Results 151 to 160 of about 22,951 (177)
HMGA2 links morphological evolution and microenvironment dynamics to systemic therapy response in clear cell renal cell carcinoma. [PDF]
J Immunother CancerNakamoto T +9 more
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G-quadruplex stabilization induces DNA breaks in pericentromeric repetitive DNA sequences in B lymphocytes. [PDF]
Proc Natl Acad Sci U S AWaisertreiger I +3 more
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An immunobiliary single-cell atlas resolves crosstalk of type 2 cDCs and γδT cells in cholangitis
Thomann S +15 more
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Current Opinion in Cell Biology, 1994
A growing family of kinases and phosphatases controls the activity of the cyclin-dependent kinase cdc2. The past year has seen the identification of the cdk activating kinase as well as considerable elucidation of the cdc25/wee1 regulatory pathways. Both cdc25 and wee1 appear to be regulated by upstream kinase/phosphatase networks.
T R, Coleman, W G, Dunphy
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A growing family of kinases and phosphatases controls the activity of the cyclin-dependent kinase cdc2. The past year has seen the identification of the cdk activating kinase as well as considerable elucidation of the cdc25/wee1 regulatory pathways. Both cdc25 and wee1 appear to be regulated by upstream kinase/phosphatase networks.
T R, Coleman, W G, Dunphy
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Trends in Biochemical Sciences, 1995
Neurofilament proteins and the neuron-specific microtubule-associated protein tau are phosphorylated in vivo at sites conforming to the phosphorylation consensus motif of the cell-cycle-control protein kinase, p34cdc2-cyclin. Abnormalities in the phosphorylation of these proteins are associated with neurodegenerative disorders, such as amylotrophic ...
J, Lew, J H, Wang
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Neurofilament proteins and the neuron-specific microtubule-associated protein tau are phosphorylated in vivo at sites conforming to the phosphorylation consensus motif of the cell-cycle-control protein kinase, p34cdc2-cyclin. Abnormalities in the phosphorylation of these proteins are associated with neurodegenerative disorders, such as amylotrophic ...
J, Lew, J H, Wang
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Phosphorylation of Dynamin by CDC2 Kinase
Biochemical and Biophysical Research Communications, 1994A 100kD microtubule-bundling protein dynamin was phosphorylated in vitro by cdc2 kinase to approximately 1 mol of phosphate/mol of dynamin at a serine residue. These phosphorylations of dynamin greatly reduced its binding ability to microtubules.
H, Hosoya +5 more
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CDK9 (PITALRE): A multifunctional cdc2-related kinase
Journal of Cellular Physiology, 1998CDK9 is a cdc2-related kinase protein. Previously named PITALRE, this protein is a serine-threonine kinase involved in many physiological processes. Unlike most of the cdc2-like kinases, its activity is not cell cycle-regulated. CDK9 acts preferentially in processes different from cell-cycle regulation, such as differentiation.
de Falco G., Giordano A.
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The fission yeast cell cycle control gene cdc2: structure of the cdc2 region
Molecular and General Genetics MGG, 1985The cdc2 cell cycle control gene of Schizosaccharomyces pombe has been identified on a 3 kb DNA fragment. The gene is unique in the genome and is located near to a 5S ribosomal RNA gene. When a plasmid containing DNA sequences adjacent to the cdc2 gene is transformed into certain temperature sensitive cdc2 mutants it allows colony formation at the ...
Barbara Durkacz +3 more
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Cloning of cDNAs encoding Bombyx homologues of Cdc2 and Cdc2‐related kinase from eggs
Insect Molecular Biology, 1997Abstract In diapausing eggs of the silkworm, Bombyx mori , embryonic cells are arrested at G 2 phase. The ability to undertake cell division is resumed in the course of diapause termination caused by such a treatment as acclimation to ...
H, Iwasaki +4 more
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Nature Cell Biology, 2003
Proteins that control the cell cycle would seem to have little to do with cell migration. However, a recent report indicates that Cdc2, a key cyclin-dependent kinase, can also enhance cell migration. Levels of Cdc2 are upregulated in cells that express high levels of the αvβ3 integrin, a protein that has long been implicated in enhanced migration and ...
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Proteins that control the cell cycle would seem to have little to do with cell migration. However, a recent report indicates that Cdc2, a key cyclin-dependent kinase, can also enhance cell migration. Levels of Cdc2 are upregulated in cells that express high levels of the αvβ3 integrin, a protein that has long been implicated in enhanced migration and ...
openaire +2 more sources