Linked Life Data

2308147

Source:http://linkedlifedata.com/resource/pubmed/id/2308147

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-4-6
pubmed:abstractText
The pentapeptide Ser-Asn-Val-Phe-Ala-OBzl has been identified as the smallest inhibitory peptide of myosin light chain kinase (MLCK) derived from the primary sequence of the light chain phosphorylation site. The specific contributions of individual amino acid side chains and backbone elements of this pentapeptide toward the stabilization of the enzyme-inhibitor (E-I) complex have been evaluated. The potency of these peptides as inhibitors of MLCK has been enhanced by the incorporation of synthetic nonnatural amino acids into the sequence. Finally, it has been demonstrated that these peptide sequences could be converted into pseudopeptides with synthetic nonpeptide subunits designed to mimic peptide bonds, and that certain pseudopeptides retained the high-affinity inhibition of the parent pentapeptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
964-72
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Small peptide inhibitors of smooth muscle myosin light chain kinase.
pubmed:affiliation
Department of Chemical Research, Schering-Plough Research, Bloomfield, New Jersey 07003.
pubmed:publicationType
Journal Article