Source:http://linkedlifedata.com/resource/pubmed/id/10574799
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1999-12-14
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pubmed:databankReference | |
pubmed:abstractText |
The kinesin superfamily of microtubule-associated motor proteins are important for intracellular transport and for cell division in eukaryotes. Conventional kinesins have the motor domain at the N terminus of the heavy chain and move towards the plus end of microtubules. The ncd protein is necessary for chromosome segregation in meiosis. It belongs to a subfamily of kinesins that have the motor domain at the C terminus and move towards the minus end of microtubules.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0969-2126
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1407-16
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10574799-Adenosine Diphosphate,
pubmed-meshheading:10574799-Amino Acid Sequence,
pubmed-meshheading:10574799-Binding Sites,
pubmed-meshheading:10574799-Catalysis,
pubmed-meshheading:10574799-Crystallography, X-Ray,
pubmed-meshheading:10574799-Dimerization,
pubmed-meshheading:10574799-Drosophila Proteins,
pubmed-meshheading:10574799-Kinesin,
pubmed-meshheading:10574799-Molecular Sequence Data,
pubmed-meshheading:10574799-Protein Conformation
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pubmed:year |
1999
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pubmed:articleTitle |
The crystal structure of the minus-end-directed microtubule motor protein ncd reveals variable dimer conformations.
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pubmed:affiliation |
Institut de Biologie Structurale (CEA/CNRS), Grenoble, 38027, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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