Actin-Binding Proteins and Disease by Cris dos Remedios, Deepak Chhabra

By Cris dos Remedios, Deepak Chhabra

This quantity, written by way of specialists within the box, is the 1st to accommodate the connection among human disorder and the actin cytoskeleton. It presents overviews of actin and chosen actin-binding proteins, after which specializes in illnesses that contain those proteins. particular chapters take care of actin, cofilin, profilin, gelsolin and thymosin ¾4. different chapters talk about the jobs of a number of actin-binding proteins in melanoma and metastasis, leukocyte issues, and middle failure, and there's a bankruptcy that describes how intracellular pathogens use the host actin cytoskeleton. This seminal quantity is meant for researchers, clinicians, physicians, and graduate scholars within the fields of biochemistry, mobile biology, microbiology, immunology, and genetics.

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Biol. 232, 334–341. Otterbein, L. , Graceffa, P. and Dominguez, R. 2001. The crystal structure of uncomplexed actin in the ADP state. Science 293, 708–711. , Holden, H. , Whittaker, C. , Holmes, K. C. and Milligan, R. A. 1993. Structure of the actin–myosin complex and its implications for muscle contraction. Science 262, 58–65. , Molloy. J. , Geeves, M. A. and Sparrow, J. C. 1999. Actin residue E93 is identified as an amino acid affecting myosin binding. J. Biol. Chem. 274, 28321–28328. Reedy, M.

G. and Gomez, M. R. 1967. Nemaline (Z disk) myopathy: Observations on the origin, structure, and solubility properties of the nemaline structures. J. Neuropathol. Exp. Neurol. 2, 601–619. Erba, H. , Kedes, L. and Gunning, P. 1988. Structure, chromosome location and expression of the human gamma-actin gene: Differential evolution, location and expression of the cytoskeletal beta- and gamma-actin genes. Mol. Cell. Biol. 8, 1775–1789. , Richardson, J. A. and Olson, E. N. 2000. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins.

The histochemical differentiation of the two fiber types, usually on the basis of staining for ATPase activity, reflects the different myosin isoforms present in each fiber type. In the monomeric actin atomic structure (Kabsch et al. 1990; Otterbein, Graceffa and Dominguez 2001) the amino acid residues affected by the three mutations (Leu221Pro, Asp292Val and Pro332Ser) form part of the monomeric actin surface and will remain exposed in the F-actin polymer. By fitting the atomic structures of both actin and the myosin S1 fragment into EM reconstructions of rigorstate S1-decorated F-actin (Rayment et al.

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