Results 41 to 50 of about 11,155,248 (357)

Pharmacological rescue of impaired mitophagy in Parkinson’s disease-related LRRK2 G2019S knock-in mice

open access: yeseLife, 2021
Parkinson’s disease (PD) is a major and progressive neurodegenerative disorder, yet the biological mechanisms involved in its aetiology are poorly understood.
Francois Singh   +5 more
doaj   +1 more source

Phosphorylation of the ARE-binding protein DAZAP1 by ERK2 induces its dissociation from DAZ

open access: yes, 2006
A protein in RAW 264.7 macrophages, which became phosphorylated in response to LPS (lipopolysaccharide), was identified as the RNA-binding protein called DAZAP1 [DAZ (deleted in azoospermia)-associated protein 1].
Yang, Huei Ting   +14 more
core   +1 more source

Insulin-stimulated phosphorylation of endothelial nitric oxide synthase at serine-615 contributes to nitric oxide synthesis [PDF]

open access: yes, 2009
Insulin stimulates endothelial NO (nitric oxide) synthesis via PKB (protein kinase B)/Akt-mediated phosphorylation and activation of eNOS (endothelial NO synthase) at Ser-1177.
Boyd, Alasdair R.   +19 more
core   +1 more source

The E3 ubiquitin ligase ZNRF2 is a substrate of mTORC1 and regulates its activation by amino acids

open access: yeseLife, 2016
The mechanistic Target of Rapamycin complex 1 (mTORC1) senses intracellular amino acid levels through an intricate machinery, which includes the Rag GTPases, Ragulator and vacuolar ATPase (V-ATPase).
Gerta Hoxhaj   +9 more
doaj   +1 more source

The role of serine/threonine phosphatases in human development: Evidence from congenital disorders

open access: yesFrontiers in Cell and Developmental Biology, 2022
Reversible protein phosphorylation is a fundamental regulation mechanism in eukaryotic cell and organismal physiology, and in human health and disease.
Pieter Vaneynde   +5 more
doaj   +1 more source

A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression

open access: yesCell, 2010
SUMMARY Although most tissues in an organism are genetically identical, the biochemistry of each is optimized to fulfill its unique physiological roles, with important consequences for human health and disease.
Edward L. Huttlin   +9 more
semanticscholar   +1 more source

EGF regulates tyrosine phosphorylation and membrane-translocation of the scaffold protein Tks5 [PDF]

open access: yes, 2013
Background: Tks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells.
Geiszt, Miklós   +5 more
core   +1 more source

A genetically-encoded crosslinker screen identifies SERBP1 as a PKCε substrate influencing translation and cell division

open access: yesNature Communications, 2021
PKCε is known to exert a role in genome protection by directly phosphorylating and switching the specificity of Aurora B. Here the authors identify SERBP1 as a parallel mitotic PKCε substrate controlling translation and ensuring the integrity of ...
Silvia Martini   +11 more
doaj   +1 more source

Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain. [PDF]

open access: yes, 2012
Scaffold proteins have an important role in the regulation of signal propagation. These proteins do not possess any enzymatic activity but can contribute to the formation of multiprotein complexes.
Roopesh Udupa   +16 more
core   +1 more source

USP45 and Spindly are part of the same complex implicated in cell migration

open access: yesScientific Reports, 2018
Ubiquitylation is a protein modification implicated in several cellular processes. This process is reversible by the action of deubiquinating enzymes (DUBs).
Claudia Conte   +3 more
doaj   +1 more source

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