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Morgan DO. Principles of CDK regulation. Nature. 374:1995;131-134.
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Galaktionov, K.1
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160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin
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160 by the cyclin-dependent kinase-interacting phosphatase KAP in the absence of cyclin. Science. 270:1995;90-93.
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Poon, R.Y.C.1
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0029024015
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Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27
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of special interest. Inhibition of the proteasome leads to the accumulation of ubiquitinated p27 in human osteosarcoma cells in culture. The authors go on the show that pure p27 is ubiquitinated and degraded in vitro and that extracts from proliferating cells are more efficient in ubiquitinating and degrading p27 than extracts from quiescent cells.
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Pagano M, Tam SW, Theodoras AM, Beer Romero P, Del Sal G, Chau V, Yew PR, Draetta GF, Rolfe M. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. of special interest Science. 269:1995;682-685 Inhibition of the proteasome leads to the accumulation of ubiquitinated p27 in human osteosarcoma cells in culture. The authors go on the show that pure p27 is ubiquitinated and degraded in vitro and that extracts from proliferating cells are more efficient in ubiquitinating and degrading p27 than extracts from quiescent cells.
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Science
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Pagano, M.1
Tam, S.W.2
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Chau, V.6
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The dynamics of CDK structure
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Morgan DO. The dynamics of CDK structure. Curr Opin Cell Biol. 8:1996;767-772.
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De Bondt HL, Rosenblatt J, Jancarik J, Jones HD, Morgan DO, Kim S-H. Crystal structure of cyclin-dependent kinase 2. Nature. 363:1993;595-602.
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De Bondt, H.L.1
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Kim, S.-H.6
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12
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0029029617
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Mechanism of CDK activation revealed by the structure of cyclinA - CDK2 complex
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of outstanding interest. The crystal structure of the CDK2 - cyclin A complex revealed drastic conformational changes in the catalytic subunit induced by cyclin-binding. Rotation and translation of the PSTAIRE helix of CDK2 upon contacting cyclin A re-orients critical residues in the active site, allowing in-line phosphotransfer from ATP to peptide substrates, whereas a large movement of the T-loop away from the catalytic cleft relieves a steric impediment to peptide substrate access.
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Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massagué J, Pavletich NP. Mechanism of CDK activation revealed by the structure of cyclinA - CDK2 complex. of outstanding interest Nature. 376:1995;313-320 The crystal structure of the CDK2 - cyclin A complex revealed drastic conformational changes in the catalytic subunit induced by cyclin-binding. Rotation and translation of the PSTAIRE helix of CDK2 upon contacting cyclin A re-orients critical residues in the active site, allowing in-line phosphotransfer from ATP to peptide substrates, whereas a large movement of the T-loop away from the catalytic cleft relieves a steric impediment to peptide substrate access.
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Nature
, vol.376
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Jeffrey, P.D.1
Russo, A.A.2
Polyak, K.3
Gibbs, E.4
Hurwitz, J.5
Massagué, J.6
Pavletich, N.P.7
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13
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0029767016
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Structural basis of cyclin-dependent kinase activation by phosphorylation
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of outstanding interest. The crystallographic last act in the CDK activation trilogy finds the phosphorylated T-loop moving ~6 Å to make new contacts on the carboxy-terminal lobe of CDK2, making the catalytic cleft still more inviting to peptide substrates. The phosphate group becomes largely buried in a pocket of arginine residues, forming an organizing center that stabilizes the kinase through a network of hydrogen bonds. The interaction with cyclin A is also strengthened. These conformational changes may seem modest (in comparison with the havoc wrought by binding of cyclin or p27) but lead to full activation of the kinase.
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Russo AA, Jeffrey PD, Pavletich NP. Structural basis of cyclin-dependent kinase activation by phosphorylation. of outstanding interest Nat Struct Biol. 3:1996;696-700 The crystallographic last act in the CDK activation trilogy finds the phosphorylated T-loop moving ~6 Å to make new contacts on the carboxy-terminal lobe of CDK2, making the catalytic cleft still more inviting to peptide substrates. The phosphate group becomes largely buried in a pocket of arginine residues, forming an organizing center that stabilizes the kinase through a network of hydrogen bonds. The interaction with cyclin A is also strengthened. These conformational changes may seem modest (in comparison with the havoc wrought by binding of cyclin or p27) but lead to full activation of the kinase.
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Nat Struct Biol
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Russo, A.A.1
Jeffrey, P.D.2
Pavletich, N.P.3
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Phosphorylation-independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro
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Connell-Crowley L, Solomon MJ, Wei N, Harper JW. Phosphorylation-independent activation of human cyclin-dependent kinase 2 by cyclin A in vitro. Mol Biol Cell. 4:1993;79-92.
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Connell-Crowley, L.1
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Wei, N.3
Harper, J.W.4
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15
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0029665852
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Kip1cyclin-dependent kinase inhibitor bound to the cyclin A - Cdk2 complex
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of outstanding interest. A truly startling revelation of how a CKI can stifle a CDK. The authors of this elegant crystallographic study manage to explain a number of old observations while at the same time prefiguring the more recently proposed roles for CKIs as substrates and assembly factors (discussed in the text). An instant classic.
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Kip1cyclin-dependent kinase inhibitor bound to the cyclin A - Cdk2 complex. of outstanding interest Nature. 382:1996;325-331 A truly startling revelation of how a CKI can stifle a CDK. The authors of this elegant crystallographic study manage to explain a number of old observations while at the same time prefiguring the more recently proposed roles for CKIs as substrates and assembly factors (discussed in the text). An instant classic.
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Nature
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Russo, A.A.1
Jeffrey, P.D.2
Patten, A.K.3
Massagué, J.4
Pavletich, N.P.5
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1 cyclin - Cdk protein kinase activity, is related to p21
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1 cyclin - Cdk protein kinase activity, is related to p21. Cell. 78:1994;67-74.
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Toyoshima, H.1
Hunter, T.2
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0029058587
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Inhibition of cyclin-dependent kinases by p21
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Harper JW, Elledge SJ, Keyomarski K, Dynlacht B, Tsai L-H, Zhang P, Dobrowolski S, Bai C, Connell-Crowley L, Swindell E, et al. Inhibition of cyclin-dependent kinases by p21. Mol Biol Cell. 6:1995;387-400.
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Harper, J.W.1
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Keyomarski, K.3
Dynlacht, B.4
Tsai, L.-H.5
Zhang, P.6
Dobrowolski, S.7
Bai, C.8
Connell-Crowley, L.9
Swindell, E.10
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19
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0028983384
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CIP1-related domain to bind cyclin/cdk2 and regulate interactions with E2F
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of special interest. An intriguing bit of protein dissection the conclusion of which - the identification of the so-called LFG motif as a potential cyclin-binding element - was strikingly borne out in the CDK2 - cyclin A - p27 ternary complex crystal structure, raising the question: what is the difference between a CDK substrate and a CKI?
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CIP1-related domain to bind cyclin/cdk2 and regulate interactions with E2F. of special interest Genes Dev. 9:1995;1740-1752 An intriguing bit of protein dissection the conclusion of which - the identification of the so-called LFG motif as a potential cyclin-binding element - was strikingly borne out in the CDK2 - cyclin A - p27 ternary complex crystal structure, raising the question: what is the difference between a CDK substrate and a CKI?
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(1995)
Genes Dev
, vol.9
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Zhu, L.1
Harlow, E.2
Dynlacht, B.D.3
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20
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0028169236
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P21-containing cyclin kinases exist in both active and inactive states
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Zhang H, Hannon GJ, Beach D. p21-containing cyclin kinases exist in both active and inactive states. Genes Dev. 8:1994;1750-1758.
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Genes Dev
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Zhang, H.1
Hannon, G.J.2
Beach, D.3
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21
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0029876639
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Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein
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1 events in fibroblasts showing that adhesion substratum profoundly influences many of the same phenomena regulated by mitogens. Together with [66], this work provides a plausible blueprint for how both anchorage- and mitogen-dependence are enforced in normal cells and lost in oncogenically transformed ones.
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1 events in fibroblasts showing that adhesion substratum profoundly influences many of the same phenomena regulated by mitogens. Together with [66], this work provides a plausible blueprint for how both anchorage- and mitogen-dependence are enforced in normal cells and lost in oncogenically transformed ones.
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J Cell Biol
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Zhu, X.1
Ohtsubo, M.2
Böhmer, R.M.3
Roberts, J.M.4
Assoian, R.K.5
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22
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0028807103
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Alternative mehanisms of CAK assembly require an assembly factor or an activating kinase
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of special interest. Describes the identification and cloning of the gene for murine MAT1 (p36), the third subunit of mammalian CAK, CDK7 and cyclin H can form a stable ternary complex with MAT1; stable binary complexes can form without MAT1, provided that the T-loop threonine of CDK7 is phosphorylated.
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Fisher RP, Jin P, Chamberlin HM, Morgan DO. Alternative mehanisms of CAK assembly require an assembly factor or an activating kinase. of special interest Cell. 83:1995;47-57 Describes the identification and cloning of the gene for murine MAT1 (p36), the third subunit of mammalian CAK, CDK7 and cyclin H can form a stable ternary complex with MAT1; stable binary complexes can form without MAT1, provided that the T-loop threonine of CDK7 is phosphorylated.
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(1995)
Cell
, vol.83
, pp. 47-57
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Fisher, R.P.1
Jin, P.2
Chamberlin, H.M.3
Morgan, D.O.4
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23
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0028856425
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MAT1 ('ménage à trois') a new RING finger protein subunit stabilizing cyclin H - cdk7 complexes in starfish and Xenopus CAK
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of special interest. Cloning of Xenopus and starfish MAT1, and demonstration of the assembly-promoting activity of its encoded product towards CDK7 and cyclin H translated in vitro; also provides evidence for CDK7 - cyclin H dimers, lacking MAT1, in frog egg extracts.
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Devault A, Martinez A-M, Fesquet D, Labbé J-C, Morin N, Cavadore J-C, Dorée M. MAT1 ('ménage à trois') a new RING finger protein subunit stabilizing cyclin H - cdk7 complexes in starfish and Xenopus CAK. of special interest EMBO J. 14:1995;5027-5036 Cloning of Xenopus and starfish MAT1, and demonstration of the assembly-promoting activity of its encoded product towards CDK7 and cyclin H translated in vitro; also provides evidence for CDK7 - cyclin H dimers, lacking MAT1, in frog egg extracts.
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(1995)
EMBO J
, vol.14
, pp. 5027-5036
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Devault, A.1
Martinez, A.-M.2
Fesquet, D.3
Labbé, J.-C.4
Morin, N.5
Cavadore, J.-C.6
Dorée, M.7
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24
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0028882228
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In vitro assembly of a functional human cdk7/cyclin H complex reauires MAT1, a novel 36 kD RING finger protein
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of special interest. Human MAT1 cloning and protein characterization. The authors show that MAT1 is associated with CDK7 and cyclin H throughout the mammalian cell cycle and that the RING finger of MAT1 is dispensable for its assembly factor function.
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Tassan J-P, Jaquenod M, Fry AM, Frutiger S, Hughes G, Nigg EA. In vitro assembly of a functional human cdk7/cyclin H complex reauires MAT1, a novel 36 kD RING finger protein. of special interest EMBO J. 14:1995;5608-5617 Human MAT1 cloning and protein characterization. The authors show that MAT1 is associated with CDK7 and cyclin H throughout the mammalian cell cycle and that the RING finger of MAT1 is dispensable for its assembly factor function.
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(1995)
EMBO J
, vol.14
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Tassan, J.-P.1
Jaquenod, M.2
Fry, A.M.3
Frutiger, S.4
Hughes, G.5
Nigg, E.A.6
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25
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0027296041
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The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues.
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Fesquet D, Labbé J-C, Derancourt J, Capony J-P, Galas S, Girard F, Lorca T, Shuttleworth J, Dorée M, Cavadore J-C. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. EMBO J. 12:1993;3111-3121.
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Fesquet, D.1
Labbé, J.-C.2
Derancourt, J.3
Capony, J.-P.4
Galas, S.5
Girard, F.6
Lorca, T.7
Shuttleworth, J.8
Dorée, M.9
Cavadore, J.-C.10
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26
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0028268284
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D-type cyclin-dependent kinase activity in mammalian cells
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Matsushime H, Quelle DE, Shurtleff SA, Shibuya M, Sherr CJ, Kato J-Y. D-type cyclin-dependent kinase activity in mammalian cells. Mol Cell Biol. 14:1994;2066-2076.
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Matsushime, H.1
Quelle, D.E.2
Shurtleff, S.A.3
Shibuya, M.4
Sherr, C.J.5
Kato, J.-Y.6
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Regulation of cyclin D-dependent kinases (cdk4) by cdk4-activating kinase
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Kato J-Y, Matsuoka M, Strom DK, Sherr CJ. Regulation of cyclin D-dependent kinases (cdk4) by cdk4-activating kinase. Mol Cell Biol. 14:1994;2713-2721.
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Kato, J.-Y.1
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D type cyclins associate with multiple protein kinases and the DNA replication and repair factor PCNA
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9044232147
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Formation pf p27 - CDK complexes during the human mitotic cell cycle
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Soos TJ, Kiyokawa H, Yan JS, Rubin MS, Giordano A, DeBlasio A, Bottega S, Wong B, Mendelsohn J, Koff A. Formation pf p27 - CDK complexes during the human mitotic cell cycle. Cell Growth Differ. 7:1996;135-146.
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Soos, T.J.1
Kiyokawa, H.2
Yan, J.S.3
Rubin, M.S.4
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Deblasio, A.6
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Wong, B.8
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0029153609
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Kip/Cip, Ink4 Cdk inhibitors cooperate to induce cell cycle arrest in, response to TGF-β
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Ink4B - which promotes redistribution of p27 (and p21) from CDK4 and CDK6 complexes to CDK2 complexes - coinciding with cell cycle arrest in mink lung cells.
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Ink4B - which promotes redistribution of p27 (and p21) from CDK4 and CDK6 complexes to CDK2 complexes - coinciding with cell cycle arrest in mink lung cells.
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Reynisdóttir, I.1
Polyak, K.2
Iavarone, A.3
Massagué, J.4
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32
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0029665779
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Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4
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Cdc37, a mammalian homolog of budding yeast Cdc37, is shown to interact with CDK4 both in vivo and in vitro. Notably absent from CDK4 - Cdc37 complexes is cyclin D but complexes formed both in insect and mammalian cells contains the molecular chaperone Hsp90.
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Cdc37, a mammalian homolog of budding yeast Cdc37, is shown to interact with CDK4 both in vivo and in vitro. Notably absent from CDK4 - Cdc37 complexes is cyclin D but complexes formed both in insect and mammalian cells contains the molecular chaperone Hsp90.
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(1996)
Genes Dev
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Stepanova, L.1
Leng, X.2
Parker, S.B.3
Harper, J.W.4
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33
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0029838168
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Physical interaction of mammalian CDC37 with CDK4
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of special interest. As in [32], the authors demonstrate an association between mammalian Cdc37 and CDK4 by immunoprecipitation of CDK4-containing complexes. They also go on to show that Hsp90 is part of the complex. Still missing is a mechanistic explanation of how this interaction might promote assembly with cyclin D.
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Dai K, Kobayashi R, Beach D. Physical interaction of mammalian CDC37 with CDK4. of special interest J Biol Chem. 271:1996;22030-22034 As in [32], the authors demonstrate an association between mammalian Cdc37 and CDK4 by immunoprecipitation of CDK4-containing complexes. They also go on to show that Hsp90 is part of the complex. Still missing is a mechanistic explanation of how this interaction might promote assembly with cyclin D.
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J Biol Chem
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Dai, K.1
Kobayashi, R.2
Beach, D.3
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34
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0028600051
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The MO15 cell cycle kinase is associated with the TFIIH transcription - DNA repair factor
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Roy R, Adamczewski JP, Seroz T, Vermuelen W, Tassan J-P, Schaffer L, Nigg EA, Hoeijmakers JHJ, Egly J-M. The MO15 cell cycle kinase is associated with the TFIIH transcription - DNA repair factor. Cell. 79:1994;1093-1101.
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Roy, R.1
Adamczewski, J.P.2
Seroz, T.3
Vermuelen, W.4
Tassan, J.-P.5
Schaffer, L.6
Nigg, E.A.7
Hoeijmakers, J.H.J.8
Egly, J.-M.9
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Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK
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Feaver VVJ, Svestrup JO, Henry NL, Kornberg RD. Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. Cell. 79:1994;1103-1109.
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Feaver, V.V.J.1
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Henry, N.L.3
Kornberg, R.D.4
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0028958673
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Association of Cdk-activating kinase subunits with transcription factor TFIIH
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Serizawa H, Mäkelä TR, Conaway JW, Conaway RC, Weinberg RA, Young RA. Association of Cdk-activating kinase subunits with transcription factor TFIIH. Nature. 374:1995;280-282.
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Nature
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Serizawa, H.1
Mäkelä, T.R.2
Conaway, J.W.3
Conaway, R.C.4
Weinberg, R.A.5
Young, R.A.6
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37
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0028954227
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Cdk-activating kinase (CAK) complex is a component of human transcription factor IIH
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Shiekhattar R, Mermelstein F, Fisher RP, Drapkin R, Dynlacht B, Westling HC, Morgan DO, Reinberg D. Cdk-activating kinase (CAK) complex is a component of human transcription factor IIH. Nature. 374:1995;283-287.
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Nature
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Shiekhattar, R.1
Mermelstein, F.2
Fisher, R.P.3
Drapkin, R.4
Dynlacht, B.5
Westling, H.C.6
Morgan, D.O.7
Reinberg, D.8
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38
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0029083795
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Identification of human cyclin-dependent kinase 8, a putative protein kinase partner for cyclin C
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of special interest. A partner for cyclin C at long last, CDK8 - like its budding yeast homolog Srb10 - contains many of the regulatory features characteristic of CDKs but conspicuously lacks a CAK phosphorylation site, having an aspartate residue at that location in its T-loop.
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Tassan J-P, Jaquernoud M, Léopold P, Schultz SJ, Nigg EA. Identification of human cyclin-dependent kinase 8, a putative protein kinase partner for cyclin C. of special interest Proc Natl Acad Sci USA. 92:1995;8871-8875 A partner for cyclin C at long last, CDK8 - like its budding yeast homolog Srb10 - contains many of the regulatory features characteristic of CDKs but conspicuously lacks a CAK phosphorylation site, having an aspartate residue at that location in its T-loop.
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Proc Natl Acad Sci USA
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Tassan, J.-P.1
Jaquernoud, M.2
Léopold, P.3
Schultz, S.J.4
Nigg, E.A.5
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39
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15844390393
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A human RNA polymerase II complex associated with SRB and DNA repair proteins
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of special interest. A description of the biochemical isolation and characterization of a -2000 kDa RNAP II holoenzyme complex from mammalian cells, which is active in both activated transcription and DNA repair. The complex contains the CDK8 - cyclin C pair, which is homologous to the SRB10-SRB11 complex that associates with yeast RNAP II holoenzyme [48]; also present are basal transcription factors: some in stoichiometric amounts (TFIIE and TFIIF); and some (TFIIH) in substoichiometric functionally rate-limiting amounts.
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Maldonado E, Shiekhattar R, Sheldon M, Cho H, Drapkin R, Rickert P, Lees E, Anderson CW, Linn S, Reinberg D. A human RNA polymerase II complex associated with SRB and DNA repair proteins. of special interest Nature. 381:1996;86-89 A description of the biochemical isolation and characterization of a -2000 kDa RNAP II holoenzyme complex from mammalian cells, which is active in both activated transcription and DNA repair. The complex contains the CDK8 - cyclin C pair, which is homologous to the SRB10-SRB11 complex that associates with yeast RNAP II holoenzyme [48]; also present are basal transcription factors: some in stoichiometric amounts (TFIIE and TFIIF); and some (TFIIH) in substoichiometric functionally rate-limiting amounts.
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Nature
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Maldonado, E.1
Shiekhattar, R.2
Sheldon, M.3
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Drapkin, R.5
Rickert, P.6
Lees, E.7
Anderson, C.W.8
Linn, S.9
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Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II
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Goodrich JA, Tjian R. Transcription factors IIE and IIH and ATP hydrolysis direct promoter clearance by RNA polymerase II. Cell. 77:1994;145-156.
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Goodrich, J.A.1
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DNA topology and a minimal set of basal factors for transcription by RNA polymerase II
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Parvin JD, Sharp PA. DNA topology and a minimal set of basal factors for transcription by RNA polymerase II. Cell. 73:1993;533-540.
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A role for ATP and TFIIH in activation of the RNA polymerase II preinitiation complex prior to transcription initiation
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Solution structure of the -terminal core domain of human TFIIB: Similarity to cyclin A and interaction with TATA-binding protein
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KIN28 encodes a C-terminal domain kinase that controls mRNA transcription in Saccharomyces cerevisiae but lacks cyclin-dependent kinase-activating kinase (CAK) activity
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A kinase - cyclin pair in the RNA polymerase II holoenzyme
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of special interest. A CDK is a component of the basal transcription machinery. The Srb10-Srb11 pair of S. cerevisiae is homologous to mammalian CDK8 - cyclin C, both associate with RNA polymerase II.
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Liao S-M, Zhang J, Jeffery DA, Koleske AJ, Thompson CM, Chao DM, Viljoen V, Van Vuuren HJJ, Young RA. A kinase - cyclin pair in the RNA polymerase II holoenzyme. of special interest Nature. 374:1995;193-196 A CDK is a component of the basal transcription machinery. The Srb10-Srb11 pair of S. cerevisiae is homologous to mammalian CDK8 - cyclin C, both associate with RNA polymerase II.
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Liao, S.-M.1
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Mäkelä, T.P.1
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Nigg EA. Cyclin-dependent kinase 7: at the cross-roads of transcription, DNA repair and cell cycle control? Curr Opin Cell Biol. 8:1996;312-317.
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Fisher RP, Morgan DO. CAK in TFIIH: crucial connection or confounding coincidence? Biochim Biophys Acta. 1288:1996;O7-O10.
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The Cdk-activating kinase (CAK) from budding yeast
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2 at the non-permissive temperature.
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2 at the non-permissive temperature.
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Kaldis, P.1
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Civ1 (CAK in vivo), a novel Cdk-activating kinase
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1. These authors also report a genetic interaction with KIN28, which encodes the TFIIH-associated CDK7 homolog.
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1. These authors also report a genetic interaction with KIN28, which encodes the TFIIH-associated CDK7 homolog.
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Thuret, J.-Y.1
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A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK
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of special interest. Purification of Cak1 (and cloning of Cak1) by different methods than those used in [57] and [58]. These authors show that Cak1 activity, as with vertebrate CDK7 activity, does not fluctuate significantly during the cell cycle.
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Espinoza FH, Farrell A, Erdjument-Bromage H, Tempst P, Morgan DO. A cyclin-dependent kinase-activating kinase (CAK) in budding yeast unrelated to vertebrate CAK. of special interest Science. 273:1996;1714-1717 Purification of Cak1 (and cloning of Cak1) by different methods than those used in [57] and [58]. These authors show that Cak1 activity, as with vertebrate CDK7 activity, does not fluctuate significantly during the cell cycle.
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Science
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Espinoza, F.H.1
Farrell, A.2
Erdjument-Bromage, H.3
Tempst, P.4
Morgan, D.O.5
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60
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Identification of a cdk-activating kinase in fission yeast
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of special interest. A CDK7 homolog in fission yeast, here called Crk1, is CAK at least in vitro. Cells lacking functional Crk1 are inviable, and show a discrete if puzzling late mitotic arrest phenotype that can be suppressed by expression of human CDK7. A role for Crk1 in activating CDKs is not demonstrated in vivo, not is the possibility of a fission yeast homolog of budding yeast Cak1 excluded by the study (or the one in [6]).
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Buck V, Russell P, Millar JBA. Identification of a cdk-activating kinase in fission yeast. of special interest EMBO J. 14:1995;6173-6183 A CDK7 homolog in fission yeast, here called Crk1, is CAK at least in vitro. Cells lacking functional Crk1 are inviable, and show a discrete if puzzling late mitotic arrest phenotype that can be suppressed by expression of human CDK7. A role for Crk1 in activating CDKs is not demonstrated in vivo, not is the possibility of a fission yeast homolog of budding yeast Cak1 excluded by the study (or the one in [6]).
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EMBO J
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Buck, V.1
Russell, P.2
Millar, J.B.A.3
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61
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Schizosaccharomyces pombe Mop1 - Mcs2 is related to mammalian CAK
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of special interest. PCR-cloning leads to the identification of the CDK7 homolog from fission yeast, here called Mop1, that is identical to Crk1 in [60]. CAK activity is reconstituted in vitro with Mcs2, a previously identified cyclin H homolog, the partner of Mop1 in vivo.
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Damagnez V, Mäkelä TP, Cottarel G. Schizosaccharomyces pombe Mop1 - Mcs2 is related to mammalian CAK. of special interest EMBO J. 14:1995;6164-6172 PCR-cloning leads to the identification of the CDK7 homolog from fission yeast, here called Mop1, that is identical to Crk1 in [60]. CAK activity is reconstituted in vitro with Mcs2, a previously identified cyclin H homolog, the partner of Mop1 in vivo.
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(1995)
EMBO J
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Damagnez, V.1
Mäkelä, T.P.2
Cottarel, G.3
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15844367100
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Drapkin R, Le Roy G, Cho H, Akoulitchev S, Reinberg D:, Human cyclin-dependent kinase-activating kinase exists, in three distinct complexes. Proc Natl Acad Sci USA. 93:1996;6488-6493.
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Drapkin, R.1
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Cho, H.3
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Reinberg, D.5
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In, T.D.C.7
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64
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0028832869
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A mammalian RNA polymerase II holoenzyme containing all components required for promoter-specific transcription initiation
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of special interest. By immunoaffinity purification with an anti-CDK7 monoclonal antibody, these authors isolate an RNAP II holoenzyme which is possibly analogous to the one reported in [39].
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Ossipow V, Tassan J-P, Nigg EA, Schibler U. A mammalian RNA polymerase II holoenzyme containing all components required for promoter-specific transcription initiation. of special interest Cell. 83:1995;137-146 By immunoaffinity purification with an anti-CDK7 monoclonal antibody, these authors isolate an RNAP II holoenzyme which is possibly analogous to the one reported in [39].
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(1995)
Cell
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Ossipow, V.1
Tassan, J.-P.2
Nigg, E.A.3
Schibler, U.4
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65
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0029987031
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MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH
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of special interest. The first evidence that different CDK7 complexes may be regulated differently, supporting the idea that CDK7 performs multiple functions. In UV-irradiated mammalian cells, the TFIIH-associated fraction of CDK7 is inhibited, whereas the TFIIH-free major form of the enzyme is unaffected.
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Adamczewski JP, Rossignol M, Tassan J-P, Nigg EA, Moncollin V, Egly J-M. MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH. of special interest EMBO J. 15:1996;1877-1884 The first evidence that different CDK7 complexes may be regulated differently, supporting the idea that CDK7 performs multiple functions. In UV-irradiated mammalian cells, the TFIIH-associated fraction of CDK7 is inhibited, whereas the TFIIH-free major form of the enzyme is unaffected.
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EMBO J
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Adamczewski, J.P.1
Rossignol, M.2
Tassan, J.-P.3
Nigg, E.A.4
Moncollin, V.5
Egly, J.-M.6
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66
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0030027049
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Dependence of cyclin E-CDK2 kinase activity on cell anchorage
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of special interest. In untransformed human diploid fibroblasts, loss of cell anchorage leads to upregulation of p27 and p21, consequent inactivation of cyclin E-CDK2, and (secondarily) decreased phosphorylation of CDK2 by CAK. The mechanism may be different than in the fibroblasts studied in [21] but the result - cell cycle arrest in suspension - is the same.
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Fang F, Orend G, Watanabe N, Hunter T, Ruoslahti E. Dependence of cyclin E-CDK2 kinase activity on cell anchorage. of special interest Science. 271:1996;499-502 In untransformed human diploid fibroblasts, loss of cell anchorage leads to upregulation of p27 and p21, consequent inactivation of cyclin E-CDK2, and (secondarily) decreased phosphorylation of CDK2 by CAK. The mechanism may be different than in the fibroblasts studied in [21] but the result - cell cycle arrest in suspension - is the same.
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Science
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Fang, F.1
Orend, G.2
Watanabe, N.3
Hunter, T.4
Ruoslahti, E.5
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67
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0029664461
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kip1 for restriction point control of the fibroblast cell cycle
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1, correlates with their ability to down-regulate p27. When p27 is inactivated with antisense oligonucleotides, cells are unable to exit the cell cycle in response to serum deprivation; the enforced expression of p27 in these cells re-imposed restriction point control.
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1, correlates with their ability to down-regulate p27. When p27 is inactivated with antisense oligonucleotides, cells are unable to exit the cell cycle in response to serum deprivation; the enforced expression of p27 in these cells re-imposed restriction point control.
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(1996)
Science
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Coats, S.1
Flanagan, W.M.2
Nourse, J.3
Roberts, J.M.4
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68
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0029670477
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Kip1 accumulation during the cell cycle
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of outstanding interest. Another mechanism to the one described in [67] for increasing cellular p27 levels is suggested in this study which demonstrates increased translation of the p27 mRNA as cells exit the division cycle.
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Kip1 accumulation during the cell cycle. of outstanding interest Science. 271:1996;1861-1864 Another mechanism to the one described in [67] for increasing cellular p27 levels is suggested in this study which demonstrates increased translation of the p27 mRNA as cells exit the division cycle.
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Science
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Hengst, L.1
Reed, S.I.2
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69
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Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activity kinase
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Aprelikova O, Xiong Y, Liu ET. Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activity kinase. J Biol Chem. 270:1995;18195-18197.
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Aprelikova, O.1
Xiong, Y.2
Liu, E.T.3
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70
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0030010591
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Kip1 display increased body size, multiple organ hyperplasia, retinal dysplasia, and pituitary tumors
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Kip1 knockout mouse is bigger than its wild-type littermates because of a proportional increase in cell number in most tissues. It also shows gonadal hyperplasia, impaired ovulation associated with female sterility, and a high incidence of tumors (benign adenomas) of the intermediate lobe of the pituitary. Interestingly, cultured cells from homozygous mutant animals exhibited no defects in their ability to arrest the cell cycle in response to standard treatments.
-
Kip1 knockout mouse is bigger than its wild-type littermates because of a proportional increase in cell number in most tissues. It also shows gonadal hyperplasia, impaired ovulation associated with female sterility, and a high incidence of tumors (benign adenomas) of the intermediate lobe of the pituitary. Interestingly, cultured cells from homozygous mutant animals exhibited no defects in their ability to arrest the cell cycle in response to standard treatments.
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(1996)
Cell
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-
Nakayama, K.1
Ishida, N.2
Shirane, M.3
Inomata, A.4
Inoue, T.5
Shishido, N.6
Horii, I.7
Loh, D.Y.8
Nakayama, K.-I.9
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71
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15844415946
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Kip1
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of outstanding interest. Another mouse similar to the one described in [70], lacking functional p27, is also larger than normal, with hyperplasia (not frank tumors) of the intermediate lobe of the pituitary and female sterility.
-
Kip1. of outstanding interest Cell. 85:1996;721-732 Another mouse similar to the one described in [70], lacking functional p27, is also larger than normal, with hyperplasia (not frank tumors) of the intermediate lobe of the pituitary and female sterility.
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(1996)
Cell
, vol.85
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-
Kiyokawa, H.1
Kineman, R.D.2
Manova-Todorova, K.O.3
Soares, V.C.4
Hoffman, E.S.5
Ono, M.6
Khanam, D.7
Hayday, A.C.8
Frohman, L.A.9
Koff, A.10
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72
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15844384256
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Kip1-deficient mice
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of outstanding interest. The association between p27 loss-of-function and endocrine abnormalities is confirmed in the third of this trio of mouse knockouts [70-72]. As in [70], the homozygous null animals develop intermediate lobe adenomas; it will be interesting to see if the subtly different phenotypes reported here and in reference [71] reflect differences in the mutagenic strategy or different strain backgrounds.
-
Kip1-deficient mice. of outstanding interest Cell. 85:1996;733-744 The association between p27 loss-of-function and endocrine abnormalities is confirmed in the third of this trio of mouse knockouts [70-72]. As in [70], the homozygous null animals develop intermediate lobe adenomas; it will be interesting to see if the subtly different phenotypes reported here and in reference [71] reflect differences in the mutagenic strategy or different strain backgrounds.
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(1996)
Cell
, vol.85
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-
Fero, M.L.1
Rivkin, M.2
Tasch, M.3
Porter, P.4
Carow, C.E.5
Firpo, E.6
Polyak, K.7
Tsai, L.-H.8
Broudy, V.9
Perlmutter, R.M.10
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73
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0028978183
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1 checkpoint control
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Cip1 causes no obvious phenotype in the intact animal. Cells from the mutant mice did grow to higher density in culture and were defective in arresting the cell cycle in response to DNA damage or perturbation of nucleotide pools.
-
Cip1 causes no obvious phenotype in the intact animal. Cells from the mutant mice did grow to higher density in culture and were defective in arresting the cell cycle in response to DNA damage or perturbation of nucleotide pools.
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(1995)
Cell
, vol.82
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Deng, C.1
Zhang, P.2
Harper, J.W.3
Elledge, S.J.4
Leder, P.5
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0029111934
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Cyclin D1 provides a link between development and oncogenesis in retina and breast
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of special interest. Mice lacking cyclin D1 are small, have hypoplastic retinas, are subtly neurologically impaired, and show decreased proliferation of mammary epithelium during pregnancy. The authors suggest that these tissues are the most cyclin during pregnancy. The authors suggest that these tissues are the most cyclin D1-dependent for their normal development; it will be fascinating to see the phenotypes associated with mutations of cyclins D2 and D3.
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Sicinski P, Donaher JL, Parker SB, Li T, Fazeli A, Gardner H, Haslam SZ, Bronson RT, Elledge SJ, Weinberg RA. Cyclin D1 provides a link between development and oncogenesis in retina and breast. of special interest Cell. 82:1995;621-630 Mice lacking cyclin D1 are small, have hypoplastic retinas, are subtly neurologically impaired, and show decreased proliferation of mammary epithelium during pregnancy. The authors suggest that these tissues are the most cyclin during pregnancy. The authors suggest that these tissues are the most cyclin D1-dependent for their normal development; it will be fascinating to see the phenotypes associated with mutations of cyclins D2 and D3.
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(1995)
Cell
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Sicinski, P.1
Donaher, J.L.2
Parker, S.B.3
Li, T.4
Fazeli, A.5
Gardner, H.6
Haslam, S.Z.7
Bronson, R.T.8
Elledge, S.J.9
Weinberg, R.A.10
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Tumor induction and tissue atrophy in mice lacking E2F-1
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Yamasaki L, Jacks T, Bronson R, Goillot E, Harlow E, Dyson NJ. Tumor induction and tissue atrophy in mice lacking E2F-1. Cell. 85:1996;537-548.
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Yamasaki, L.1
Jacks, T.2
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Goillot, E.4
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Krek W, Xu G, Livingston DM. Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint. Cell. 83:1995;1149-1158.
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Krek, W.1
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Geng, Y.1
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