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Volumn 1703, Issue 1, 2004, Pages 83-85

Crystallization and preliminary X-ray diffraction analysis of suramin, a highly charged polysulfonated napthylurea, complexed with a myotoxic PLA 2 from Bothrops asper venom

Author keywords

Lys49 PLA 2s; Myotoxicity; Snake venom; Suramin; X ray diffraction

Indexed keywords

NAPHTHALENE DERIVATIVE; PHOSPHOLIPASE A2; SNAKE VENOM; SURAMIN; UREA DERIVATIVE;

EID: 9644258969     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.08.009     Document Type: Article
Times cited : (8)

References (30)
  • 1
    • 0022370712 scopus 로고
    • Suramin binds to platelet-derived growth factor and inhibits its biological activity
    • M. Hosang Suramin binds to platelet-derived growth factor and inhibits its biological activity J. Cell. Biochem. 29 1985 265 273
    • (1985) J. Cell. Biochem. , vol.29 , pp. 265-273
    • Hosang, M.1
  • 2
    • 0024242552 scopus 로고
    • Rapid turnover of the platelet-derived growth factor receptor in cis-transformed cells and reversal by suramin: Implications for the mechanism of autocrine transformation
    • S.S. Huang, and J.S. Huang Rapid turnover of the platelet-derived growth factor receptor in cis-transformed cells and reversal by suramin: Implications for the mechanism of autocrine transformation J. Biol. Chem. 263 1988 12608 12618
    • (1988) J. Biol. Chem. , vol.263 , pp. 12608-12618
    • Huang, S.S.1    Huang, J.S.2
  • 3
    • 0024370274 scopus 로고
    • Recent developments in the cell biology of basic fibroblast growth factor
    • D.B. Rifkin, and D. Moscatelli Recent developments in the cell biology of basic fibroblast growth factor J. Cell Biol. 109 1989 1 6
    • (1989) J. Cell Biol. , vol.109 , pp. 1-6
    • Rifkin, D.B.1    Moscatelli, D.2
  • 5
    • 0024461389 scopus 로고
    • Suramin, anti-cancer drug, inhibits protein kinase C and induces differentiation in neuroblastoma cell clone NB2A
    • C.E. Hensey, D. Boscoboinik, and A. Azzi Suramin, anti-cancer drug, inhibits protein kinase C and induces differentiation in neuroblastoma cell clone NB2A FEBS Lett. 258 1989 156 158
    • (1989) FEBS Lett. , vol.258 , pp. 156-158
    • Hensey, C.E.1    Boscoboinik, D.2    Azzi, A.3
  • 8
    • 0032785794 scopus 로고    scopus 로고
    • Phase II trial of suramin in patients with metastatic renal cell carcinoma
    • R. Dreicer, D.C. Smith, R.D. Williams, and W.A. See Phase II trial of suramin in patients with metastatic renal cell carcinoma Invest. New Drugs 17 1999 183 186
    • (1999) Invest. New Drugs , vol.17 , pp. 183-186
    • Dreicer, R.1    Smith, D.C.2    Williams, R.D.3    See, W.A.4
  • 9
  • 10
    • 0036297332 scopus 로고    scopus 로고
    • Effect of suramin on myotoxicity of some crotalid snake venoms. Antimyotoxic effect of suramin
    • E.Z. Arruda, N.M.V. Silva, R.A.M. Moraes, and P.A. Melo Effect of suramin on myotoxicity of some crotalid snake venoms. Antimyotoxic effect of suramin Braz. J. Med. Biol. Res. 35 2002 723 726
    • (2002) Braz. J. Med. Biol. Res. , vol.35 , pp. 723-726
    • Arruda, E.Z.1    Silva, N.M.V.2    Moraes, R.A.M.3    Melo, P.A.4
  • 13
    • 0002677718 scopus 로고
    • Phospholipases in snake venoms and their effects on nerve and muscle
    • A.L. Harvey Pergamon Press New York
    • J.B. Harris Phospholipases in snake venoms and their effects on nerve and muscle A.L. Harvey Snake Toxins 1991 Pergamon Press New York 91 121
    • (1991) Snake Toxins , pp. 91-121
    • Harris, J.B.1
  • 17
    • 0023009920 scopus 로고
    • Structure-function relationships of phospholipases: II. Charge density distribution and the myotoxicity of presynaptically neurotoxic phospholipases
    • R.M. Kini, and S. Iwanaga Structure-function relationships of phospholipases: II. Charge density distribution and the myotoxicity of presynaptically neurotoxic phospholipases Toxicon 24 1986 895 905
    • (1986) Toxicon , vol.24 , pp. 895-905
    • Kini, R.M.1    Iwanaga, S.2
  • 18
    • 0024451779 scopus 로고
    • Role of cationic residues in cytolytic activity: Modification of lysine residues in the cardiotoxin from Naja nigricollis venom and correlation between cytolytic and antiplatelet activity
    • R.M. Kini, and H.J. Evans Role of cationic residues in cytolytic activity: modification of lysine residues in the cardiotoxin from Naja nigricollis venom and correlation between cytolytic and antiplatelet activity Biochemistry-US 28 1989 9209 9216
    • (1989) Biochemistry-US , vol.28 , pp. 9209-9216
    • Kini, R.M.1    Evans, H.J.2
  • 19
    • 0031081513 scopus 로고    scopus 로고
    • 2 isolated from Bothrops asper and Bothrops godmani snake venoms: Effects on enzymatic and pharmacological properties
    • 2 isolated from Bothrops asper and Bothrops godmani snake venoms: effects on enzymatic and pharmacological properties Toxicon 35 1997 241 252
    • (1997) Toxicon , vol.35 , pp. 241-252
    • Díaz-Oreiro, C.1    Gutiérrez, J.M.2
  • 22
    • 0034899916 scopus 로고    scopus 로고
    • 2 from Agkistrodon piscivorus piscivorus snake venom: Synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities
    • 2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities Toxicon 39 2001 1587 1594
    • (2001) Toxicon , vol.39 , pp. 1587-1594
    • Núnez, C.E.1    Angulo, Y.2    Lomonte, B.3
  • 23
    • 1042287120 scopus 로고    scopus 로고
    • 2 by sequence analysis and site directed mutagenesis
    • 2 by sequence analysis and site directed mutagenesis Toxicon 42 2003 869 883
    • (2003) Toxicon , vol.42 , pp. 869-883
    • Chioato, L.1    Ward, R.J.2
  • 24
    • 1042275597 scopus 로고    scopus 로고
    • A structure based model for liposome disruption and the role of catalytic activity in myotoxic phospholipase A2s
    • M.T. Murakami, and R.K. Arni A structure based model for liposome disruption and the role of catalytic activity in myotoxic phospholipase A2s Toxicon 42 2003 903 913
    • (2003) Toxicon , vol.42 , pp. 903-913
    • Murakami, M.T.1    Arni, R.K.2
  • 26
    • 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
  • 27
    • 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
  • 28
    • 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
  • 30
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.