ArticleProceedings of the National Academy of Sciences of the United States of America1985
Mapping the cysteine residues and actin-binding regions of villin by using antisera to the amino and carboxyl termini of the molecule.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Protein footprinting at cysteines: probing ATP-modulated contacts in cysteine-substitution mutants of yeast DNA topoisomerase II.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- A method for probing the topography and interactions of proteins: footprinting of myoglobin.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ.The Journal of cell biology · 1991Article
- Proteolysis patterns of epitopically labeled yeast DNA topoisomerase II suggest an allosteric transition in the enzyme induced by ATP binding.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins.The Journal of cell biology · 1990Article
- Interactions of synapsin I with small synaptic vesicles: distinct sites in synapsin I bind to vesicle phospholipids and vesicle proteins.The Journal of cell biology · 1989Article
- Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers.The Journal of cell biology · 1989Article
- Characterization of synapsin I fragments produced by cysteine-specific cleavage: a study of their interactions with F-actin.The Journal of cell biology · 1989Article
- Villin sequence and peptide map identify six homologous domains.Proceedings of the National Academy of Sciences of the United States of America · 1988Article
- Tropomyosin distinguishes between the two actin-binding sites of villin and affects actin-binding properties of other brush border proteins.The Journal of cell biology · 1987Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Peptide antisera specific for either the amino- or carboxyl-terminal regions of villin were used to locate the position of cysteine residues in immunoblots of villin cleaved with 2-nitro-5-thiocyanobenzoic acid. Maps constructed from the cleavage pattern suggest that villin contains six cysteine residues, two located in its amino-terminal peptide of Mr 44,000, and four located in the carboxyl-terminal peptide of Mr 51,000. Gel overlays of the partial cleavage fragments with 125I-labeled actin identified a calcium-dependent actin-binding region located within the amino-terminal peptide of Mr 32,000 of villin. The peptide antibody method used, called cleavage mapping, should be a convenient technique for mapping residues and ligand binding sites in proteins.
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