Results 51 to 60 of about 83,211 (264)

Lamins and nesprin-1 mediate inside-out mechanical coupling in muscle cell precursors through FHOD1

open access: yesScientific Reports, 2017
LINC complexes are crucial for the response of muscle cell precursors to the rigidity of their environment, but the mechanisms explaining this behaviour are not known. Here we show that pathogenic mutations in LMNA or SYNE-1 responsible for severe muscle
Christine Schwartz   +12 more
doaj   +1 more source

N-terminal and C-terminal heparin-binding domain polypeptides derived from fibronectin reduce adhesion and invasion of liver cancer cells

open access: yesBMC Cancer, 2010
Background Fibronectin (FN) is known to be a large multifunction glycoprotein with binding sites for many substances, including N-terminal and C-terminal heparin-binding domains.
Wu Yong   +6 more
doaj   +1 more source

Enterophilin-1 Interacts with Focal Adhesion Kinase and Decreases β1 Integrins in Intestinal Caco-2 Cells [PDF]

open access: yesJournal of Biological Chemistry, 2004
Intestinal cell growth and differentiation are tightly regulated by growth factors and extracellular matrix components along the crypt-villus axis. We previously described enterophilin-1 (Ent-1) as a new intestinal protein associated with growth arrest and enterocyte differentiation.
Véronique, Pons   +9 more
openaire   +2 more sources

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

open access: yesFEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

FAK regulates IL-33 expression by controlling chromatin accessibility at c-Jun motifs

open access: yesScientific Reports, 2021
Focal adhesion kinase (FAK) localizes to focal adhesions and is overexpressed in many cancers. FAK can also translocate to the nucleus, where it binds to, and regulates, several transcription factors, including MBD2, p53 and IL-33, to control gene ...
Billie G. C. Griffith   +7 more
doaj   +1 more source

Angiopoietin-1 Induces Endothelial Cell Sprouting Through the Activation of Focal Adhesion Kinase and Plasmin Secretion [PDF]

open access: yesCirculation Research, 2000
Abstract —Angiopoietin-1 (Ang1) is a strong inducer of endothelial cell sprouting, which is a first step in both angiogenesis and neovascularization. We examined the mechanisms underlying Ang1-induced cell sprouting using porcine pulmonary artery endothelial cells.
Kim I Kim, Injune   +7 more
openaire   +2 more sources

ADP ribosylation factor guanylate kinase 1 promotes the malignant phenotype of gastric cancer by regulating focal adhesion kinase activation

open access: yesLife Sciences, 2021
ADP ribosylation factor guanylate kinase 1 (ASAP1), a phospholipid-dependent guanosine triphosphate (GTP)ase activating protein, has been reported to be involved in the development of various malignant tumors. However, the biological function of ASAP1 in gastric cancer (GC) remains unclear.
Sunyun, Zhang   +6 more
openaire   +2 more sources

Modelling stem cell differentiation related processes—A practical overview for biologists

open access: yesFEBS Letters, EarlyView.
Stem cell differentiation is complex and difficult to control experimentally. This review introduces suitable computational modelling approaches that can support stem cell research, from mechanistic ODE and abstract models to multiscale and deep learning methods.
Ricco Zeegelaar   +4 more
wiley   +1 more source

Insulin and insulin-like growth factor-1 stimulate dephosphorylation of paxillin in parallel with focal adhesion kinase [PDF]

open access: yesBiochemical Journal, 1996
Paxillin and focal adhesion kinase (pp125FAK) co-localize in focal adhesions; recently insulin has been shown to stimulate the dephosphorylation of pp125FAK; however, its effect on paxillin is unknown. We show that insulin and IGF-1 can stimulate the dephosphorylation of paxillin in CHOT (overexpress human insulin receptors) and CHO∆CT69 (overexpress ...
N, Konstantopoulos, S, Clark
openaire   +2 more sources

ABL kinase‐dependent phosphorylation of SH proteins promotes their direct interaction with CRK family SH2 domains

open access: yesFEBS Letters, EarlyView.
CT10 regulator of kinase (CRK) and CRK‐Like (CRKL) are signaling adaptors driving cell adhesion, motility, differentiation, and proliferation. SH2‐domain containing (SH) proteins are enriched in YXXP motifs which when phosphorylated create preferred binding sites for CRK family SH2 domains.
Phoebe M. Cousens   +8 more
wiley   +1 more source

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