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Refinado por: Base de dados/Biblioteca: HighWire Press (Free Journals) remover Nome da Publicação: The Embo Journal remover
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1
mdm2 expression is induced by wild type p53 activity
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mdm2 expression is induced by wild type p53 activity

Barak, Y. ; Juven, T. ; Haffner, R. ; Oren, M.

The EMBO journal, 1993-02, Vol.12 (2), p.461-468 [Periódico revisado por pares]

London: Nature Publishing Group

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2
Cdc25A is a novel phosphatase functioning early in the cell cycle
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Cdc25A is a novel phosphatase functioning early in the cell cycle

Jinno, S. ; Suto, K. ; Nagata, A. ; Igarashi, M. ; Kanaoka, Y. ; Nojima, H. ; Okayama, H.

The EMBO journal, 1994-04, Vol.13 (7), p.1549-1556 [Periódico revisado por pares]

London: Nature Publishing Group

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3
Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast
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Destruction of the CDC28/CLB mitotic kinase is not required for the metaphase to anaphase transition in budding yeast

Surana, U ; Amon, A ; Dowzer, C ; McGrew, J ; Byers, B ; Nasmyth, K

The EMBO journal, 1993-05, Vol.12 (5), p.1969-1978 [Periódico revisado por pares]

London: Nature Publishing Group

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4
Phosphorylation and activation of human cdc25‐C by cdc2‐‐cyclin B and its involvement in the self‐amplification of MPF at mitosis
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Phosphorylation and activation of human cdc25‐C by cdc2‐‐cyclin B and its involvement in the self‐amplification of MPF at mitosis

Hoffmann, I. ; Clarke, P.R. ; Marcote, M.J. ; Karsenti, E. ; Draetta, G.

The EMBO journal, 1993-01, Vol.12 (1), p.53-63 [Periódico revisado por pares]

London: Nature Publishing Group

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5
Comparison of the Saccharomyces cerevisiae G1 cyclins: Cln3 may be an upstream activator of Cln1, Cln2 and other cyclins
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Comparison of the Saccharomyces cerevisiae G1 cyclins: Cln3 may be an upstream activator of Cln1, Cln2 and other cyclins

Tyers, M. ; Tokiwa, G. ; Futcher, B.

The EMBO journal, 1993-05, Vol.12 (5), p.1955-1968 [Periódico revisado por pares]

London: Nature Publishing Group

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6
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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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

Fesquet, D. ; Labbé, J.C. ; Derancourt, J. ; Capony, J.P. ; Galas, S. ; Girard, F. ; Lorca, T. ; Shuttleworth, J. ; Dorée, M. ; Cavadore, J.C.

The EMBO journal, 1993-08, Vol.12 (8), p.3111-3121 [Periódico revisado por pares]

London: Nature Publishing Group

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7
Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates
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Regulatory phosphorylation of the p34cdc2 protein kinase in vertebrates

Norbury, C. ; Blow, J. ; Nurse, P.

The EMBO journal, 1991-11, Vol.10 (11), p.3321-3329 [Periódico revisado por pares]

London: Nature Publishing Group

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8
The metaphase II arrest in mouse oocytes is controlled through microtubule‐dependent destruction of cyclin B in the presence of CSF
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The metaphase II arrest in mouse oocytes is controlled through microtubule‐dependent destruction of cyclin B in the presence of CSF

Kubiak, J.Z. ; Weber, M. ; Pennart, H. ; Winston, N.J. ; Maro, B.

The EMBO journal, 1993-10, Vol.12 (10), p.3773-3778 [Periódico revisado por pares]

London: Nature Publishing Group

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9
p80cdc25 mitotic inducer is the tyrosine phosphatase that activates p34cdc2 kinase in fission yeast
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p80cdc25 mitotic inducer is the tyrosine phosphatase that activates p34cdc2 kinase in fission yeast

Millar, J.B. ; McGowan, C.H. ; Lenaers, G. ; Jones, R. ; Russell, P.

The EMBO journal, 1991-12, Vol.10 (13), p.4301-4309 [Periódico revisado por pares]

London: Nature Publishing Group

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10
Suppression of DNA replication via Mos function during meiotic divisions in Xenopus oocytes
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Suppression of DNA replication via Mos function during meiotic divisions in Xenopus oocytes

Furuno, N. ; Nishizawa, M. ; Okazaki, K. ; Tanaka, H. ; Iwashita, J. ; Nakajo, N. ; Ogawa, Y. ; Sagata, N.

The EMBO journal, 1994-05, Vol.13 (10), p.2399-2410 [Periódico revisado por pares]

London: Nature Publishing Group

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