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Animal cell cycles and their control
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Norbury C, Nurse P. Animal cell cycles and their control. Annu Rev Biochem. 61:1992;441-470.
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Principles of CDK regulation
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Morgan DO. Principles of CDK regulation. Nature. 374:1995;131-134.
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Nature
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Morgan, D.O.1
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Inhibitors of mammalian G1-cyclin-dependent kinases
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Sherr CJ, Roberts JM. Inhibitors of mammalian G1-cyclin-dependent kinases. Genes Dev. 9:1995;1149-1163.
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Cyclin dependent kinase regulation
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Lees E. Cyclin dependent kinase regulation. Curr Opin Cell Biol. 7:1995;773-780.
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Lees, E.1
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0029644478
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The cell cycle and suc1: From structure to function?
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Endicott JA, Nurse P. The cell cycle and suc1: from structure to function? Structure. 3:1995;321-325.
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Structure
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Endicott, J.A.1
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0029645932
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Bound to activate: Conformational consequences of cyclin binding to CDK2
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Radzio-Andzelm E, Lew J, Taylor S. Bound to activate: conformational consequences of cyclin binding to CDK2. Structure. 3:1995;1135-1141.
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Structure
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Radzio-Andzelm, E.1
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Active and inactive protein kinases: Structural basis for regulation
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Johnson LN, Noble MEM, Owen DJ. Active and inactive protein kinases: structural basis for regulation. Cell. 85:1996;149-158.
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Cell
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Johnson, L.N.1
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Crystal structure of cyclin-dependent kinase 2
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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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Nature
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De Bondt, H.L.1
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Morgan, D.O.5
Kim, S.-H.6
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9
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0029645935
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The crystal structure of cyclin A
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of outstanding interest. of special interest. The structure of a truncated cyclin A fragment, like that of the CDK2-bound protein [10], contains a 10-helix core and two additional helices. This paper includes an extensive discussion of features of cyclin structure that are probably conserved among cyclin-family members.
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of outstanding interest Brown NR, Noble MEM, Endicott JA, Garman EF, Wakatsuki S, Mitchell E, Rasmussen B, Hunt T, Johnson LN. The crystal structure of cyclin A. of special interest Structure. 3:1995;1235-1247 The structure of a truncated cyclin A fragment, like that of the CDK2-bound protein [10], contains a 10-helix core and two additional helices. This paper includes an extensive discussion of features of cyclin structure that are probably conserved among cyclin-family members.
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(1995)
Structure
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Brown, N.R.1
Noble, M.E.M.2
Endicott, J.A.3
Garman, E.F.4
Wakatsuki, S.5
Mitchell, E.6
Rasmussen, B.7
Hunt, T.8
Johnson, L.N.9
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10
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0029029617
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Mechanism of CDK activation revealed by the structure of a cyclin A-CDK2 complex
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of outstanding interest. Destined to be a classic in CDK structural analysis, showing the complex conformational changes that occur in CDK2 upon cyclin A binding.
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Jeffrey PD, Russo AA, Polyak K, Gibbs E, Hurwitz J, Massague J, Pavletich NP. Mechanism of CDK activation revealed by the structure of a cyclin A-CDK2 complex. of outstanding interest Nature. 376:1995;313-320 Destined to be a classic in CDK structural analysis, showing the complex conformational changes that occur in CDK2 upon cyclin A binding.
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(1995)
Nature
, vol.376
, pp. 313-320
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Jeffrey, P.D.1
Russo, A.A.2
Polyak, K.3
Gibbs, E.4
Hurwitz, J.5
Massague, J.6
Pavletich, N.P.7
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11
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0027532449
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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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Mol Biol Cell
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Connell-Crowley, L.1
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Wei, N.3
Harper, J.W.4
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12
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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. Describes the structural basis of CDK2 activation by Thr160 phosphorylation. Together with [8,10], this paper completes our understanding of the two major steps in CDK activation.
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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 Describes the structural basis of CDK2 activation by Thr160 phosphorylation. Together with [8,10], this paper completes our understanding of the two major steps in CDK activation.
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(1996)
Nat Struct Biol
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Russo, A.A.1
Jeffrey, P.D.2
Pavletich, N.P.3
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13
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0028950016
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The effect of phosphorylation by CAK on cyclin binding by CDC2 and CDK2
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Desai D, Wessling HC, Fisher RP, Morgan DO. The effect of phosphorylation by CAK on cyclin binding by CDC2 and CDK2. Mol Cell Biol. 15:1995;345-350.
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Mol Cell Biol
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Desai, D.1
Wessling, H.C.2
Fisher, R.P.3
Morgan, D.O.4
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14
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0029665852
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Kip1 cyclin-dependent kinase inhibitor bound to the cyclinA - CDK2 complex
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of outstanding interest. This year's major CDK structural study, which describes the astonishing conformational changes underlying CDK2 inhibition by the inhibitor p27.
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Kip1 cyclin-dependent kinase inhibitor bound to the cyclinA - CDK2 complex. of outstanding interest Nature. 382:1996;325-331 This year's major CDK structural study, which describes the astonishing conformational changes underlying CDK2 inhibition by the inhibitor p27.
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(1996)
Nature
, vol.382
, pp. 325-331
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Russo, A.A.1
Jeffrey, P.D.2
Patten, A.3
Massague, J.4
Pavletich, N.P.5
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15
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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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Beach, D.3
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0029058587
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Inhibition of cyclin-dependent kinases by p21
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Harper JW, Elledge SJ, Keyomarsi 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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Mol Biol Cell
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Harper, J.W.1
Elledge, S.J.2
Keyomarsi, 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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17
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0027482006
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Human CksHs2 atomic structure: A role for its hexameric assembly in cell cycle control
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Parge HE, Arvai AS, Murtari DJ, Reed SI, Tainer JA. Human CksHs2 atomic structure: a role for its hexameric assembly in cell cycle control. Science. 262:1993;387-395.
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Science
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Parge, H.E.1
Arvai, A.S.2
Murtari, D.J.3
Reed, S.I.4
Tainer, J.A.5
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19
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0028877368
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Crystal structure of the cell cycle-regulatory protein suc1 reveals a β-hinge conformational switch
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Bourne Y, Arvai AS, Bernstein SL, Watson MH, Reed SI, Endicott JE, Noble ME, Johnson LN, Tainer JA. Crystal structure of the cell cycle-regulatory protein suc1 reveals a β-hinge conformational switch. Proc Natl Acad Sci USA. 92:1995;10232-10236.
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Proc Natl Acad Sci USA
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Bourne, Y.1
Arvai, A.S.2
Bernstein, S.L.3
Watson, M.H.4
Reed, S.I.5
Endicott, J.E.6
Noble, M.E.7
Johnson, L.N.8
Tainer, J.A.9
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20
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0029034120
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Crystal structure of the human cell cycle protein CksHs1: Single domain fold with similarity to kinase N-lobe domain
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Arvai AS, Bourne Y, Hickey MJ, Tainer JA. Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain. J Mol Biol. 249:1995;835-842.
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J Mol Biol
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Arvai, A.S.1
Bourne, Y.2
Hickey, M.J.3
Tainer, J.A.4
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21
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0029918062
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Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1
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of outstanding interest. By revealing the site on CDK2 where the CKS protein binds, this paper provided evidence that CKS proteins serve to target the CDK to substrates or regulators.
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Bourne Y, Watson MH, Hickey MJ, Holmes W, Rocque W, Reed SI, Tainer JA. Crystal structure and mutational analysis of the human CDK2 kinase complex with cell cycle-regulatory protein CksHs1. of outstanding interest Cell. 84:1996;863-874 By revealing the site on CDK2 where the CKS protein binds, this paper provided evidence that CKS proteins serve to target the CDK to substrates or regulators.
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(1996)
Cell
, vol.84
, pp. 863-874
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Bourne, Y.1
Watson, M.H.2
Hickey, M.J.3
Holmes, W.4
Rocque, W.5
Reed, S.I.6
Tainer, J.A.7
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23
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0029784224
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Xe-p9, a Xenopus Suc1/Cks homolog, has multiple essential roles in cell cycle control
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of special interest. A provocative study suggesting that CKS proteins are required for interactions between the CDK subunit and regulatory proteins involved in CDK phosphorylation and cyclin degradation.
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Patra D, Dunphy WG. Xe-p9, a Xenopus Suc1/Cks homolog, has multiple essential roles in cell cycle control. of special interest Genes Dev. 10:1996;1503-1515 A provocative study suggesting that CKS proteins are required for interactions between the CDK subunit and regulatory proteins involved in CDK phosphorylation and cyclin degradation.
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(1996)
Genes Dev
, vol.10
, pp. 1503-1515
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Patra, D.1
Dunphy, W.G.2
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24
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0028332528
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The decision to enter mitosis
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Dunphy WG. The decision to enter mitosis. Trends Cell Biol. 4:1994;202-207.
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Trends Cell Biol
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Dunphy, W.G.1
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25
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0001212842
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Three dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase
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The second cyclin structure to be determined reveals structural features that are conserved among cyclins, in addition to structural features underyling the unique properties of the cyclin H - CDK complex. of special interest
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Kim KK, Chamberlin HM, Morgan DO, Kim S-H. Three dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. of special interest Nat Struct Biol. 1996; The second cyclin structure to be determined reveals structural features that are conserved among cyclins, in addition to structural features underyling the unique properties of the cyclin H - CDK complex.
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(1996)
Nat Struct Biol
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Kim, K.K.1
Chamberlin, H.M.2
Morgan, D.O.3
Kim, S.-H.4
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26
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0028807103
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Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase
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Fisher RP, Jin P, Chamberlin HM, Morgan DO. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell. 83:1995;47-57.
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(1995)
Cell
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Fisher, R.P.1
Jin, P.2
Chamberlin, H.M.3
Morgan, D.O.4
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27
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0028856425
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MAT1 (menage à trois), a new RING finger protein subunit stabilizing cyclin H - Cdk7 complexes in starfish and Xenopus CAK
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Devault A, Martinez A-M, Fesquet D, Labbe J-C, Morin N, Tassan J-P, Nigg EA, Cavadore J-C, Doree M. MAT1 (menage à trois), a new RING finger protein subunit stabilizing cyclin H - cdk7 complexes in starfish and Xenopus CAK. EMBO J. 14:1995;5027-5036.
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EMBO J
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Devault, A.1
Martinez, A.-M.2
Fesquet, D.3
Labbe, J.-C.4
Morin, N.5
Tassan, J.-P.6
Nigg, E.A.7
Cavadore, J.-C.8
Doree, M.9
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28
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0028882228
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In vitro assembly of a functional human CDK7 - Cyclin H complex requires MAT1, a novel 36 kDa RING finger protein
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Tassan J-P, Jaquenod M, Fry AM, Frutiger S, Hughes GJ, Nigg EA. In vitro assembly of a functional human CDK7 - cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. EMBO J. 14:1995;5608-5617.
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EMBO J
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Tassan, J.-P.1
Jaquenod, M.2
Fry, A.M.3
Frutiger, S.4
Hughes, G.J.5
Nigg, E.A.6
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29
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0029741552
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Under arrest at atomic resolution
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Morgan DO. Under arrest at atomic resolution. Nature. 382:1996;295-296.
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Nature
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Morgan, D.O.1
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