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Volumn 12, Issue 4, 2000, Pages 467-474

Structural insights into clathrin-mediated endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN;

EID: 0033948978     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(00)00118-6     Document Type: Review
Times cited : (47)

References (62)
  • 1
    • 0030957355 scopus 로고    scopus 로고
    • Clathrin-coated vesicle formation and protein sorting: An integrated process
    • Schmid S.L. Clathrin-coated vesicle formation and protein sorting: an integrated process. Annu Rev Biochem. 66:1997;511-548.
    • (1997) Annu Rev Biochem , vol.66 , pp. 511-548
    • Schmid, S.L.1
  • 2
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • Mellman I., Warren G. The road taken: past and future foundations of membrane traffic. Cell. 100:2000;99-112.
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 3
    • 0033990428 scopus 로고    scopus 로고
    • Coat proteins regulating membrane traffic
    • Scales S.J., Gomez M., Kreis T.E. Coat proteins regulating membrane traffic. Int Rev Cytol. 195:2000;67-144.
    • (2000) Int Rev Cytol , vol.195 , pp. 67-144
    • Scales, S.J.1    Gomez, M.2    Kreis, T.E.3
  • 4
    • 0006857840 scopus 로고    scopus 로고
    • New twists for dynamin
    • Kelly R.B. New twists for dynamin. Nat Cell Biol. 1:1999;E8-E9.
    • (1999) Nat Cell Biol , vol.1
    • Kelly, R.B.1
  • 7
    • 0029584896 scopus 로고
    • A clathrin-binding site in the hinge of the β 2 chain of mammalian AP-2 complexes
    • Shih W., Gallusser A., Kirchhausen T. A clathrin-binding site in the hinge of the β 2 chain of mammalian AP-2 complexes. J Biol Chem. 270:1995;31083-31090.
    • (1995) J Biol Chem , vol.270 , pp. 31083-31090
    • Shih, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 8
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David C., McPherson P.S., Mundigl O., de Camilli P. A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc Natl Acad Sci USA. 93:1996;331-335.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 331-335
    • David, C.1    McPherson, P.S.2    Mundigl, O.3    De Camilli, P.4
  • 9
    • 0032893679 scopus 로고    scopus 로고
    • Eps15 is recruited to the plasma membrane upon epidermal growth factor receptor activation and localizes to components of the endocytic pathway during receptor internalization
    • Torrisi M.R., Lotti L.V., Belleudi F., Gradini R., Salcini A.E., Confalonieri S., Pelicci P.G., Di Fiore P.P. Eps15 is recruited to the plasma membrane upon epidermal growth factor receptor activation and localizes to components of the endocytic pathway during receptor internalization. Mol Biol Cell. 10:1999;417-434.
    • (1999) Mol Biol Cell , vol.10 , pp. 417-434
    • Torrisi, M.R.1    Lotti, L.V.2    Belleudi, F.3    Gradini, R.4    Salcini, A.E.5    Confalonieri, S.6    Pelicci, P.G.7    Di Fiore, P.P.8
  • 10
    • 0034602956 scopus 로고    scopus 로고
    • Mapping of Eps15 domains involved in its targeting to clathrin-coated pits
    • Benmerah A., Poupon V., Cerf-Bensussan N., Dautry-Varsat A. Mapping of Eps15 domains involved in its targeting to clathrin-coated pits. J Biol Chem. 275:2000;3288-3295.
    • (2000) J Biol Chem , vol.275 , pp. 3288-3295
    • Benmerah, A.1    Poupon, V.2    Cerf-Bensussan, N.3    Dautry-Varsat, A.4
  • 12
    • 0033529507 scopus 로고    scopus 로고
    • AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrin
    • Hao W., Luo Z., Zheng L., Prasad K., Lafer E.M. AP180 and AP-2 interact directly in a complex that cooperatively assembles clathrin. J Biol Chem. 274:1999;22785-22794.
    • (1999) J Biol Chem , vol.274 , pp. 22785-22794
    • Hao, W.1    Luo, Z.2    Zheng, L.3    Prasad, K.4    Lafer, E.M.5
  • 13
    • 0033000498 scopus 로고    scopus 로고
    • A structural explanation for the binding of multiple ligands by the α adaptin appendage domain
    • Owen D.J., Vallis Y., Noble M.E., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T. A structural explanation for the binding of multiple ligands by the α adaptin appendage domain. Cell. 97:1999;805-815.
    • (1999) Cell , vol.97 , pp. 805-815
    • Owen, D.J.1    Vallis, Y.2    Noble, M.E.3    Hunter, J.B.4    Dafforn, T.R.5    Evans, P.R.6    McMahon, H.T.7
  • 16
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals
    • Takei K., McPherson P.S., Schmid S.L., De Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-γS in nerve terminals. Nature. 374:1995;186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 19
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 angstrom resolution: A cellular assembly designed to recycle multiple membrane receptors
    • Smith C.J., Grigorieff N., Pearse B.M.F. Clathrin coats at 21 angstrom resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J. 17:1998;4943-4953.
    • (1998) EMBO J , vol.17 , pp. 4943-4953
    • Smith, C.J.1    Grigorieff, N.2    Pearse, B.M.F.3
  • 20
    • 0024075871 scopus 로고
    • Deep-etch visualization of proteins involved in clathrin assembly
    • Heuser J.E., Keen J.H. Deep-etch visualization of proteins involved in clathrin assembly. J Cell Biol. 107:1988;877-886.
    • (1988) J Cell Biol , vol.107 , pp. 877-886
    • Heuser, J.E.1    Keen, J.H.2
  • 21
    • 0031467675 scopus 로고    scopus 로고
    • Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15 (Eps15)
    • Cupers P., ter Haar E., Boll W., Kirchhausen T. Parallel dimers and anti-parallel tetramers formed by epidermal growth factor receptor pathway substrate clone 15 (Eps15). J Biol Chem. 272:1997;33430-33434.
    • (1997) J Biol Chem , vol.272 , pp. 33430-33434
    • Cupers, P.1    Ter Haar, E.2    Boll, W.3    Kirchhausen, T.4
  • 22
    • 0033967923 scopus 로고    scopus 로고
    • Peptide-in-groove interactions link target proteins to the β-propeller of clathrin
    • Describes the molecular detail of the binding of the clathrin box motif to the clathrin heavy chain amino-terminal β-propellor for the first time.
    • Ter Haar E., Harrison S.C., Kirchhausen T. Peptide-in-groove interactions link target proteins to the β-propeller of clathrin. Proc Natl Acad Sci USA. 97:2000;1096-1100. Describes the molecular detail of the binding of the clathrin box motif to the clathrin heavy chain amino-terminal β-propellor for the first time.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1096-1100
    • Ter Haar, E.1    Harrison, S.C.2    Kirchhausen, T.3
  • 23
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine based endocytic signals
    • Owen D.J., Evans P.R. A structural explanation for the recognition of tyrosine based endocytic signals. Science. 282:1998;1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 24
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A β-propeller terminal domain joins an α zigzag linker
    • Ter Haar E., Musacchio A., Harrison S.C., Kirchhausen T. Atomic structure of clathrin: a β-propeller terminal domain joins an α zigzag linker. Cell. 95:1998;563-573.
    • (1998) Cell , vol.95 , pp. 563-573
    • Ter Haar, E.1    Musacchio, A.2    Harrison, S.C.3    Kirchhausen, T.4
  • 26
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • Das A.K., Cohen P.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17:1998;1192-1199.
    • (1998) EMBO J , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.W.2    Barford, D.3
  • 27
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman G.B., Krupnick J.G., Gurevich V.V., Benovic J.L., Keen J.H. Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. J Biol Chem. 272:1997;15017-15022.
    • (1997) J Biol Chem , vol.272 , pp. 15017-15022
    • Goodman, G.B.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 29
    • 0033153279 scopus 로고    scopus 로고
    • Functional organization of clathrin in coats: Combining cryo electron microscopy and X-ray crystallography
    • This paper describes the fitting the structure of the amino-terminal domain of clathrin determined by X-ray crystallography into the single particle EM reconstruction of a hexagonal clathrin barrel.
    • Musacchio A., Smith C.J., Roseman A.M., Harrison S.C., Kirchhausen T., Pearse B.M.F. Functional organization of clathrin in coats: combining cryo electron microscopy and X-ray crystallography. Mol Cell. 3:1999;761-770. This paper describes the fitting the structure of the amino-terminal domain of clathrin determined by X-ray crystallography into the single particle EM reconstruction of a hexagonal clathrin barrel.
    • (1999) Mol Cell , vol.3 , pp. 761-770
    • Musacchio, A.1    Smith, C.J.2    Roseman, A.M.3    Harrison, S.C.4    Kirchhausen, T.5    Pearse, B.M.F.6
  • 30
    • 0033620656 scopus 로고    scopus 로고
    • Dell'Angelica EMolecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino J.S. Dell'Angelica EMolecular bases for the recognition of tyrosine-based sorting signals. J Cell Biol. 145:1999;923-926.
    • (1999) J Cell Biol , vol.145 , pp. 923-926
    • Bonifacino, J.S.1
  • 31
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site
    • Rapoport I., Chen Y.C., Cupers P., Shoelson S.E., Kirchhausen T. Dileucine-based sorting signals bind to the β chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J. 17:1998;2148-2155.
    • (1998) EMBO J , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 32
    • 0025635559 scopus 로고
    • Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis
    • Collawn J.F., Stangel M., Kuhn L.A., Esekogwu V., Jing S.Q., Trowbridge I.S., Tainer J.A. Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis. Cell. 63:1990;1061-1072.
    • (1990) Cell , vol.63 , pp. 1061-1072
    • Collawn, J.F.1    Stangel, M.2    Kuhn, L.A.3    Esekogwu, V.4    Jing, S.Q.5    Trowbridge, I.S.6    Tainer, J.A.7
  • 33
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison S.C. Peptide-surface association: the case of PDZ and PTB domains. Cell. 86:1996;341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 34
    • 0032476017 scopus 로고    scopus 로고
    • The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals
    • Ohno H., Aguilar R.C., Yeh D., Taura D., Saito T., Bonifacino J.S. The medium subunits of adaptor complexes recognize distinct but overlapping sets of tyrosine-based sorting signals. J Biol Chem. 273:1998;25915-25921.
    • (1998) J Biol Chem , vol.273 , pp. 25915-25921
    • Ohno, H.1    Aguilar, R.C.2    Yeh, D.3    Taura, D.4    Saito, T.5    Bonifacino, J.S.6
  • 35
    • 0033522506 scopus 로고    scopus 로고
    • Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant μ2 subunit and its effects on endocytosis
    • An example of the design of specific point mutations that interfere with function.
    • Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A. Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant μ2 subunit and its effects on endocytosis. EMBO J. 18:1999;2489-2499. An example of the design of specific point mutations that interfere with function.
    • (1999) EMBO J , vol.18 , pp. 2489-2499
    • Nesterov, A.1    Carter, R.E.2    Sorkina, T.3    Gill, G.N.4    Sorkin, A.5
  • 36
    • 0033529768 scopus 로고    scopus 로고
    • Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly
    • Traub L.M., Downs M.A., Westrich J.L., Fremont D.H. Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly. Proc Natl Acad Sci USA. 96:1999;8907-8912.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8907-8912
    • Traub, L.M.1    Downs, M.A.2    Westrich, J.L.3    Fremont, D.H.4
  • 37
    • 0033280324 scopus 로고    scopus 로고
    • Adaptors for clathrin-mediated traffic
    • Kirchhausen T. Adaptors for clathrin-mediated traffic. Annu Rev Cell Dev Biol. 15:1999;705-732.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 705-732
    • Kirchhausen, T.1
  • 38
    • 0032489873 scopus 로고    scopus 로고
    • Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis
    • Wendland B., Emr S.D. Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates protein-protein interactions essential for endocytosis. J Cell Biol. 141:1998;71-84.
    • (1998) J Cell Biol , vol.141 , pp. 71-84
    • Wendland, B.1    Emr, S.D.2
  • 39
    • 0033622305 scopus 로고    scopus 로고
    • Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis
    • Tang H.Y., Xu J., Cai M. Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Mol Cell Biol. 20:2000;12-25.
    • (2000) Mol Cell Biol , vol.20 , pp. 12-25
    • Tang, H.Y.1    Xu, J.2    Cai, M.3
  • 40
    • 0031974491 scopus 로고    scopus 로고
    • Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral
    • Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A. Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. J Biol Chem. 273:1998;814-821.
    • (1998) J Biol Chem , vol.273 , pp. 814-821
    • Ikeda, M.1    Ishida, O.2    Hinoi, T.3    Kishida, S.4    Kikuchi, A.5
  • 41
    • 0032845769 scopus 로고    scopus 로고
    • γ-synergin: An EH domain-containing protein that interacts with γ-adaptin
    • Page, L. J., Sowerby, P. J., Lui, W. W. and Robinson, M. S. γ-synergin: an EH domain-containing protein that interacts with γ-adaptin. J Cell Biol 146:993-104.
    • J Cell Biol , vol.146 , pp. 993-104
    • Page, L.J.1    Sowerby, P.J.2    Lui, W.W.3    Robinson, M.S.4
  • 42
    • 0032575695 scopus 로고    scopus 로고
    • Structure and asn-pro-phe binding pocket of the Eps15 homology domain
    • De Beer T., Carter R.E., Lobel-Rice K.E., Sorkin A., Overduin M. Structure and asn-pro-phe binding pocket of the Eps15 homology domain. Science. 281:1998;1357-1360.
    • (1998) Science , vol.281 , pp. 1357-1360
    • De Beer, T.1    Carter, R.E.2    Lobel-Rice, K.E.3    Sorkin, A.4    Overduin, M.5
  • 44
    • 0033621184 scopus 로고    scopus 로고
    • The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins
    • Whitehead B., Tessari M., Carotenuto A., van Bergen en Henegouwen P.M., Vuister G.W. The EH1 domain of Eps15 is structurally classified as a member of the S100 subclass of EF-hand-containing proteins. Biochemistry. 38:1999;11271-11277.
    • (1999) Biochemistry , vol.38 , pp. 11271-11277
    • Whitehead, B.1    Tessari, M.2    Carotenuto, A.3    Van Bergen En Henegouwen, P.M.4    Vuister, G.W.5
  • 45
    • 0032908611 scopus 로고    scopus 로고
    • Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)
    • Koshiba S., Kigawa T., Iwahara J., Kikuchi A., Yokoyama S. Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1). FEBS Lett. 442:1999;138-142.
    • (1999) FEBS Lett , vol.442 , pp. 138-142
    • Koshiba, S.1    Kigawa, T.2    Iwahara, J.3    Kikuchi, A.4    Yokoyama, S.5
  • 46
    • 0031214092 scopus 로고    scopus 로고
    • Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain
    • Wigge P., Vallis Y., McMahon H.T. Inhibition of receptor-mediated endocytosis by the amphiphysin SH3 domain. Curr Biol. 7:1997;554-560.
    • (1997) Curr Biol , vol.7 , pp. 554-560
    • Wigge, P.1    Vallis, Y.2    McMahon, H.T.3
  • 48
    • 0032530315 scopus 로고    scopus 로고
    • Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation
    • Owen D.J., Wigge P., Vallis Y., Moore J.D.A., Evans P.R., McMahon H.T. Crystal structure of the amphiphysin-2 SH3 domain and its role in the prevention of dynamin ring formation. EMBO J. 17:1998;5273-5285.
    • (1998) EMBO J , vol.17 , pp. 5273-5285
    • Owen, D.J.1    Wigge, P.2    Vallis, Y.3    Moore, J.D.A.4    Evans, P.R.5    McMahon, H.T.6
  • 49
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim W.A., Richards F.M., Fox R.O. Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature. 372:1994;375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 50
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio A., Saraste M., Wilmanns M. High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides. Nat Struct Biol. 1:1994;546-551.
    • (1994) Nat Struct Biol , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 51
    • 0033005568 scopus 로고    scopus 로고
    • Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery
    • Kay B.K., Yamabhai M., Wendland B., Emr S.D. Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery. Protein Sci. 8:1999;435-438.
    • (1999) Protein Sci , vol.8 , pp. 435-438
    • Kay, B.K.1    Yamabhai, M.2    Wendland, B.3    Emr, S.D.4
  • 52
    • 0033575748 scopus 로고    scopus 로고
    • Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis
    • Wendland B., Steece K.E., Emr S.D. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis. EMBO J. 18:1999;4383-4393.
    • (1999) EMBO J , vol.18 , pp. 4383-4393
    • Wendland, B.1    Steece, K.E.2    Emr, S.D.3
  • 53
    • 0034192540 scopus 로고    scopus 로고
    • Epsin1 undergoes nucleocytosolic shuttling and its ENTH domain, structurally similar to armadillo and HEAT repeats, interacts with the transcription factor PLZF
    • Hyman J., Chen H., Di Fiore P.P., De Camilli P., Brunger A.T. Epsin1 undergoes nucleocytosolic shuttling and its ENTH domain, structurally similar to armadillo and HEAT repeats, interacts with the transcription factor PLZF. J Cell Biol. 149:2000;537-546.
    • (2000) J Cell Biol , vol.149 , pp. 537-546
    • Hyman, J.1    Chen, H.2    Di Fiore, P.P.3    De Camilli, P.4    Brunger, A.T.5
  • 54
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of β-catenin
    • Huber A.H., Nelson W.J., Weiss W.I. Three-dimensional structure of the armadillo repeat region of β-catenin. Cell. 90:1997;871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weiss, W.I.3
  • 55
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α
    • Conti E., Uy M., Leighton L., Blobel G., Kuriyan J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α Cell. 94:1998;193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 56
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-β2-RanGppNHp
    • Chook Y.M., Blobel G. Structure of the nuclear transport complex karyopherin-β2-RanGppNHp. Nature. 399:1999;230-237.
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 57
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • Cingolani G., Petosa C., Weiss K., Muller C.W. Structure of importin-β bound to the IBB domain of importin-α Nature. 399:1999;221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weiss, K.3    Muller, C.W.4
  • 58
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2.3 Å resolution
    • Vetter I.R., Arndt A., Kutay U., Gorlich D., Wittinghoffer A. Structural view of the Ran-importin β interaction at 2.3 Å resolution. Cell. 97:1999;635-646.
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Gorlich, D.4    Wittinghoffer, A.5
  • 59
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • Mao Y., Nickitenko A., Duan X., Lloyd T.E., Wu M.N., Bellen H., Quiocho F.A. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell. 100:2000;447-456.
    • (2000) Cell , vol.100 , pp. 447-456
    • Mao, Y.1    Nickitenko, A.2    Duan, X.3    Lloyd, T.E.4    Wu, M.N.5    Bellen, H.6    Quiocho, F.A.7
  • 61
    • 0033545698 scopus 로고    scopus 로고
    • Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis
    • Vallis Y., Wigge P., Marks B., Evans P.R., McMahon H.T. Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis. Curr Biol. 9:1999;257-260.
    • (1999) Curr Biol , vol.9 , pp. 257-260
    • Vallis, Y.1    Wigge, P.2    Marks, B.3    Evans, P.R.4    McMahon, H.T.5
  • 62
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw J.E., Schmid S.L. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature. 374:1995;190-192.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.