Another piece of the p27Kip1 puzzle

Philipp Kaldis

doi:10.1016/j.cell.2007.01.006

Another piece of the p27Kip1 puzzle

Philipp Kaldis

National Cancer Institute at Frederick

Research output: Contribution to journal › Review article › peer-review

Abstract

How extracellular signals communicate with the cell cycle is poorly understood. In this issue, two papers (Grimmler et al., 2007; Chu et al., 2007) address this problem by reporting phosphorylation of the cyclin-dependent kinase inhibitor p27^Kip1 on a tyrosine residue by nonreceptor tyrosine kinases, which decreases p27 stability. This new mechanism could explain how cells enter the cell cycle from a quiescent state.

Original language	English
Pages (from-to)	241-244
Journal	Cell
Volume	128
Issue number	2
DOIs	https://doi.org/10.1016/j.cell.2007.01.006
Publication status	Published - 2007 Jan 26
Externally published	Yes

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10.1016/j.cell.2007.01.006

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title = "Another piece of the p27Kip1 puzzle",

abstract = "How extracellular signals communicate with the cell cycle is poorly understood. In this issue, two papers (Grimmler et al., 2007; Chu et al., 2007) address this problem by reporting phosphorylation of the cyclin-dependent kinase inhibitor p27Kip1 on a tyrosine residue by nonreceptor tyrosine kinases, which decreases p27 stability. This new mechanism could explain how cells enter the cell cycle from a quiescent state.",

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AB - How extracellular signals communicate with the cell cycle is poorly understood. In this issue, two papers (Grimmler et al., 2007; Chu et al., 2007) address this problem by reporting phosphorylation of the cyclin-dependent kinase inhibitor p27Kip1 on a tyrosine residue by nonreceptor tyrosine kinases, which decreases p27 stability. This new mechanism could explain how cells enter the cell cycle from a quiescent state.

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DO - 10.1016/j.cell.2007.01.006

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JO - Cell.

JF - Cell.

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Another piece of the p27Kip1 puzzle

Abstract

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