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Volumn 61, Issue 1, 2005, Pages 213-216

Crystal structure of human SH3BGRL protein: The first structure of the human SH3BGR family representing a novel class of thioredoxin fold proteins

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAREDOXIN; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; HELIX LOOP HELIX PROTEIN; SH3BGRL PROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 24344478136     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20523     Document Type: Article
Times cited : (13)

References (11)
  • 2
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    • Mazzocco M, Maffei M, Egeo A, Vergano A, Arrigo P, Lisi RD, Ghiotto F, Scartezzini P. The identification of a novel human homologue of the SH3 binding glutamic acid-rich (SH3BGR) gene establishes a new family of highly conserved small proteins related to thioredoxin superfamily. Gene 2002;291:233-239.
    • (2002) Gene , vol.291 , pp. 233-239
    • Mazzocco, M.1    Maffei, M.2    Egeo, A.3    Vergano, A.4    Arrigo, P.5    Lisi, R.D.6    Ghiotto, F.7    Scartezzini, P.8
  • 3
    • 0031457622 scopus 로고    scopus 로고
    • Signaling through scaffold, anchoring, and adaptor proteins
    • Powson T, Scott JD. Signaling through scaffold, anchoring, and adaptor proteins. Science 1997;278:2075-2080.
    • (1997) Science , vol.278 , pp. 2075-2080
    • Powson, T.1    Scott, J.D.2
  • 4
    • 0030864520 scopus 로고    scopus 로고
    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr K, Ebel F, Frank R, Reinhard M, Domain E, Carl UD, Walter U, Gertler FB, Wehland J, Chakraborty T. A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J 1997;16:5433-5444.
    • (1997) EMBO J , vol.16 , pp. 5433-5444
    • Niebuhr, K.1    Ebel, F.2    Frank, R.3    Reinhard, M.4    Domain, E.5    Carl, U.D.6    Walter, U.7    Gertler, F.B.8    Wehland, J.9    Chakraborty, T.10
  • 6
    • 0029165589 scopus 로고
    • Thioredoxin-a fold for all reasons
    • Martin JL. Thioredoxin-a fold for all reasons. Structure 1995;3:245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 8
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods
    • Sweet RM and Carter CW, editors. New York: Academic Press
    • De La Fortelle E, Bricogne G. Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. In: Sweet RM and Carter CW, editors. Methods in enzymology, Volume 276. Macromolecular crystallography. New York: Academic Press; 1997. p 472-494.
    • (1997) Methods in Enzymology, Volume 276. Macromolecular Crystallography , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 9
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and thelocation of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and thelocation of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.