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Alexey Kotlyarov
Researcher at Hannover Medical School
Publications - 27
Citations - 2646
Alexey Kotlyarov is an academic researcher from Hannover Medical School. The author has contributed to research in topics: Kinase & Protein kinase A. The author has an hindex of 20, co-authored 27 publications receiving 2524 citations. Previous affiliations of Alexey Kotlyarov include Hochschule Hannover & Max Delbrück Center for Molecular Medicine.
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Journal ArticleDOI
Mitogen-activated protein kinase-activated protein kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/uridine-rich element.
Edward Hitti,Tatiana Iakovleva,Matthew Brook,Stefanie Deppenmeier,Achim D. Gruber,Danuta Radzioch,Andrew R. Clark,Perry J. Blackshear,Alexey Kotlyarov,Matthias Gaestel +9 more
TL;DR: It is suggested that MK2 inhibits the mRNA destabilizing activity of TTP and, in parallel, codegradation of TNP together, with the target mRNA resulting in increased cellular levels of T TP.
Journal ArticleDOI
Genetic dissection of the cellular pathways and signaling mechanisms in modeled tumor necrosis factor-induced Crohn's-like inflammatory bowel disease.
Dimitris L. Kontoyiannis,George Boulougouris,Menelaos Manoloukos,Maria Armaka,Maria Apostolaki,Theresa T. Pizarro,Alexey Kotlyarov,Irmgard Förster,Richard A. Flavell,Matthias Gaestel,Philip N. Tsichlis,Fabio Cominelli,George Kollias +12 more
TL;DR: It is shown that development of intestinal pathology in this model depends on Th1-like cytokines such as interleukin 12 and interferon γ and requires the function of CD8+ T lymphocytes and the existence of redundant cellular pathways operating downstream of TNF in inflammatory bowel disease is established.
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Leptomycin B‐sensitive nuclear export of MAPKAP kinase 2 is regulated by phosphorylation
TL;DR: The region responsible for nuclear export in MK2 is identified which is partially overlapping with and C‐terminal to the autoinhibitory motif, which contains a cluster of hydrophobic amino acids in the characteristic spacing of a leucine‐rich Rev‐type NES which is necessary to direct GFP–MK2 to the cytoplasm.
Journal ArticleDOI
Distinct Cellular Functions of MK2
Alexey Kotlyarov,Yvonne M. Yannoni,Susann Fritz,Kathrin Laass,Jean-Baptiste Telliez,Deborah Pitman,Lih-Ling Lin,Matthias Gaestel +7 more
TL;DR: It is shown that the amount of p38 MAPK is significantly reduced in cells and tissues lacking MK2, indicating a stabilizing effect of MK2 for p38, and that MK2 catalytic activity does not contribute to this stabilization, and it is demonstrated that stabilizing p38MAPK does not restore TNF biosynthesis.
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The p38/MK2-Driven Exchange between Tristetraprolin and HuR Regulates AU–Rich Element–Dependent Translation
Christopher Tiedje,Natalia Ronkina,Mohammad Tehrani,Sonam Dhamija,Kathrin Laass,Helmut Holtmann,Alexey Kotlyarov,Matthias Gaestel +7 more
TL;DR: It is shown that phosphorylation of TTP by MK2 decreases its affinity to the ARE, inhibits its ability to replace HuR, and permits HuR-mediated initiation of translation of TNF mRNA, which provides a reversible switch between unstable/non-translatable and stable/efficiently translated mRNAs.