Cambp 190 is an actin bundling protein based on low speed actin sedimentation assay (1990)
- Authors:
- Autor USP: LARSON, ROY EDWARD - FMRP
- Unidade: FMRP
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Program and Abstracts
- Conference titles: Paabs Congress
-
ABNT
ESPINDOLA, F S e LARSON, R E. Cambp 190 is an actin bundling protein based on low speed actin sedimentation assay. 1990, Anais.. São Paulo: Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, 1990. . Acesso em: 12 out. 2024. -
APA
Espindola, F. S., & Larson, R. E. (1990). Cambp 190 is an actin bundling protein based on low speed actin sedimentation assay. In Program and Abstracts. São Paulo: Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo. -
NLM
Espindola FS, Larson RE. Cambp 190 is an actin bundling protein based on low speed actin sedimentation assay. Program and Abstracts. 1990 ;[citado 2024 out. 12 ] -
Vancouver
Espindola FS, Larson RE. Cambp 190 is an actin bundling protein based on low speed actin sedimentation assay. Program and Abstracts. 1990 ;[citado 2024 out. 12 ] - Ca2+ / cam dependent protein phosphorylation in saccharomyces cals bengensis - identification of cam binding proteins
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- Calcium dependent interaction of brain cytosol protein kinase with a calmodulin affinity column
- Tissue localization of cam-bp190 by immunodetection on western blots
- Purification of camp-bp190 from avian brain , immunological evidence for shared epitope with nyosin atp- brinding domain
- Characterization of atpase activities associated with a novel calmodulikin - binding protein from rabbit brain
- Chicken brain p190: a member of a new class of unconventional myosin that includes to mouse homolog, iolute , and the niyo2 gene product
- 'CA POT.2+' - dependent phosphorylation of the tail domain of myosin - v a calmadolin - binding myosin in vertebrate brian
- Calcium regulates the binding affinity of brain myosin-v for f-actin
- Calcium-induced quenching of intrinsic fluorescence in brain myosin V is linked to dissociation of calmodulin light chains
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