M
Mark J. Solomon
Researcher at Yale University
Publications - 65
Citations - 11787
Mark J. Solomon is an academic researcher from Yale University. The author has contributed to research in topics: Cyclin-dependent kinase & Cyclin-dependent kinase 1. The author has an hindex of 41, co-authored 65 publications receiving 11513 citations. Previous affiliations of Mark J. Solomon include Baylor College of Medicine & Massachusetts Institute of Technology.
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Journal ArticleDOI
p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest.
Kornelia Polyak,Jun-ya Kato,Mark J. Solomon,Charles J. Sherr,Joan Massagué,James M. Roberts,Andrew Koff +6 more
TL;DR: Cyclin D2-Cdk4 complexes bind competitively to and down-regulate the activity of p27 and may thereby act in a pathway that reverses Cdk2 inhibition and enables G1 progression.
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The role of cyclin synthesis and degradation in the control of maturation promoting factor activity
TL;DR: It is shown that cyclin plays a pivotal role in the control of mitosis and a proteolysis-resistant mutant of cyclin prevents the inactivation of maturation promoting factor and the exit from mitosis both in vivo and in vitro.
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cdc25 is a specific tyrosine phosphatase that directly activates p34cdc2
TL;DR: It is found that the cdc25 sequence shows weak but significant homology to a phylogenetically diverse group of protein tyrosine phosphatases, and is a specific protein phosphatase that dephosphorylates tyrosines and possibly threonine residues on p34cdc2 and regulates MPF activation.
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Cyclin activation of p34cdc2
TL;DR: The concerted transition into mitosis involves both a reduction in the rate of p34cdc2 phosphorylation on tyrosine and an increase in its rate of dephosphorylation.
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Mapping proteinDNA interactions in vivo with formaldehyde: Evidence that histone H4 is retained on a highly transcribed gene
TL;DR: Contrary to earlier in vitro evidence that histones may be absent from actively transcribed genes, it is shown directly, by immunoprecipitation of in vivo-crosslinked chromatin fragments, that at least histone H4 remains bound to hsp70 DNA in vivo, irrespective of its rate of transcription.