin alphaIIb beta3 J. Cell Biol. 141 1998 1685 1695
    • (1998) J. Cell Biol. , vol.141 , pp. 1685-1695
    • Hato, T.1    Pampori2    Shattil, S.J.N.3
  • 53
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4
    • Collaborative Computational Project Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallog. sect. D 50 1994 760 763
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collection in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski1    Minor, W.Z.2
  • 56
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • T.C. Terwilliger Maximum-likelihood density modification Acta Crystallog. sect. D 56 2000 965 972
    • (2000) Acta Crystallog. Sect. D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 57
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nature Struct. Biol. 6 1999 458 463
    • (1999) Nature Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris2    Lamzin, V.S.R.3
  • 58
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • G.N. Murshudov, A.A. Vagin, and E.J. Dodson Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallog. sect. D 53 1997 240 255
    • (1997) Acta Crystallog. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin2    Dodson, E.J.A.A.3
  • 59
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallog. sect. A 47 1991 110 119
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan3    Kjeldgaard, M.S.W.4
  • 60
    • 0026244229 scopus 로고
    • "mOLSCRIPT: A program to produce both detailed and schematic plots of protein structures"
    • P.J. Kraulis "MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures" J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 61
    • 0028057108 scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • E.A. Merritt, and M.E.P. Murphy Raster3D version 2.0: a program for photorealistic molecular graphics Acta Crystallog. sect. D 50 1994 869 873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.