ArticleThe Biochemical journal1987
Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin.
Article in The Biochemical journal, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Interaction of skeletal-muscle myosin subfragment-1 with the actin-(338-348) peptide.The Biochemical journal · 1994Article
- Localization of a myosin subfragment-1 interaction site on the C-terminal part of actin.The Biochemical journal · 1992Article
- The interaction of caldesmon with the COOH terminus of actin.The Journal of biological chemistry · 1991Article
- Definition of a Ca2(+)-sensitive interface in the plasma gelsolin-actin complex.The Biochemical journal · 1991Article
- Characterization of an actin-myosin head interface in the 40-113 region of actin using specific antibodies as probes.The Biochemical journal · 1990Article
- Antigenic probes locate binding sites for the glycolytic enzymes glyceraldehyde-3-phosphate dehydrogenase, aldolase and phosphofructokinase on the actin monomer in microfilaments.The Biochemical journal · 1989Article
- Acanthamoeba actin and profilin can be cross-linked between glutamic acid 364 of actin and lysine 115 of profilin.The Journal of cell biology · 1989Article
- Comparative study of invertebrate actins: antigenic cross-reactivity versus sequence variability.Journal of muscle research and cell motility · 1989Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The implication of part of the C-terminal of actin (within the 285-375 sequence) in the interaction of serum gelsolin was investigated by the use of specific antibodies. These antibodies were directed against two or three discrete epitopes, one of which was specific for skeletal-muscle actin. Some of these epitopes were found to be near the serum gelsolin-actin interface. Thus it can be assumed that part of the C-terminal of actin is exposed at the barbed end of the actin filament. The interaction between tropomyosin and actin was also studied.
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Registered trials
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