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Volumn 257, Issue 2, 2000, Pages 332-340

WW- and SH3-domain interactions with epstein-barr virus LMP2A

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; MEMBRANE PROTEIN; VIRUS PROTEIN;

EID: 0034660244     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.2000.4900     Document Type: Article
Times cited : (29)

References (57)
  • 1
    • 0001658316 scopus 로고    scopus 로고
    • Epstein-Barr virus and its replication
    • B. N. Fields, D. M. Knipe, & P. M. Howley. Lippincott-Raven
    • Kieff E. Epstein-Barr virus and its replication. Fields B. N., Knipe D. M., Howley P. M. Fundamental Virology. 1996;1109-1162 Lippincott-Raven.
    • (1996) Fundamental Virology , pp. 1109-1162
    • Kieff, E.1
  • 2
    • 0001403023 scopus 로고    scopus 로고
    • Molecular biology of Epstein-Barr virus
    • Dennis McCaance. Am. Soc. for Microbiol
    • Longnecker R. Molecular biology of Epstein-Barr virus. McCaance Dennis. Human Tumor Viruses. 1998;133-172 Am. Soc. for Microbiol.
    • (1998) Human Tumor Viruses , pp. 133-172
    • Longnecker, R.1
  • 3
    • 0000942113 scopus 로고    scopus 로고
    • Epstein-Barr virus
    • B. N. Fields, D. M. Knipe, & P. M. Howley. Philadelphia: Lippincott-Raven
    • Rickinson A. B., Kieff E. Epstein-Barr virus. Fields B. N., Knipe D. M., Howley P. M. Fields Virology. 1996;2397-2446 Lippincott-Raven, Philadelphia.
    • (1996) Fields Virology , pp. 2397-2446
    • Rickinson, A.B.1    Kieff, E.2
  • 4
    • 0001368045 scopus 로고    scopus 로고
    • Epstein-Barr Pathogenesis
    • Dennis McCaance. Am. Soc. for Microbiol
    • Liebowitz D. Epstein-Barr Pathogenesis. McCaance Dennis. Human Tumor Viruses. 1998;173-198 Am. Soc. for Microbiol.
    • (1998) Human Tumor Viruses , pp. 173-198
    • Liebowitz, D.1
  • 5
    • 0029067481 scopus 로고
    • A subpopulation of normal B cells latently infected with Epstein-Barr virus resembles Burkitt lymphoma cells in expressing EBNA-1 but not EBNA-2 or LMP1
    • Chen F., Zou J. Z., di Renzo L. A subpopulation of normal B cells latently infected with Epstein-Barr virus resembles Burkitt lymphoma cells in expressing EBNA-1 but not EBNA-2 or LMP1. J. Virol. 69:1995;3752-3758.
    • (1995) J. Virol. , vol.69 , pp. 3752-3758
    • Chen, F.1    Zou, J.Z.2    Di Renzo, L.3
  • 6
    • 0031007613 scopus 로고    scopus 로고
    • Identification of the site of Epstein-Barr virus persistence in vivo as a resting B cell
    • Miyashita E. M., Yang B., Babcock G. J., Thorley-Lawson D. A. Identification of the site of Epstein-Barr virus persistence in vivo as a resting B cell. J. Virol. 71:1997;4882-4891.
    • (1997) J. Virol. , vol.71 , pp. 4882-4891
    • Miyashita, E.M.1    Yang, B.2    Babcock, G.J.3    Thorley-Lawson, D.A.4
  • 7
    • 0026764617 scopus 로고
    • Epstein-Barr virus latent gene expression in uncultured peripheral blood lymphocytes
    • Qu L., Rowe D. Epstein-Barr virus latent gene expression in uncultured peripheral blood lymphocytes. J. Virol. 66:1992;3715-3724.
    • (1992) J. Virol. , vol.66 , pp. 3715-3724
    • Qu, L.1    Rowe, D.2
  • 8
    • 0028130271 scopus 로고
    • Epstein-Barr virus latency in blood mononuclear cells: Analysis of viral gene transcription during primary infection and in the carrier state
    • Tierney R. J., Steven N., Young L. S., Rickinson A. B. Epstein-Barr virus latency in blood mononuclear cells: analysis of viral gene transcription during primary infection and in the carrier state. J. Virol. 68:1994;7374-7385.
    • (1994) J. Virol. , vol.68 , pp. 7374-7385
    • Tierney, R.J.1    Steven, N.2    Young, L.S.3    Rickinson, A.B.4
  • 9
    • 0024535280 scopus 로고
    • Two related Epstein-Barr virus membrane proteins are encoded by separate genes
    • Sample J., Liebowitz D., Kieff E. Two related Epstein-Barr virus membrane proteins are encoded by separate genes. J. Virol. 63:1989;933-937.
    • (1989) J. Virol. , vol.63 , pp. 933-937
    • Sample, J.1    Liebowitz, D.2    Kieff, E.3
  • 10
    • 0023970454 scopus 로고
    • A spliced Epstein-Barr virus gene expressed in immortalized lymphocytes is created by circularization of the linear viral genome
    • Laux G., Perricaudet M., Farrell P. J. A spliced Epstein-Barr virus gene expressed in immortalized lymphocytes is created by circularization of the linear viral genome. EMBO J. 7:1988;769-774.
    • (1988) EMBO J. , vol.7 , pp. 769-774
    • Laux, G.1    Perricaudet, M.2    Farrell, P.J.3
  • 11
    • 0024451816 scopus 로고
    • The terminal protein gene 2 of Epstein-Barr virus is transcribed from a bidirectional latent promoter region
    • Laux G., Economou A., Farrell P. J. The terminal protein gene 2 of Epstein-Barr virus is transcribed from a bidirectional latent promoter region. J. Gen. Virol. 70:1989;3079-3084.
    • (1989) J. Gen. Virol. , vol.70 , pp. 3079-3084
    • Laux, G.1    Economou, A.2    Farrell, P.J.3
  • 12
    • 0025915585 scopus 로고
    • An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase
    • Longnecker R., Druker B., Roberts T. M., Kieff E. An Epstein-Barr virus protein associated with cell growth transformation interacts with a tyrosine kinase. J. Virol. 65:1991;3681-3692.
    • (1991) J. Virol. , vol.65 , pp. 3681-3692
    • Longnecker, R.1    Druker, B.2    Roberts, T.M.3    Kieff, E.4
  • 13
    • 0025305417 scopus 로고
    • A second Epstein-Barr virus membrane protein (LMP2) is expressed in latent infection and colocalizes with LMP1
    • Longnecker R., Kieff E. A second Epstein-Barr virus membrane protein (LMP2) is expressed in latent infection and colocalizes with LMP1. J. Virol. 64:1990;2319-2326.
    • (1990) J. Virol. , vol.64 , pp. 2319-2326
    • Longnecker, R.1    Kieff, E.2
  • 14
    • 0028971196 scopus 로고
    • 5′ Coding and regulatory region sequence divergence with conserved function of the Epstein-Barr virus LMP2A homolog in herpesvirus papio
    • Franken M., Annis B., Ali A. N., Wang F. 5′ Coding and regulatory region sequence divergence with conserved function of the Epstein-Barr virus LMP2A homolog in herpesvirus papio. J. Virol. 69:1995;8011-8019.
    • (1995) J. Virol. , vol.69 , pp. 8011-8019
    • Franken, M.1    Annis, B.2    Ali, A.N.3    Wang, F.4
  • 15
    • 0033025948 scopus 로고    scopus 로고
    • Signal transduction from the B cell antigen-receptor
    • Campbell K. S. Signal transduction from the B cell antigen-receptor. Curr. Opin. Immunol. 11:1999;256-264.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 256-264
    • Campbell, K.S.1
  • 16
    • 0033118746 scopus 로고    scopus 로고
    • B cell development: Signal transduction by antigen receptors and their surrogates
    • Benschop R. J., Cambier J. C. B cell development: signal transduction by antigen receptors and their surrogates. Curr. Opin. Immunol. 11:1999;143-151.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 143-151
    • Benschop, R.J.1    Cambier, J.C.2
  • 17
    • 0031661310 scopus 로고    scopus 로고
    • Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latency
    • Fruehling S., Swart R., Dolwick K. M., Kremmer E., Longnecker R. Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latency. J. Virol. 72:1998;7796-7806.
    • (1998) J. Virol. , vol.72 , pp. 7796-7806
    • Fruehling, S.1    Swart, R.2    Dolwick, K.M.3    Kremmer, E.4    Longnecker, R.5
  • 18
    • 0030754766 scopus 로고    scopus 로고
    • The immunoreceptor tyrosine-based activation motif of Epstein-Barr virus LMP2A is essential for blocking BCR-mediated signal transduction
    • Fruehling S., Longnecker R. The immunoreceptor tyrosine-based activation motif of Epstein-Barr virus LMP2A is essential for blocking BCR-mediated signal transduction. Virology. 235:1997;241-251.
    • (1997) Virology , vol.235 , pp. 241-251
    • Fruehling, S.1    Longnecker, R.2
  • 19
    • 0028970289 scopus 로고
    • Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases
    • Miller C. L., Burkhardt A. L., Lee J. H., Stealey B., Longnecker R., Bolen J. B., Kieff E. Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases. Immunity. 2:1995;155-166.
    • (1995) Immunity , vol.2 , pp. 155-166
    • Miller, C.L.1    Burkhardt, A.L.2    Lee, J.H.3    Stealey, B.4    Longnecker, R.5    Bolen, J.B.6    Kieff, E.7
  • 20
    • 0026720952 scopus 로고
    • An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases
    • Burkhardt A. L., Bolen J. B., Kieff E., Longnecker R. An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinases. J. Virol. 66:1992;5161-5167.
    • (1992) J. Virol. , vol.66 , pp. 5161-5167
    • Burkhardt, A.L.1    Bolen, J.B.2    Kieff, E.3    Longnecker, R.4
  • 21
    • 0032913903 scopus 로고    scopus 로고
    • Sequence polymorphisms between latent membrane proteins LMP1 and LMP2A do not correlate in EBV-associated reactive and malignant lympho-proliferations
    • Berger C., Rothenberger S., Bachmann E., McQuain C., Nadal D., Knecht H. Sequence polymorphisms between latent membrane proteins LMP1 and LMP2A do not correlate in EBV-associated reactive and malignant lympho-proliferations. Int. J. Cancer. 81:1999;371-375.
    • (1999) Int. J. Cancer , vol.81 , pp. 371-375
    • Berger, C.1    Rothenberger, S.2    Bachmann, E.3    McQuain, C.4    Nadal, D.5    Knecht, H.6
  • 22
    • 0028890805 scopus 로고
    • Sequence polymorphism in the Epstein-Barr virus latent membrane protein (LMP)-2 gene
    • Busson P., Edwards R. H., Tursz T., Raab Traub N. Sequence polymorphism in the Epstein-Barr virus latent membrane protein (LMP)-2 gene. J. Gen. Virol. 76:1995;139-145.
    • (1995) J. Gen. Virol. , vol.76 , pp. 139-145
    • Busson, P.1    Edwards, R.H.2    Tursz, T.3    Raab Traub, N.4
  • 23
    • 0032541641 scopus 로고    scopus 로고
    • From Src Homology domains to other signaling modules: Proposal of the 'protein recognition code'
    • Sudol M. From Src Homology domains to other signaling modules: proposal of the 'protein recognition code'. Oncogene. 17:1998;1469-1474.
    • (1998) Oncogene , vol.17 , pp. 1469-1474
    • Sudol, M.1
  • 25
    • 0030910308 scopus 로고    scopus 로고
    • FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands
    • Bedford M. T., Chan D. C., Leder P. FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands. EMBO J. 16:1997;2376-2383.
    • (1997) EMBO J. , vol.16 , pp. 2376-2383
    • Bedford, M.T.1    Chan, D.C.2    Leder, P.3
  • 26
    • 0029146950 scopus 로고
    • Characterization of a novel protein-binding module - The WW domain
    • Sudol M., Chen H. I., Bougeret C., Einbond A., Bork P. Characterization of a novel protein-binding module - the WW domain. FEBS Lett. 369:1995;67-71.
    • (1995) FEBS Lett. , vol.369 , pp. 67-71
    • Sudol, M.1    Chen, H.I.2    Bougeret, C.3    Einbond, A.4    Bork, P.5
  • 27
    • 0030424581 scopus 로고    scopus 로고
    • Structure and function of the WW domain
    • Sudol M. Structure and function of the WW domain. Prog. Biophys. Mol. Biol. 65:1996;113-132.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 113-132
    • Sudol, M.1
  • 28
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay B. K., Williamson M. P., Sudol M. The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14:1999;231-241.
    • (1999) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 29
    • 0033546329 scopus 로고    scopus 로고
    • A single point mutation in a group I WW domain shifts its specificity to that of group II WW domains
    • Espanel X., Sudol M. A single point mutation in a group I WW domain shifts its specificity to that of group II WW domains. J. Biol. Chem. 274:1999;17284-17289.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17284-17289
    • Espanel, X.1    Sudol, M.2
  • 30
    • 0029099161 scopus 로고
    • The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules
    • Chen H. I., Sudol M. The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. Proc. Natl. Acad. Sci. USA. 92:1995;7819-7823.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7819-7823
    • Chen, H.I.1    Sudol, M.2
  • 31
    • 0029915066 scopus 로고    scopus 로고
    • Towards prediction of cognate complexes between the WW domain and proline-rich ligands
    • Einbond A., Sudol M. Towards prediction of cognate complexes between the WW domain and proline-rich ligands. FEBS Lett. 384:1996;1-8.
    • (1996) FEBS Lett. , vol.384 , pp. 1-8
    • Einbond, A.1    Sudol, M.2
  • 32
    • 0029775570 scopus 로고    scopus 로고
    • Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide
    • Macias M. J., Hyvonen M., Baraldi E., Schultz J., Sudol M., Saraste M., Oschkinat H. Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature. 382:1996;646-649.
    • (1996) Nature , vol.382 , pp. 646-649
    • Macias, M.J.1    Hyvonen, M.2    Baraldi, E.3    Schultz, J.4    Sudol, M.5    Saraste, M.6    Oschkinat, H.7
  • 33
    • 0030858496 scopus 로고    scopus 로고
    • Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands
    • Chen H. I., Einbond A., Kwak S. J., Linn H., Koepf E., Peterson S., Kelly J. W., Sudol M. Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands. J. Biol. Chem. 272:1997;17070-17077.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17070-17077
    • Chen, H.I.1    Einbond, A.2    Kwak, S.J.3    Linn, H.4    Koepf, E.5    Peterson, S.6    Kelly, J.W.7    Sudol, M.8
  • 35
    • 0033050343 scopus 로고    scopus 로고
    • Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras
    • Craven R. C., Harty R. N., Paragas J., Palese P., Wills J. W. Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras. J. Virol. 73:1999;3359-3365.
    • (1999) J. Virol. , vol.73 , pp. 3359-3365
    • Craven, R.C.1    Harty, R.N.2    Paragas, J.3    Palese, P.4    Wills, J.W.5
  • 37
    • 0033050750 scopus 로고    scopus 로고
    • A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding
    • Harty R. N., Paragas J., Sudol M., Palese P. A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding. J. Virol. 73:1999;2921-2929.
    • (1999) J. Virol. , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 38
    • 0028283579 scopus 로고
    • Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product
    • Sudol M. Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product. Oncogene. 9:1994;2145-2152.
    • (1994) Oncogene , vol.9 , pp. 2145-2152
    • Sudol, M.1
  • 39
    • 0028997651 scopus 로고
    • Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain
    • Sudol M., Bork P., Einbond A., Kastury K., Druck T., Negrini M., Huebner K., Lehman D. Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain. J. Biol. Chem. 270:1995;14733-14741.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14733-14741
    • Sudol, M.1    Bork, P.2    Einbond, A.3    Kastury, K.4    Druck, T.5    Negrini, M.6    Huebner, K.7    Lehman, D.8
  • 41
    • 0031553972 scopus 로고    scopus 로고
    • Examining the specificity of Src homology 3 domain - Ligand interactions with alkaline phosphatase fusion proteins
    • Yamabhai M., Kay B. K. Examining the specificity of Src homology 3 domain - ligand interactions with alkaline phosphatase fusion proteins. Anal. Biochem. 247:1997;143-151.
    • (1997) Anal. Biochem. , vol.247 , pp. 143-151
    • Yamabhai, M.1    Kay, B.K.2
  • 43
    • 0030796010 scopus 로고    scopus 로고
    • Inhibition of Lyn function in mast cell activation by SH3 domain binding peptides
    • Stauffer T. P., Martenson C. H., Rider J. E., Kay B. K., Meyer T. Inhibition of Lyn function in mast cell activation by SH3 domain binding peptides. Biochemistry. 36:1997;9388-9394.
    • (1997) Biochemistry , vol.36 , pp. 9388-9394
    • Stauffer, T.P.1    Martenson, C.H.2    Rider, J.E.3    Kay, B.K.4    Meyer, T.5
  • 44
    • 0034007009 scopus 로고    scopus 로고
    • The Epstein-Barr virus (EBV) latent membrane protein 2A (LMP2A) PY motif recruits WW domain-containing ubiquitin-protein ligases
    • Ikeda M., Ikeda A., Longan L. C., Longnecker R. The Epstein-Barr virus (EBV) latent membrane protein 2A (LMP2A) PY motif recruits WW domain-containing ubiquitin-protein ligases. Virology. 268:2000;178-191.
    • (2000) Virology , vol.268 , pp. 178-191
    • Ikeda, M.1    Ikeda, A.2    Longan, L.C.3    Longnecker, R.4
  • 46
    • 0032915455 scopus 로고    scopus 로고
    • The WW domain of dystrophin requires EF-hands region to interact with Beta-dystroglycan
    • Rentschler S., Linn H., Deininger K., Bedford M. T., Espanel X., Sudol M. The WW domain of dystrophin requires EF-hands region to interact with Beta-dystroglycan. Biol. Chem. 380:1999;431-442.
    • (1999) Biol. Chem. , vol.380 , pp. 431-442
    • Rentschler, S.1    Linn, H.2    Deininger, K.3    Bedford, M.T.4    Espanel, X.5    Sudol, M.6
  • 47
    • 9444288215 scopus 로고    scopus 로고
    • Identification of latent membrane protein 2A (LMP2A) domains essential for the LMP2A dominant-negative effect on B-lymphocyte surface immunoglobulin signal transduction
    • Fruehling S., Lee S. K., Herrold R., Frech B., Laux G., Kremmer E., Grasser F. A., Longnecker R. Identification of latent membrane protein 2A (LMP2A) domains essential for the LMP2A dominant-negative effect on B-lymphocyte surface immunoglobulin signal transduction. J. Virol. 70:1996;6216-6226.
    • (1996) J. Virol. , vol.70 , pp. 6216-6226
    • Fruehling, S.1    Lee, S.K.2    Herrold, R.3    Frech, B.4    Laux, G.5    Kremmer, E.6    Grasser, F.A.7    Longnecker, R.8
  • 48
    • 0028088994 scopus 로고
    • An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking
    • Miller C. L., Lee J. H., Kieff E., Longnecker R. An integral membrane protein (LMP2) blocks reactivation of Epstein-Barr virus from latency following surface immunoglobulin crosslinking. Proc. Natl. Acad. Sci. USA. 91:1994;772-776.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 772-776
    • Miller, C.L.1    Lee, J.H.2    Kieff, E.3    Longnecker, R.4
  • 49
    • 0027170920 scopus 로고
    • SH3 domains direct cellular localization of signaling molecules
    • Bar-Sagi D., Rotin D., Batzer A., Mandiyan V., Schlessinger J. SH3 domains direct cellular localization of signaling molecules. Cell. 74:1993;83-91.
    • (1993) Cell , vol.74 , pp. 83-91
    • Bar-Sagi, D.1    Rotin, D.2    Batzer, A.3    Mandiyan, V.4    Schlessinger, J.5
  • 51
    • 0028198388 scopus 로고
    • Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit
    • Pleiman C. M., Hertz W. M., Cambier J. C. Activation of phosphatidylinositol-3′ kinase by Src-family kinase SH3 binding to the p85 subunit. Science. 263:1994;1609-1612.
    • (1994) Science , vol.263 , pp. 1609-1612
    • Pleiman, C.M.1    Hertz, W.M.2    Cambier, J.C.3
  • 53
    • 0029874436 scopus 로고    scopus 로고
    • WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome
    • Staub O., Dho S., Henry P., Correa J., Ishikawa T., McGlade J., Rotin D. WW domains of Nedd4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle's syndrome. EMBO J. 15:1996;2371-2380.
    • (1996) EMBO J. , vol.15 , pp. 2371-2380
    • Staub, O.1    Dho, S.2    Henry, P.3    Correa, J.4    Ishikawa, T.5    McGlade, J.6    Rotin, D.7
  • 54
    • 0032907946 scopus 로고    scopus 로고
    • Functional domains of the Rsp5 ubiquitin-protein ligase
    • Wang G., Yang J., Huibregtse J. M. Functional domains of the Rsp5 ubiquitin-protein ligase. Mol. Cell. Biol. 19:1999;342-352.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 342-352
    • Wang, G.1    Yang, J.2    Huibregtse, J.M.3
  • 55
    • 0029981652 scopus 로고    scopus 로고
    • Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan D. C., Bedford M. T., Leder P. Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15:1996;1045-1054.
    • (1996) EMBO J. , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 56
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- Or phosphothreonine-binding modules
    • Lu P. J., Zhou X. Z., Shen M., Lu K. P. Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science. 283:1999;1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1    Zhou, X.Z.2    Shen, M.3    Lu, K.P.4
  • 57
    • 0033571594 scopus 로고    scopus 로고
    • Yes-associated protein 65 localizes p62 (c-Yes) to the apical compartment of airway epithelial cells
    • Mohler P. J., Kreda S. M., Boucher R. C., Sudol M., Stutts M. J., Milgram S. L. Yes-associated protein 65 localizes p62 (c-Yes) to the apical compartment of airway epithelial cells. J. Cell Biol. 147:1999;879-890.
    • (1999) J. Cell Biol. , vol.147 , pp. 879-890
    • Mohler, P.J.1    Kreda, S.M.2    Boucher, R.C.3    Sudol, M.4    Stutts, M.J.5    Milgram, S.L.6


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