M
Michael Karin
Researcher at University of California, San Diego
Publications - 753
Citations - 246120
Michael Karin is an academic researcher from University of California, San Diego. The author has contributed to research in topics: IκB kinase & Signal transduction. The author has an hindex of 236, co-authored 704 publications receiving 226485 citations. Previous affiliations of Michael Karin include Sanford-Burnham Institute for Medical Research & University of California, Los Angeles.
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c-Jun N-terminal phosphorylation correlates with activation of the JNK subgroup but not the ERK subgroup of mitogen-activated protein kinases.
Audrey Minden,Anning Lin,Tod Smeal,Benoit Dérijard,Melanie H. Cobb,Roger J. Davis,Michael Karin +6 more
TL;DR: This study suggests that two different branches of the mitogen-activated protein (MAP) kinase group are involved in the stimulation of AP-1 activity through two different mechanisms.
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A new group of conserved coactivators that increase the specificity of AP-1 transcription factors
TL;DR: This work has identified a protein, JAB1, that interacts with c-Jun and JunD, but not with JunB or v-Jun, and defines a new group of coactivators that increase the specificity of target gene activation by AP-1 proteins.
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Transcriptional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB
Masatoshi Hagiwara,Arthur S. Alberts,Paul K. Brindle,Judy L. Meinkoth,James R. Feramisco,Tiliang Deng,Michael Karin,Shirish Shenolikar,Marc Montminy +8 more
TL;DR: It is proposed that PP-1 specifically dephosphorylates CREB at Ser-133 and inhibits cAMP-dependent transcription, and this phosphatase is the major regulator of CREB activity in camp-responsive cells.
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Limiting inflammation-the negative regulation of NF-κB and the NLRP3 inflammasome.
TL;DR: The key molecular mechanisms that contribute to the self-limiting nature of inflammatory signaling are discussed, with emphasis on the negative regulation of the NF-κB pathway and the NLRP3 inflammasome.
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Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway
TL;DR: Targeting of Sos to the plasma membrane in the vicinity of Ras appears to be the primary mechanism leading to activation of the Ras pathway and a secondary mechanism could involve relief of the inhibitory effect of the Sos C-terminal region.