|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
2-3
|
|
pubmed:dateCreated |
1994-9-26
|
|
pubmed:abstractText |
It is concluded from structure predictions of the primary amino acid sequence by computer analyses that two segments of non-muscle filamin could facilitate lipid membrane attachment or anchoring. Residues 49-71 of the amino-terminal may attach to phospholipid membranes, and residues 131-155 may anchor in the hydrophobic region of lipid membranes.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0014-5793
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
22
|
|
pubmed:volume |
350
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
169-72
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Computer analyses suggest interactions of non-muscle filamin with lipid membranes.
|
|
pubmed:affiliation |
Technical University of Munich, Garching, Germany.
|
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|
