C
Christopher J. Herring
Researcher at National Institutes of Health
Publications - 5
Citations - 473
Christopher J. Herring is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Phosphorylation & Kinase. The author has an hindex of 4, co-authored 5 publications receiving 462 citations.
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Journal ArticleDOI
Autophosphorylation in the Activation Loop Is Required for Full Kinase Activity In Vivo of Human and Yeast Eukaryotic Initiation Factor 2α Kinases PKR and GCN2
Patrick R. Romano,Minerva T. Garcia-Barrio,Xiaolong Zhang,Qizhi Wang,Deborah R. Taylor,Fan Zhang,Christopher J. Herring,Michael B. Mathews,Jun Qin,Alan G. Hinnebusch +9 more
TL;DR: It is shown that Thr-446 and Thr-451 in the PKR activation loop are required in vivo and in vitro for high-level kinase activity and striking similarities between GCN2 and PKR in the importance of autophosphorylation and the conserved Thr residues in the activation loop.
Journal ArticleDOI
Identification of phosphorylation sites in proteins separated by polyacrylamide gel electrophoresis.
Xiaolong Zhang,Christopher J. Herring,Patrick R. Romano,Joanna Szczepanowska,Hanna Brzeska,and Alan G. Hinnebusch,Jun Qin +6 more
TL;DR: A fast, sensitive, and robust procedure for the identification of precise phosphorylation sites in proteins separated by polyacrylamide gel electrophoresis by a combination of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI/TOF) and online capillary liquid chromatography electrospray tandem ion trap mass spectromaetry (LC/ESI/MS/MS).
Journal ArticleDOI
Identification by mass spectrometry of the phosphorylated residue responsible for activation of the catalytic domain of myosin I heavy chain kinase, a member of the PAK/STE20 family
Joanna Szczepanowska,Xiaolong Zhang,Christopher J. Herring,Jun Qin,Edward D. Korn,Hanna Brzeska +5 more
TL;DR: Phosphorylation of Ser-627, which is in the same position as the Ser and Thr residues that are phosphorylated in many other kinases, is necessary and sufficient for full activity of the catalytic domain.
Journal ArticleDOI
Effect of mutating the regulatory phosphoserine and conserved threonine on the activity of the expressed catalytic domain of Acanthamoeba myosin I heavy chain kinase.
Joanna Szczepanowska,Umamaheswari Ramachandran,Christopher J. Herring,James M. Gruschus,Jun Qin,Edward D. Korn,Hanna Brzeska +6 more
TL;DR: Molecular modeling indicated that Thr-631 can hydrogen bond with conserved residue Asp-591 in the catalytic loop and that similar interactions are possible for other kinases whose activities also are regulated by phosphorylation in the variable loop, so this conserved Thr residue may be essential for the activities of other Ser/Thr protein kinases as well as for the activity of MIHCK.
Book ChapterDOI
Identification of in-vivo Phosphorylation Sites with Mass Spectrometry
TL;DR: This work states that mass spectrometry is becoming the method of choice for the identification of protein phosphorylation sites because it is accurate, fast and does not require 32P labeling.