Results 21 to 30 of about 25,087 (234)

Non-overlapping functions for Pyk2 and FAK in osteoblasts during fluid shear stress-induced mechanotransduction. [PDF]

open access: yesPLoS ONE, 2011
Mechanotransduction, the process by which cells convert external mechanical stimuli such as fluid shear stress (FSS) into biochemical changes, plays a critical role in maintenance of the skeleton.
Suzanne R L Young   +4 more
doaj   +1 more source

Protein tyrosine kinase 2 beta (PTK2B), but not focal adhesion kinase (FAK), is expressed in a sexually dimorphic pattern in developing mouse gonads [PDF]

open access: yesDevelopmental Dynamics, 2010
AbstractSexual reproduction is essential for the propagation and the maintenance of fitness of our species, and is dependent on the correct development of the bipotential genital ridges into testes and ovaries. Although several transcription factors, secreted signaling molecules, and their receptors have been found to be important for testis ...
Beverdam, Annemiek   +6 more
openaire   +5 more sources

Recruitment of focal adhesion kinase and paxillin to β1 integrin promotes cancer cell migration via mitogen activated protein kinase activation

open access: yesBMC Cancer, 2004
Background Integrin-extracellular matrix interactions activate signaling cascades such as mitogen activated protein kinases (MAPK). Integrin binding to extracellular matrix increases tyrosine phosphorylation of focal adhesion kinase (FAK).
Ohannessian Arthur, Crowe David L
doaj   +1 more source

The Non-receptor Tyrosine Kinase Pyk2 in Brain Function and Neurological and Psychiatric Diseases

open access: yesFrontiers in Synaptic Neuroscience, 2021
Pyk2 is a non-receptor tyrosine kinase highly enriched in forebrain neurons. Pyk2 is closely related to focal adhesion kinase (FAK), which plays an important role in sensing cell contacts with extracellular matrix and other extracellular signals ...
Benoit de Pins   +12 more
doaj   +1 more source

Oxidative stress‐induced FAK activation contributes to uterine serous carcinoma aggressiveness

open access: yesMolecular Oncology, 2023
Uterine serous carcinoma (USC) is an aggressive form of endometrial cancer (EC), characterized by its high propensity for metastases. In fact, while endometrioid endometrial carcinoma (EEC), which accounts for 85% of EC, presents a good prognosis, USC is
Isabel C. Lopez‐Mejia   +19 more
doaj   +1 more source

Phosphorylation of p130Cas initiates Rac activation and membrane ruffling

open access: yesBMC Cell Biology, 2008
Background Non-receptor tyrosine kinases (NTKs) regulate physiological processes such as cell migration, differentiation, proliferation, and survival by interacting with and phosphorylating a large number of substrates simultaneously.
Sharma Alok, Mayer Bruce J
doaj   +1 more source

SHP-2 Mediates Cryptosporidium parvum Infectivity in Human Intestinal Epithelial Cells. [PDF]

open access: yesPLoS ONE, 2015
The parasite, Cryptosporidium parvum, induces human gastroenteritis through infection of host epithelial cells in the small intestine. During the initial stage of infection, C.
Eunice A Varughese   +3 more
doaj   +1 more source

A p130Cas tyrosine phosphorylated substrate domain decoy disrupts v-Crk signaling

open access: yesBMC Cell Biology, 2002
Background The adaptor protein p130Cas (Cas) has been shown to be involved in different cellular processes including cell adhesion, migration and transformation.
Hanafusa Hidesaburo   +3 more
doaj   +1 more source

Mertk deficiency affects macrophage directional migration via disruption of cytoskeletal organization. [PDF]

open access: yesPLoS ONE, 2015
Mertk belongs to the Tyro3, Axl and Mertk (TAM) family of receptor tyrosine kinases, and plays a pivotal role in regulation of cytoskeletal rearrangement during phagocytosis.
Yong Tang   +7 more
doaj   +1 more source

Receptor Protein-tyrosine Phosphatase α Regulates Focal Adhesion Kinase Phosphorylation and ErbB2 Oncoprotein-mediated Mammary Epithelial Cell Motility [PDF]

open access: yesJournal of Biological Chemistry, 2013
We investigated the role of protein-tyrosine phosphatase α (PTPα) in regulating signaling by the ErbB2 oncoprotein in mammary epithelial cells. Using this model, we demonstrated that activation of ErbB2 led to the transient inactivation of PTPα, suggesting that attenuation of PTPα activity may contribute to enhanced ErbB2 signaling.
Boivin, Benoit   +6 more
openaire   +4 more sources

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