pubmed-article:9490638 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C0061928 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C1419277 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C1412517 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C1423613 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C1705994 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C1513492 | lld:lifeskim |
pubmed-article:9490638 | lifeskim:mentions | umls-concept:C1720675 | lld:lifeskim |
pubmed-article:9490638 | pubmed:dateCreated | 1998-8-6 | lld:pubmed |
pubmed-article:9490638 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9490638 | pubmed:abstractText | The heavy chains of the class IX myosins, rat myr5 and human myosin-IXb, contain within their tail domains a region with sequence homology to GTPase activating proteins for the rho family of G proteins. Because low levels of myosin-IXb expression preclude purification by conventional means, we have employed an immunoadsorption strategy to purify myosin-IXb, enabling us to characterize the mechanochemical and rho-GTPase activation properties of the native protein. In this report we have examined the light chain content, actin binding properties, in vitro motility and rho-GTPase activity of human myosin-IXb purified from leukocytes. The results presented here indicate that myosin-IXb contains calmodulin as a light chain and that it binds to actin with high affinity in both the absence and presence of ATP. Myosin-IXb is an active motor which, like other calmodulin-containing myosins, exhibits maximal velocity of actin filaments (15 nm/second) in the absence of Ca2+. Native myosin-IXb exhibits GAP activity on rho. Class IX myosins may be an important link between rho and rho-dependent remodeling of the actin cytoskeleton. | lld:pubmed |
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pubmed-article:9490638 | pubmed:language | eng | lld:pubmed |
pubmed-article:9490638 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9490638 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9490638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9490638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9490638 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9490638 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9490638 | pubmed:month | Apr | lld:pubmed |
pubmed-article:9490638 | pubmed:issn | 0021-9533 | lld:pubmed |
pubmed-article:9490638 | pubmed:author | pubmed-author:MoosekerM SMS | lld:pubmed |
pubmed-article:9490638 | pubmed:author | pubmed-author:BokochG MGM | lld:pubmed |
pubmed-article:9490638 | pubmed:author | pubmed-author:PostP LPL | lld:pubmed |
pubmed-article:9490638 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9490638 | pubmed:volume | 111 ( Pt 7) | lld:pubmed |
pubmed-article:9490638 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9490638 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9490638 | pubmed:pagination | 941-50 | lld:pubmed |
pubmed-article:9490638 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:9490638 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9490638 | pubmed:articleTitle | Human myosin-IXb is a mechanochemically active motor and a GAP for rho. | lld:pubmed |
pubmed-article:9490638 | pubmed:affiliation | Department of Molecular Biology, Yale University, New Haven, CT 06520, USA. penny.post@yale.edu | lld:pubmed |
pubmed-article:9490638 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9490638 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9490638 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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