Results 101 to 110 of about 2,497,817 (373)

Improved control of tuberculosis and activation of macrophages in mice lacking protein kinase R. [PDF]

open access: yesPLoS ONE, 2012
Host factors that microbial pathogens exploit for their propagation are potential targets for therapeuic countermeasures. No host enzyme has been identified whose genetic absence benefits the intact mammalian host in vivo during infection with ...
Kangyun Wu   +5 more
doaj   +1 more source

Phosphatidylglycerol Is a Physiologic Activator of Nuclear Protein Kinase C*

open access: yesJournal of Biological Chemistry, 1998
A major mechanism by which protein kinase C (PKC) function is regulated is through the selective targeting and activation of individual PKC isotypes at distinct subcellular locations.
N. Murray, A. Fields
semanticscholar   +1 more source

Function‐driven design of a surrogate interleukin‐2 receptor ligand

open access: yesFEBS Letters, EarlyView.
Interleukin (IL)‐2 signaling can be achieved and precisely fine‐tuned through the affinity, distance, and orientation of the heterodimeric receptors with their ligands. We designed a biased IL‐2 surrogate ligand that selectively promotes effector T and natural killer cell activation and differentiation. Interleukin (IL) receptors play a pivotal role in
Ziwei Tang   +9 more
wiley   +1 more source

Regulation of protein kinase B and glycogen synthase kinase-3 by insulin and beta-adrenergic agonists in rat epididymal fat cells - Activation of protein kinase B by wortmannin-sensitive and -insensittve mechanisms [PDF]

open access: yes, 1997
Previous studies using L6 myotubes have suggested that glycogen synthase kinase-3 (GSK-3) is phosphoryl ated and inactivated in response to insulin by protein kinase B (PKB, also known as Akt or RAG) (Cross, D, A, E., Alessi, D, R., Cohen, P ...
Denton, Richard M.   +5 more
core  

Phospho.ELM:a database of experimentally verified phosphorylation sites in eukaryotic proteins [PDF]

open access: yes, 2004
BACKGROUND: Post-translational phosphorylation is one of the most common protein modifications. Phosphoserine, threonine and tyrosine residues play critical roles in the regulation of many cellular processes.
Blom, Nikolaj   +8 more
core   +4 more sources

Baicalin Attenuates Oxygen–Glucose Deprivation/Reoxygenation–Induced Injury by Modulating the BDNF-TrkB/PI3K/Akt and MAPK/Erk1/2 Signaling Axes in Neuron–Astrocyte Cocultures

open access: yesFrontiers in Pharmacology, 2021
Background: Baicalin (BCL), a candidate drug for ischemic stroke, has been indicated to protect neurons by promoting brain-derived neurotrophic factor (BDNF).
Changxiang Li   +9 more
doaj   +1 more source

Domain Stabilities in Protein Kinase R (PKR): Evidence for Weak Interdomain Interactions [PDF]

open access: yesBiochemistry, 2008
PKR (protein kinase R) is induced by interferon and is a key component of the innate immunity antiviral pathway. Upon binding dsRNA, PKR undergoes autophosphorylation reactions that activate the kinase, leading it to phosphorylate eIF2alpha, thus inhibiting protein synthesis in virally infected cells.
Eric, Anderson, James L, Cole
openaire   +2 more sources

The newfound relationship between extrachromosomal DNAs and excised signal circles

open access: yesFEBS Letters, EarlyView.
Extrachromosomal DNAs (ecDNAs) contribute to the progression of many human cancers. In addition, circular DNA by‐products of V(D)J recombination, excised signal circles (ESCs), have roles in cancer progression but have largely been overlooked. In this Review, we explore the roles of ecDNAs and ESCs in cancer development, and highlight why these ...
Dylan Casey, Zeqian Gao, Joan Boyes
wiley   +1 more source

Biological functions of CDK5 and potential CDK5 targeted clinical treatments. [PDF]

open access: yes, 2017
Cyclin dependent kinases are proline-directed serine/threonine protein kinases that are traditionally activated upon association with a regulatory subunit.
Casimiro, Mathew C.   +2 more
core   +2 more sources

An upstream open reading frame regulates expression of the mitochondrial protein Slm35 and mitophagy flux

open access: yesFEBS Letters, EarlyView.
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva   +5 more
wiley   +1 more source

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