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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    BioEssays 19 (1997), S. 137-145 
    ISSN: 0265-9247
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Focal adhesion kinase (FAK) is a nonreceptor protein-tyrosine kinase implicated in controlling cellular responses to the engagement of cell-surface integrins, including cell spreading and migration, survival and proliferation. Aberrant FAK signaling may contribute to the process of cell transformation by certain oncoproteins, including v-Src. Progress toward elucidating the events leading to FAK activation following integrin-mediated cell adhesion, as well as events downstream of FAK, has come through the identification of FAK phosphorylation sites and interacting proteins. A signaling partnership is formed between FAK and Src-family kinases, leading to tyrosine phosphorylation of FAK and associated ‘docking’ proteins Cas and paxillin. Subsequent recruitment of proteins containing Src homology 2 domains, including Grb2 and c-Crk, to the complex is likely to trigger adhesion-induced cellular responses, including changes to the actin cytoskeleton and activation of the Ras-MAP kinase pathway.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 620 (1994), S. 1947-1952 
    ISSN: 0044-2313
    Keywords: System vanadium pentoxide - niobium pentoxide ; alkoxide hydrolysis ; metastable compounds ; Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Formation and Transformation of Oxide Phases in the Quasibinary System V2O5—Nb2O5In the quasibinary system V2O5—Nb2O5 three phases exist in addition to the boundary phases: VNbO5, V2Nb9O27.5, and VNb9O25. Only the latter phase is a thermodynamically stable one. The metastable phases VNbO5 and V2Nb9O27.5 are formed by thermal decomposition of freeze-dryed products of alkoxide hydrolysis. VNb9O25 can be formed by thermal treatment of a metastable solid solution with TT-Nb2O5 structure or, beside V2O5, by thermal decomposition of the other metastable phases. A reaction scheme of formation and decomposition of phases in the quasi- binary system is given and discussed.
    Notes: Im quasibinären System V2O5—Nb2O5 existieren zusätzlich zu den beiden Randphasen drei weitere Phasen: VNbO5, V2Nb9O27,5 und VNb9O25. Nur die letztere Phase ist thermodynamisch stabil. Die metastabilen Phasen VNbO5 und V2Nb9O27,5 entstehen durch thermische Zersetzung gefriergetrockneter Produkte von Alkoxidhydrolysen. VNb9O25 kann durch thermische Behandlung einer metastabilen festen Lösung mit der Struktur des Nb2O5 oder, neben V2O5, durch thermische Zersetzung der anderen metastabilen Phasen erhalten werden. Ein Reaktionsschema der Phasenbildung und -Zersetzung im quasibinären System wird angegeben und diskutiert.
    Additional Material: 5 Ill.
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  • 3
    ISSN: 0730-2312
    Keywords: protein-tyrosine kinase ; embryogenesis ; extracellular matrix ; fibronectin ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Focal adhesion kinase (FAK) is a structurally unique nonreceptor protein-tyrosine kinase that localizes to focal adhesion plaques. Regulation of its activity has been implicated in diverse signaling pathways, including those mediated by extracellular matrix/integrin interactions, G-protein coupled receptors for mitogenic neuropeptides, and certain oncogene products. To gain evidence for specific processes in which FAK may be involved in vivo, a study was initiated to determine its expression pattern during mouse development. FAK expression was detected in early embryos and appeared to be distributed throughout all cell types at about the time of neurulation. Subsequent to neural tube closure, expression became particularly abundant in the developing vasculature. This included expression in the medial layer of arteries populated by smooth muscle cells. In vitro studies using cultured rat aortic vascular smooth muscle cells demonstrate that FAK phosphotyrosine content is dramatically elevated in response to plating cells onto the adhesive glycoprotein, fibronectin. Also, enhanced tyrosine phosphorylation of FAK is observed in these cells upon stimulation with the vasoconstrictor angiotensin II. Thus, in vascular smooth muscle cells, like fibroblasts, FAK appears to play a role in signaling mechanisms induced by extracellular matrix components as well as G-protein coupled receptor agonists. The combined results of this study suggest that signaling through FAK may play an important role in blood vessel morphogenesis and function. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Chemie Ingenieur Technik - CIT 57 (1985), S. 789-792 
    ISSN: 0009-286X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 5 Ill.
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  • 5
    ISSN: 0009-286X
    Keywords: Mehrkomponenten-Adsorption ; bidisperse Porenstruktur ; Molekularsieb 5Å ; zeolithische Diffusion ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 3 Ill.
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  • 6
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Chemie Ingenieur Technik - CIT 60 (1988), S. 148-149 
    ISSN: 0009-286X
    Keywords: Blähkinetik ; Kohlenpartikeln ; Formalkinetik ; Pyrolyse ; Blasenbilanz ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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