Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1994-8-1
pubmed:databankReference
pubmed:abstractText
We have determined the primary structure of a myosin I (called mammalian myosin I beta, MMI beta) from bovine brain and identified its functional domains. The protein was previously purified from brain and adrenal gland. Several constructs were generated and expressed in Escherichia coli as glutathione S-transferase fusion proteins and the recombinant proteins were recognized by monoclonal antibodies that recognize either "head" or "tail" domains of native myosin I. A gel overlay method was used to confirm that calmodulin binds to the consensus calmodulin-binding sequence in MMI beta. Binding assays were used to detect interaction with anionic phospholipid vesicles. We conclude that MMI beta consists of an amino-terminal 80.5-kDa domain that contains the ATP- and actin-binding sites, followed by an 8.5-kDa domain with three calmodulin-binding sequences and a basic 30-kDa carboxyl-terminal tail segment that binds to anionic phospholipids and membranes.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1447297, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1469047, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1527166, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1530945, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1530990, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1558751, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1607386, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-181375, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1824693, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1824700, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-1996138, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2042976, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2139032, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2143194, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2183843, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2229179, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2365078, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2406017, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2448875, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2449973, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-2645293, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-3047011, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-3318880, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-518835, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-6316075, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-6546423, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-6849869, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8398149, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8413662, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8413668, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8448033, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8449985, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8449986, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-8467525, http://linkedlifedata.com/resource/pubmed/commentcorrection/8022785-942051
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6349-53
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:8022785-Animals, pubmed-meshheading:8022785-Cattle, pubmed-meshheading:8022785-Rats, pubmed-meshheading:8022785-Brain Chemistry, pubmed-meshheading:8022785-Myosins, pubmed-meshheading:8022785-Mammals, pubmed-meshheading:8022785-Actins, pubmed-meshheading:8022785-Adenosine Triphosphate, pubmed-meshheading:8022785-Escherichia coli, pubmed-meshheading:8022785-Base Sequence, pubmed-meshheading:8022785-Chickens, pubmed-meshheading:8022785-Amino Acid Sequence, pubmed-meshheading:8022785-Binding Sites, pubmed-meshheading:8022785-Molecular Sequence Data, pubmed-meshheading:8022785-Cloning, Molecular, pubmed-meshheading:8022785-Sequence Homology, Amino Acid, pubmed-meshheading:8022785-Glutathione Transferase, pubmed-meshheading:8022785-Calmodulin, pubmed-meshheading:8022785-Recombinant Proteins, pubmed-meshheading:8022785-Recombinant Fusion Proteins, pubmed-meshheading:8022785-DNA Primers, pubmed-meshheading:8022785-Consensus Sequence
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