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Volumn 399, Issue 4, 2010, Pages 587-592

Crystal structure of human programmed cell death 10 complexed with inositol-(1,3,4,5)-tetrakisphosphate: A novel adaptor protein involved in human cerebral cavernous malformation

Author keywords

Adaptor protein; Binding partner recruitment; Conformational variability; Phosphatidylinositide binding; Programmed cell death 10; Unique dimeric assembly

Indexed keywords

ADAPTOR PROTEIN; DIMER; FOCAL ADHESION KINASE; INOSITOL 1,3,4,5 TETRAKISPHOSPHATE; MONOMER; PAXILLIN; PHOSPHATIDYLINOSITIDE; PROGRAMMED CELL DEATH 10; UNCLASSIFIED DRUG; APOPTOSIS REGULATORY PROTEIN; INOSITOL PHOSPHATE; INOSITOL-1,2,4,5-TETRAKISPHOSPHATE; MEMBRANE PROTEIN; ONCOPROTEIN; PDCD10 PROTEIN, HUMAN;

EID: 77956262153     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.07.119     Document Type: Article
Times cited : (17)

References (25)
  • 1
    • 0034614490 scopus 로고    scopus 로고
    • Signaling-2000 and beyond
    • Hunter T. Signaling-2000 and beyond. Cell 2000, 100:113-127.
    • (2000) Cell , vol.100 , pp. 113-127
    • Hunter, T.1
  • 2
    • 0035473482 scopus 로고    scopus 로고
    • Adaptor proteins
    • Flynn D.C. Adaptor proteins. Oncogene 2001, 20:6270-6272.
    • (2001) Oncogene , vol.20 , pp. 6270-6272
    • Flynn, D.C.1
  • 3
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. Protein modules and signalling networks. Nature 1995, 373:573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 4
    • 11144299824 scopus 로고    scopus 로고
    • CDNA cloning and expression of an apoptosis-related gene, humanTFAR15 gene
    • Wang Y., Liu H., Zhang Y., Ma D. CDNA cloning and expression of an apoptosis-related gene, humanTFAR15 gene. Sci. China C Life Sci. 1999, 42:323-329.
    • (1999) Sci. China C Life Sci. , vol.42 , pp. 323-329
    • Wang, Y.1    Liu, H.2    Zhang, Y.3    Ma, D.4
  • 6
    • 33749263696 scopus 로고    scopus 로고
    • Cerebral cavernous malformation: new molecular and clinical insights
    • Revencu N., Vikkula M. Cerebral cavernous malformation: new molecular and clinical insights. J. Med. Genet. 2006, 43:716-721.
    • (2006) J. Med. Genet. , vol.43 , pp. 716-721
    • Revencu, N.1    Vikkula, M.2
  • 8
  • 9
    • 65249182536 scopus 로고    scopus 로고
    • Apoptotic functions of PDCD10/CCM3, the gene mutated in cerebral cavernous malformation 3
    • Chen L., Tanriover G., Yano H., Friedlander R., Louvi A., Gunel M. Apoptotic functions of PDCD10/CCM3, the gene mutated in cerebral cavernous malformation 3. Stroke 2009, 40:1474-1481.
    • (2009) Stroke , vol.40 , pp. 1474-1481
    • Chen, L.1    Tanriover, G.2    Yano, H.3    Friedlander, R.4    Louvi, A.5    Gunel, M.6
  • 10
    • 34250330782 scopus 로고    scopus 로고
    • PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway
    • Ma X., Zhao H., Shan J., Long F., Chen Y., Zhang Y., Han X., Ma D. PDCD10 interacts with Ste20-related kinase MST4 to promote cell growth and transformation via modulation of the ERK pathway. Mol. Biol. Cell 2007, 18:1965-1978.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1965-1978
    • Ma, X.1    Zhao, H.2    Shan, J.3    Long, F.4    Chen, Y.5    Zhang, Y.6    Han, X.7    Ma, D.8
  • 11
    • 77951194603 scopus 로고    scopus 로고
    • CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation
    • Fidalgo M., Fraile M., Pires A., Force T., Pombo C., Zalvide J. CCM3/PDCD10 stabilizes GCKIII proteins to promote Golgi assembly and cell orientation. J. Cell Sci. 2010, 123:1274-1284.
    • (2010) J. Cell Sci. , vol.123 , pp. 1274-1284
    • Fidalgo, M.1    Fraile, M.2    Pires, A.3    Force, T.4    Pombo, C.5    Zalvide, J.6
  • 12
    • 0028103275 scopus 로고
    • Programs for protein crystallography
    • Collaborative. Computational. Project Number 4
    • Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50:760-763. Collaborative. Computational. Project Number 4.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 15
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger T.C. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. D Biol. Crystallogr. 2003, 59:38-44.
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 1991, 47(Pt 2):110-119.
    • (1991) Acta Crystallogr. A , vol.47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 20
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L., Sander C. Touring protein fold space with Dali/FSSP. Nucleic Acids Res. 1998, 26:316-319.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 21
    • 66349137330 scopus 로고    scopus 로고
    • Functional analyses of human and zebrafish 18-amino acid in-frame deletion pave the way for domain mapping of the cerebral cavernous malformation 3 protein
    • Voss K., Stahl S., Hogan B.M., Reinders J., Schleider E., Schulte-Merker S., Felbor U. Functional analyses of human and zebrafish 18-amino acid in-frame deletion pave the way for domain mapping of the cerebral cavernous malformation 3 protein. Hum. Mutat. 2009, 30:1003-1011.
    • (2009) Hum. Mutat. , vol.30 , pp. 1003-1011
    • Voss, K.1    Stahl, S.2    Hogan, B.M.3    Reinders, J.4    Schleider, E.5    Schulte-Merker, S.6    Felbor, U.7
  • 22
    • 0036118284 scopus 로고    scopus 로고
    • The structural basis of localization and signaling by the focal adhesion targeting domain
    • Arold S.T., Hoellerer M.K., Noble M.E. The structural basis of localization and signaling by the focal adhesion targeting domain. Structure 2002, 10:319-327.
    • (2002) Structure , vol.10 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.3
  • 23
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • Hayashi I., Vuori K., Liddington R.C. The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat. Struct. Biol. 2002, 9:101-106.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 24
    • 67349236641 scopus 로고    scopus 로고
    • Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2
    • Lulo J., Yuzawa S., Schlessinger J. Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2. Biochem. Biophys. Res. Commun. 2009, 383:347-352.
    • (2009) Biochem. Biophys. Res. Commun. , vol.383 , pp. 347-352
    • Lulo, J.1    Yuzawa, S.2    Schlessinger, J.3
  • 25
    • 77954926292 scopus 로고    scopus 로고
    • Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity
    • Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J. Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity. J. Biol. Chem. 2010, 10.1074/jbc.M1110.128470.
    • (2010) J. Biol. Chem.
    • Li, X.1    Zhang, R.2    Zhang, H.3    He, Y.4    Ji, W.5    Min, W.6    Boggon, T.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.