Results 191 to 200 of about 7,148,227 (413)
Mitochondria‐associated membranes (MAMs) are contact sites between the endoplasmic reticulum and mitochondria that regulate calcium signaling, lipid metabolism, autophagy, and stress responses. This review outlines their molecular organization, roles in cellular homeostasis, and how dysfunction drives neurodegeneration, metabolic disease, cancer, and ...
Viet Bui +3 more
wiley +1 more source
Acetylcholine Receptor (AChR) Clustering Is Regulated Both by Glycogen Synthase Kinase 3β (GSK3β)-dependent Phosphorylation and the Level of CLIP-associated Protein 2 (CLASP2) Mediating the Capture of Microtubule Plus-ends [PDF]
Sreya Basu +7 more
openalex +1 more source
CAF‐mediated immunosuppression in ovarian cancer is driven by IDO1, reducing T‐cell function. Inhibiting IDO1 restores T‐cell proliferation and cytotoxicity, increases cancer cell apoptosis, and may help overcome CAF‐induced immune suppression in high‐grade serous ovarian cancer. Targeting IDO1 may improve antitumor immunity.
Hyewon Lee +3 more
wiley +1 more source
Cooperation of Gq, Gi, and G12/13 in Protein Kinase D Activation and Phosphorylation Induced by Lysophosphatidic Acid [PDF]
To examine the contribution of different G-protein pathways to lysophosphatidic acid (LPA)-induced protein kinase D (PKD) activation, we tested the effect of LPA on PKD activity in murine embryonic cell lines deficient in Galpha q/11 (Galpha q/11 KO ...
Gu, Jennifer +3 more
core
Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling
T. Hunter
semanticscholar +1 more source
CDT1 is an essential protein for DNA replication licensing that loads the MCM complex, the eukaryotic replicative DNA helicase, onto replication origins. Overexpression of CDT1 induces cell cycle arrest at the S phase. Here we showed CDT1 inhibits the progression of replication forks by interacting with the MCM complex, leading to the stalling and ...
Takashi Tsuyama +7 more
wiley +1 more source
Phosphorylation-site mutagenesis of the growth-associated protein GAP-43 modulates its effects on cell spreading and morphology. [PDF]
Franco Widmer, Pico Caroni
openalex +1 more source
HSP70 governs permeability and mechanotransduction in primary human endothelial cells
HSP70 chemical inhibition reduces endothelial cell proliferation and increases permeability, the latter supported by normal interendothelial junctional protein distribution. HSP70 also plays a role in shear stress response, a hemodynamic force naturally present in blood vessels and correlated with vessel protection.
Andrea Pinto‐Martinez +5 more
wiley +1 more source

