Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1991-10-4
|
| pubmed:abstractText |
The ability to exchange reversibly the regulatory light chains (RLCs) from scallop myosin has provided us with a test system to probe the mechanisms of regulation mediated by the RLCs from vertebrate skeletal, vertebrate smooth and molluscan myosins. The cloning and expression of these RLCs, together with domain-swapping and site-directed mutagenesis approaches, has allowed us to explore further the mechanisms involved and identify the functional importance of specific regions of the RLC molecule; for example, the presence of a high affinity metal binding site in the N-terminal domain and its interaction with the intact C-terminal domains are required for regulation.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0269-3518
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
14
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
55-8
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading | |
| pubmed:year |
1991
|
| pubmed:articleTitle |
Recombinant DNA approaches to study the role of the regulatory light chains (RLC) using scallop myosin as a test system.
|
| pubmed:affiliation |
MRC Laboratory of Molecular Biology, Cambridge, UK.
|
| pubmed:publicationType |
Journal Article,
Review
|