K
Kathleen L. Gould
Researcher at Vanderbilt University
Publications - 233
Citations - 15753
Kathleen L. Gould is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Schizosaccharomyces pombe & Cytokinesis. The author has an hindex of 69, co-authored 206 publications receiving 15016 citations. Previous affiliations of Kathleen L. Gould include University of California, San Diego & University of Washington.
Papers
More filters
Journal ArticleDOI
Tyrosine phosphorylation of the fission yeast cdc2 + protein kinase regulates entry into mitosis
Kathleen L. Gould,Paul Nurse +1 more
TL;DR: The cdc2+ protein kinase (pp34) is found to be phosphorylated on tyrosine as well as serine and threonine residues in exponentially growing Schizosaccharomyces pombe, establishing that tyrosines phosphorylation/dephosphorylation directly regulates pp34 function.
Journal ArticleDOI
Shotgun identification of protein modifications from protein complexes and lens tissue
Michael J. MacCoss,W. Hayes McDonald,Anita Saraf,Rovshan G. Sadygov,Judy M. Clark,Joseph J. Tasto,Kathleen L. Gould,Dirk Wolters,Michael P. Washburn,Avery H. Weiss,John I. Clark,John R. Yates +11 more
TL;DR: This work describes a process for the analysis of posttranslational modifications that is simple, robust, general, and can be applied to complicated protein mixtures and lens tissue from a patient with congenital cataracts.
Journal ArticleDOI
Tyr527 is phosphorylated in pp60c-src: implications for regulation.
TL;DR: Results suggest that the increase in transforming ability and kinase activity that occurred in the genesis of pp60v-src may have resulted from the loss of a tyrosine involved in negative regulation.
Journal ArticleDOI
Substrate specificity of protein kinase C: use of synthetic peptides corresponding to physiological sites as probes for substrate recognition requirements
TL;DR: Comparative studies have demonstrated that, in vivo, the enzyme exhibits a preference for one basic residue C-terminal to the phosphorylatable residue, as in the sequence: Ser/Thr-Xaa-Lys/Arg, where Xaa is usually an uncharged residue.
Journal ArticleDOI
Phosphorylation at Thr167 is required for Schizosaccharomyces pombe p34cdc2 function.
TL;DR: It is established that Thr167 phosphorylation is required for p34CDc2 kinase activity at mitosis and is involved in the association of p34cdc2 with cyclin B, and might also play a role in the exit from mitosis.