|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
2008-1-7
|
|
pubmed:abstractText |
Formin proteins nucleate actin filaments de novo and stay associated with the growing barbed end. Whereas the formin-homology (FH) 2 domains mediate processive association, the FH1 domains-in concert with the actin-monomer-binding protein profilin-increase the rate of barbed-end elongation. The mechanism by which this effect is achieved is not well understood.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0960-9822
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
8
|
|
pubmed:volume |
18
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
9-19
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:18160294-Actin Cytoskeleton,
pubmed-meshheading:18160294-Amino Acid Sequence,
pubmed-meshheading:18160294-Microfilament Proteins,
pubmed-meshheading:18160294-Models, Biological,
pubmed-meshheading:18160294-Molecular Sequence Data,
pubmed-meshheading:18160294-Peptides,
pubmed-meshheading:18160294-Profilins,
pubmed-meshheading:18160294-Protein Structure, Tertiary,
pubmed-meshheading:18160294-Saccharomyces cerevisiae,
pubmed-meshheading:18160294-Saccharomyces cerevisiae Proteins
|
|
pubmed:year |
2008
|
|
pubmed:articleTitle |
The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation.
|
|
pubmed:affiliation |
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8103, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
|
