메뉴 건너뛰기




Volumn 6, Issue 8, 2005, Pages 787-793

The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex

Author keywords

BET3 protein family; Golgi membrane; TPC6 protein; TRAPP complex; Vesicle tethering

Indexed keywords

BET3 PROTEIN; BINDING PROTEIN; CARRIER PROTEIN; TPC5 PROTEIN; TPC6 PROTEIN; UNCLASSIFIED DRUG;

EID: 26844574974     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400463     Document Type: Article
Times cited : (31)

References (24)
  • 1
    • 0034161259 scopus 로고    scopus 로고
    • TRAPP stably associates with the Golgi and is required for vesicle docking
    • Barrowman J, Sacher M, Ferro-Novick S (2000) TRAPP stably associates with the Golgi and is required for vesicle docking. EMBO J 19: 862-869
    • (2000) EMBO J , vol.19 , pp. 862-869
    • Barrowman, J.1    Sacher, M.2    Ferro-Novick, S.3
  • 2
    • 0029064088 scopus 로고
    • High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli
    • Budisa N, Steipe B, Demange P, Eckerskorn C, Kellermann J, Huber R (1995) High-level biosynthetic substitution of methionine in proteins by its analogs 2-aminohexanoic acid, selenomethionine, telluromethionine and ethionine in Escherichia coli. Eur J Biochem 230: 788-796
    • (1995) Eur J Biochem , vol.230 , pp. 788-796
    • Budisa, N.1    Steipe, B.2    Demange, P.3    Eckerskorn, C.4    Kellermann, J.5    Huber, R.6
  • 4
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin AC et al (2002) Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 415: 141-147
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.C.1
  • 5
    • 0026605537 scopus 로고
    • CLUSTAL V: Improved software for multiple sequence alignment
    • Higgins DG, Bleasby AJ, Fuchs R (1992) CLUSTAL V: Improved software for multiple sequence alignment. Comput Appl Biosci 8: 189-191
    • (1992) Comput Appl Biosci , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 7
    • 0037147148 scopus 로고    scopus 로고
    • Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda
    • Jang SB, Kim Y-G, Cho Y-S, Suh P-G, Kim K-H, Oh B-H (2002) Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda. J Biol Chem 277: 49863-49869
    • (2002) J Biol Chem , vol.277 , pp. 49863-49869
    • Jang, S.B.1    Kim, Y.-G.2    Cho, Y.-S.3    Suh, P.-G.4    Kim, K.-H.5    Oh, B.-H.6
  • 8
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 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
  • 9
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W (1976) A solution for the best rotation to relate two sets of vectors. Acta Crystallogr A 32: 922-923
    • (1976) Acta Crystallogr A , vol.32 , pp. 922-923
    • Kabsch, W.1
  • 11
  • 13
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53: 240-255
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 14
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct Funct Genet 11: 281-296
    • (1991) Proteins Struct Funct Genet , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 0035913537 scopus 로고    scopus 로고
    • Extending the applicability of the nonlinear Poisson-Boltzmann equation: Multiple dielectric constants and multivalent ions
    • Rocchia W, Alexov E, Honig B (2001) Extending the applicability of the nonlinear Poisson-Boltzmann equation: Multiple dielectric constants and multivalent ions. J Phys Chem B 105: 6507-6514
    • (2001) J Phys Chem B , vol.105 , pp. 6507-6514
    • Rocchia, W.1    Alexov, E.2    Honig, B.3
  • 19
    • 1642493929 scopus 로고    scopus 로고
    • An automated in vitro protein folding screen applied to human dynactin subunit
    • Scheich C, Niesen FH, Seckler R, Büssow K (2004) An automated in vitro protein folding screen applied to human dynactin subunit. Protein Sci 13: 370-380
    • (2004) Protein Sci , vol.13 , pp. 370-380
    • Scheich, C.1    Niesen, F.H.2    Seckler, R.3    Büssow, K.4
  • 20
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger TC (2000) Maximum-likelihood density modification. Acta Crystallogr D 56: 965-972
    • (2000) Acta Crystallogr D , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 22
    • 20144388984 scopus 로고    scopus 로고
    • Structure of palmitoylated BET3: Insights into TRAPP complex assembly and membrane localization
    • Turnbull AP et al (2005) Structure of palmitoylated BET3: Insights into TRAPP complex assembly and membrane localization. EMBO J 24: 875-884
    • (2005) EMBO J , vol.24 , pp. 875-884
    • Turnbull, A.P.1
  • 23
    • 9444254040 scopus 로고    scopus 로고
    • SMART amplification combined with cDNA size fractionation in order to obtain large full-length clones
    • The German cDNA Consortium, Poustka A, Wiemann S
    • Wellenreuther R, Schupp I, The German cDNA Consortium, Poustka A, Wiemann S (2004) SMART amplification combined with cDNA size fractionation in order to obtain large full-length clones. BMC Genom 5: 36
    • (2004) BMC Genom , vol.5 , pp. 36
    • Wellenreuther, R.1    Schupp, I.2
  • 24
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle membrane complexes in membrane traffic
    • Whyte JR, Munro S (2002) Vesicle membrane complexes in membrane traffic. J Cell Sci 115: 2627-2637
    • (2002) J Cell Sci , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.