Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Tomi P. Mäkelä"'
Publikováno v:
EMBO reports. 14:741-747
Loss of primary cilia is frequently observed in tumour cells, including glioblastoma cells, and proposed to benefit tumour growth, but a causal link has not been established. Here, we show that CCRK (cell cycle-related kinase) and its substrate ICK (
Autor:
Derrick J. Rossi, Eero Lehtonen, Anou Londesborough, Mark Henkemeyer, Arno Pihlak, Tomi P. Mäkelä, Nina Korsisaari
Publikováno v:
The EMBO Journal. 20:2844-2856
The trimeric Cdk7-cyclin H-Mat1 complex comprises the kinase subunit of basal transcription factor TFIIH and has been shown to function as a cyclin-dependent kinase (Cdk)-activating kinase. Herein we report that disruption of the murine Mat1 gene lea
Autor:
Tomi P. Mäkelä, Nina Korsisaari
Publikováno v:
Journal of Biological Chemistry. 275:34837-34840
Cyclin-dependent kinase 7 (Cdk7) forms a trimeric complex with cyclin H and Mat1 to form the mammalian Cdk-activating kinase, CAK, as well as a part of the basal transcription factor TFIIH, where Cdk7 phosphorylates the C-terminal domain (CTD) of the
Autor:
Arno Pihlak, Véronique Damagnez, Tomi P. Mäkelä, Damien Hermand, Guillaume Cottarel, Thomas Westerling, Jean Vandenhaute
Publikováno v:
The EMBO Journal. 17:7230-7238
Cell cycle progression is dependent on the sequential activity of cyclin-dependent kinases (CDKs). For full activity, CDKs require an activating phosphorylation of a conserved residue (corresponding to Thr160 in human CDK2) carried out by the CDK-act
Publikováno v:
Experimental Cell Research. 242:211-221
The carboxyl-terminal domain (CTD) of the largest RNA polymerase II (pol II) subunit is a target for extensive phosphorylation in vivo. Using in vitro kinase assays it was found that several different protein kinases can phosphorylate the CTD includi
Publikováno v:
Nature. 377:557-560
AN array of tandem heptapeptide repeats at the carboxv -terminal domain (CTD) of the largest subunit of RNA polymerase II constitute a highly conserved structure essential for viability1a¤-3. Studies have established that the CTD is phosphorylated a
Publikováno v:
Molecular biology of the cell. 12(12)
In normal cells, activation of cyclin-dependent kinases (cdks) requires binding to a cyclin and phosphorylation by the cdk-activating kinase (CAK). The Kaposi's sarcoma-associated herpesvirus encodes a protein with similarity to D-type cyclins. This
Autor:
Arno Pihlak, Tomi P. Mäkelä, Marianne Tiainen, Jean Vandenhaute, Thomas Westerling, Jean-Yves Thuret, Damien Hermand, Tea Vallenius, Guillaume Cottarel, Carl Mann
Publikováno v:
The EMBO journal. 20(1-2)
Activating phosphorylation of cyclin-dependent kinases (Cdks) is mediated by at least two structurally distinct types of Cdk-activating kinases (Caks): the trimeric Cdk7-cyclin H-Mat1 complex in metazoans and the single-subunit Cak1 in budding yeast.
Publikováno v:
The EMBO journal. 14(24)
The cyclin-dependent kinase (CDK)-activating kinase, CAK, from mammals and amphibians consists of MO15/CDK7 and cyclin H, a complex which has been identified also as a RNA polymerase II C-terminal domain (CTD) kinase. While the Schizosaccharomyces po
Autor:
Robert A. Weinberg, Jaesang Kim, Jeffrey D. Parvin, L. J. Huber, Tomi P. Mäkelä, Phillip A. Sharp
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 92(11)
Phosphorylation of the carboxyl-terminal domain (CTD) of the large subunit of RNA polymerase II has been suggested to be critical for transcription initiation, activation, or elongation. A kinase activity specific for CTD is a component of the genera