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0028786330
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The Wiskott-Aldrich syndrome and X-linked congenital thrombocytopenia are caused by mutations of the same gene
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X-linked thrombocytopenia and Wiskott-Aldrich syndrome are allelic diseases with mutations in the WASP gene
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Villa A, Notarangelo L, Macchi P, Mantuano E, Cavagni G, Brugnoni D, Strina D, Patrosso MC, Ramenghi U, Sacco MG, et al. X-linked thrombocytopenia and Wiskott-Aldrich syndrome are allelic diseases with mutations in the WASP gene. Nat Genet. 9:1995;414-417.
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Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus
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Kolluri R, Shehabeldin A, Peacocke M, Lamhonwah AM, Teichert-Kuliszewska K, Weissman SM, Siminovitch KA. Identification of WASP mutations in patients with Wiskott-Aldrich syndrome and isolated thrombocytopenia reveals allelic heterogeneity at the WAS locus. Hum Mol Genet. 4:1995;1119-1126.
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8
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11
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Gröttum KA, Hovig T, Holmsen H, Abrahamsen AF, Jeremic M, Seip M. Wiskott-Aldrich syndrome: qualitative platelet defects and short platelet survival. Br J Haematol. 17:1969;373-388.
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Litzman J, Jones A, Hann I, Chapel H, Strobel S, Morgan G. Intravenous immunoglobulin, splenectomy, and antibiotic prophylaxis in Wiskott-Aldrich syndrome. Arch Dis Child. 75:1996;436-439.
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15
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Isolation of a novel gene mutated in Wiskott-Aldrich syndrome
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Derry JMJ, Ochs HD, Francke U. Isolation of a novel gene mutated in Wiskott-Aldrich syndrome. Cell. 78:1994;635-644. [Published erratum appears in Cell 1994, 79: following p922.].
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Derry, J.M.J.1
Ochs, H.D.2
Francke, U.3
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16
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0029112720
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The mouse homolog of the Wiskott-Aldrich syndrome protein (WASP) gene is highly conserved and maps near the scurfy (sf) mutation on the X chromosome
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Derry JMJ, Wiedermann P, Blair P, Wang Y, Kerns JA, Lemahieu V, Godfrey VL, Wilkinson JE, Francke U. The mouse homolog of the Wiskott-Aldrich syndrome protein (WASP) gene is highly conserved and maps near the scurfy (sf) mutation on the X chromosome. Genomics. 29:1995;471-477.
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Genomics
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Derry, J.M.J.1
Wiedermann, P.2
Blair, P.3
Wang, Y.4
Kerns, J.A.5
Lemahieu, V.6
Godfrey, V.L.7
Wilkinson, J.E.8
Francke, U.9
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17
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0029815611
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N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
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Miki H, Miura K, Takenawa T. N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15:1996;5326-5335.
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Miki, H.1
Miura, K.2
Takenawa, T.3
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18
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0030767455
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Identification of N-WASP homologs in human and rat brain
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Fukuoka M, Miki H, Takenawa T. Identification of N-WASP homologs in human and rat brain. Gene. 196:1997;43-48.
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Gene
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Fukuoka, M.1
Miki, H.2
Takenawa, T.3
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19
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0031045512
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Bee1, a yeast protein with homology to Wiskott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton
-
of special interest. This paper reports that Bee1 is a yeast homologue of WASP and plays an important role in cytoskeletal organization.
-
of special interest Li R. Bee1, a yeast protein with homology to Wiskott-Aldrich syndrome protein, is critical for the assembly of cortical actin cytoskeleton. J Cell Biol. 136:1997;649-658 This paper reports that Bee1 is a yeast homologue of WASP and plays an important role in cytoskeletal organization.
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(1997)
J Cell Biol
, vol.136
, pp. 649-658
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Li, R.1
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20
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0030006284
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Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
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Symons M, Derry JMJ, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell. 84:1996;723-734.
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(1996)
Cell
, vol.84
, pp. 723-734
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Symons, M.1
Derry, J.M.J.2
Karlak, B.3
Jiang, S.4
Lemahieu, V.5
McCormick, F.6
Francke, U.7
Abo, A.8
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21
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0030728030
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Identification of homer as a homologue of the Wiskott-Aldrich syndrome protein suggests a receptor-binding function for WH1 domains
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Ponting CP, Phillips C. Identification of homer as a homologue of the Wiskott-Aldrich syndrome protein suggests a receptor-binding function for WH1 domains. J Mol Med. 75:1997;769-771.
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(1997)
J Mol Med
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, pp. 769-771
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Ponting, C.P.1
Phillips, C.2
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22
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20244379555
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WASPbase: A database of WAS- And XLT-causing mutations
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Schwarz K, Nonoyama S, Peitsch MC, de Saint Basile G, Espanol T, Fasth A, Fischer A, Freitag K, Friedrich W, Fugmann S, et al. WASPbase: a database of WAS- and XLT-causing mutations. Immunol Today. 17:1996;496-502.
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(1996)
Immunol Today
, vol.17
, pp. 496-502
-
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Schwarz, K.1
Nonoyama, S.2
Peitsch, M.C.3
De Saint Basile, G.4
Espanol, T.5
Fasth, A.6
Fischer, A.7
Freitag, K.8
Friedrich, W.9
Fugmann, S.10
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23
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0030820924
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A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
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Rameh LE, Arvidsson AK, Carraway KL III, Couvillon AD, Rathbun G, Crompton A, VanRenterghem B, Czech MP, Ravichandran KS, Burakoff SJ, et al. A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains. J Biol Chem. 272:1997;22059-22066.
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(1997)
J Biol Chem
, vol.272
, pp. 22059-22066
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Rameh, L.E.1
Arvidsson, A.K.2
Carraway K.L. III3
Couvillon, A.D.4
Rathbun, G.5
Crompton, A.6
Vanrenterghem, B.7
Czech, M.P.8
Ravichandran, K.S.9
Burakoff, S.J.10
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24
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0029939448
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PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
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Lemmon MA, Ferguson KM, Schlessinger J. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell. 85:1996;621-624.
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(1996)
Cell
, vol.85
, pp. 621-624
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Lemmon, M.A.1
Ferguson, K.M.2
Schlessinger, J.3
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25
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0029680639
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Two GTPases, cdc42 and rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich Syndrome
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Aspenström P, Lindberg U, Hall A. Two GTPases, cdc42 and rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich Syndrome. Curr Biol. 6:1996;70-75.
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(1996)
Curr Biol
, vol.6
, pp. 70-75
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Aspenström, P.1
Lindberg, U.2
Hall, A.3
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26
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0029953158
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Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42
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Kolluri R, Tolias KF, Carpenter CL, Rosen FS, Kirchhausen T. Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42. Proc Natl Acad Sci USA. 93:1996;5615-5618.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 5615-5618
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Kolluri, R.1
Tolias, K.F.2
Carpenter, C.L.3
Rosen, F.S.4
Kirchhausen, T.5
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27
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0030298138
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PAK and the JNK/SAPK MAP kinase cascade
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PAK and the JNK/SAPK MAP kinase cascade. Cell. 87:1996;519-529.
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(1996)
Cell
, vol.87
, pp. 519-529
-
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Lamarche, N.1
Tapon, N.2
Stowers, L.3
Burbelo, P.D.4
Aspenström, P.5
Bridges, T.6
Chant, J.7
Hall, A.8
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28
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0031952518
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Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
-
of outstanding interest. This article demonstrates that N-WASP is an effector molecule of Cdc42 and is involved in filopodium induction; it proposes a model that conformational change of N-WASP caused by binding with Cdc42 is necessary for the regulation of actin polymerization.
-
of outstanding interest Miki H, Sasaki T, Takai Y, Takenawa T. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature. 391:1998;93-96 This article demonstrates that N-WASP is an effector molecule of Cdc42 and is involved in filopodium induction; it proposes a model that conformational change of N-WASP caused by binding with Cdc42 is necessary for the regulation of actin polymerization.
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(1998)
Nature
, vol.391
, pp. 93-96
-
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Miki, H.1
Sasaki, T.2
Takai, Y.3
Takenawa, T.4
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29
-
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0030773047
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Characterization of the interactions between the small GTPase Cdc42 and its GTPase-activating proteins and putative effectors. Comparison of kinetic properties of Cdc42 binding to the Cdc42-interactive domains
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Zhang B, Wang ZX, Zheng Y. Characterization of the interactions between the small GTPase Cdc42 and its GTPase-activating proteins and putative effectors. Comparison of kinetic properties of Cdc42 binding to the Cdc42-interactive domains. J Biol Chem. 272:1997;21999-22007.
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(1997)
J Biol Chem
, vol.272
, pp. 21999-22007
-
-
Zhang, B.1
Wang, Z.X.2
Zheng, Y.3
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30
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0031032251
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Tyrosine kinase signaling regulates Wiskott-Aldrich syndrome protein function, which is essential for megakaryocyte differentiation
-
of outstanding interest. This article describes the involvement of WASP in megakaryocyte differentiation in a manner dependent on tyrosine kinases.
-
of outstanding interest Miki H, Nonoyama S, Zhu Q, Aruffo A, Ochs HD, Takenawa T. Tyrosine kinase signaling regulates Wiskott-Aldrich syndrome protein function, which is essential for megakaryocyte differentiation. Cell Growth Differ. 8:1997;195-202 This article describes the involvement of WASP in megakaryocyte differentiation in a manner dependent on tyrosine kinases.
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(1997)
Cell Growth Differ
, vol.8
, pp. 195-202
-
-
Miki, H.1
Nonoyama, S.2
Zhu, Q.3
Aruffo, A.4
Ochs, H.D.5
Takenawa, T.6
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31
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0029126878
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Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains
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Rivero-Lezcano OM, Marcilla A, Sameshima JH, Robbins KC. Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains. Mol Cell Biol. 15:1995;5725-5731.
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(1995)
Mol Cell Biol
, vol.15
, pp. 5725-5731
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Rivero-Lezcano, O.M.1
Marcilla, A.2
Sameshima, J.H.3
Robbins, K.C.4
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32
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0030793720
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Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells
-
of special interest. This group demonstrates that, functionally, WASP is located downstream of the EGF receptor and suggests that WASP links receptor tyrosine kinases to the actin cytoskeleton.
-
of special interest She H-Y, Rockow S, Tang J, Nishimura R, Skolink EY, Chen M, Margolis B, Li W. Wiskott-Aldrich syndrome protein is associated with the adapter protein Grb2 and the epidermal growth factor receptor in living cells. Mol Biol Cell. 8:1997;1709-1721 This group demonstrates that, functionally, WASP is located downstream of the EGF receptor and suggests that WASP links receptor tyrosine kinases to the actin cytoskeleton.
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(1997)
Mol Biol Cell
, vol.8
, pp. 1709-1721
-
-
She H-Y1
Rockow, S.2
Tang, J.3
Nishimura, R.4
Skolink, E.Y.5
Chen, M.6
Margolis, B.7
Li, W.8
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33
-
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0030221475
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Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases
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Banin S, Truong O, Katz DR, Waterfield MD, Brickell PM, Gout I. Wiskott-Aldrich syndrome protein (WASp) is a binding partner for c-Src family protein-tyrosine kinases. Curr Biol. 6:1996;981-988.
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(1996)
Curr Biol
, vol.6
, pp. 981-988
-
-
Banin, S.1
Truong, O.2
Katz, D.R.3
Waterfield, M.D.4
Brickell, P.M.5
Gout, I.6
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34
-
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0030804315
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Wiskott-Aldrich syndrome/X-linked thrombocytopenia: WASP mutations, protein expression, and phenotype
-
of outstanding interest. This paper reports a phenotype/genotype correlation by analyzing mutations in WASP, the gene responsible for WAS, in 48 unrelated families. The clinical phenotype of X-linked thrombocytopenia (XLT) is delineated and the mutations associated with XLT described. The effect of WASP mutations on expression of WAS protein has been analyzed in patients with either classic WAS or XLT.
-
of outstanding interest Zhu Q, Watanabe C, Liu T, Hollenbaugh D, Blaese RM, Kanner SB, Aruffo A, Ochs HD. Wiskott-Aldrich syndrome/X-linked thrombocytopenia: WASP mutations, protein expression, and phenotype. Blood. 90:1997;2680-2689 This paper reports a phenotype/genotype correlation by analyzing mutations in WASP, the gene responsible for WAS, in 48 unrelated families. The clinical phenotype of X-linked thrombocytopenia (XLT) is delineated and the mutations associated with XLT described. The effect of WASP mutations on expression of WAS protein has been analyzed in patients with either classic WAS or XLT.
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(1997)
Blood
, vol.90
, pp. 2680-2689
-
-
Zhu, Q.1
Watanabe, C.2
Liu, T.3
Hollenbaugh, D.4
Blaese, R.M.5
Kanner, S.B.6
Aruffo, A.7
Ochs, H.D.8
-
35
-
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0030000795
-
Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains
-
Finan PM, Soames CJ, Wilson L, Nelson DL, Stewart DM, Truong O, Hsuan JJ, Kellie S. Identification of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains. J Biol Chem. 271:1996;26291-26295.
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(1996)
J Biol Chem
, vol.271
, pp. 26291-26295
-
-
Finan, P.M.1
Soames, C.J.2
Wilson, L.3
Nelson, D.L.4
Stewart, D.M.5
Truong, O.6
Hsuan, J.J.7
Kellie, S.8
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36
-
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0030292702
-
Evidence that the Wiskott-Aldrich syndrome protein may be involved in lymphoid cell signaling pathways
-
Cory GOC, MacCarthy-Morrogh L, Banin S, Gout I, Brickell PM, Levinsky RJ, Kinnon C, Lovering RC. Evidence that the Wiskott-Aldrich syndrome protein may be involved in lymphoid cell signaling pathways. J Immunol. 157:1996;3791-3795.
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(1996)
J Immunol
, vol.157
, pp. 3791-3795
-
-
Cory, G.O.C.1
MacCarthy-Morrogh, L.2
Banin, S.3
Gout, I.4
Brickell, P.M.5
Levinsky, R.J.6
Kinnon, C.7
Lovering, R.C.8
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37
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0029834340
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Identification of ltk/Tsk Src homology 3 domain ligands
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Bunnell SC, Henry PA, Kolluri R, Kirchhausen T, Rickles RJ, Berg LJ. Identification of ltk/Tsk Src homology 3 domain ligands. J Biol Chem. 271:1996;25646-25656.
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(1996)
J Biol Chem
, vol.271
, pp. 25646-25656
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Bunnell, S.C.1
Henry, P.A.2
Kolluri, R.3
Kirchhausen, T.4
Rickles, R.J.5
Berg, L.J.6
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38
-
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0032489515
-
Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein
-
of special interest. This group found that association of WASP and PSTPIP (proline-, serine-threonine- phosphatase interactive protein) decreases the actin-bundling activity of WASP and that the association is regulated by the phosphorylation of a tyrosine residue in the Src-homology-3 domain of PSTPIP.
-
of special interest Wu Y, Spencer SD, Lasky LA. Tyrosine phosphorylation regulates the SH3-mediated binding of the Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein. J Biol Chem. 273:1998;5765-5770 This group found that association of WASP and PSTPIP (proline-, serine-threonine- phosphatase interactive protein) decreases the actin-bundling activity of WASP and that the association is regulated by the phosphorylation of a tyrosine residue in the Src-homology-3 domain of PSTPIP.
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(1998)
J Biol Chem
, vol.273
, pp. 5765-5770
-
-
Wu, Y.1
Spencer, S.D.2
Lasky, L.A.3
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39
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0032481290
-
Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization
-
Miki H, Takenawa T. Direct binding of the verprolin-homology domain in N-WASP to actin is essential for cytoskeletal reorganization. Biochem Biophys Res Commun. 243:1998;73-78.
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(1998)
Biochem Biophys Res Commun
, vol.243
, pp. 73-78
-
-
Miki, H.1
Takenawa, T.2
-
40
-
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0027488669
-
A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae
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Donnelly SF, Pocklington MJ, Pallotta D, Orr E. A proline-rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiae. Mol Microbiol. 10:1993;585-596.
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(1993)
Mol Microbiol
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, pp. 585-596
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Donnelly, S.F.1
Pocklington, M.J.2
Pallotta, D.3
Orr, E.4
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41
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0021749110
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Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin
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Nishida E, Maekawa S, Sakai H. Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interactions with myosin and tropomyosin. Biochemistry USA. 23:1984;5307-5313.
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Nishida, E.1
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42
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0031446340
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WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells
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of outstanding interest. This group has identified a new WASP-associating molecule, WIP, which induces actin polymerization in lymphoid cells.
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of outstanding interest Ramesh N, Antón IM, Hartwig JH, Geha RS. WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proc Natl Acad Sci USA. 94:1997;14671-14676 This group has identified a new WASP-associating molecule, WIP, which induces actin polymerization in lymphoid cells.
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Ramesh, N.1
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0028932527
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Nonrandom inactivation of the X chromosome in early lineage hematopoietic cells in carriers of Wiskott-Aldrich syndrome
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Wengler G, Gorlin JB, Williamson JM, Rosen FS, Bing DH. Nonrandom inactivation of the X chromosome in early lineage hematopoietic cells in carriers of Wiskott-Aldrich syndrome. Blood. 85:1995;2471-2477.
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44
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0030816363
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Defective actin reorganization and polymerization of Wiskott-Aldrich T cells in response to CD3-mediated stimulation
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of special interest. This article reports that cell lines from patients with Wiskott - Aldrich syndrome fail to reorganize actin cytoskeleton in response to anti-CD3 stimulation
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of special interest Gallego MD, Santamaria M, Peña J, Molina IJ. Defective actin reorganization and polymerization of Wiskott-Aldrich T cells in response to CD3-mediated stimulation. Blood. 90:1997;3089-3097 This article reports that cell lines from patients with Wiskott - Aldrich syndrome fail to reorganize actin cytoskeleton in response to anti-CD3 stimulation.
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Gallego, M.D.1
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Peña, J.3
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Actin polymerization and pseudopod reorganization accompany anti-CD3-induced growth arrest in Jurkat T cells
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Parsey MV, Lewis GK. Actin polymerization and pseudopod reorganization accompany anti-CD3-induced growth arrest in Jurkat T cells. J Immunol. 151:1993;1881-1893.
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Parsey, M.V.1
Lewis, G.K.2
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Regulation of the polarization of T cells toward antigen-presenting cells by Ras-related GTPase CDC42
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Stowers, L.1
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Chant, J.4
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