Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1992-6-25
pubmed:abstractText
We have developed a procedure to isolate the microtubule-associated protein 2c (MAP2c), a juvenile form of MAP2 occurring in mammalian brain. The shape, size, self-association, and antibody interactions of MAP2c were studied. Monomeric MAP2c is an elongated molecule with a length approximately 48 nm, considerably shorter than the higher molecular weight forms MAP2a or b of adult brain. Two monoclonal antibodies whose epitopes are near the N or C terminus, respectively, are located close to the opposite ends of the MAP2c rods. This places constraints on the types of internal folding of the molecule. MAP2c self-associates into dimers and fibrous aggregates. The dimers are predominantly antiparallel and nearly in register, as judged by antibody labeling.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10737-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
The juvenile microtubule-associated protein MAP2c is a rod-like molecule that forms antiparallel dimers.
pubmed:affiliation
Max-Planck-Unit for Structural Molecular Biology, Deutsches Elektronen Synchrotron, Hamburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't