메뉴 건너뛰기




Volumn 85, Issue 9-10, 2006, Pages 925-936

Trafficking and developmental signaling: Alix at the crossroads

Author keywords

ALG 2; Alix; Development; Dictyostelium; Endocytic trafficking; ESCRT

Indexed keywords

ADAPTOR PROTEIN; CALCIUM BINDING PROTEIN; CELL PROTEIN; ISOPROTEIN; MEMBRANE PROTEIN; MUTANT PROTEIN; PROTEIN ALG 2; PROTEIN ALIX; PROTEIN ALX; UNCLASSIFIED DRUG;

EID: 33748422691     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2006.04.002     Document Type: Short Survey
Times cited : (16)

References (68)
  • 3
    • 0037383273 scopus 로고    scopus 로고
    • pH regulation in Aspergillus and parallels with higher eukaryotic regulatory systems
    • Arst H.N., and Penalva M.A. pH regulation in Aspergillus and parallels with higher eukaryotic regulatory systems. Trends Genet. 19 (2003) 224-231
    • (2003) Trends Genet. , vol.19 , pp. 224-231
    • Arst, H.N.1    Penalva, M.A.2
  • 4
    • 0033279835 scopus 로고    scopus 로고
    • Integration of signaling networks that regulate Dictyostelium differentiation
    • Aubry L., and Firtel R. Integration of signaling networks that regulate Dictyostelium differentiation. Annu. Rev. Cell Dev. Biol. 15 (1999) 469-517
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 469-517
    • Aubry, L.1    Firtel, R.2
  • 5
    • 0037077226 scopus 로고    scopus 로고
    • Biochemical characterization of two analogues of the apoptosis-linked gene 2 protein in Dictyostelium discoideum and interaction with a physiological partner in mammals, murine Alix
    • Aubry L., Mattei S., Blot B., Sadoul R., Satre M., and Klein G. Biochemical characterization of two analogues of the apoptosis-linked gene 2 protein in Dictyostelium discoideum and interaction with a physiological partner in mammals, murine Alix. J. Biol. Chem. 277 (2002) 21947-21954
    • (2002) J. Biol. Chem. , vol.277 , pp. 21947-21954
    • Aubry, L.1    Mattei, S.2    Blot, B.3    Sadoul, R.4    Satre, M.5    Klein, G.6
  • 6
    • 12444347534 scopus 로고    scopus 로고
    • A protein's final ESCRT
    • Babst M. A protein's final ESCRT. Traffic 6 (2005) 2-9
    • (2005) Traffic , vol.6 , pp. 2-9
    • Babst, M.1
  • 7
    • 0038323973 scopus 로고    scopus 로고
    • STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes
    • Bache K.G., Raiborg C., Mehlum A., and Stenmark H. STAM and Hrs are subunits of a multivalent ubiquitin-binding complex on early endosomes. J. Biol. Chem. 278 (2003) 12513-12521
    • (2003) J. Biol. Chem. , vol.278 , pp. 12513-12521
    • Bache, K.G.1    Raiborg, C.2    Mehlum, A.3    Stenmark, H.4
  • 8
    • 4544337932 scopus 로고    scopus 로고
    • Increased Alix (apoptosis-linked gene-2 interacting protein X) immunoreactivity in the degenerating striatum of rats chronically treated by 3-nitropropionic acid
    • Blum D., Hemming F.J., Galas M.C., Torch S., Cuvelier L., Schiffmann S.N., and Sadoul R. Increased Alix (apoptosis-linked gene-2 interacting protein X) immunoreactivity in the degenerating striatum of rats chronically treated by 3-nitropropionic acid. Neurosci. Lett. 368 (2004) 309-313
    • (2004) Neurosci. Lett. , vol.368 , pp. 309-313
    • Blum, D.1    Hemming, F.J.2    Galas, M.C.3    Torch, S.4    Cuvelier, L.5    Schiffmann, S.N.6    Sadoul, R.7
  • 9
    • 33646171781 scopus 로고    scopus 로고
    • Degradation of endocytosed epidermal growth factor and virally ubiquitinated MHC class I is independent of mammalian ESCRTII
    • Bowers K., Piper S.C., Edeling M.A., Gray S.R., Owen D.J., Lehner P.J., and Luzio J.P. Degradation of endocytosed epidermal growth factor and virally ubiquitinated MHC class I is independent of mammalian ESCRTII. J. Biol. Chem. 281 (2006) 5094-5105
    • (2006) J. Biol. Chem. , vol.281 , pp. 5094-5105
    • Bowers, K.1    Piper, S.C.2    Edeling, M.A.3    Gray, S.R.4    Owen, D.J.5    Lehner, P.J.6    Luzio, J.P.7
  • 10
    • 0034682695 scopus 로고    scopus 로고
    • Apoptosis. Mitochondria - the death signal integrators
    • Brenner C., and Kroemer G. Apoptosis. Mitochondria - the death signal integrators. Science 289 (2000) 1150-1151
    • (2000) Science , vol.289 , pp. 1150-1151
    • Brenner, C.1    Kroemer, G.2
  • 11
    • 0037047287 scopus 로고    scopus 로고
    • Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization
    • Chatellard-Causse C., Blot B., Cristina N., Torch S., Missotten M., and Sadoul R. Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization. J. Biol. Chem. 277 (2002) 29108-29115
    • (2002) J. Biol. Chem. , vol.277 , pp. 29108-29115
    • Chatellard-Causse, C.1    Blot, B.2    Cristina, N.3    Torch, S.4    Missotten, M.5    Sadoul, R.6
  • 12
    • 0034705484 scopus 로고    scopus 로고
    • The glioma-associated protein SETA interacts with AIP1/Alix and ALG-2 and modulates apoptosis in astrocytes
    • Chen B., Borinstein S.C., Gillis J., Sykes V.W., and Bogler O. The glioma-associated protein SETA interacts with AIP1/Alix and ALG-2 and modulates apoptosis in astrocytes. J. Biol. Chem. 275 (2000) 19275-19281
    • (2000) J. Biol. Chem. , vol.275 , pp. 19275-19281
    • Chen, B.1    Borinstein, S.C.2    Gillis, J.3    Sykes, V.W.4    Bogler, O.5
  • 14
    • 0029077310 scopus 로고
    • Patterns of free calcium in multicellular stages of Dictyostelium expressing jellyfish apoaequorin
    • Cubitt A.B., Firtel R.A., Fischer G., Jaffe L.F., and Miller A.L. Patterns of free calcium in multicellular stages of Dictyostelium expressing jellyfish apoaequorin. Development 121 (1995) 2291-2301
    • (1995) Development , vol.121 , pp. 2291-2301
    • Cubitt, A.B.1    Firtel, R.A.2    Fischer, G.3    Jaffe, L.F.4    Miller, A.L.5
  • 17
    • 0038813721 scopus 로고    scopus 로고
    • Calcium modulates promoter occupancy by the Entamoeba histolytica Ca2+-binding transcription factor URE3-BP
    • Gilchrist C.A., Leo M., Line C.G., Mann B.J., and Petri Jr. W.A. Calcium modulates promoter occupancy by the Entamoeba histolytica Ca2+-binding transcription factor URE3-BP. J. Biol. Chem. 278 (2003) 4646-4653
    • (2003) J. Biol. Chem. , vol.278 , pp. 4646-4653
    • Gilchrist, C.A.1    Leo, M.2    Line, C.G.3    Mann, B.J.4    Petri Jr., W.A.5
  • 18
  • 19
    • 1642482409 scopus 로고    scopus 로고
    • Early increase of apoptosis-linked gene-2 interacting protein X in areas of kainate-induced neurodegeneration
    • Hemming F.J., Fraboulet S., Blot B., and Sadoul R. Early increase of apoptosis-linked gene-2 interacting protein X in areas of kainate-induced neurodegeneration. Neuroscience 123 (2004) 887-895
    • (2004) Neuroscience , vol.123 , pp. 887-895
    • Hemming, F.J.1    Fraboulet, S.2    Blot, B.3    Sadoul, R.4
  • 21
    • 0036258163 scopus 로고    scopus 로고
    • Apoptosis-linked gene 2-deficient mice exhibit normal T-cell development and function
    • Jang I.K., Hu R., Lacana E., D'Adamio L., and Gu H. Apoptosis-linked gene 2-deficient mice exhibit normal T-cell development and function. Mol. Cell. Biol. 22 (2002) 4094-4100
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4094-4100
    • Jang, I.K.1    Hu, R.2    Lacana, E.3    D'Adamio, L.4    Gu, H.5
  • 22
    • 0034892270 scopus 로고    scopus 로고
    • Structure of apoptosis-linked protein ALG-2: insights into Ca2+-induced changes in penta-EF-hand proteins
    • Jia J., Tarabykina S., Hansen C., Berchtold M., and Cygler M. Structure of apoptosis-linked protein ALG-2: insights into Ca2+-induced changes in penta-EF-hand proteins. Structure 9 (2001) 267-275
    • (2001) Structure , vol.9 , pp. 267-275
    • Jia, J.1    Tarabykina, S.2    Hansen, C.3    Berchtold, M.4    Cygler, M.5
  • 23
    • 0141643096 scopus 로고    scopus 로고
    • The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting
    • Katoh K., Shibata H., Suzuki H., Nara A., Ishidoh K., Kominami E., Yoshimori T., and Maki M. The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. J. Biol. Chem. 278 (2003) 39104-39113
    • (2003) J. Biol. Chem. , vol.278 , pp. 39104-39113
    • Katoh, K.1    Shibata, H.2    Suzuki, H.3    Nara, A.4    Ishidoh, K.5    Kominami, E.6    Yoshimori, T.7    Maki, M.8
  • 24
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann D.J., Babst M., and Emr S.D. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106 (2001) 145-155
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 26
    • 0023063763 scopus 로고
    • Cell differentiation in monolayers and the investigation of slime mold morphogens
    • Kay R.R. Cell differentiation in monolayers and the investigation of slime mold morphogens. Methods Cell Biol. 28 (1987) 433-448
    • (1987) Methods Cell Biol. , vol.28 , pp. 433-448
    • Kay, R.R.1
  • 28
    • 0035958070 scopus 로고    scopus 로고
    • Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner
    • Kitaura Y., Matsumoto S., Satoh H., Hitomi K., and Maki M. Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner. J. Biol. Chem. 276 (2001) 14053-14058
    • (2001) J. Biol. Chem. , vol.276 , pp. 14053-14058
    • Kitaura, Y.1    Matsumoto, S.2    Satoh, H.3    Hitomi, K.4    Maki, M.5
  • 32
    • 0037596749 scopus 로고    scopus 로고
    • TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation
    • Lu Q., Hope L.W., Brasch M., Reinhard C., and Cohen S.N. TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation. Proc. Natl. Acad. Sci. USA 100 (2003) 7626-7631
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7626-7631
    • Lu, Q.1    Hope, L.W.2    Brasch, M.3    Reinhard, C.4    Cohen, S.N.5
  • 33
    • 4444342179 scopus 로고    scopus 로고
    • Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes
    • Luhtala N., and Odorizzi G. Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes. J. Cell Biol. 166 (2004) 717-729
    • (2004) J. Cell Biol. , vol.166 , pp. 717-729
    • Luhtala, N.1    Odorizzi, G.2
  • 34
    • 1242351264 scopus 로고    scopus 로고
    • Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins
    • Maki M., Kitaura Y., Satoh H., Ohkouchi S., and Shibata H. Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins. Biochim. Biophys. Acta 1600 (2002) 51-60
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 51-60
    • Maki, M.1    Kitaura, Y.2    Satoh, H.3    Ohkouchi, S.4    Shibata, H.5
  • 35
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins
    • Martin-Serrano J., Yarovoy A., Perez-Caballero D., and Bieniasz P.D. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. Proc. Natl. Acad. Sci. USA 100 (2003) 12414-12419
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yarovoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 36
  • 39
    • 0033043513 scopus 로고    scopus 로고
    • Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein
    • Missotten M., Nichols A., Rieger K., and Sadoul R. Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. Cell Death Differ. 6 (1999) 124-129
    • (1999) Cell Death Differ. , vol.6 , pp. 124-129
    • Missotten, M.1    Nichols, A.2    Rieger, K.3    Sadoul, R.4
  • 40
    • 0346599157 scopus 로고    scopus 로고
    • Properties of the co-chaperone protein p23 erroneously attributed to ALG-2 (apoptosis-linked gene 2)
    • Mollerup J., Krogh T.N., Nielsen P.F., and Berchtold M.W. Properties of the co-chaperone protein p23 erroneously attributed to ALG-2 (apoptosis-linked gene 2). FEBS Lett. 555 (2003) 478-482
    • (2003) FEBS Lett. , vol.555 , pp. 478-482
    • Mollerup, J.1    Krogh, T.N.2    Nielsen, P.F.3    Berchtold, M.W.4
  • 41
    • 0029892928 scopus 로고    scopus 로고
    • BRO1, a novel gene that interacts with components of the Pkc1p-mitogen-activated protein kinase pathway in Saccharomyces cerevisiae
    • Nickas M.E., and Yaffe M.P. BRO1, a novel gene that interacts with components of the Pkc1p-mitogen-activated protein kinase pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 16 (1996) 2585-2593
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2585-2593
    • Nickas, M.E.1    Yaffe, M.P.2
  • 42
    • 0347379848 scopus 로고    scopus 로고
    • Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway
    • Nikko E., Marini A.M., and Andre B. Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway. J. Biol. Chem. 278 (2003) 50732-50743
    • (2003) J. Biol. Chem. , vol.278 , pp. 50732-50743
    • Nikko, E.1    Marini, A.M.2    Andre, B.3
  • 43
    • 0038784064 scopus 로고    scopus 로고
    • Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae
    • Odorizzi G., Katzmann D.J., Babst M., Audhya A., and Emr S.D. Bro1 is an endosome-associated protein that functions in the MVB pathway in Saccharomyces cerevisiae. J. Cell Sci. 116 (2003) 1893-1903
    • (2003) J. Cell Sci. , vol.116 , pp. 1893-1903
    • Odorizzi, G.1    Katzmann, D.J.2    Babst, M.3    Audhya, A.4    Emr, S.D.5
  • 44
    • 0034859261 scopus 로고    scopus 로고
    • Identification and characterization of two penta-EF hand Ca2+-binding proteins in Dictyostelium discoideum
    • Ohkouchi S., Nishio K., Maeda M., Hitomi K., Adachi H., and Maki M. Identification and characterization of two penta-EF hand Ca2+-binding proteins in Dictyostelium discoideum. J. Biochem. 130 (2001) 207-215
    • (2001) J. Biochem. , vol.130 , pp. 207-215
    • Ohkouchi, S.1    Nishio, K.2    Maeda, M.3    Hitomi, K.4    Adachi, H.5    Maki, M.6
  • 45
    • 3242769162 scopus 로고    scopus 로고
    • DdAlix, an Alix/AIP1 homolog in Dictyostelium discoideum, is required for multicellular development under low Ca2+ conditions
    • Ohkouchi S., El-Halawany M.S., Aruga F., Shibata H., Hitomi K., and Maki M. DdAlix, an Alix/AIP1 homolog in Dictyostelium discoideum, is required for multicellular development under low Ca2+ conditions. Gene 337 (2004) 131-139
    • (2004) Gene , vol.337 , pp. 131-139
    • Ohkouchi, S.1    El-Halawany, M.S.2    Aruga, F.3    Shibata, H.4    Hitomi, K.5    Maki, M.6
  • 46
    • 14844307589 scopus 로고    scopus 로고
    • Dictyostelium discoideum requires an Alix/AIP1 homolog, DdAlix, for morphogenesis in alkaline environments
    • Ohkouchi S., Saito H., Aruga F., Maeda T., Shibata H., and Maki M. Dictyostelium discoideum requires an Alix/AIP1 homolog, DdAlix, for morphogenesis in alkaline environments. FEBS Lett. 579 (2005) 1745-1750
    • (2005) FEBS Lett. , vol.579 , pp. 1745-1750
    • Ohkouchi, S.1    Saito, H.2    Aruga, F.3    Maeda, T.4    Shibata, H.5    Maki, M.6
  • 48
    • 1842577042 scopus 로고    scopus 로고
    • Dictyostelium macroautophagy mutants vary in the severity of their developmental defects
    • Otto G.P., Wu M.Y., Kazgan N., Anderson O.R., and Kessin R.H. Dictyostelium macroautophagy mutants vary in the severity of their developmental defects. J. Biol. Chem. 279 (2004) 15621-15629
    • (2004) J. Biol. Chem. , vol.279 , pp. 15621-15629
    • Otto, G.P.1    Wu, M.Y.2    Kazgan, N.3    Anderson, O.R.4    Kessin, R.H.5
  • 51
    • 22544442436 scopus 로고    scopus 로고
    • Components of the ESCRT pathway, DFG16, and YGR122w are required for Rim101 to act as a corepressor with Nrg1 at the negative regulatory element of the DIT1 gene of Saccharomyces cerevisiae
    • Rothfels K., Tanny J.C., Molnar E., Friesen H., Commisso C., and Segall J. Components of the ESCRT pathway, DFG16, and YGR122w are required for Rim101 to act as a corepressor with Nrg1 at the negative regulatory element of the DIT1 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 25 (2005) 6772-6788
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6772-6788
    • Rothfels, K.1    Tanny, J.C.2    Molnar, E.3    Friesen, H.4    Commisso, C.5    Segall, J.6
  • 52
    • 0037020677 scopus 로고    scopus 로고
    • The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner
    • Satoh H., Nakano Y., Shibata H., and Maki M. The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner. Biochim. Biophys. Acta 1600 (2002) 61-67
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 61-67
    • Satoh, H.1    Nakano, Y.2    Shibata, H.3    Maki, M.4
  • 53
    • 0029791315 scopus 로고    scopus 로고
    • A slow sustained increase in cytosolic Ca2+ levels mediates stalk gene induction by differentiation inducing factor in Dictyostelium
    • Schaap P., Nebl T., and Fisher P.R. A slow sustained increase in cytosolic Ca2+ levels mediates stalk gene induction by differentiation inducing factor in Dictyostelium. EMBO J. 15 (1996) 5177-5183
    • (1996) EMBO J. , vol.15 , pp. 5177-5183
    • Schaap, P.1    Nebl, T.2    Fisher, P.R.3
  • 54
    • 0041669448 scopus 로고    scopus 로고
    • SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion
    • Schmidt M.H., Chen B., Randazzo L.M., and Bogler O. SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion. J. Cell Sci. 116 (2003) 2845-2855
    • (2003) J. Cell Sci. , vol.116 , pp. 2845-2855
    • Schmidt, M.H.1    Chen, B.2    Randazzo, L.M.3    Bogler, O.4
  • 55
    • 4744365071 scopus 로고    scopus 로고
    • Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex
    • Schmidt M.H., Hoeller D., Yu J., Furnari F.B., Cavenee W.K., Dikic I., and Bogler O. Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex. Mol. Cell. Biol. 24 (2004) 8981-8993
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8981-8993
    • Schmidt, M.H.1    Hoeller, D.2    Yu, J.3    Furnari, F.B.4    Cavenee, W.K.5    Dikic, I.6    Bogler, O.7
  • 56
    • 1642421938 scopus 로고    scopus 로고
    • The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1
    • Shibata H., Yamada K., Mizuno T., Yorikawa C., Takahashi H., Satoh H., Kitaura Y., and Maki M. The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1. J. Biochem. 135 (2004) 117-128
    • (2004) J. Biochem. , vol.135 , pp. 117-128
    • Shibata, H.1    Yamada, K.2    Mizuno, T.3    Yorikawa, C.4    Takahashi, H.5    Satoh, H.6    Kitaura, Y.7    Maki, M.8
  • 58
    • 0037165612 scopus 로고    scopus 로고
    • Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking
    • Springael J.Y., Nikko E., Andre B., and Marini A.M. Yeast Npi3/Bro1 is involved in ubiquitin-dependent control of permease trafficking. FEBS Lett. 517 (2002) 103-109
    • (2002) FEBS Lett. , vol.517 , pp. 103-109
    • Springael, J.Y.1    Nikko, E.2    Andre, B.3    Marini, A.M.4
  • 59
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • Strack B., Calistri A., Craig S., Popova E., and Gottlinger H.G. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114 (2003) 689-699
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 61
    • 0037370013 scopus 로고    scopus 로고
    • YPXL/I is a protein interaction motif recognized by Aspergillus PalA and its human homologue, AIP1/Alix
    • Vincent O., Rainbow L., Tilburn J., Arst Jr. H.N., and Penalva M.A. YPXL/I is a protein interaction motif recognized by Aspergillus PalA and its human homologue, AIP1/Alix. Mol. Cell. Biol. 23 (2003) 1647-1655
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 1647-1655
    • Vincent, O.1    Rainbow, L.2    Tilburn, J.3    Arst Jr., H.N.4    Penalva, M.A.5
  • 62
    • 0029671219 scopus 로고    scopus 로고
    • Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3
    • Vito P., Lacana E., and D'Adamio L. Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science 271 (1996) 521-525
    • (1996) Science , vol.271 , pp. 521-525
    • Vito, P.1    Lacana, E.2    D'Adamio, L.3
  • 63
    • 0033556043 scopus 로고    scopus 로고
    • Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction
    • Vito P., Pellegrini L., Guiet C., and D'Adamio L. Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction. J. Biol. Chem. 274 (1999) 1533-1540
    • (1999) J. Biol. Chem. , vol.274 , pp. 1533-1540
    • Vito, P.1    Pellegrini, L.2    Guiet, C.3    D'Adamio, L.4
  • 66
    • 0037015680 scopus 로고    scopus 로고
    • Hp95 promotes anoikis and inhibits tumorigenicity of HeLa cells
    • Wu Y., Pan S., Luo W., Lin S.H., and Kuang J. Hp95 promotes anoikis and inhibits tumorigenicity of HeLa cells. Oncogene 21 (2002) 6801-6808
    • (2002) Oncogene , vol.21 , pp. 6801-6808
    • Wu, Y.1    Pan, S.2    Luo, W.3    Lin, S.H.4    Kuang, J.5
  • 67
    • 0035174117 scopus 로고    scopus 로고
    • Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and is required for its proteolytic cleavage
    • Xu W., and Mitchell A.P. Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and is required for its proteolytic cleavage. J. Bacteriol. 183 (2001) 6917-6923
    • (2001) J. Bacteriol. , vol.183 , pp. 6917-6923
    • Xu, W.1    Mitchell, A.P.2
  • 68
    • 0029919409 scopus 로고    scopus 로고
    • Intracellular free calcium responses during chemotaxis of Dictyostelium cells
    • Yumura S., Furuya K., and Takeuchi I. Intracellular free calcium responses during chemotaxis of Dictyostelium cells. J. Cell Sci. 109 (1996) 2673-2678
    • (1996) J. Cell Sci. , vol.109 , pp. 2673-2678
    • Yumura, S.1    Furuya, K.2    Takeuchi, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.