Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1988-8-24
pubmed:databankReference
pubmed:abstractText
Site-specific proteases and antisera to the amino terminus of villin have been used to show that villin is organized into seven protease-resistant domains. Six are contained in the amino-terminal Mr 87,000 villin core, a Ca2+-regulated actin-severing fragment, whereas the carboxyl-terminal domain includes the villin "headpiece," a fragment involved in bundling of actin filaments. Ca2+ inhibits proteolytic cleavage between domains in the amino-terminal half of villin. The protein sequence of villin deduced from a single cDNA clone contains a conserved sequence that is repeated six times and is found in each domain of the villin core. The conserved repeats are found in other actin-severing proteins but not in the villin headpiece. Our results suggest that actin-severing proteins are organized around a common Mr 14,000-17,000 domain.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-2413446, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-2826459, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-2832154, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-2987700, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-2999108, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3017407, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3020431, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3021782, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3028773, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3030380, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3082893, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3087992, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3104800, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3453110, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3474623, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3510866, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3527055, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-3611052, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-518835, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6198242, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6540784, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6546423, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6790532, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6848508, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6893158, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6893424, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-6894120, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-7019912, http://linkedlifedata.com/resource/pubmed/commentcorrection/2839826-7068756
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsin, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Gelsolin, http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin, http://linkedlifedata.com/resource/pubmed/chemical/glutamyl endopeptidase, http://linkedlifedata.com/resource/pubmed/chemical/villin
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4986-90
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:2839826-Amino Acid Sequence, pubmed-meshheading:2839826-Animals, pubmed-meshheading:2839826-Base Sequence, pubmed-meshheading:2839826-Calcium, pubmed-meshheading:2839826-Calcium-Binding Proteins, pubmed-meshheading:2839826-Carrier Proteins, pubmed-meshheading:2839826-Chickens, pubmed-meshheading:2839826-Chymotrypsin, pubmed-meshheading:2839826-DNA, pubmed-meshheading:2839826-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2839826-Gelsolin, pubmed-meshheading:2839826-Immunoassay, pubmed-meshheading:2839826-Microfilament Proteins, pubmed-meshheading:2839826-Molecular Sequence Data, pubmed-meshheading:2839826-Molecular Weight, pubmed-meshheading:2839826-Peptide Fragments, pubmed-meshheading:2839826-Repetitive Sequences, Nucleic Acid, pubmed-meshheading:2839826-Sequence Homology, Nucleic Acid, pubmed-meshheading:2839826-Serine Endopeptidases, pubmed-meshheading:2839826-Trypsin
pubmed:year
1988
pubmed:articleTitle
Villin sequence and peptide map identify six homologous domains.
pubmed:affiliation
Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Cambridge 02142.
pubmed:publicationType
Journal Article, Comparative Study
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