نتایج جستجو برای: fak

تعداد نتایج: 3501  

Journal: :The Journal of biological chemistry 2003
Haiping Mao Fanghong Li Kathleen Ruchalski Dick D Mosser John H Schwartz Yihan Wang Steven C Borkan

Prior heat stress (HS) or the selective overexpression of hsp72 prevents apoptosis caused by exposure to metabolic inhibitors by protecting the mitochondrial membrane and partially reducing caspase-3 activation. Focal adhesion kinase (FAK), a tyrosine kinase, exhibits anti-apoptotic properties and is a potential target for degradation by caspase-3. This study tested the hypothesis that hsp72 in...

2013
Kirat Kumar Ganguly Triparna Sen Syamsundar Mandal Jaydip Biswas Amitava Chatterjee

Aim: To study Expression and Phosphorylation status of Focal Adhesion Kinase (FAK) in Human Breast Cancer tissue. To study the relation of FAK with standard clinicopathological parameters of Human Breast Cancer. Methods: Tissue collection, Protein extraction, RNA isolation, Western Blot, Immunohistochemistry, RT-PCR, ELISA, Statistical analysis. Results: All the four techniques showed upregulat...

Journal: :Hypertension 2003
Xian Ping Yi Xuejun Wang A Martin Gerdes Faqian Li

Focal adhesion kinase (FAK) and focal adhesion kinase-related nonkinase (FRNK) are likely involved in mechanical signaling during hypertension. We investigated expression, subcellular distribution, and phosphorylation of FAK, as well as FRNK in left ventricles of spontaneously hypertensive heart failure rats. Compared with normotensive controls, FAK and FRNK increased in left ventricles of hype...

Journal: :The Journal of Cell Biology 1997
Tsung H. Lin Andrew E. Aplin Yu Shen Qiming Chen Michael Schaller Lewis Romer Ikramuddin Aukhil R.L. Juliano

Integrin-mediated cell adhesion causes activation of MAP kinases and increased tyrosine phosphorylation of focal adhesion kinase (FAK). Autophosphorylation of FAK leads to the binding of SH2-domain proteins including Src-family kinases and the Grb2-Sos complex. Since Grb2-Sos is a key regulator of the Ras signal transduction pathway, one plausible hypothesis has been that integrin-mediated tyro...

Journal: :Cancer research 2009
Joerg Schwock Neesha Dhani Mary Ping-Jiang Cao Jinzi Zheng Richard Clarkson Nikolina Radulovich Roya Navab Lars-Christian Horn David W Hedley

Focal adhesion kinase (FAK), a nonreceptor protein tyrosine kinase and key modulator of integrin signaling, is widely expressed in different tissues and cell types. Recent evidence indicates a central function of FAK in neoplasia where the kinase contributes to cell proliferation, resistance to apoptosis and anoikis, invasiveness, and metastasis. FAK, like other signaling kinases, is dependent ...

Journal: :Molecular cancer therapeutics 2014
Isabelle Tancioni Sean Uryu Florian J Sulzmaier Nina R Shah Christine Lawson Nichol L G Miller Christine Jean Xiao Lei Chen Kristy K Ward David D Schlaepfer

Ovarian cancer ascites fluid contains matrix proteins that can impact tumor growth via integrin receptor binding. In human ovarian tumor tissue arrays, we find that activation of the cytoplasmic focal adhesion (FAK) tyrosine kinase parallels increased tumor stage, β5 integrin, and osteopontin matrix staining. Elevated osteopontin, β5 integrin, and FAK mRNA levels are associated with decreased s...

Journal: :Journal of Molecular Signaling 2008
Danielle M Scheswohl Jessica R Harrell Zenon Rajfur Guanghua Gao Sharon L Campbell Michael D Schaller

BACKGROUND FAK localization to focal adhesions is essential for its activation and function. Localization of FAK is mediated through the C-terminal focal adhesion targeting (FAT) domain. Recent structural analyses have revealed two paxillin-binding sites in the FAT domain of FAK. To define the role of paxillin binding to each site on FAK, point mutations have been engineered to specifically dis...

2002
Timothy P. Hecker J. Robert Grammer G. Yancey Gillespie Jerry Stewart Candece L. Gladson

Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase that on activation generates signals that can modulate crucial cell functions, including cell proliferation, migration, and survival. In vitro, overexpression of FAK has been shown to promote cell proliferation by signaling through the Ras/mitogen-activated protein kinase cascade in several cell types. We have shown previously that ov...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2014
Guillermina M Goñi Carolina Epifano Jasminka Boskovic Marta Camacho-Artacho Jing Zhou Agnieszka Bronowska M Teresa Martín Michael J Eck Leonor Kremer Frauke Gräter Francesco Luigi Gervasio Mirna Perez-Moreno Daniel Lietha

Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase (NRTK) with key roles in integrating growth and cell matrix adhesion signals, and FAK is a major driver of invasion and metastasis in cancer. Cell adhesion via integrin receptors is well known to trigger FAK signaling, and many of the players involved are known; however, mechanistically, FAK activation is not understood. Here, using a...

Journal: :The EMBO journal 2009
Shi-Wen Luo Chun Zhang Bin Zhang Chang-Hoon Kim Yuan-Zheng Qiu Quan-Sheng Du Lin Mei Wen-Cheng Xiong

Focal adhesion kinase (FAK), a major cell adhesion-activated tyrosine kinase, has an important function in cell adhesion and migration. Here, we report a new signalling of FAK in regulating chromatin remodelling by its interaction with MBD2 (methyl CpG-binding protein 2), underlying FAK regulation of myogenin expression and muscle differentiation. FAK interacts with MBD2 in vitro, in myotubes, ...

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