Results 71 to 80 of about 167,856 (315)

Recurrent cancer‐associated ERBB4 mutations are transforming and confer resistance to targeted therapies

open access: yesMolecular Oncology, EarlyView.
We show that the majority of the 18 analyzed recurrent cancer‐associated ERBB4 mutations are transforming. The most potent mutations are activating, co‐operate with other ERBB receptors, and are sensitive to pan‐ERBB inhibitors. Activating ERBB4 mutations also promote therapy resistance in EGFR‐mutant lung cancer.
Veera K. Ojala   +15 more
wiley   +1 more source

Actin dynamics controlled by IqgC, a RasGAP at the crossroads between the IQGAP and fungal GAP1 families

open access: yesFEBS Open Bio, EarlyView.
IqgC is a RasGAP from Dictyostelium discoideum. IqgC binds RasG via its RasGAP domain and deactivates it on macroendocytic cups, thereby suppressing the uptake of fluid and particles. IqgC has a positive effect on cell‐substratum adhesion, and its RGCt domain is required for recruitment to ventral foci.
Vedrana Filić   +3 more
wiley   +1 more source

Short‐term actions of epigalocatechin‐3‐gallate in the liver: a mechanistic insight into hypoglycemic and potential toxic effects

open access: yesFEBS Open Bio, EarlyView.
Epigallocatechin‐3‐gallate (EGCG) acutely inhibited gluconeogenesis and enhanced glycolysis, glycogenolysis, and fatty acid oxidation in perfused rat livers. Mechanistic assays revealed mitochondrial uncoupling, inhibition of pyruvate carboxylation and glucose‐6‐phosphatase, shift of NADH/NAD+ ratios toward oxidation, and loss of membrane integrity ...
Carla Indianara Bonetti   +8 more
wiley   +1 more source

Signaling by insulin receptors and related protein tyrosine kinases

open access: yesBiomedical Reviews, 1996
The insulin receptor is a member of the largely expanding family of plasma membrane receptors. In general, ligand binding induces receptor dimerization leading to activation and tyrosine phosphorylation of the cytoplasmic catalytic domain of the receptor.
D. Margriet Ouwens, J. Antonie Maassen
openaire   +2 more sources

Mitochondria‐associated membranes (MAMs): molecular organization, cellular functions, and their role in health and disease

open access: yesFEBS Open Bio, EarlyView.
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

Molecular determinants of signal transduction in tropomyosin receptor kinases

open access: yesFEBS Open Bio, EarlyView.
Tropomyosin receptor kinases control critical neuronal functions, but how do the same receptors produce diverse cellular responses? This review explores the structural mechanisms behind Trk signaling diversity, focusing on allosteric modulation and ligand bias.
Giray Enkavi
wiley   +1 more source

A distinctive family of embryonic protein-tyrosine kinase receptors. [PDF]

open access: yesProceedings of the National Academy of Sciences, 1990
Two closely related protein-tyrosine kinases with the characteristics of growth factor receptors were identified by screening a chicken embryo cDNA expression library with anti-phosphotyrosine antibodies and were designated Cek2 and Cek3 (chicken embryo kinases 2 and 3).
openaire   +2 more sources

Multi‐Omics Integration for Advancing Glioma Precision Medicine

open access: yesAnnals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Gliomas are among the most malignant and aggressive tumors of the central nervous system, characterized by the absence of early diagnostic markers, poor prognosis, and a lack of effective treatments. Advances in high‐throughput technologies have facilitated a refined molecular classification of gliomas, incorporating genetic features. However,
Maria Guarnaccia   +4 more
wiley   +1 more source

Protein tyrosine kinases couple the interleukin‐2 receptor to p21ras

open access: yesEuropean Journal of Immunology, 1993
AbstractThe T cell growth factor interleukin‐2 (IL‐2) induces p21ras activation in T lymphocytes. We have previously shown that a protein kinase C (PKC)‐mediated pathway for p21ras regulation exists in T cells and that the IL‐2 receptor (IL‐2R) can couple to p21ras independently of the presence of the PKC pathway for p21ras regulation.
Izquierdo, Manuel, Cantrell, Doreen A.
openaire   +4 more sources

Home - About - Disclaimer - Privacy