|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0000879,
umls-concept:C0010851,
umls-concept:C0027103,
umls-concept:C0039259,
umls-concept:C0205117,
umls-concept:C0444930,
umls-concept:C0851285,
umls-concept:C1514562,
umls-concept:C1706853,
umls-concept:C1879748,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2267219
|
|
pubmed:issue |
2
|
|
pubmed:dateCreated |
1988-8-18
|
|
pubmed:abstractText |
Polyclonal antibodies raised against a synthetic peptide consisting of the last 19 amino acids at the end of the coiled-coil region of the heavy chains inhibited the actin-activated Mg2+-ATPase activity of myosin II and its ability to form filaments. Antibodies against a synthetic peptide corresponding to the 21 adjacent amino acids at the beginning of the non-helical tailpiece, which include the three regulatory phosphorylatable serines, had no effect on either activity.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
18
|
|
pubmed:volume |
234
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
435-8
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1988
|
|
pubmed:articleTitle |
Enzymatic activity and filament assembly of Acanthamoeba myosin II are regulated by adjacent domains at the end of the tail.
|
|
pubmed:affiliation |
Laboratory of Cell Biology, National Heart, Lung and Blood Institute, Bethesda, MD 20892.
|
|
pubmed:publicationType |
Journal Article
|
