Results 31 to 40 of about 84,022 (261)

Focal adhesion kinase: from biological functions to therapeutic strategies

open access: yesExperimental Hematology & Oncology, 2023
Focal adhesion kinase (FAK), a nonreceptor cytoplasmic tyrosine kinase, is a vital participant in primary cellular functions, such as proliferation, survival, migration, and invasion. In addition, FAK regulates cancer stem cell activities and contributes
Ximin Tan   +5 more
doaj   +1 more source

Novel Phosphotidylinositol 4,5-Bisphosphate Binding Sites on Focal Adhesion Kinase. [PDF]

open access: yesPLoS ONE, 2015
Focal adhesion kinase (FAK) is a protein tyrosine kinase that is ubiquitously expressed, recruited to focal adhesions, and engages in a variety of cellular signaling pathways.
Jun Feng, Blake Mertz
doaj   +1 more source

CaMKK2 Regulates Mechanosensitive Assembly of Contractile Actin Stress Fibers

open access: yesCell Reports, 2018
Summary: Stress fibers are contractile actomyosin bundles that guide cell adhesion, migration, and morphogenesis. Their assembly and alignment are under precise mechanosensitive control.
Sari Tojkander   +2 more
doaj   +1 more source

Requirement for focal adhesion kinase in tumor cell adhesion [PDF]

open access: yesOncogene, 1999
Focal adhesion kinase (FAK) is a nonreceptor protein tyrosine kinase and a major phosphotyrosine-containing protein. FAK is found in cell-matrix attachment sites (focal adhesions), and is activated on integrin-ligand binding and by other signaling pathways. Several roles have been proposed for FAK; here we report a novel function.
K, Maung   +3 more
openaire   +2 more sources

Differential Signaling by the Focal Adhesion Kinase and Cell Adhesion Kinase β [PDF]

open access: yesJournal of Biological Chemistry, 1997
pp125(FAK) and CAKbeta/Pyk2/CadTK/RAFTK are related protein-tyrosine kinases. It is therefore of interest whether CAKbeta shares some of the properties of pp125(FAK). Using recombinant glutathione S-transferase fusion proteins, we show that the C-terminal domains of both proteins bind paxillin in vitro.
M D, Schaller, T, Sasaki
openaire   +2 more sources

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Abnormal Endothelial Gene Expression Associated With Early Coronary Atherosclerosis

open access: yesJournal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2020
Background We examined feasibility of a unique approach towards gaining insight into heritable risk for early atherosclerosis: surveying gene expression by endothelial cells from living subjects. Methods and Results Subjects aged
Robert P. Hebbel   +9 more
doaj   +1 more source

AMBRA1 and FAK1: crosstalking for improved targeted therapy in melanoma

open access: yesMolecular & Cellular Oncology, 2021
Through genetically engineered mouse models of melanoma, we identified Autophagy/beclin 1 regulator 1 (Ambra1) as novel tumor-suppressor in melanoma. In these settings, loss of Ambra1 associated with the hyperactivation of focal adhesion kinase 1 (Fak1 ...
Luca Di Leo, Daniela De Zio
doaj   +1 more source

Focal Adhesion Kinase: The Reversible Molecular Mechanosensor [PDF]

open access: yesBiophysical Journal, 2017
Sensors are the first element of the pathways that control the response of cells to their environment. Protein complexes that produce or enable a chemical signal in response to a mechanical stimulus are called “mechanosensors”. In this work, we develop a theoretical model describing the physical mechanism of a reversible single-molecule stiffness ...
Bell, S, Terentjev, EM
openaire   +4 more sources

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

Home - About - Disclaimer - Privacy