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

Forskningsoutput: Tidskriftsbidrag › Översiktsartikel › Peer review

Sammanfattning

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.

Originalspråk	engelska
Sidor (från-till)	241-244
Tidskrift	Cell
Volym	128
Nummer	2
DOI	https://doi.org/10.1016/j.cell.2007.01.006
Status	Published - 2007 jan. 26
Externt publicerad	Ja

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10.1016/j.cell.2007.01.006

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@article{9846ea4ec17045f99955b652461789cf,

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.",

author = "Philipp Kaldis",

year = "2007",

month = jan,

day = "26",

doi = "10.1016/j.cell.2007.01.006",

language = "English",

volume = "128",

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journal = "Cell",

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AU - Kaldis, Philipp

PY - 2007/1/26

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N2 - 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.

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.

U2 - 10.1016/j.cell.2007.01.006

DO - 10.1016/j.cell.2007.01.006

M3 - Review article

C2 - 17254963

AN - SCOPUS:33846330967

SN - 1097-4172

VL - 128

SP - 241

EP - 244

JO - Cell

JF - Cell

IS - 2

ER -

Another piece of the p27Kip1 puzzle

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