نتایج جستجو برای: activated protein kinase

تعداد نتایج: 1443388  

2016
Rachel J. Roth Flach Laura V. Danai Marina T. DiStefano Mark Kelly Lorena Garcia Menendez Agata Jurczyk Rohit B. Sharma Dae Young Jung Jong Hun Kim Jason K. Kim Rita Bortell Laura C. Alonso Michael P. Czech

Previous studies revealed a paradox whereby mitogen-activated protein kinase kinase kinase kinase 4 (Map4k4) acted as a negative regulator of insulin sensitivity in chronically obese mice, yet systemic deletion of Map4k4 did not improve glucose tolerance. Here, we report markedly reduced glucose-responsive plasma insulin and C-peptide levels in whole body Map4k4-depleted mice (M4K4 iKO) as well...

Journal: :journal of genetic resources 2015
fereshteh mir mohammadrezaei

abstract accumulation of gene changes and chromosomal instability in response to cellular dna damage lead to cancer. dna damage induces cell cycle checkpoints pathways. checkpoints regulate dna replication and cell cycle progression, chromatin restructuring, and apoptosis. checkpoint kinase 2 (chk2) is activated in response to dna lesions. atm phosphorylate chk2. the activated chk2 kinase can p...

Journal: :The Journal of pharmacology and experimental therapeutics 2011
Qiyan Li Hong Yu Robert Zinna Kylie Martin Bethany Herbert Angen Liu Carlos Rossa Keith L Kirkwood

p38 mitogen-activated protein kinases (MAPKs) are critical for innate immune signaling and subsequent cytokine expression in periodontal inflammation and bone destruction. In fact, previous studies show that systemic p38 MAPK inhibitors block periodontal disease progression. However, development of p38 MAPK inhibitors with favorable toxicological profiles is difficult. Here, we report our findi...

Journal: :The Journal of biological chemistry 1997
D D Hirsch P J Stork

The c-Jun N-terminal protein kinases (JNKs), also called stress-activated protein kinases, are members of the growing family of serine/threonine kinases in the mitogen-activated protein (MAP) kinase superfamily. Like other MAP kinases, JNKs are activated via phosphorylation on adjacent threonine and tyrosine residues and can be inactivated by a unique family of dual specificity phosphatases, ca...

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