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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1989-4-25
|
pubmed:abstractText |
The protein titin has been localized by electron microscopy of myofibrils labelled with monoclonal antibodies. The data are consistent with individual titin molecules extending from near the M-line to beyond the ends of thick filaments, a distance of approximately 1 micron. In the A-band, titin appears to be bound to thick filaments, probably to the outside of the filament shaft. Molecules of titin in this configuration provided an obvious mechanism by which the length of thick filaments could be regulated accurately.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jan
|
pubmed:issn |
0022-2836
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
205
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
263-8
|
pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading | |
pubmed:year |
1989
|
pubmed:articleTitle |
Does titin regulate the length of muscle thick filaments?
|
pubmed:affiliation |
Muscle Biology Department, A.F.R.C. Institute of Food Research, Langford, Bristol, U.K.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|