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Volumn 12, Issue 7, 2016, Pages

Static Clathrin Assemblies at the Peripheral Vacuole—Plasma Membrane Interface of the Parasitic Protozoan Giardia lamblia

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN ASSEMBLY PROTEIN; CLATHRIN HEAVY CHAIN; CLATHRIN LIGHT CHAIN; DYNAMIN; LIPID BINDING PROTEIN; PHOSPHOLIPID BINDING PROTEIN; CLATHRIN;

EID: 84982953409     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005756     Document Type: Article
Times cited : (39)

References (102)
  • 1
    • 84908503140 scopus 로고    scopus 로고
    • Immunological aspects of Giardia infections
    • 25347704, .,.: p.
    • Heyworth M.F., Immunological aspects of Giardia infections. Parasite, 2014. 21: p. 55. doi: 10.1051/parasite/201405625347704
    • (2014) Parasite , vol.21 , pp. 55
    • Heyworth, M.F.1
  • 2
    • 33947425595 scopus 로고    scopus 로고
    • Cell division of Giardia intestinalis: assembly and disassembly of the adhesive disc, and the cytokinesis
    • 17205565, .,.(): p.–.
    • Tumova P., Kulda J., Nohynkova E., Cell division of Giardia intestinalis: assembly and disassembly of the adhesive disc, and the cytokinesis. Cell motility and the cytoskeleton, 2007. 64(4): p. 288–98. 17205565
    • (2007) Cell motility and the cytoskeleton , vol.64 , Issue.4 , pp. 288-298
    • Tumova, P.1    Kulda, J.2    Nohynkova, E.3
  • 3
    • 37249064198 scopus 로고    scopus 로고
    • The single dynamin family protein in the primitive protozoan Giardia lamblia is essential for stage conversion and endocytic transport
    • 17892527, .,.,.(): p.–.
    • Gaechter V., et al., The single dynamin family protein in the primitive protozoan Giardia lamblia is essential for stage conversion and endocytic transport. Traffic, 2008. 9(1): p. 57–71. 17892527
    • (2008) Traffic , vol.9 , Issue.1 , pp. 57-71
    • Gaechter, V.1
  • 4
    • 0032215218 scopus 로고    scopus 로고
    • The peripheral vesicles of trophozoites of the primitive protozoan Giardia lamblia may correspond to early and late endosomes and to lysosomes
    • 9878577, .,.,.(): p.–.
    • Lanfredi-Rangel A., et al., The peripheral vesicles of trophozoites of the primitive protozoan Giardia lamblia may correspond to early and late endosomes and to lysosomes. Journal of structural biology, 1998. 123(3): p. 225–35. 9878577
    • (1998) Journal of structural biology , vol.123 , Issue.3 , pp. 225-235
    • Lanfredi-Rangel, A.1
  • 5
    • 43049100037 scopus 로고    scopus 로고
    • Release of metabolic enzymes by Giardia in response to interaction with intestinal epithelial cells
    • 18359106, .,.,.(): p.–.
    • Ringqvist E., et al., Release of metabolic enzymes by Giardia in response to interaction with intestinal epithelial cells. Molecular and biochemical parasitology, 2008. 159(2): p. 85–91. doi: 10.1016/j.molbiopara.2008.02.00518359106
    • (2008) Molecular and biochemical parasitology , vol.159 , Issue.2 , pp. 85-91
    • Ringqvist, E.1
  • 6
    • 0028153085 scopus 로고
    • Giardia lamblia: traffic of a trophozoite variant surface protein and a major cyst wall epitope during growth, encystation, and antigenic switching
    • 7525336, .,.(): p.–.
    • McCaffery J.M., Faubert G.M., Gillin F.D., Giardia lamblia: traffic of a trophozoite variant surface protein and a major cyst wall epitope during growth, encystation, and antigenic switching. Experimental parasitology, 1994. 79(3): p. 236–49. 7525336
    • (1994) Experimental parasitology , vol.79 , Issue.3 , pp. 236-249
    • McCaffery, J.M.1    Faubert, G.M.2    Gillin, F.D.3
  • 7
    • 0036072751 scopus 로고    scopus 로고
    • Dephosphorylation of cyst wall proteins by a secreted lysosomal acid phosphatase is essential for excystation of Giardia lamblia
    • 12076774, .,.,.(): p.–.
    • Slavin I., et al., Dephosphorylation of cyst wall proteins by a secreted lysosomal acid phosphatase is essential for excystation of Giardia lamblia. Molecular and biochemical parasitology, 2002. 122(1): p. 95–8. 12076774
    • (2002) Molecular and biochemical parasitology , vol.122 , Issue.1 , pp. 95-98
    • Slavin, I.1
  • 8
    • 0037884975 scopus 로고    scopus 로고
    • The secretory apparatus of an ancient eukaryote: protein sorting to separate export pathways occurs before formation of transient Golgi-like compartments
    • 12686599, .,.,.(): p.–.
    • Marti M., et al., The secretory apparatus of an ancient eukaryote: protein sorting to separate export pathways occurs before formation of transient Golgi-like compartments. Molecular biology of the cell, 2003. 14(4): p. 1433–47. 12686599
    • (2003) Molecular biology of the cell , vol.14 , Issue.4 , pp. 1433-1447
    • Marti, M.1
  • 9
    • 0030952807 scopus 로고    scopus 로고
    • A primitive enzyme for a primitive cell: the protease required for excystation of Giardia
    • 9150143, .,.,.(): p.–.
    • Ward W., et al., A primitive enzyme for a primitive cell: the protease required for excystation of Giardia. Cell, 1997. 89(3): p. 437–44. 9150143
    • (1997) Cell , vol.89 , Issue.3 , pp. 437-444
    • Ward, W.1
  • 10
    • 84955173009 scopus 로고    scopus 로고
    • Forty Years of Clathrin-coated Vesicles
    • 26403691, .,.(): p.–.
    • Robinson M.S., Forty Years of Clathrin-coated Vesicles. Traffic, 2015. 16(12): p. 1210–38. doi: 10.1111/tra.1233526403691
    • (2015) Traffic , vol.16 , Issue.12 , pp. 1210-1238
    • Robinson, M.S.1
  • 11
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • 21779028, .,.(): p.–.
    • McMahon H.T., Boucrot E., Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nature reviews. Molecular cell biology, 2011. 12(8): p. 517–33. doi: 10.1038/nrm315121779028
    • (2011) Nature reviews. Molecular cell biology , vol.12 , Issue.8 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 12
    • 0022095974 scopus 로고
    • Deep-etch views of clathrin assemblies
    • 2870198, .,.(): p.–.
    • Heuser J., Kirchhausen T., Deep-etch views of clathrin assemblies. Journal of ultrastructure research, 1985. 92(1–2): p. 1–27. 2870198
    • (1985) Journal of ultrastructure research , vol.92 , Issue.1-2 , pp. 1-27
    • Heuser, J.1    Kirchhausen, T.2
  • 13
    • 14844331402 scopus 로고    scopus 로고
    • Visualization of the binding of Hsc70 ATPase to clathrin baskets: implications for an uncoating mechanism
    • 15596443, .,.,.(): p.–.
    • Heymann J.B., et al., Visualization of the binding of Hsc70 ATPase to clathrin baskets: implications for an uncoating mechanism. The Journal of biological chemistry, 2005. 280(8): p. 7156–61. 15596443
    • (2005) The Journal of biological chemistry , vol.280 , Issue.8 , pp. 7156-7161
    • Heymann, J.B.1
  • 14
    • 84933565978 scopus 로고    scopus 로고
    • ENDOCYTOSIS. Endocytic sites mature by continuous bending and remodeling of the clathrin coat
    • 26089517, .,.,.(): p.–.
    • Avinoam O., et al., ENDOCYTOSIS. Endocytic sites mature by continuous bending and remodeling of the clathrin coat. Science, 2015. 348(6241): p. 1369–72. doi: 10.1126/science.aaa955526089517
    • (2015) Science , vol.348 , Issue.6241 , pp. 1369-1372
    • Avinoam, O.1
  • 15
    • 0018827560 scopus 로고
    • Three-dimensional visualization of coated vesicle formation in fibroblasts
    • 6987244, .,.(): p.–.
    • Heuser J., Three-dimensional visualization of coated vesicle formation in fibroblasts. The Journal of cell biology, 1980. 84(3): p. 560–83. 6987244
    • (1980) The Journal of cell biology , vol.84 , Issue.3 , pp. 560-583
    • Heuser, J.1
  • 16
    • 0025799606 scopus 로고
    • Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells
    • .,.(): p.–.
    • Sanan D.A., Anderson R.G., Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells. The journal of histochemistry and cytochemistry: official journal of the Histochemistry Society, 1991. 39(8): p. 1017–24.
    • (1991) The journal of histochemistry and cytochemistry: official journal of the Histochemistry Society , vol.39 , Issue.8 , pp. 1017-1024
    • Sanan, D.A.1    Anderson, R.G.2
  • 17
    • 0020462085 scopus 로고
    • Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane-particle interactions and clathrin
    • 6813339, .,.(): p.–.
    • Aggeler J., Werb Z., Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane-particle interactions and clathrin. The Journal of cell biology, 1982. 94(3): p. 613–23. 6813339
    • (1982) The Journal of cell biology , vol.94 , Issue.3 , pp. 613-623
    • Aggeler, J.1    Werb, Z.2
  • 18
    • 84899704909 scopus 로고    scopus 로고
    • Molecular structure, function, and dynamics of clathrin-mediated membrane traffic
    • 24789820, .,.(): p.
    • Kirchhausen T., Owen D., Harrison S.C., Molecular structure, function, and dynamics of clathrin-mediated membrane traffic. Cold Spring Harbor perspectives in biology, 2014. 6(5): p. a016725. doi: 10.1101/cshperspect.a01672524789820
    • (2014) Cold Spring Harbor perspectives in biology , vol.6 , Issue.5 , pp. a016725
    • Kirchhausen, T.1    Owen, D.2    Harrison, S.C.3
  • 19
    • 77953365536 scopus 로고    scopus 로고
    • Adaptor protein 2 regulates receptor-mediated endocytosis and cyst formation in Giardia lamblia
    • 20199400, .,.,.(): p.–.
    • Rivero M.R., et al., Adaptor protein 2 regulates receptor-mediated endocytosis and cyst formation in Giardia lamblia. The Biochemical journal, 2010. 428(1): p. 33–45. doi: 10.1042/BJ2010009620199400
    • (2010) The Biochemical journal , vol.428 , Issue.1 , pp. 33-45
    • Rivero, M.R.1
  • 20
    • 0034035538 scopus 로고    scopus 로고
    • Stage-specific expression and targeting of cyst wall protein-green fluorescent protein chimeras in Giardia
    • 10793152, .,.(): p.–.
    • Hehl A.B., Marti M., Kohler P., Stage-specific expression and targeting of cyst wall protein-green fluorescent protein chimeras in Giardia. Molecular biology of the cell, 2000. 11(5): p. 1789–800. 10793152
    • (2000) Molecular biology of the cell , vol.11 , Issue.5 , pp. 1789-1800
    • Hehl, A.B.1    Marti, M.2    Kohler, P.3
  • 21
    • 0025047749 scopus 로고
    • Excystation of in vitro-derived Giardia lamblia cysts
    • 2228222, .,.(): p.–.
    • Boucher S.E., Gillin F.D., Excystation of in vitro-derived Giardia lamblia cysts. Infection and immunity, 1990. 58(11): p. 3516–22. 2228222
    • (1990) Infection and immunity , vol.58 , Issue.11 , pp. 3516-3522
    • Boucher, S.E.1    Gillin, F.D.2
  • 22
    • 77957816717 scopus 로고    scopus 로고
    • The transcriptional response to encystation stimuli in Giardia lamblia is restricted to a small set of genes
    • 20693303, .,.,.(): p.–.
    • Morf L., et al., The transcriptional response to encystation stimuli in Giardia lamblia is restricted to a small set of genes. Eukaryotic cell, 2010. 9(10): p. 1566–76. doi: 10.1128/EC.00100-1020693303
    • (2010) Eukaryotic cell , vol.9 , Issue.10 , pp. 1566-1576
    • Morf, L.1
  • 23
    • 70350007287 scopus 로고    scopus 로고
    • Neogenesis and maturation of transient Golgi-like cisternae in a simple eukaryote
    • 19622633, .,.,.(): p.–.
    • Stefanic S., et al., Neogenesis and maturation of transient Golgi-like cisternae in a simple eukaryote. Journal of cell science, 2009. 122(Pt 16): p. 2846–56. doi: 10.1242/jcs.04941119622633
    • (2009) Journal of cell science , vol.122 , pp. 2846-2856
    • Stefanic, S.1
  • 24
    • 48349101285 scopus 로고    scopus 로고
    • Identification of nucleoli in the early branching protist Giardia duodenalis
    • 18625508, .,.,.(): p.–.
    • Jimenez-Garcia L.F., et al., Identification of nucleoli in the early branching protist Giardia duodenalis. International journal for parasitology, 2008. 38(11): p. 1297–304. doi: 10.1016/j.ijpara.2008.04.01218625508
    • (2008) International journal for parasitology , vol.38 , Issue.11 , pp. 1297-1304
    • Jimenez-Garcia, L.F.1
  • 25
    • 34547817697 scopus 로고    scopus 로고
    • Successful co-immunoprecipitation of Oct4 and Nanog using cross-linking
    • 17669361, .,.,.(): p.–.
    • Zhang L., et al., Successful co-immunoprecipitation of Oct4 and Nanog using cross-linking. Biochemical and biophysical research communications, 2007. 361(3): p. 611–4. 17669361
    • (2007) Biochemical and biophysical research communications , vol.361 , Issue.3 , pp. 611-614
    • Zhang, L.1
  • 26
    • 59449092912 scopus 로고    scopus 로고
    • Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal cells
    • 19010779, .,.,.(): p.–.
    • Salazar G., et al., Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase type II alpha in neuronal and non-neuronal cells. The Journal of biological chemistry, 2009. 284(3): p. 1790–802. doi: 10.1074/jbc.M80599120019010779
    • (2009) The Journal of biological chemistry , vol.284 , Issue.3 , pp. 1790-1802
    • Salazar, G.1
  • 27
    • 77951153298 scopus 로고    scopus 로고
    • Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6
    • 19738201, .,.,.(): p.
    • Humphries J.D., et al., Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Science signaling, 2009. 2(87): p. ra51. doi: 10.1126/scisignal.200039619738201
    • (2009) Science signaling , vol.2 , Issue.87 , pp. ra51
    • Humphries, J.D.1
  • 28
    • 79251606813 scopus 로고    scopus 로고
    • ReCLIP (reversible cross-link immuno-precipitation): an efficient method for interrogation of labile protein complexes
    • 21283770, .,.,.(): p.
    • Smith A.L., et al., ReCLIP (reversible cross-link immuno-precipitation): an efficient method for interrogation of labile protein complexes. PloS one, 2011. 6(1): p. e16206. doi: 10.1371/journal.pone.001620621283770
    • (2011) PloS one , vol.6 , Issue.1 , pp. e16206
    • Smith, A.L.1
  • 29
    • 77954060029 scopus 로고    scopus 로고
    • Selective condensation drives partitioning and sequential secretion of cyst wall proteins in differentiating Giardia lamblia
    • 20386711, .,.(): p.
    • Konrad C., Spycher C., Hehl A.B., Selective condensation drives partitioning and sequential secretion of cyst wall proteins in differentiating Giardia lamblia. PLoS pathogens, 2010. 6(4): p. e1000835. doi: 10.1371/journal.ppat.100083520386711
    • (2010) PLoS pathogens , vol.6 , Issue.4 , pp. e1000835
    • Konrad, C.1    Spycher, C.2    Hehl, A.B.3
  • 30
    • 84976871411 scopus 로고    scopus 로고
    • 2016 update of the PRIDE database and its related tools
    • 26527722, .,.,.(): p.–.
    • Vizcaino J.A., et al., 2016 update of the PRIDE database and its related tools. Nucleic Acids Res, 2016. 44(D1): p. D447–56. doi: 10.1093/nar/gkv114526527722
    • (2016) Nucleic Acids Res , vol.44 , Issue.D1 , pp. D447-D456
    • Vizcaino, J.A.1
  • 31
    • 77956801705 scopus 로고    scopus 로고
    • Glucosylceramide synthesis inhibition affects cell cycle progression, membrane trafficking, and stage differentiation in Giardia lamblia
    • 20335568, .,.,.(): p.–.
    • Stefanic S., et al., Glucosylceramide synthesis inhibition affects cell cycle progression, membrane trafficking, and stage differentiation in Giardia lamblia. Journal of lipid research, 2010. 51(9): p. 2527–45. doi: 10.1194/jlr.M00339220335568
    • (2010) Journal of lipid research , vol.51 , Issue.9 , pp. 2527-2545
    • Stefanic, S.1
  • 33
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • 20360767, .,.(): p.–.
    • Roy A., Kucukural A., Zhang Y., I-TASSER: a unified platform for automated protein structure and function prediction. Nature protocols, 2010. 5(4): p. 725–38. doi: 10.1038/nprot.2010.520360767
    • (2010) Nature protocols , vol.5 , Issue.4 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 34
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER Suite: protein structure and function prediction
    • 25549265, .,.,.(): p.–.
    • Yang J., et al., The I-TASSER Suite: protein structure and function prediction. Nature methods, 2015. 12(1): p. 7–8. doi: 10.1038/nmeth.321325549265
    • (2015) Nature methods , vol.12 , Issue.1 , pp. 7-8
    • Yang, J.1
  • 35
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • 18215316, .,.: p.
    • Zhang Y., I-TASSER server for protein 3D structure prediction. BMC bioinformatics, 2008. 9: p. 40. doi: 10.1186/1471-2105-9-4018215316
    • (2008) BMC bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1
  • 36
    • 0023734573 scopus 로고
    • Structure of human clathrin light chains. Conservation of light chain polymorphism in three mammalian species
    • 3267234, .,.(): p.–.
    • Jackson A.P., Parham P., Structure of human clathrin light chains. Conservation of light chain polymorphism in three mammalian species. The Journal of biological chemistry, 1988. 263(32): p. 16688–95. 3267234
    • (1988) The Journal of biological chemistry , vol.263 , Issue.32 , pp. 16688-16695
    • Jackson, A.P.1    Parham, P.2
  • 37
    • 33749442647 scopus 로고    scopus 로고
    • MultiSeq: unifying sequence and structure data for evolutionary analysis
    • 16914055, .,.,.: p.
    • Roberts E., et al., MultiSeq: unifying sequence and structure data for evolutionary analysis. BMC Bioinformatics, 2006. 7: p. 382. 16914055
    • (2006) BMC Bioinformatics , vol.7 , pp. 382
    • Roberts, E.1
  • 38
    • 72449160258 scopus 로고    scopus 로고
    • A contiguous compartment functions as endoplasmic reticulum and endosome/lysosome in Giardia lamblia
    • 19749174, .,.,.(): p.–.
    • Abodeely M., et al., A contiguous compartment functions as endoplasmic reticulum and endosome/lysosome in Giardia lamblia. Eukaryotic cell, 2009. 8(11): p. 1665–76. doi: 10.1128/EC.00123-0919749174
    • (2009) Eukaryotic cell , vol.8 , Issue.11 , pp. 1665-1676
    • Abodeely, M.1
  • 39
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • 12215646, .,.,.(): p.–.
    • Doray B., et al., Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science, 2002. 297(5587): p. 1700–3. 12215646
    • (2002) Science , vol.297 , Issue.5587 , pp. 1700-1703
    • Doray, B.1
  • 40
    • 0022392709 scopus 로고
    • Possible pathways for lysosomal enzyme delivery
    • 2933416, .,.,.(): p.–.
    • Geuze H.J., et al., Possible pathways for lysosomal enzyme delivery. J Cell Biol, 1985. 101(6): p. 2253–62. 2933416
    • (1985) J Cell Biol , vol.101 , Issue.6 , pp. 2253-2262
    • Geuze, H.J.1
  • 41
    • 0027210570 scopus 로고
    • Differences in the endosomal distributions of the two mannose 6-phosphate receptors
    • 8099077, .,.,.(): p.–.
    • Klumperman J., et al., Differences in the endosomal distributions of the two mannose 6-phosphate receptors. J Cell Biol, 1993. 121(5): p. 997–1010. 8099077
    • (1993) J Cell Biol , vol.121 , Issue.5 , pp. 997-1010
    • Klumperman, J.1
  • 42
    • 84869458315 scopus 로고    scopus 로고
    • Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy
    • 23086203, .,.,.(): p.–.
    • Martell J.D., et al., Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy. Nature biotechnology, 2012. 30(11): p. 1143–8. doi: 10.1038/nbt.237523086203
    • (2012) Nature biotechnology , vol.30 , Issue.11 , pp. 1143-1148
    • Martell, J.D.1
  • 43
    • 84926166583 scopus 로고    scopus 로고
    • Directed evolution of APEX2 for electron microscopy and proximity labeling
    • 25419960, .,.,.(): p.–.
    • Lam S.S., et al., Directed evolution of APEX2 for electron microscopy and proximity labeling. Nature methods, 2015. 12(1): p. 51–4. doi: 10.1038/nmeth.317925419960
    • (2015) Nature methods , vol.12 , Issue.1 , pp. 51-54
    • Lam, S.S.1
  • 44
    • 84902840121 scopus 로고    scopus 로고
    • The Cre/loxP system in Giardia lamblia: genetic manipulations in a binucleate tetraploid protozoan
    • 24747534, .,.(): p.–.
    • Wampfler P.B., Faso C., Hehl A.B., The Cre/loxP system in Giardia lamblia: genetic manipulations in a binucleate tetraploid protozoan. Int J Parasitol, 2014. 44(8): p. 497–506. doi: 10.1016/j.ijpara.2014.03.00824747534
    • (2014) Int J Parasitol , vol.44 , Issue.8 , pp. 497-506
    • Wampfler, P.B.1    Faso, C.2    Hehl, A.B.3
  • 45
    • 66749190056 scopus 로고    scopus 로고
    • Using morpholinos for gene knockdown in Giardia intestinalis
    • 19377039, .,.(): p.–.
    • Carpenter M.L., Cande W.Z., Using morpholinos for gene knockdown in Giardia intestinalis. Eukaryot Cell, 2009. 8(6): p. 916–9. doi: 10.1128/EC.00041-0919377039
    • (2009) Eukaryot Cell , vol.8 , Issue.6 , pp. 916-919
    • Carpenter, M.L.1    Cande, W.Z.2
  • 46
    • 0032498792 scopus 로고    scopus 로고
    • A dominant-negative clathrin mutant differentially affects trafficking of molecules with distinct sorting motifs in the class II major histocompatibility complex (MHC) pathway
    • 9490717, .,.(): p.–.
    • Liu S.H., Marks M.S., Brodsky F.M., A dominant-negative clathrin mutant differentially affects trafficking of molecules with distinct sorting motifs in the class II major histocompatibility complex (MHC) pathway. J Cell Biol, 1998. 140(5): p. 1023–37. 9490717
    • (1998) J Cell Biol , vol.140 , Issue.5 , pp. 1023-1037
    • Liu, S.H.1    Marks, M.S.2    Brodsky, F.M.3
  • 47
    • 38749145560 scopus 로고    scopus 로고
    • A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction
    • 17978091, .,.,.(): p.–.
    • Rapoport I., et al., A motif in the clathrin heavy chain required for the Hsc70/auxilin uncoating reaction. Molecular biology of the cell, 2008. 19(1): p. 405–13. 17978091
    • (2008) Molecular biology of the cell , vol.19 , Issue.1 , pp. 405-413
    • Rapoport, I.1
  • 48
    • 79952359360 scopus 로고    scopus 로고
    • Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating
    • .,.,.(): p.–.
    • Bocking T., et al., Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating. Nature structural & molecular biology, 2011. 18(3): p. 295–301.
    • (2011) Nature structural & molecular biology , vol.18 , Issue.3 , pp. 295-301
    • Bocking, T.1
  • 49
    • 10344262047 scopus 로고    scopus 로고
    • Molecular model for a complete clathrin lattice from electron cryomicroscopy
    • 15502812, .,.,.(): p.–.
    • Fotin A., et al., Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature, 2004. 432(7017): p. 573–9. 15502812
    • (2004) Nature , vol.432 , Issue.7017 , pp. 573-579
    • Fotin, A.1
  • 50
    • 18744400775 scopus 로고    scopus 로고
    • Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans
    • 12426379, .,.,.(): p.–.
    • Chen C.Y., et al., Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans. The EMBO journal, 2002. 21(22): p. 6072–82. 12426379
    • (2002) The EMBO journal , vol.21 , Issue.22 , pp. 6072-6082
    • Chen, C.Y.1
  • 51
    • 0030957964 scopus 로고    scopus 로고
    • A novel structural model for regulation of clathrin function
    • 9171338, .,.(): p.–.
    • Pishvaee B., Munn A., Payne G.S., A novel structural model for regulation of clathrin function. The EMBO journal, 1997. 16(9): p. 2227–39. 9171338
    • (1997) The EMBO journal , vol.16 , Issue.9 , pp. 2227-2239
    • Pishvaee, B.1    Munn, A.2    Payne, G.S.3
  • 52
    • 33745043237 scopus 로고    scopus 로고
    • Clathrin light chain: importance of the conserved carboxy terminal domain to function in living cells
    • 16734666, .,.(): p.–.
    • Wang J., Wang Y., O'Halloran T.J., Clathrin light chain: importance of the conserved carboxy terminal domain to function in living cells. Traffic, 2006. 7(7): p. 824–32. 16734666
    • (2006) Traffic , vol.7 , Issue.7 , pp. 824-832
    • Wang, J.1    Wang, Y.2    O'Halloran, T.J.3
  • 53
    • 0348013276 scopus 로고    scopus 로고
    • Contribution of cysteines to clathrin trimerization domain stability and mapping of light chain binding
    • 14617348, .,.,.(): p.–.
    • Ybe J.A., et al., Contribution of cysteines to clathrin trimerization domain stability and mapping of light chain binding. Traffic, 2003. 4(12): p. 850–6. 14617348
    • (2003) Traffic , vol.4 , Issue.12 , pp. 850-856
    • Ybe, J.A.1
  • 54
    • 34548176765 scopus 로고    scopus 로고
    • Integrating molecular and network biology to decode endocytosis
    • 17713526, .,.(): p.–.
    • Schmid E.M., McMahon H.T., Integrating molecular and network biology to decode endocytosis. Nature, 2007. 448(7156): p. 883–8. 17713526
    • (2007) Nature , vol.448 , Issue.7156 , pp. 883-888
    • Schmid, E.M.1    McMahon, H.T.2
  • 55
    • 34250873448 scopus 로고    scopus 로고
    • In vivo crosslinking methods for analyzing the assembly and architecture of chemoreceptor arrays
    • 17609143, .,.: p.–.
    • Studdert C.A., Parkinson J.S., In vivo crosslinking methods for analyzing the assembly and architecture of chemoreceptor arrays. Methods in enzymology, 2007. 423: p. 414–31. 17609143
    • (2007) Methods in enzymology , vol.423 , pp. 414-431
    • Studdert, C.A.1    Parkinson, J.S.2
  • 56
    • 50949127636 scopus 로고    scopus 로고
    • Identification and characterization of Inc766, an inclusion membrane protein in Chlamydophila abortus-infected cells
    • 18675895, .,.,.(): p.–.
    • Vretou E., et al., Identification and characterization of Inc766, an inclusion membrane protein in Chlamydophila abortus-infected cells. Microbial pathogenesis, 2008. 45(4): p. 265–72. doi: 10.1016/j.micpath.2008.06.00718675895
    • (2008) Microbial pathogenesis , vol.45 , Issue.4 , pp. 265-272
    • Vretou, E.1
  • 57
    • 0027320431 scopus 로고
    • Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation
    • 8347619, .,.,.(): p.–.
    • Zhou M., et al., Real-time measurements of kinetics of EGF binding to soluble EGF receptor monomers and dimers support the dimerization model for receptor activation. Biochemistry, 1993. 32(32): p. 8193–8. 8347619
    • (1993) Biochemistry , vol.32 , Issue.32 , pp. 8193-8198
    • Zhou, M.1
  • 58
    • 79960603102 scopus 로고    scopus 로고
    • The minimal kinome of Giardia lamblia illuminates early kinase evolution and unique parasite biology
    • 21787419, .,.,.(): p.
    • Manning G., et al., The minimal kinome of Giardia lamblia illuminates early kinase evolution and unique parasite biology. Genome biology, 2011. 12(7): p. R66. doi: 10.1186/gb-2011-12-7-r6621787419
    • (2011) Genome biology , vol.12 , Issue.7 , pp. R66
    • Manning, G.1
  • 59
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: selecting cargo for clathrin-regulated internalization
    • 19696796, .,.(): p.–.
    • Traub L.M., Tickets to ride: selecting cargo for clathrin-regulated internalization. Nature reviews. Molecular cell biology, 2009. 10(9): p. 583–96. doi: 10.1038/nrm275119696796
    • (2009) Nature reviews. Molecular cell biology , vol.10 , Issue.9 , pp. 583-596
    • Traub, L.M.1
  • 60
    • 0034282751 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
    • 10970851, .,.,.(): p.–.
    • Gillooly D.J., et al., Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells. The EMBO journal, 2000. 19(17): p. 4577–88. 10970851
    • (2000) The EMBO journal , vol.19 , Issue.17 , pp. 4577-4588
    • Gillooly, D.J.1
  • 61
    • 0033492236 scopus 로고    scopus 로고
    • FYVE-finger proteins—effectors of an inositol lipid
    • 10564636, .,.(): p.–.
    • Stenmark H., Aasland R., FYVE-finger proteins—effectors of an inositol lipid. Journal of cell science, 1999. 112 (Pt 23): p. 4175–83. 10564636
    • (1999) Journal of cell science , vol.112 , pp. 4175-4183
    • Stenmark, H.1    Aasland, R.2
  • 62
    • 79954417537 scopus 로고    scopus 로고
    • Identification and characterization of a FYVE domain from the early diverging eukaryote Giardia lamblia
    • 21165741, .,.,.(): p.–.
    • Sinha A., et al., Identification and characterization of a FYVE domain from the early diverging eukaryote Giardia lamblia. Current microbiology, 2011. 62(4): p. 1179–84. doi: 10.1007/s00284-010-9845-521165741
    • (2011) Current microbiology , vol.62 , Issue.4 , pp. 1179-1184
    • Sinha, A.1
  • 63
    • 33748461590 scopus 로고    scopus 로고
    • The Phox (PX) domain proteins and membrane traffic
    • 16782399, .,.(): p.–.
    • Seet L.F., Hong W., The Phox (PX) domain proteins and membrane traffic. Biochimica et biophysica acta, 2006. 1761(8): p. 878–96. 16782399
    • (2006) Biochimica et biophysica acta , vol.1761 , Issue.8 , pp. 878-896
    • Seet, L.F.1    Hong, W.2
  • 64
    • 84881544899 scopus 로고    scopus 로고
    • Advances in analysis of low signal-to-noise images link dynamin and AP2 to the functions of an endocytic checkpoint
    • 23891661, .,.,.(): p.–.
    • Aguet F., et al., Advances in analysis of low signal-to-noise images link dynamin and AP2 to the functions of an endocytic checkpoint. Developmental cell, 2013. 26(3): p. 279–91. doi: 10.1016/j.devcel.2013.06.01923891661
    • (2013) Developmental cell , vol.26 , Issue.3 , pp. 279-291
    • Aguet, F.1
  • 65
    • 33845401403 scopus 로고    scopus 로고
    • Functional analysis of AP-2 alpha and mu2 subunits
    • 17035630, .,.,.(): p.–.
    • Motley A.M., et al., Functional analysis of AP-2 alpha and mu2 subunits. Molecular biology of the cell, 2006. 17(12): p. 5298–308. 17035630
    • (2006) Molecular biology of the cell , vol.17 , Issue.12 , pp. 5298-5308
    • Motley, A.M.1
  • 66
    • 8544266082 scopus 로고    scopus 로고
    • Dual engagement regulation of protein interactions with the AP-2 adaptor alpha appendage
    • 15292237, .,.,.(): p.–.
    • Mishra S.K., et al., Dual engagement regulation of protein interactions with the AP-2 adaptor alpha appendage. The Journal of biological chemistry, 2004. 279(44): p. 46191–203. 15292237
    • (2004) The Journal of biological chemistry , vol.279 , Issue.44 , pp. 46191-46203
    • Mishra, S.K.1
  • 67
    • 20844433378 scopus 로고    scopus 로고
    • Evolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosis
    • 15496985, .,.,.(): p.–.
    • Praefcke G.J., et al., Evolving nature of the AP2 alpha-appendage hub during clathrin-coated vesicle endocytosis. The EMBO journal, 2004. 23(22): p. 4371–83. 15496985
    • (2004) The EMBO journal , vol.23 , Issue.22 , pp. 4371-4383
    • Praefcke, G.J.1
  • 68
    • 0015824623 scopus 로고
    • Mechanism of attachment of Giardia to the wall of the small intestine
    • .,.(): p.–.
    • Holberton D.V., Mechanism of attachment of Giardia to the wall of the small intestine. Trans R Soc Trop Med Hyg, 1973. 67(1): p. 29–30.
    • (1973) Trans R Soc Trop Med Hyg , vol.67 , Issue.1 , pp. 29-30
    • Holberton, D.V.1
  • 69
    • 84901726613 scopus 로고    scopus 로고
    • The genome of Spironucleus salmonicida highlights a fish pathogen adapted to fluctuating environments
    • 24516394, .,.,.(): p.
    • Xu F., et al., The genome of Spironucleus salmonicida highlights a fish pathogen adapted to fluctuating environments. PLoS Genet, 2014. 10(2): p. e1004053. doi: 10.1371/journal.pgen.100405324516394
    • (2014) PLoS Genet , vol.10 , Issue.2 , pp. e1004053
    • Xu, F.1
  • 70
    • 40649122026 scopus 로고    scopus 로고
    • Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum
    • 18263733, .,.,.(): p.–.
    • Elliott D.A., et al., Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum. Proceedings of the National Academy of Sciences of the United States of America, 2008. 105(7): p. 2463–8. doi: 10.1073/pnas.071106710518263733
    • (2008) Proceedings of the National Academy of Sciences of the United States of America , vol.105 , Issue.7 , pp. 2463-2468
    • Elliott, D.A.1
  • 71
    • 46749085536 scopus 로고    scopus 로고
    • A new model for hemoglobin ingestion and transport by the human malaria parasite Plasmodium falciparum
    • 18477610, .,.(): p.–.
    • Lazarus M.D., Schneider T.G., Taraschi T.F., A new model for hemoglobin ingestion and transport by the human malaria parasite Plasmodium falciparum. Journal of cell science, 2008. 121(11): p. 1937–49. doi: 10.1242/jcs.02315018477610
    • (2008) Journal of cell science , vol.121 , Issue.11 , pp. 1937-1949
    • Lazarus, M.D.1    Schneider, T.G.2    Taraschi, T.F.3
  • 72
    • 0141530903 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis is essential in Trypanosoma brucei
    • 14517238, .,.(): p.–.
    • Allen C.L., Goulding D., Field M.C., Clathrin-mediated endocytosis is essential in Trypanosoma brucei. The EMBO journal, 2003. 22(19): p. 4991–5002. 14517238
    • (2003) The EMBO journal , vol.22 , Issue.19 , pp. 4991-5002
    • Allen, C.L.1    Goulding, D.2    Field, M.C.3
  • 73
    • 84860851074 scopus 로고    scopus 로고
    • Lysosomal protein trafficking in Giardia lamblia: common and distinct features
    • .,.,.: p.–.
    • Touz M.C., et al., Lysosomal protein trafficking in Giardia lamblia: common and distinct features. Frontiers in bioscience, 2012. 4: p. 1898–909.
    • (2012) Frontiers in bioscience , vol.4 , pp. 1898-1909
    • Touz, M.C.1
  • 74
    • 0042090355 scopus 로고    scopus 로고
    • An ancestral secretory apparatus in the protozoan parasite Giardia intestinalis
    • 12711599, .,.,.(): p.–.
    • Marti M., et al., An ancestral secretory apparatus in the protozoan parasite Giardia intestinalis. The Journal of biological chemistry, 2003. 278(27): p. 24837–48. 12711599
    • (2003) The Journal of biological chemistry , vol.278 , Issue.27 , pp. 24837-24848
    • Marti, M.1
  • 75
    • 0020662678 scopus 로고
    • Improved preservation and staining of HeLa cell actin filaments, clathrin-coated membranes, and other cytoplasmic structures by tannic acid-glutaraldehyde-saponin fixation
    • 6186673, .,.(): p.–.
    • Maupin P., Pollard T.D., Improved preservation and staining of HeLa cell actin filaments, clathrin-coated membranes, and other cytoplasmic structures by tannic acid-glutaraldehyde-saponin fixation. The Journal of cell biology, 1983. 96(1): p. 51–62. 6186673
    • (1983) The Journal of cell biology , vol.96 , Issue.1 , pp. 51-62
    • Maupin, P.1    Pollard, T.D.2
  • 76
    • 0025823445 scopus 로고
    • Transferrin receptors promote the formation of clathrin lattices
    • 1903330, .,.,.(): p.–.
    • Miller K., et al., Transferrin receptors promote the formation of clathrin lattices. Cell, 1991. 65(4): p. 621–32. 1903330
    • (1991) Cell , vol.65 , Issue.4 , pp. 621-632
    • Miller, K.1
  • 77
    • 84908576799 scopus 로고    scopus 로고
    • Flat clathrin lattices: stable features of the plasma membrane
    • 25165141, .,.,.(): p.–.
    • Grove J., et al., Flat clathrin lattices: stable features of the plasma membrane. Molecular biology of the cell, 2014. 25(22): p. 3581–94. doi: 10.1091/mbc.E14-06-115425165141
    • (2014) Molecular biology of the cell , vol.25 , Issue.22 , pp. 3581-3594
    • Grove, J.1
  • 78
    • 24944525034 scopus 로고    scopus 로고
    • Differential control of clathrin subunit dynamics measured with EW-FRAP microscopy
    • 16138905, .,.,.(): p.–.
    • Loerke D., et al., Differential control of clathrin subunit dynamics measured with EW-FRAP microscopy. Traffic, 2005. 6(10): p. 918–29. 16138905
    • (2005) Traffic , vol.6 , Issue.10 , pp. 918-929
    • Loerke, D.1
  • 79
    • 70350347712 scopus 로고    scopus 로고
    • Imaging endocytic clathrin structures in living cells
    • 19836955, .,.(): p.–.
    • Kirchhausen T., Imaging endocytic clathrin structures in living cells. Trends in cell biology, 2009. 19(11): p. 596–605. doi: 10.1016/j.tcb.2009.09.00219836955
    • (2009) Trends in cell biology , vol.19 , Issue.11 , pp. 596-605
    • Kirchhausen, T.1
  • 80
    • 77955263413 scopus 로고    scopus 로고
    • A comparison of GFP-tagged clathrin light chains with fluorochromated light chains in vivo and in vitro
    • 20545906, .,.,.(): p.–.
    • Hoffmann A., et al., A comparison of GFP-tagged clathrin light chains with fluorochromated light chains in vivo and in vitro. Traffic, 2010. 11(9): p. 1129–40. doi: 10.1111/j.1600-0854.2010.01084.x20545906
    • (2010) Traffic , vol.11 , Issue.9 , pp. 1129-1140
    • Hoffmann, A.1
  • 81
    • 47649101722 scopus 로고    scopus 로고
    • A functional GFP fusion for imaging clathrin-mediated endocytosis
    • 18498437, .,.(): p.–.
    • Rappoport J.Z., Simon S.M., A functional GFP fusion for imaging clathrin-mediated endocytosis. Traffic, 2008. 9(8): p. 1250–5. doi: 10.1111/j.1600-0854.2008.00770.x18498437
    • (2008) Traffic , vol.9 , Issue.8 , pp. 1250-1255
    • Rappoport, J.Z.1    Simon, S.M.2
  • 82
    • 84874547066 scopus 로고    scopus 로고
    • Clathrin-mediated hemoglobin endocytosis is essential for survival of Leishmania
    • 23328080, .,.,.(): p.–.
    • Agarwal S., et al., Clathrin-mediated hemoglobin endocytosis is essential for survival of Leishmania. Biochimica et biophysica acta, 2013. 1833(5): p. 1065–77. doi: 10.1016/j.bbamcr.2013.01.00623328080
    • (2013) Biochimica et biophysica acta , vol.1833 , Issue.5 , pp. 1065-1077
    • Agarwal, S.1
  • 83
    • 55449130503 scopus 로고    scopus 로고
    • Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin
    • 16276403, .,.,.(): p.
    • Elde N.C., et al., Elucidation of clathrin-mediated endocytosis in tetrahymena reveals an evolutionarily convergent recruitment of dynamin. PLoS Genet, 2005. 1(5): p. e52. 16276403
    • (2005) PLoS Genet , vol.1 , Issue.5 , pp. e52
    • Elde, N.C.1
  • 84
    • 84902706392 scopus 로고    scopus 로고
    • Clathrin expression in Trypanosoma cruzi
    • 24947310, .,.,.: p.
    • Kalb L.C., et al., Clathrin expression in Trypanosoma cruzi. BMC Cell Biol, 2014. 15: p. 23. doi: 10.1186/1471-2121-15-2324947310
    • (2014) BMC Cell Biol , vol.15 , pp. 23
    • Kalb, L.C.1
  • 85
    • 34249932612 scopus 로고    scopus 로고
    • Clathrin in Trypanosoma cruzi: in silico gene identification, isolation, and localization of protein expression sites
    • 17552985, .,.,.(): p.–.
    • Corrêa J.R., et al., Clathrin in Trypanosoma cruzi: in silico gene identification, isolation, and localization of protein expression sites. J Eukaryot Microbiol, 2007. 54(3): p. 297–302. 17552985
    • (2007) J Eukaryot Microbiol , vol.54 , Issue.3 , pp. 297-302
    • Corrêa, J.R.1
  • 86
    • 84890154610 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis and adaptor proteins
    • 24307937, .,.(): p.–.
    • Popova N.V., Deyev I.E., Petrenko A.G., Clathrin-mediated endocytosis and adaptor proteins. Acta Naturae, 2013. 5(3): p. 62–73. 24307937
    • (2013) Acta Naturae , vol.5 , Issue.3 , pp. 62-73
    • Popova, N.V.1    Deyev, I.E.2    Petrenko, A.G.3
  • 87
    • 84864634144 scopus 로고    scopus 로고
    • The first five seconds in the life of a clathrin-coated pit
    • 22863004, .,.,.(): p.–.
    • Cocucci E., et al., The first five seconds in the life of a clathrin-coated pit. Cell, 2012. 150(3): p. 495–507. doi: 10.1016/j.cell.2012.05.04722863004
    • (2012) Cell , vol.150 , Issue.3 , pp. 495-507
    • Cocucci, E.1
  • 88
    • 44049089141 scopus 로고    scopus 로고
    • Differential evanescence nanometry: live-cell fluorescence measurements with 10-nm axial resolution on the plasma membrane
    • 17993495, .,.(): p.–.
    • Saffarian S., Kirchhausen T., Differential evanescence nanometry: live-cell fluorescence measurements with 10-nm axial resolution on the plasma membrane. Biophysical journal, 2008. 94(6): p. 2333–42. 17993495
    • (2008) Biophysical journal , vol.94 , Issue.6 , pp. 2333-2342
    • Saffarian, S.1    Kirchhausen, T.2
  • 89
    • 33845601755 scopus 로고    scopus 로고
    • Cryo-electron tomography of clathrin-coated vesicles: structural implications for coat assembly
    • 17095010, .,.,.(): p.–.
    • Cheng Y., et al., Cryo-electron tomography of clathrin-coated vesicles: structural implications for coat assembly. Journal of molecular biology, 2007. 365(3): p. 892–9. 17095010
    • (2007) Journal of molecular biology , vol.365 , Issue.3 , pp. 892-899
    • Cheng, Y.1
  • 90
    • 0039252786 scopus 로고    scopus 로고
    • The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains
    • 10593899, .,.,.(): p.–.
    • Hofmann M.W., et al., The leucine-based sorting motifs in the cytoplasmic domain of the invariant chain are recognized by the clathrin adaptors AP1 and AP2 and their medium chains. J Biol Chem, 1999. 274(51): p. 36153–8. 10593899
    • (1999) J Biol Chem , vol.274 , Issue.51 , pp. 36153-36158
    • Hofmann, M.W.1
  • 91
    • 0028840355 scopus 로고
    • Interaction of tyrosine-based sorting signals with clathrin-associated proteins
    • 7569928, .,.,.(): p.–.
    • Ohno H., et al., Interaction of tyrosine-based sorting signals with clathrin-associated proteins. Science, 1995. 269(5232): p. 1872–5. 7569928
    • (1995) Science , vol.269 , Issue.5232 , pp. 1872-1875
    • Ohno, H.1
  • 92
    • 84904822861 scopus 로고    scopus 로고
    • Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-activated switch
    • 25061211, .,.,.(): p.–.
    • Kelly B.T., et al., Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-activated switch. Science, 2014. 345(6195): p. 459–63. doi: 10.1126/science.125483625061211
    • (2014) Science , vol.345 , Issue.6195 , pp. 459-463
    • Kelly, B.T.1
  • 93
    • 0037458651 scopus 로고    scopus 로고
    • Sorting of encystation-specific cysteine protease to lysosome-like peripheral vacuoles in Giardia lamblia requires a conserved tyrosine-based motif
    • 12466276, .,.,.(): p.–.
    • Touz M.C., et al., Sorting of encystation-specific cysteine protease to lysosome-like peripheral vacuoles in Giardia lamblia requires a conserved tyrosine-based motif. The Journal of biological chemistry, 2003. 278(8): p. 6420–6. 12466276
    • (2003) The Journal of biological chemistry , vol.278 , Issue.8 , pp. 6420-6426
    • Touz, M.C.1
  • 94
    • 77951249001 scopus 로고    scopus 로고
    • Mechanism of aldolase control of sorting nexin 9 function in endocytosis
    • 20129922, .,.,.(): p.–.
    • Rangarajan E.S., et al., Mechanism of aldolase control of sorting nexin 9 function in endocytosis. J Biol Chem, 2010. 285(16): p. 11983–90. doi: 10.1074/jbc.M109.09204920129922
    • (2010) J Biol Chem , vol.285 , Issue.16 , pp. 11983-11990
    • Rangarajan, E.S.1
  • 95
    • 0037119952 scopus 로고    scopus 로고
    • Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor
    • 12234931, .,.,.(): p.–.
    • Mishra S.K., et al., Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor. The EMBO journal, 2002. 21(18): p. 4915–26. 12234931
    • (2002) The EMBO journal , vol.21 , Issue.18 , pp. 4915-4926
    • Mishra, S.K.1
  • 96
    • 0037059006 scopus 로고    scopus 로고
    • The autosomal recessive hypercholesterolemia (ARH) protein interfaces directly with the clathrin-coat machinery
    • 12451172, .,.(): p.–.
    • Mishra S.K., Watkins S.C., Traub L.M., The autosomal recessive hypercholesterolemia (ARH) protein interfaces directly with the clathrin-coat machinery. Proceedings of the National Academy of Sciences of the United States of America, 2002. 99(25): p. 16099–104. 12451172
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.25 , pp. 16099-16104
    • Mishra, S.K.1    Watkins, S.C.2    Traub, L.M.3
  • 97
    • 70349764506 scopus 로고    scopus 로고
    • Distinct dynamics of endocytic clathrin-coated pits and coated plaques
    • 19809571, .,.(): p.
    • Saffarian S., Cocucci E., Kirchhausen T., Distinct dynamics of endocytic clathrin-coated pits and coated plaques. PLoS biology, 2009. 7(9): p. e1000191. doi: 10.1371/journal.pbio.100019119809571
    • (2009) PLoS biology , vol.7 , Issue.9 , pp. e1000191
    • Saffarian, S.1    Cocucci, E.2    Kirchhausen, T.3
  • 98
    • 84873443433 scopus 로고    scopus 로고
    • Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids
    • 23337175, .,.(): p.–.
    • Manna P.T., Kelly S., Field M.C., Adaptin evolution in kinetoplastids and emergence of the variant surface glycoprotein coat in African trypanosomatids. Mol Phylogenet Evol, 2013. 67(1): p. 123–8. doi: 10.1016/j.ympev.2013.01.00223337175
    • (2013) Mol Phylogenet Evol , vol.67 , Issue.1 , pp. 123-128
    • Manna, P.T.1    Kelly, S.2    Field, M.C.3
  • 99
    • 84874677712 scopus 로고    scopus 로고
    • Proteomic analysis of clathrin interactions in trypanosomes reveals dynamic evolution of endocytosis
    • 23305527, .,.(): p.–.
    • Adung'a V.O., Gadelha C., Field M.C., Proteomic analysis of clathrin interactions in trypanosomes reveals dynamic evolution of endocytosis. Traffic, 2013. 14(4): p. 440–57. doi: 10.1111/tra.1204023305527
    • (2013) Traffic , vol.14 , Issue.4 , pp. 440-457
    • Adung'a, V.O.1    Gadelha, C.2    Field, M.C.3
  • 100
    • 84907055355 scopus 로고    scopus 로고
    • The cell biology of the endocytic system from an evolutionary perspective
    • 24478384, .,.,.(): p.
    • Wideman J.G., et al., The cell biology of the endocytic system from an evolutionary perspective. Cold Spring Harbor perspectives in biology, 2014. 6(4): p. a016998. doi: 10.1101/cshperspect.a01699824478384
    • (2014) Cold Spring Harbor perspectives in biology , vol.6 , Issue.4 , pp. a016998
    • Wideman, J.G.1
  • 101
    • 84861868826 scopus 로고    scopus 로고
    • Roles for actin assembly in endocytosis
    • 22663081, .,.: p.–.
    • Mooren O.L., Galletta B.J., Cooper J.A., Roles for actin assembly in endocytosis. Annu Rev Biochem, 2012. 81: p. 661–86. doi: 10.1146/annurev-biochem-060910-09441622663081
    • (2012) Annu Rev Biochem , vol.81 , pp. 661-686
    • Mooren, O.L.1    Galletta, B.J.2    Cooper, J.A.3
  • 102
    • 79954993081 scopus 로고    scopus 로고
    • An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins
    • 21444821, .,.,.(): p.–.
    • Paredez A.R., et al., An actin cytoskeleton with evolutionarily conserved functions in the absence of canonical actin-binding proteins. Proc Natl Acad Sci U S A, 2011. 108(15): p. 6151–6. doi: 10.1073/pnas.101859310821444821
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.15 , pp. 6151-6156
    • Paredez, A.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.