By Cris dos Remedios, Deepak Chhabra
This quantity, written by means of specialists within the box, is the 1st to accommodate the connection among human sickness and the actin cytoskeleton. It offers overviews of actin and chosen actin-binding proteins, after which makes a speciality of illnesses that contain those proteins. particular chapters take care of actin, cofilin, profilin, gelsolin and thymosin ¾4. different chapters speak about the jobs of a number of actin-binding proteins in melanoma and metastasis, leukocyte problems, 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, phone biology, microbiology, immunology, and genetics.
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Extra info for Actin-Binding Proteins and Disease
Wilton, S. , WallgrenPettersson, C. and Laing, N. G. 1999. Homozygosity for a nonsense mutation in the alpha-tropomyosin gene TPM3 in a patient with severe infantile nemaline myopathy. Neuromuscul. Disord. 9, 573–579. , Mishima, M. and Nishida, E. 1998. Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J. 17, 1635–1641. , Newman, G. , Morris, G. , Holmberg, C. and Rapola, J. 1995. α-actinin in nemaline rods in congenital nemaline myopathy: Immunological confirmation by light and electron microscopy.
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. , Beall, C.
ACTA1 mutations that lead to intranuclear rods in patients, in transfected C2C12 myoblast cells (Ilkovski et al. 2005; Domazetovska et al. submitted) or in transfected NIH 3T3 fibroblasts (Costa et al. , V163M are close (Hutchinson et al. 2006). Why specific ACTA1 mutations cause the mutant actins to accumulate in the nucleus is far from clear, nor is there any evidence that α-skeletal actin, rather than the cytoplasmic actins, normally traffic through the nucleus. Congenital Fiber-Type Disproportion (CFTD) Congenital fiber-type disproportion (CFTD) is a rare genetic disease that causes generalized skeletal muscle weakness in which a subset of muscle fibers is significantly reduced in size (Brooke 1973).
Actin-Binding Proteins and Disease by Cris dos Remedios, Deepak Chhabra