A
A J Rossomando
Researcher at University of Virginia
Publications - 10
Citations - 2068
A J Rossomando is an academic researcher from University of Virginia. The author has contributed to research in topics: MAP2K7 & MAP kinase kinase kinase. The author has an hindex of 9, co-authored 10 publications receiving 2046 citations.
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Journal ArticleDOI
Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase).
D M Payne,A J Rossomando,Paul A. Martino,A. K. Erickson,J.-H. Her,J. Shabanowitz,Donald F. Hunt,Michael J. Weber,Thomas W. Sturgill +8 more
TL;DR: The regulation of activity by dual phosphorylations at closely spaced threonyl and tyrosyl residues has a functional correlate in p34cdc2, and may be characteristic of a family of protein kinases regulating cell cycle transitions.
Journal ArticleDOI
Evidence that pp42, a major tyrosine kinase target protein, is a mitogen-activated serine/threonine protein kinase.
TL;DR: It is reported that pp42 phosphorylation and MAP kinase activation occur in fibroblasts in response to similar mitogens, that the two proteins comigrate on one- and two-dimensional polyacrylamide gels, and that theTwo proteins copurify chromatographically.
Journal ArticleDOI
Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase.
A. K. Erickson,D M Payne,Paul A. Martino,A J Rossomando,J. Shabanowitz,Michael J. Weber,Donald F. Hunt,Thomas W. Sturgill +7 more
TL;DR: The sequence surrounding threonine 97 in bovine MBP may contain essential features of a recognition sequence for MAP kinase, as well as a known in vivo phosphorylation site in MBP, which was determined using mass spectrometry.
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Autophosphorylation in vitro of recombinant 42-kilodalton mitogen-activated protein kinase on tyrosine.
TL;DR: The finding that the tyrosine-phosphorylated protein displays a small fraction of the activity seen with the fully activated, doubly phosphorylated enzyme isolated from mammalian cells raises the possibility that regulation of MAP kinase activity in response to agonist stimulation could occur in part through the enhancement of autophosphorylation on tyosine.
Journal ArticleDOI
The phorbol ester-dependent activator of the mitogen-activated protein kinase p42mapk is a kinase with specificity for the threonine and tyrosine regulatory sites
TL;DR: Findings indicate that phorbol ester-stimulated MAP kinase kinase can activate p42 mapk by threonine and tyrosine phosphorylations, and that p42mapk thus does not require an autophosphorylation reaction.