-
2
-
-
0028827312
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The complete sequence of the coding region of the ATM gene reveals similarity to cell cycle regulators in different species
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Savitsky K, Sfez S, Tagle DA, Ziv Y, Sartiel A, Collins FS, Shiloh Y, Rotman G. The complete sequence of the coding region of the ATM gene reveals similarity to cell cycle regulators in different species. Hum Mol Genet. 4:1995;2025-2032.
-
(1995)
Hum Mol Genet
, vol.4
, pp. 2025-2032
-
-
Savitsky, K.1
Sfez, S.2
Tagle, D.A.3
Ziv, Y.4
Sartiel, A.5
Collins, F.S.6
Shiloh, Y.7
Rotman, G.8
-
3
-
-
0030933152
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The genetic defect in ataxia-telangiectasia
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Lavin M, Shiloh Y. The genetic defect in ataxia-telangiectasia. Annu Rev Immunol. 15:1997;177-202.
-
(1997)
Annu Rev Immunol
, vol.15
, pp. 177-202
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-
Lavin, M.1
Shiloh, Y.2
-
4
-
-
15844426692
-
Atm-deficient mice: A paradigm of ataxia telangiectasia
-
of special interest. The first description of a mouse deficient in ATM function. A number of ataxia telangiectasia phenotypes were detected with the ATM-deficient mice, including growth defects, sterility, meiotic chromosome fragmentation, reduction in mature lymphocytes, thymoma formation through chromosomal translocations and hypersensitivity to ionizing radiation.
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Barlow C, Hirotsune S, Paylor R, Liyanage M, Eckhaus M, Collins F, Shiloh Y, Crawley JN, Ried T, Tagle D, Wynshaw-Boris A. Atm-deficient mice: a paradigm of ataxia telangiectasia. of special interest Cell. 86:1996;159-171 The first description of a mouse deficient in ATM function. A number of ataxia telangiectasia phenotypes were detected with the ATM-deficient mice, including growth defects, sterility, meiotic chromosome fragmentation, reduction in mature lymphocytes, thymoma formation through chromosomal translocations and hypersensitivity to ionizing radiation.
-
(1996)
Cell
, vol.86
, pp. 159-171
-
-
Barlow, C.1
Hirotsune, S.2
Paylor, R.3
Liyanage, M.4
Eckhaus, M.5
Collins, F.6
Shiloh, Y.7
Crawley, J.N.8
Ried, T.9
Tagle, D.10
Wynshaw-Boris, A.11
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5
-
-
0029844048
-
Targeted disruption of ATM leads to growth retardation, chromosomal fragmentation during meiosis, immune defects and thymic lymphoma
-
of special interest. The second, independently generated strain of ATM-deficient mice exhibiting the same phenotypes as those prepared by Barlow et al. [4].
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Xu Y, Ashley T, Brainerd EE, Bronson T, Meyn MS, Baltimore D. Targeted disruption of ATM leads to growth retardation, chromosomal fragmentation during meiosis, immune defects and thymic lymphoma. of special interest Genes Dev. 10:1996;2411-2422 The second, independently generated strain of ATM-deficient mice exhibiting the same phenotypes as those prepared by Barlow et al. [4].
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(1996)
Genes Dev
, vol.10
, pp. 2411-2422
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-
Xu, Y.1
Ashley, T.2
Brainerd, E.E.3
Bronson, T.4
Meyn, M.S.5
Baltimore, D.6
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6
-
-
0029848286
-
Pleiotropic defects in ataxia-telangiectasia protein-deficient mice
-
of special interest. The third, independently generated strain of ATM-deficient mice with phenotypes similar to the other two ATM-deficient strains generated by Barlow et al. [4] and Xu et al. [5].
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Elson A, Wang Y, Daugherty C, Morton C, Zhou F, Campos-Torres J, Leder P. Pleiotropic defects in ataxia-telangiectasia protein-deficient mice. of special interest Proc Natl Acad Sci USA. 93:1996;13084-13089 The third, independently generated strain of ATM-deficient mice with phenotypes similar to the other two ATM-deficient strains generated by Barlow et al. [4] and Xu et al. [5].
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 13084-13089
-
-
Elson, A.1
Wang, Y.2
Daugherty, C.3
Morton, C.4
Zhou, F.5
Campos-Torres, J.6
Leder, P.7
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7
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0030977349
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Responses to DNA damage and regulation of cell cycle checkpoints by the ATM protein kinase family
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Hoekstra M. Responses to DNA damage and regulation of cell cycle checkpoints by the ATM protein kinase family. Curr Opin Genet Dev. 7:1997;170-175.
-
(1997)
Curr Opin Genet Dev
, vol.7
, pp. 170-175
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Hoekstra, M.1
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8
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0030052137
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From DNA damage to cell cycle arrest and suicide: A budding yeast perspective
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Lydall D, Weinert T. From DNA damage to cell cycle arrest and suicide: a budding yeast perspective. Curr Opin Genet Dev. 6:1996;4-11.
-
(1996)
Curr Opin Genet Dev
, vol.6
, pp. 4-11
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Lydall, D.1
Weinert, T.2
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9
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0029821651
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Dual roles of ATM in the cellular response to radiation and in cell growth control
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waf1/cip1.
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waf1/cip1.
-
(1996)
Genes Dev
, vol.10
, pp. 2401-2410
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Xu, Y.1
Baltimore, D.2
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10
-
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10244227923
-
The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes
-
of special interest. The cloning and the initial characterization of ATR, another Rad3/ATM family member, are described in this report. The differential localization of ATM and ATR on the pachytene chromosome pairs suggests that these two proteins may have distinct functions during spermatogenesis.
-
Keegan KS, Holtzman DA, Plug AW, Christenson ER, Brainerd EE, Flaggs G, Bentley NJ, Taylor EM, Meyn S, Moss S, et al. The Atr and Atm protein kinases associate with different sites along meiotically pairing chromosomes. of special interest Genes Dev. 10:1996;2423-2437 The cloning and the initial characterization of ATR, another Rad3/ATM family member, are described in this report. The differential localization of ATM and ATR on the pachytene chromosome pairs suggests that these two proteins may have distinct functions during spermatogenesis.
-
(1996)
Genes Dev
, vol.10
, pp. 2423-2437
-
-
Keegan, K.S.1
Holtzman, D.A.2
Plug, A.W.3
Christenson, E.R.4
Brainerd, E.E.5
Flaggs, G.6
Bentley, N.J.7
Taylor, E.M.8
Meyn, S.9
Moss, S.10
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11
-
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0029156599
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DNA-dependent protein kinase catalytic subunit: A relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product
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Hartley K, Gell D, Smith G, Zhang H, Divecha N, Connelly M, Admon A, Lees-Miller S, Anderson C, Jackson S. DNA-dependent protein kinase catalytic subunit: a relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product. Cell. 82:1995;849-856.
-
(1995)
Cell
, vol.82
, pp. 849-856
-
-
Hartley, K.1
Gell, D.2
Smith, G.3
Zhang, H.4
Divecha, N.5
Connelly, M.6
Admon, A.7
Lees-Miller, S.8
Anderson, C.9
Jackson, S.10
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12
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0028960511
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Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine SCID mutation.
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Blunt T, Finnie N, Taccioli G, Smith G, Demengeot J, Gottlieb T, Mizuta R, Varghese A, Alt F, Jeggo P. Defective DNA-dependent protein kinase activity is linked to V(D)J recombination and DNA repair defects associated with the murine SCID mutation. Cell. 80:1995;813-823.
-
(1995)
Cell
, vol.80
, pp. 813-823
-
-
Blunt, T.1
Finnie, N.2
Taccioli, G.3
Smith, G.4
Demengeot, J.5
Gottlieb, T.6
Mizuta, R.7
Varghese, A.8
Alt, F.9
Jeggo, P.10
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13
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0028902932
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Loss of the catalytic subunit of the DNA-dependent protein kinase in DNA double-strand-break-repair mutant mammalian cells
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Peterson S, Kurimasa A, Oshimura M, Dynan W, Bradbury E, Chen D. Loss of the catalytic subunit of the DNA-dependent protein kinase in DNA double-strand-break-repair mutant mammalian cells. Proc Natl Acad Sci USA. 92:1995;3171-3174.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 3171-3174
-
-
Peterson, S.1
Kurimasa, A.2
Oshimura, M.3
Dynan, W.4
Bradbury, E.5
Chen, D.6
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14
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0029858143
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V(D)J recombination activates a p53-dependent DNA damage checkpoint in SCID lymphocyte precursors
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Guidos C, Williams C, Grandal I, Knowles G, Manley T, Huang L-C, Danska J. V(D)J recombination activates a p53-dependent DNA damage checkpoint in SCID lymphocyte precursors. Genes Dev. 10:1996;1038-1054.
-
(1996)
Genes Dev
, vol.10
, pp. 1038-1054
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-
Guidos, C.1
Williams, C.2
Grandal, I.3
Knowles, G.4
Manley, T.5
Huang L-C6
Danska, J.7
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15
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0030925565
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Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation
-
of outstanding interest. The activation of c-Abl tyrosine kinase by ionizing radiation is shown to be defective in ATM-deficient mouse embryo fibroblasts, thymocytes and AT patient cells. IR activation of c-Abl is intact in p53-null cells. The coexpression of the ATM PI3K domain with c-Abl leads to the activation of c-Abl tyrosine kinase. Mutant ATM P13K does not activate c-Abl. Finally, IR induces the tyrosine phosphorylation of RNA polymerase II and this does not occur in AT patient cells. These results suggest that ATM may directly phosphorylate c-Abl at Ser465 to activate the tyrosine phosphorylation of RNA polymerase II.
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Baskaran R, Wood L, Whitaker L, Canman C, Morgan S, Xu Y, Barlow C, Baltimore D, Wynshaw-Boris A, Kastan M, Wang J. Ataxia telangiectasia mutant protein activates c-Abl tyrosine kinase in response to ionizing radiation. of outstanding interest Nature. 387:1997;516-519 The activation of c-Abl tyrosine kinase by ionizing radiation is shown to be defective in ATM-deficient mouse embryo fibroblasts, thymocytes and AT patient cells. IR activation of c-Abl is intact in p53-null cells. The coexpression of the ATM PI3K domain with c-Abl leads to the activation of c-Abl tyrosine kinase. Mutant ATM P13K does not activate c-Abl. Finally, IR induces the tyrosine phosphorylation of RNA polymerase II and this does not occur in AT patient cells. These results suggest that ATM may directly phosphorylate c-Abl at Ser465 to activate the tyrosine phosphorylation of RNA polymerase II.
-
(1997)
Nature
, vol.387
, pp. 516-519
-
-
Baskaran, R.1
Wood, L.2
Whitaker, L.3
Canman, C.4
Morgan, S.5
Xu, Y.6
Barlow, C.7
Baltimore, D.8
Wynshaw-Boris, A.9
Kastan, M.10
Wang, J.11
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16
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0030667702
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DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
-
of outstanding interest. The exposure of cells to ionizing radiation leads to the phosphorylation of p53 at Ser15, which is demonstrated using an antibody specific for the PS15 epitope; this is correlated with a reduction in the p53-Mdm2 complex. In vitro phosphorylation of p53 by DNA-PK at Ser15 and Ser37 can inhibit the binding of p53 to Mdm2. The phosphorylation of p53 by DNA-PK at Ser15 and Ser37 also alleviates Mdm2-mediated inhibition of p53-dependent transcription in vitro. These results suggest that the phosphorylation of p53 at Ser15 and Ser37 by DNA-PK or a DNA-PK-like protein kinase can disrupt the p53-Mdm2 interaction leading to the activation of p53.
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Shieh S-Y, Ikeda M, Taya Y, Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. of outstanding interest Cell. 91:1997;325-334 The exposure of cells to ionizing radiation leads to the phosphorylation of p53 at Ser15, which is demonstrated using an antibody specific for the PS15 epitope; this is correlated with a reduction in the p53-Mdm2 complex. In vitro phosphorylation of p53 by DNA-PK at Ser15 and Ser37 can inhibit the binding of p53 to Mdm2. The phosphorylation of p53 by DNA-PK at Ser15 and Ser37 also alleviates Mdm2-mediated inhibition of p53-dependent transcription in vitro. These results suggest that the phosphorylation of p53 at Ser15 and Ser37 by DNA-PK or a DNA-PK-like protein kinase can disrupt the p53-Mdm2 interaction leading to the activation of p53.
-
(1997)
Cell
, vol.91
, pp. 325-334
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-
Shieh S-Y1
Ikeda, M.2
Taya, Y.3
Prives, C.4
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17
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0030593033
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Regulation of RAD53 by the ATM-like kinases Mec1 and Tel1 in yeast cell cycle checkpoint pathways
-
of special interest. RAD53 is shown to become phosphorylated when budding yeast is exposed to DNA-damaging agents and this increased phosphorylation is not observed in mec1 mutants. The overproduction of TEL1 can rescue RAD53 phosphorylation and mec1 mutant phenotypes. A point mutation that disrupts RAD53 kinase activity can still become phosphorylated in response to DNA damage. These results suggest that MEC1 and TEL1 are upstream regulators of RAD53 phosphorylation in the DNA damage response.
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Sanchez Y, Desany BA, Jones WJ, Liu Q, Wang B, Ellegdge SJ. Regulation of RAD53 by the ATM-like kinases Mec1 and Tel1 in yeast cell cycle checkpoint pathways. of special interest Science. 271:1996;357-360 RAD53 is shown to become phosphorylated when budding yeast is exposed to DNA-damaging agents and this increased phosphorylation is not observed in mec1 mutants. The overproduction of TEL1 can rescue RAD53 phosphorylation and mec1 mutant phenotypes. A point mutation that disrupts RAD53 kinase activity can still become phosphorylated in response to DNA damage. These results suggest that MEC1 and TEL1 are upstream regulators of RAD53 phosphorylation in the DNA damage response.
-
(1996)
Science
, vol.271
, pp. 357-360
-
-
Sanchez, Y.1
Desany, B.A.2
Jones, W.J.3
Liu, Q.4
Wang, B.5
Ellegdge, S.J.6
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18
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0029928222
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Spk1/Rad53 is regulated by Mec1-dependent protein phosphorylation in DNA replication and DNA damage checkpoint pathways
-
of special interest. An independent study arriving at the same conclusion as Sanchez et al. [17]. RAD53 phosphorylation is linked to the activation of RAD53 kinase activity in this study. Thus, MEC1 and TEL1 are required to activate RAD53 kinase in the DNA damage response.
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Sun Z, Fay DS, Marini F, Foiani M, Stern DF. Spk1/Rad53 is regulated by Mec1-dependent protein phosphorylation in DNA replication and DNA damage checkpoint pathways. of special interest Genes Dev. 10:1996;395-406 An independent study arriving at the same conclusion as Sanchez et al. [17]. RAD53 phosphorylation is linked to the activation of RAD53 kinase activity in this study. Thus, MEC1 and TEL1 are required to activate RAD53 kinase in the DNA damage response.
-
(1996)
Genes Dev
, vol.10
, pp. 395-406
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-
Sun, Z.1
Fay, D.S.2
Marini, F.3
Foiani, M.4
Stern, D.F.5
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19
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0029664616
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Rad-dependent response of the Chk1-encoded protein kinase at the DNA damage checkpoint
-
of special interest. This report first describes the Rad3-dependent activation of Chk1 in the DNA damage response. A panel of S. pombe mutants were examined for the activation of Chk1. In addition to Rad3, several other Rad mutants were found to affect the activation of Chk1, indicating that several protein functions are required as upstream regulators of Chk1 activity. A UV repair mutant, however, shows normal activation of Chk1. The repair mutant is hypersensitive to UV, despite the normal checkpoint response. These results confirm that DNA repair and cell-cycle checkpoints are distinct downstream components of the DNA damage response pathways and both DNA repair and cell-cycle checkpoints are essential to surviving DNA damage.
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Walworth N, Bernards R. Rad-dependent response of the Chk1-encoded protein kinase at the DNA damage checkpoint. of special interest Science. 271:1996;353-356 This report first describes the Rad3-dependent activation of Chk1 in the DNA damage response. A panel of S. pombe mutants were examined for the activation of Chk1. In addition to Rad3, several other Rad mutants were found to affect the activation of Chk1, indicating that several protein functions are required as upstream regulators of Chk1 activity. A UV repair mutant, however, shows normal activation of Chk1. The repair mutant is hypersensitive to UV, despite the normal checkpoint response. These results confirm that DNA repair and cell-cycle checkpoints are distinct downstream components of the DNA damage response pathways and both DNA repair and cell-cycle checkpoints are essential to surviving DNA damage.
-
(1996)
Science
, vol.271
, pp. 353-356
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-
Walworth, N.1
Bernards, R.2
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20
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0031035528
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Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation
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of special interest. This report describes the maintenance of Cdc2 tyrosine phosphorylation in S. pombe treated with UV. The overproduction of Chk1 can cause G2 arrest and this requires Wee1. Chk1 can phosphorylate Wee1 in vitro. UV also induces hyperphosphorylation of Wee1; however, hyperphosphorylated Wee1 is not more active. If tyrosine phosphorylation of Cdc2 is the key to the G2/M checkpoint, Wee1 must be required even if the Wee1 activity itself is not the critical target of the Chk1-regulated pathway.
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O'Connell M, Raleigh J, Verkade H, Nurse P. Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation. of special interest EMBO J. 16:1997;545-554 This report describes the maintenance of Cdc2 tyrosine phosphorylation in S. pombe treated with UV. The overproduction of Chk1 can cause G2 arrest and this requires Wee1. Chk1 can phosphorylate Wee1 in vitro. UV also induces hyperphosphorylation of Wee1; however, hyperphosphorylated Wee1 is not more active. If tyrosine phosphorylation of Cdc2 is the key to the G2/M checkpoint, Wee1 must be required even if the Wee1 activity itself is not the critical target of the Chk1-regulated pathway.
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(1997)
EMBO J
, vol.16
, pp. 545-554
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-
O'Connell, M.1
Raleigh, J.2
Verkade, H.3
Nurse, P.4
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21
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0030768948
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Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint kinase
-
of special interest. Using a temperature-sensitive Wee1 mutant, this report convincingly demonstrates that radiation-induced G2/M checkpoint can be observed after Wee1 and Mik1 are both inactivated. This result strongly implicated that pre-existing phosphotyrosine on Cdc2 must not be dephosphorylated after DNA damage. In S. pombe, Cdc25 is found to associate with Chk1 and can be phosphorylated by Chk1 in vitro.
-
Furnari B, Thind N, Russell P. Cdc25 mitotic inducer targeted by Chk1 DNA damage checkpoint kinase. of special interest Science. 277:1997;1495-1497 Using a temperature-sensitive Wee1 mutant, this report convincingly demonstrates that radiation-induced G2/M checkpoint can be observed after Wee1 and Mik1 are both inactivated. This result strongly implicated that pre-existing phosphotyrosine on Cdc2 must not be dephosphorylated after DNA damage. In S. pombe, Cdc25 is found to associate with Chk1 and can be phosphorylated by Chk1 in vitro.
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(1997)
Science
, vol.277
, pp. 1495-1497
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Furnari, B.1
Thind, N.2
Russell, P.3
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22
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0030867582
-
Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to Cdk regulation through Cdc25
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of special interest. This report describes the cloning of hChk1. Sequence alignment of human, mouse, Drosophila, Caenorhabditis elegans and yeast Chk1 is shown. The exposure of cells to IR leads to a change in the electrophoretic mobility of hChk1, most likely due to phosphorylation. hChk1 is found to phosphorylate hCDC25A, B and C in vitro. The site of phosphorylation in CDC25C is determined to be Ser216.
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Sanchez Y, Wong C, Thoma R, Richman R, Wu Z, Piwnica-Worms H, Ellledge S. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25. of special interest Science. 277:1997;1497-1501 This report describes the cloning of hChk1. Sequence alignment of human, mouse, Drosophila, Caenorhabditis elegans and yeast Chk1 is shown. The exposure of cells to IR leads to a change in the electrophoretic mobility of hChk1, most likely due to phosphorylation. hChk1 is found to phosphorylate hCDC25A, B and C in vitro. The site of phosphorylation in CDC25C is determined to be Ser216.
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(1997)
Science
, vol.277
, pp. 1497-1501
-
-
Sanchez, Y.1
Wong, C.2
Thoma, R.3
Richman, R.4
Wu, Z.5
Piwnica-Worms, H.6
Ellledge, S.7
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23
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0030611095
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Mitotic and G2 checkpoint control: Regulation of 14-3-3 protein binding by phosphorylation of Cdc25c on Serine-216
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of outstanding interest. This report characterizes the effect of Ser216 phosphorylation on the biochemical and the biological activity of CDC25C. Ser216 is shown to be phosphorylated in S and G2 HeLa cells but not in metaphase-arrested cells: thus, Ser216 phosphorylation is correlated with the activation of CDC25C at metaphase. The overproduction of a Ser216Ala mutant of CDC25C interfered with the replication checkpoint (which ensures that mitosis does not occur until the DNA is replicated) as well as the IR-induced G2 checkpoint. Phosphorylation at Ser216 stimulates the binding of CDC25C to 14-3-3, but has no effect on the CDC25C phosphatase activity. S. pombe Chk1 is shown to phosphorylate CDC25C at Ser216.
-
Peng C, Graves P, Thoma R, Wu Z, Shaw A, Piwnica-Worms H. Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25c on Serine-216. of outstanding interest Science. 277:1997;1501-1505 This report characterizes the effect of Ser216 phosphorylation on the biochemical and the biological activity of CDC25C. Ser216 is shown to be phosphorylated in S and G2 HeLa cells but not in metaphase-arrested cells: thus, Ser216 phosphorylation is correlated with the activation of CDC25C at metaphase. The overproduction of a Ser216Ala mutant of CDC25C interfered with the replication checkpoint (which ensures that mitosis does not occur until the DNA is replicated) as well as the IR-induced G2 checkpoint. Phosphorylation at Ser216 stimulates the binding of CDC25C to 14-3-3, but has no effect on the CDC25C phosphatase activity. S. pombe Chk1 is shown to phosphorylate CDC25C at Ser216.
-
(1997)
Science
, vol.277
, pp. 1501-1505
-
-
Peng, C.1
Graves, P.2
Thoma, R.3
Wu, Z.4
Shaw, A.5
Piwnica-Worms, H.6
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24
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0028101138
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14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast
-
Ford J, Al-Khodairy F, Fotou E, Sheldrick K, Griffiths D, Carr A. 14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast. Science. 265:1994;533-535.
-
(1994)
Science
, vol.265
, pp. 533-535
-
-
Ford, J.1
Al-Khodairy, F.2
Fotou, E.3
Sheldrick, K.4
Griffiths, D.5
Carr, A.6
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25
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0031051042
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P53: From inductive signal to cellular effect
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Hansen R, Oren M. p53: from inductive signal to cellular effect. Curr Opin Genet Dev. 7:1997;46-51.
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(1997)
Curr Opin Genet Dev
, vol.7
, pp. 46-51
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Hansen, R.1
Oren, M.2
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26
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0030860911
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Repression of p53-mediated transcription by MDM2: A dual mechanism
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Thut C, Goodrich J, Tjian R. Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev. 11:1997;1974-1986.
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(1997)
Genes Dev
, vol.11
, pp. 1974-1986
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Thut, C.1
Goodrich, J.2
Tjian, R.3
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27
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0030905284
-
Mdm2 promotes the rapid degradation of p53
-
of special interest. Increased expression of Mdm2 is found to reduce the steady state levels of p53 and decrease the stability of p53 without affecting p53 mRNA levels. This is observed in several different cell types. The precise mechanism of Mdm2-dependent degradation of p53 was not elucidated.
-
Haupt Y, Maya R, Kazaz A, Oren M. Mdm2 promotes the rapid degradation of p53. of special interest Nature. 387:1997;296-299 Increased expression of Mdm2 is found to reduce the steady state levels of p53 and decrease the stability of p53 without affecting p53 mRNA levels. This is observed in several different cell types. The precise mechanism of Mdm2-dependent degradation of p53 was not elucidated.
-
(1997)
Nature
, vol.387
, pp. 296-299
-
-
Haupt, Y.1
Maya, R.2
Kazaz, A.3
Oren, M.4
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28
-
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0030965946
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Regulation of p53 stability by Mdm2
-
of special interest. This research yielded similar results to those given above in Haupt et al. [27]. The Mdm2-mediated reduction in p53 is inhibited by lactacystin, an inhibitor of proteosomes, suggesting that the Mdm2-p53 complex may be targeted to the proteosomes.
-
Kubbutat M, Jones S, Vousden K. Regulation of p53 stability by Mdm2. of special interest Nature. 387:1997;299-303 This research yielded similar results to those given above in Haupt et al. [27]. The Mdm2-mediated reduction in p53 is inhibited by lactacystin, an inhibitor of proteosomes, suggesting that the Mdm2-p53 complex may be targeted to the proteosomes.
-
(1997)
Nature
, vol.387
, pp. 299-303
-
-
Kubbutat, M.1
Jones, S.2
Vousden, K.3
-
29
-
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0030459950
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Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic - Nuclear transport
-
Lewis J, Baskaran R, Taagepera S, Schwartz M, Wang J. Integrin regulation of c-Abl tyrosine kinase activity and cytoplasmic - nuclear transport. Proc Natl Acad Sci USA. 93:1996;15174-15179.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 15174-15179
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-
Lewis, J.1
Baskaran, R.2
Taagepera, S.3
Schwartz, M.4
Wang, J.5
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30
-
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0029093830
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Abrogation of retinoblastoma protein function by c-Abl through tyrosine kinase-dependent and -independent mechanisms
-
Welch PJ, Wang JYJ. Abrogation of retinoblastoma protein function by c-Abl through tyrosine kinase-dependent and -independent mechanisms. Mol Cell Biol. 15:1995;5542-5551.
-
(1995)
Mol Cell Biol
, vol.15
, pp. 5542-5551
-
-
Welch, P.J.1
Wang, J.Y.J.2
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31
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0029856557
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Three distinct signaling responses by murine fibroblasts to genotoxic stress
-
note
-
Liu Z, Baskaran R, Lea-Chou E, Wood L, Chen Y, Karin M, Wang J. Three distinct signaling responses by murine fibroblasts to genotoxic stress. of outstanding interest Nature. 384:1996;273-276 Studies described here demonstrated DNA lesion-specific and cell-cycle dependent activation of c-Abl tyrosine kinase. In murine fibroblasts, the nuclear pool of c-Abl is shown to be activated by ionizing radiation, cisplatin, methylmethane sulfonate, mitomycin C but not by UV. The cytoplasmic c-Abl is not activated by these DNA damage inducers. Previous results have demonstrated that nuclear c-Abl is cell-cycle regulated and is only active after RB phosphorylation. Methylmethane sulfonate is shown to active c-Abl after cells have committed to S phase entry, suggesting that RB can limit the activation of c-Abl by DNA damage. Methylmethane sulfonate induces the tyrosine phosphorylation of RNA polymerase II only in cells that express c-Abl. Unlike c-Abl, JNK is not activated by ionizing radiation (IR) in murine fibroblasts but it is strongly activated by UV. In addition, JNK can be activated by a high concentration (lethal dose) of methylmethane sulfonate (MMS). The activation of JNK by methylmethane sulfonate is observed in Abl-deficient cells; however, the activation of JNK is compromised in Src-deficient cells. Thus, the activation of c-Abl is not correlated with the activation of JNK in murine fibroblasts. The increase in p53 is induced by all DNA-damaging agents tested and the p53 response is also independent of c-Abl.
-
(1996)
Nature
, vol.384
, pp. 273-276
-
-
Liu, Z.1
Baskaran, R.2
Lea-Chou, E.3
Wood, L.4
Chen, Y.5
Karin, M.6
Wang, J.7
-
32
-
-
0030992749
-
Interaction between ATM protein and c-Abl in response to DNA damage
-
of outstanding interest. The ATM gene product and c-Abl tyrosine kinase can be co-immunoprecipitated from cell lysates. The association of ATM and c-Abl is detected in untreated cells and IR does not appear to stimulate the complex formation. The ATM protein can bind to the Src homology 3 region of c-Abl in vitro. In AT patient cells, c-Abl is not activated by ionizing radiation. In lymphoblasts derived from AT patients, IR also failed to activate JNK. This suggests that JNK activation may require c-Abl, although direct evidence for this is not shown.
-
Shafman T, Khanna K, Kedar P, Spring K, Kozlov S, Yen T, Hobson K, Gatei M, Zhang N, Watters D, et al. Interaction between ATM protein and c-Abl in response to DNA damage. of outstanding interest Nature. 387:1997;520-523 The ATM gene product and c-Abl tyrosine kinase can be co-immunoprecipitated from cell lysates. The association of ATM and c-Abl is detected in untreated cells and IR does not appear to stimulate the complex formation. The ATM protein can bind to the Src homology 3 region of c-Abl in vitro. In AT patient cells, c-Abl is not activated by ionizing radiation. In lymphoblasts derived from AT patients, IR also failed to activate JNK. This suggests that JNK activation may require c-Abl, although direct evidence for this is not shown.
-
(1997)
Nature
, vol.387
, pp. 520-523
-
-
Shafman, T.1
Khanna, K.2
Kedar, P.3
Spring, K.4
Kozlov, S.5
Yen, T.6
Hobson, K.7
Gatei, M.8
Zhang, N.9
Watters, D.10
-
33
-
-
0030945148
-
Functional interaction between DNA-PK and c-Abl in response to DNA damage
-
Kharbanda S, Pandey P, Jin S, Inoue S, Bharti A, Yuan Z-M, Weichselbaum R, Weaver D, Kufe D. Functional interaction between DNA-PK and c-Abl in response to DNA damage. Nature. 386:1997;732-735.
-
(1997)
Nature
, vol.386
, pp. 732-735
-
-
Kharbanda, S.1
Pandey, P.2
Jin, S.3
Inoue, S.4
Bharti, A.5
Yuan Z-M6
Weichselbaum, R.7
Weaver, D.8
Kufe, D.9
-
34
-
-
0029940385
-
Identification of a binding site in c-Abl tyrosine kinase for the C-terminal repeated domain of RNA polymerase II
-
Baskaran R, Chiang GG, Wang JYJ. Identification of a binding site in c-Abl tyrosine kinase for the C-terminal repeated domain of RNA polymerase II. Mol Cell Biol. 16:1996;3361-3369.
-
(1996)
Mol Cell Biol
, vol.16
, pp. 3361-3369
-
-
Baskaran, R.1
Chiang, G.G.2
Wang, J.Y.J.3
-
35
-
-
0028924422
-
Phosphorylation of the C-terminal domain of RNA polymerase II
-
Dahmus ME. Phosphorylation of the C-terminal domain of RNA polymerase II. Biochim Biophys Acta. 1261:1995;171-182.
-
(1995)
Biochim Biophys Acta
, vol.1261
, pp. 171-182
-
-
Dahmus, M.E.1
-
36
-
-
0025780879
-
Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl photo-oncogene
-
Tybulewicz VLJ, Crawford CE, Jackson PK, Bronson RT, Mulligan RC. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl photo-oncogene. Cell. 65:1991;1153-1163.
-
(1991)
Cell
, vol.65
, pp. 1153-1163
-
-
Tybulewicz, V.L.J.1
Crawford, C.E.2
Jackson, P.K.3
Bronson, R.T.4
Mulligan, R.C.5
-
37
-
-
0029879676
-
The cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products
-
Wen S-T, Jackson PK, Van Etten RA. The cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products. EMBO J. 15:1996;1583-1595.
-
(1996)
EMBO J
, vol.15
, pp. 1583-1595
-
-
Wen S-T1
Jackson, P.K.2
Van Etten, R.A.3
-
38
-
-
0029973738
-
Role of c-Abl tyrosine kinase in growth arrest response to DNA damage
-
Yuan Z-M, Huang Y, Whang Y, Sawyer C, Weichselbaum R, Kharbanda S, Kufe D. Role of c-Abl tyrosine kinase in growth arrest response to DNA damage. Nature. 382:1996;272-274.
-
(1996)
Nature
, vol.382
, pp. 272-274
-
-
Yuan Z-M1
Huang, Y.2
Whang, Y.3
Sawyer, C.4
Weichselbaum, R.5
Kharbanda, S.6
Kufe, D.7
-
39
-
-
0031020908
-
Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine kinase
-
Yuan Z-M, Huang Y, Ishiko T, Kharbanda S, Weichselbaum R, Kufe D. Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine kinase. Proc Natl Acad Sci USA. 94:1997;1437-1440.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 1437-1440
-
-
Yuan Z-M1
Huang, Y.2
Ishiko, T.3
Kharbanda, S.4
Weichselbaum, R.5
Kufe, D.6
-
40
-
-
0030795331
-
Tyrosine phosphorylation of RNA polymerase II carboxyl-terminal domain by Abl-related gene (Arg) encoded tyrosine kinase
-
Baskaran R, Chiang G, Mysliwiec T, Krul G, Wang J. Tyrosine phosphorylation of RNA polymerase II carboxyl-terminal domain by Abl-related gene (Arg) encoded tyrosine kinase. J Biol Chem. 272:1997;18905-18909.
-
(1997)
J Biol Chem
, vol.272
, pp. 18905-18909
-
-
Baskaran, R.1
Chiang, G.2
Mysliwiec, T.3
Krul, G.4
Wang, J.5
-
41
-
-
0029860936
-
Ultraviolet light and osmotic stress: Activation of the JNK cascade through multiple growth factor and cytokine receptors
-
Rosette C, Karin M. Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors. Science. 274:1996;1194-1197.
-
(1996)
Science
, vol.274
, pp. 1194-1197
-
-
Rosette, C.1
Karin, M.2
-
42
-
-
0030850047
-
Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage
-
of special interest. This paper describes the interesting observation that the BRCA1 gene product exhibits DNA damage induced phosphorylation in several human tumor cell lines. In the breast cancer cell line MCF-7, BRCA1 has a slower mobility on SDS gels in S phase cells. The mobility is further reduced when cells are exposed to hydroxyurea, UV or IR. The mobility shift is likely to be due to phosphorylation, although this was not directly demonstrated. Hydroxyurea and UV-induced phosphorylation of BRCA1 is independent of DNA-PK and ATM. These results suggest that BRCA1 may be a downstream target of a damage-induced kinase signaling pathway, although the components of that pathway were not identified.
-
Scully R, Chen J, Ochs R, Keegan K, Hoekstra MF, Feunteun J, Livingston D. Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage. of special interest Cell. 90:1997;425-435 This paper describes the interesting observation that the BRCA1 gene product exhibits DNA damage induced phosphorylation in several human tumor cell lines. In the breast cancer cell line MCF-7, BRCA1 has a slower mobility on SDS gels in S phase cells. The mobility is further reduced when cells are exposed to hydroxyurea, UV or IR. The mobility shift is likely to be due to phosphorylation, although this was not directly demonstrated. Hydroxyurea and UV-induced phosphorylation of BRCA1 is independent of DNA-PK and ATM. These results suggest that BRCA1 may be a downstream target of a damage-induced kinase signaling pathway, although the components of that pathway were not identified.
-
(1997)
Cell
, vol.90
, pp. 425-435
-
-
Scully, R.1
Chen, J.2
Ochs, R.3
Keegan, K.4
Hoekstra, M.F.5
Feunteun, J.6
Livingston, D.7
-
43
-
-
15844371372
-
The tumor suppressor gene BRCA1 is required for embryonic cellular proliferation in the mouse
-
Hakem R, de la Pompa J, Sirard C, Mo MR, Woo M, Hakem A, Wakeham A, Potter J, Reitmair A, Billia F, et al. The tumor suppressor gene BRCA1 is required for embryonic cellular proliferation in the mouse. Cell. 85:1996;1009-1023.
-
(1996)
Cell
, vol.85
, pp. 1009-1023
-
-
Hakem, R.1
De La Pompa, J.2
Sirard, C.3
Mo, M.R.4
Woo, M.5
Hakem, A.6
Wakeham, A.7
Potter, J.8
Reitmair, A.9
Billia, F.10
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