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Volumn 10, Issue 2, 2000, Pages 220-228

Clathrin coat construction in endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CLATHRIN;

EID: 0034116722     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00071-3     Document Type: Review
Times cited : (101)

References (76)
  • 2
    • 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
  • 4
    • 0032807691 scopus 로고    scopus 로고
    • Clathrin assembly lymphoid myeloid leukemia (CALM) protein: Localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic
    • Tebar F., Bohlander S.K., Sorkin A. Clathrin assembly lymphoid myeloid leukemia (CALM) protein. localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic Mol Biol Cell. 10:1999;2687-2702.
    • (1999) Mol Biol Cell , vol.10 , pp. 2687-2702
    • Tebar, F.1    Bohlander, S.K.2    Sorkin, A.3
  • 5
    • 0015619310 scopus 로고
    • Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction
    • Heuser J.E., Reese T.S. Evidence for recycling of synaptic vesicle membrane during transmitter release at the frog neuromuscular junction. J Cell Biol. 57:1973;315-344.
    • (1973) J Cell Biol , vol.57 , pp. 315-344
    • Heuser, J.E.1    Reese, T.S.2
  • 7
    • 0033153460 scopus 로고    scopus 로고
    • Optical detection of synaptic vesicle exocytosis and endocytosis
    • Murthy V.N. Optical detection of synaptic vesicle exocytosis and endocytosis. Curr Opin Neurobiol. 9:1999;314-320.
    • (1999) Curr Opin Neurobiol , vol.9 , pp. 314-320
    • Murthy, V.N.1
  • 8
    • 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
  • 9
    • 0033538576 scopus 로고    scopus 로고
    • The structural era of endocytosis
    • Marsh M., McMahon H.T. The structural era of endocytosis. Science. 285:1999;215-220.
    • (1999) Science , vol.285 , pp. 215-220
    • Marsh, M.1    McMahon, H.T.2
  • 10
    • 0032878703 scopus 로고    scopus 로고
    • Clathrin: Anatomy of a coat protein
    • Smith C.J., Pearse B.M. Clathrin. anatomy of a coat protein Trends Cell Biol. 9:1999;335-338.
    • (1999) Trends Cell Biol , vol.9 , pp. 335-338
    • Smith, C.J.1    Pearse, B.M.2
  • 11
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A beta propeller terminal domain joins an alpha zigzag linker
    • ter Haar E., Musacchio A., Harrison S.C., Kirchhausen T. Atomic structure of clathrin. a beta propeller terminal domain joins an alpha 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
  • 12
    • 0033153279 scopus 로고    scopus 로고
    • Functional organization of clathrin in coats: Combining cryo-electron microscopy and X-ray crystallography
    • 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.
    • (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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0033000498 scopus 로고    scopus 로고
    • A structural explanation for the binding of multiple ligands by the alpha-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 alpha-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
  • 18
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel J.J., Wiley D.C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell. 95:1998;871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 19
    • 0026727853 scopus 로고
    • Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling
    • Maycox P.R., Link E., Reetz A., Morris S.A., Jahn R. Clathrin-coated vesicles in nervous tissue are involved primarily in synaptic vesicle recycling. J Cell Biol. 118:1992;1379-1388.
    • (1992) J Cell Biol , vol.118 , pp. 1379-1388
    • Maycox, P.R.1    Link, E.2    Reetz, A.3    Morris, S.A.4    Jahn, R.5
  • 20
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer S.R. Transport-vesicle targeting. tethers before SNAREs Nat Cell Biol. 1:1999;17-22.
    • (1999) Nat Cell Biol , vol.1 , pp. 17-22
    • Pfeffer, S.R.1
  • 21
    • 0033529564 scopus 로고    scopus 로고
    • Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13
    • McBride H.M., Rybin V., Murphy C., Giner A., Teasdale R., Zerial M. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell. 98:1999;377-386.
    • (1999) Cell , vol.98 , pp. 377-386
    • McBride, H.M.1    Rybin, V.2    Murphy, C.3    Giner, A.4    Teasdale, R.5    Zerial, M.6
  • 22
    • 0033609083 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes
    • Zhu Y., Drake M.T., Kornfeld S. ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes. Proc Natl Acad Sci USA. 96:1999;5013-5018.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5013-5018
    • Zhu, Y.1    Drake, M.T.2    Kornfeld, S.3
  • 24
    • 0033574678 scopus 로고    scopus 로고
    • A primer on vesicle budding
    • Springer S., Spang A., Schekman R. A primer on vesicle budding. Cell. 97:1999;145-148.
    • (1999) Cell , vol.97 , pp. 145-148
    • Springer, S.1    Spang, A.2    Schekman, R.3
  • 25
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell. 95:1998;237-248.
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 26
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1 ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • A single author making a breakthrough in understanding in the complex field of sorting in the Golgi region.
    • Goldberg J. Structural and functional analysis of the ARF1 ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell. 96:1999;893-902. A single author making a breakthrough in understanding in the complex field of sorting in the Golgi region.
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 28
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats- purification of an uncoating ATPase
    • Schlossman D.M., Schmid S.L., Braell W.A., Rothman J.E. An enzyme that removes clathrin coats- purification of an uncoating ATPase. J Cell Biol. 99:1984;723-733.
    • (1984) J Cell Biol , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Braell, W.A.3    Rothman, J.E.4
  • 29
    • 0024433249 scopus 로고
    • Trimeric binding of the 70-Kd uncoating ATPase to the vertices of clathrin triskelia - A candidate intermediate in the vesicle uncoating reaction
    • Heuser J., Steer C.J. Trimeric binding of the 70-Kd uncoating ATPase to the vertices of clathrin triskelia - a candidate intermediate in the vesicle uncoating reaction. J Cell Biol. 109:1989;1457-1466.
    • (1989) J Cell Biol , vol.109 , pp. 1457-1466
    • Heuser, J.1    Steer, C.J.2
  • 30
    • 0031595549 scopus 로고    scopus 로고
    • An arf1Δ synthetic lethal screen identifies a new clathrin heavy chain conditional allele that perturbs vacuolar protein transport in Saccharomyces cerevisiae
    • Chen C.Y., Graham T.R. An arf1Δ synthetic lethal screen identifies a new clathrin heavy chain conditional allele that perturbs vacuolar protein transport in Saccharomyces cerevisiae. Genetics. 150:1998;577-589.
    • (1998) Genetics , vol.150 , pp. 577-589
    • Chen, C.Y.1    Graham, T.R.2
  • 31
    • 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
  • 33
    • 0033202889 scopus 로고    scopus 로고
    • Formation of AP-3 transport intermediates requires Vps41p function
    • Rehling P., Darsow T., Katzmann D.J., Emr S.D. Formation of AP-3 transport intermediates requires Vps41p function. Nat Cell Biol. 1:1999;346-353.
    • (1999) Nat Cell Biol , vol.1 , pp. 346-353
    • Rehling, P.1    Darsow, T.2    Katzmann, D.J.3    Emr, S.D.4
  • 34
    • 12644259509 scopus 로고    scopus 로고
    • Arrestin/clathrin interaction - Localization of the arrestin binding locus to the clathrin terminal domain
    • Goodman O.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, O.B.1    Krupnick, J.G.2    Gurevich, V.V.3    Benovic, J.L.4    Keen, J.H.5
  • 35
    • 0032568021 scopus 로고    scopus 로고
    • X-ray crystal structure of arrestin from bovine rod outer segments
    • Granzin J., Wilden U., Choe H.W., Labahn J., Krafft B., Buldt G. X-ray crystal structure of arrestin from bovine rod outer segments. Nature. 391:1998;918-921.
    • (1998) Nature , vol.391 , pp. 918-921
    • Granzin, J.1    Wilden, U.2    Choe, H.W.3    Labahn, J.4    Krafft, B.5    Buldt, G.6
  • 40
    • 0022780984 scopus 로고
    • Location of the 100 Kd-50 Kd accessory proteins in clathrin coats
    • Vigers G.P.A., Crowther R.A., Pearse B.M.F. Location of the 100 Kd-50 Kd accessory proteins in clathrin coats. EMBO J. 5:1986;2079-2085.
    • (1986) EMBO J , vol.5 , pp. 2079-2085
    • Vigers, G.P.A.1    Crowther, R.A.2    Pearse, B.M.F.3
  • 41
    • 0021487739 scopus 로고
    • Purification and properties of 100-Kd proteins from coated vesicles and their reconstitution with clathrin
    • Pearse B.M.F., Robinson M.S. Purification and properties of 100-Kd proteins from coated vesicles and their reconstitution with clathrin. EMBO J. 3:1984;1951-1957.
    • (1984) EMBO J , vol.3 , pp. 1951-1957
    • Pearse, B.M.F.1    Robinson, M.S.2
  • 42
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and the plasma-membrane
    • Ahle S., Mann A., Eichelsbacher U., Ungewickell E. Structural relationships between clathrin assembly proteins from the Golgi and the plasma-membrane. EMBO J. 7:1988;919-929.
    • (1988) EMBO J , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickell, E.4
  • 44
    • 0033007616 scopus 로고    scopus 로고
    • Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor
    • Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A., Bonifacino J.S. Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor. Mol Cell. 3:1999;11-21.
    • (1999) Mol Cell , vol.3 , pp. 11-21
    • Dell'Angelica, E.C.1    Shotelersuk, V.2    Aguilar, R.C.3    Gahl, W.A.4    Bonifacino, J.S.5
  • 45
    • 0032784330 scopus 로고    scopus 로고
    • Characterization of a fourth adaptor-related protein complex
    • Hirst J., Bright N.A., Rous B., Robinson M.S. Characterization of a fourth adaptor-related protein complex. Mol Biol Cell. 10:1999;2787-2802.
    • (1999) Mol Biol Cell , vol.10 , pp. 2787-2802
    • Hirst, J.1    Bright, N.A.2    Rous, B.3    Robinson, M.S.4
  • 46
    • 0033548575 scopus 로고    scopus 로고
    • AP-4, a novel protein complex related to clathrin adaptors
    • Dell'Angelica E.C., Mullins C., Bonifacino J.S. AP-4, a novel protein complex related to clathrin adaptors. J Biol Chem. 274:1999;7278-7285.
    • (1999) J Biol Chem , vol.274 , pp. 7278-7285
    • Dell'Angelica, E.C.1    Mullins, C.2    Bonifacino, J.S.3
  • 47
    • 0024075871 scopus 로고
    • Deep-etch visualization of proteins involved in clathrin assembly
    • Heuser J.E., Keen J. 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.2
  • 48
    • 0029584896 scopus 로고
    • A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes
    • Shih W., Gallusser A., Kirchhausen T. A clathrin-binding site in the hinge of the beta 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
  • 52
    • 0032488027 scopus 로고    scopus 로고
    • A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor
    • Bresnahan P.A., Yonemoto W., Ferrell S., Williams-Herman D., Geleziunas R., Greene W.C. A dileucine motif in HIV-1 Nef acts as an internalization signal for CD4 downregulation and binds the AP-1 clathrin adaptor. Curr Biol. 8:1998;1235-1238.
    • (1998) Curr Biol , vol.8 , pp. 1235-1238
    • Bresnahan, P.A.1    Yonemoto, W.2    Ferrell, S.3    Williams-Herman, D.4    Geleziunas, R.5    Greene, W.C.6
  • 53
    • 0033568211 scopus 로고    scopus 로고
    • Cutting edge: SIV Nef protein utilizes both leucine- And tyrosine-based protein sorting pathways for down-regulation of CD4
    • Bresnahan P.A., Yonemoto W., Greene W.C. Cutting edge: SIV Nef protein utilizes both leucine- and tyrosine-based protein sorting pathways for down-regulation of CD4. J Immunol. 163:1999;2977-2981.
    • (1999) J Immunol , vol.163 , pp. 2977-2981
    • Bresnahan, P.A.1    Yonemoto, W.2    Greene, W.C.3
  • 54
    • 0032488055 scopus 로고    scopus 로고
    • A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4
    • Greenberg M., DeTulleo L., Rapoport I., Skowronski J., Kirchhausen T. A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4. Curr Biol. 8:1998;1239-1242.
    • (1998) Curr Biol , vol.8 , pp. 1239-1242
    • Greenberg, M.1    DeTulleo, L.2    Rapoport, I.3    Skowronski, J.4    Kirchhausen, T.5
  • 55
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the beta 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 beta 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
  • 56
    • 0026315047 scopus 로고
    • The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation
    • Bansal A., Gierasch L.M. The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell. 67:1991;1195-1201.
    • (1991) Cell , vol.67 , pp. 1195-1201
    • Bansal, A.1    Gierasch, L.M.2
  • 57
    • 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
  • 59
    • 0030917081 scopus 로고    scopus 로고
    • Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2
    • Shiratori T., Miyatake S., Ohno H., Nakaseko C., Isono K., Bonifacino J.S., Saito T. Tyrosine phosphorylation controls internalization of CTLA-4 by regulating its interaction with clathrin-associated adaptor complex AP-2. Immunity. 6:1997;583-589.
    • (1997) Immunity , vol.6 , pp. 583-589
    • Shiratori, T.1    Miyatake, S.2    Ohno, H.3    Nakaseko, C.4    Isono, K.5    Bonifacino, J.S.6    Saito, T.7
  • 60
    • 15844361829 scopus 로고    scopus 로고
    • The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps15 protein
    • Benmerah A., Begue B., Dautry-Varsat A., Cerf-Bensussan N. The ear of alpha-adaptin interacts with the COOH-terminal domain of the Eps15 protein. J Biol Chem. 271:1996;12111-12116.
    • (1996) J Biol Chem , vol.271 , pp. 12111-12116
    • Benmerah, A.1    Begue, B.2    Dautry-Varsat, A.3    Cerf-Bensussan, N.4
  • 62
    • 0033529056 scopus 로고    scopus 로고
    • Endocytosis: An assembly protein for clathrin cages
    • McMahon H.T. Endocytosis. an assembly protein for clathrin cages Curr Biol. 9:1999;332-335.
    • (1999) Curr Biol , vol.9 , pp. 332-335
    • McMahon, H.T.1
  • 63
    • 0032937170 scopus 로고    scopus 로고
    • Clathrin: A good view of a shapely leg
    • Ungewickell E. Clathrin. a good view of a shapely leg Curr Biol. 9:1999;32-35.
    • (1999) Curr Biol , vol.9 , pp. 32-35
    • Ungewickell, E.1
  • 64
    • 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
  • 65
    • 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
  • 67
    • 0033611490 scopus 로고    scopus 로고
    • Endocytosis: EH domains lend a hand
    • Mayer B.J. Endocytosis: EH domains lend a hand. Curr Biol. 9:1999;70-73.
    • (1999) Curr Biol , vol.9 , pp. 70-73
    • Mayer, B.J.1
  • 68
    • 0033106167 scopus 로고    scopus 로고
    • The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15
    • Sengar A.S., Wang W., Bishay J., Cohen S., Egan S.E. The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15. EMBO J. 18:1999;1159-1171.
    • (1999) EMBO J , vol.18 , pp. 1159-1171
    • Sengar, A.S.1    Wang, W.2    Bishay, J.3    Cohen, S.4    Egan, S.E.5
  • 71
    • 0006857840 scopus 로고    scopus 로고
    • New twists for dynamin
    • Kelly R.B. New twists for dynamin. Nat Cell Biol. 1:1999;8-9.
    • (1999) Nat Cell Biol , vol.1 , pp. 8-9
    • Kelly, R.B.1
  • 72
    • 0033539180 scopus 로고    scopus 로고
    • Lipid membranes shape up
    • Scales S.J., Scheller R.H. Lipid membranes shape up. Nature. 401:1999;123-124.
    • (1999) Nature , vol.401 , pp. 123-124
    • Scales, S.J.1    Scheller, R.H.2
  • 73
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell M.H.B., Marks B., Wigge P., McMahon H.T. Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat Cell Biol. 1:1999;27-32.
    • (1999) Nat Cell Biol , vol.1 , pp. 27-32
    • Stowell, M.H.B.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 74
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei T., Slepnev V.I., Haucke V., De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat Cell Biol. 1:1999;33-39.
    • (1999) Nat Cell Biol , vol.1 , pp. 33-39
    • Takei, T.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 75
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
    • Sever S., Muhlberg A.B., Schmid S.L. Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature. 398:1999;481-486.
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.