Progress in Biophysics & Molecular Biology 

About: Progress in Biophysics & Molecular Biology is an academic journal published by Elsevier BV. The journal publishes majorly in the area(s): Medicine & Protein structure. It has an ISSN identifier of 0079-6107. Over the lifetime, 2020 publications have been published receiving 127231 citations. The journal is also known as: Progress in Biophysics and Molecular Biology & Progress in biophysics & molecular biology.

Signaling through focal adhesion kinase

Abstract: Integrin receptor binding to extracellular matrix proteins generates intracellular signals via enhanced tyrosine phosphorylation events that are important for cell growth, survival, and migration. This review will focus on the functions of the focal adhesion kinase (FAK) protein-tyrosine kinase (PTK) and its role in linking integrin receptors to intracellular signaling pathways. FAK associates with several diAerent signaling proteins such as Src-family PTKs, p130 Cas , Shc, Grb2, PI 3-kinase, and paxillin. This enables FAK to function within a network of integrin-stimulated signaling pathways leading to the activation of targets such as the ERK and JNK/mitogen-activated protein kinase pathways. Focus will be placed on the structural domains and sites of FAK tyrosine phosphorylation important for FAKmediated signaling events and how these sites are conserved in the FAK-related PTK, Pyk2. We will review what is known about FAK activation by integrin receptor-mediated events and also non-integrin stimuli. In addition, we discuss the emergence of a consensus FAK substrate phosphorylation sequence. Emphasis will also be placed on the role of FAK in generating cell survival signals and the cleavage of FAK during caspase-mediated apoptosis. An in-depth discussion will be presented of integrin-stimulated signaling events occurring in the FAK knockout fibroblasts (FAK ˇ ) and how these cells exhibit deficits

The infrared absorption of amino acid side chains.

Abstract: Amino acid side chains play fundamental roles in stabilising protein structures and in catalysing enzymatic reactions. These fields are increasingly investigated by infrared spectroscopy at the molecular level. To help the interpretation of the spectra, a review of the infrared absorption of amino acid side chains in H(2)O and 2H(2)O is given. The spectral region of 2600-900cm(-1) is covered.