| pubmed-article:8900193 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C0027108 | lld:lifeskim |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C1948023 | lld:lifeskim |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C1148926 | lld:lifeskim |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8900193 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:8900193 | pubmed:issue | 43 | lld:pubmed |
| pubmed-article:8900193 | pubmed:dateCreated | 1996-12-16 | lld:pubmed |
| pubmed-article:8900193 | pubmed:abstractText | The N-terminal region of skeletal myosin light chain-1 (MLC-1) binds to the C terminus of actin, yet the functional significance of this interaction is unclear. We studied a fragment (MLC-pep; residues 5-14) of the ventricular MLC-1. When added to rat cardiac myofibrils, 10 nM MLC-pep induced a supramaximal increase in the MgATPase activity at submaximal Ca2+ levels with no effect at low and maximal Ca2+ levels. A nonsense, scrambled sequence peptide had no effect at any pCa value. MLC-pep did not affect myosin KEDTA and CaATPase activities or actin-activated MgATPase activities in the absence or presence of tropomyosin. The MLC-pep did not alter the ability of troponin I to inhibit MgATPase activity. Moreover, when troponin I and troponin C were extracted from the myofibrils, the MLC-pep lost its ability to stimulate the ATPase rate. This effect was fully restored upon reconstitution of the extracted myofibrils with troponin I-troponin C complex. Thus, activation of MgATPase activity by the peptide required a full complement of thin filament regulatory proteins. Interestingly, the stimulatory effect occurred at a ratio of 4 peptides to 1 thin filament, suggesting that the peptide engages in a highly cooperative process that may involve activation of the entire thin filament. | lld:pubmed |
| pubmed-article:8900193 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8900193 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8900193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8900193 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8900193 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8900193 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8900193 | pubmed:author | pubmed-author:SolaroR JRJ | lld:pubmed |
| pubmed-article:8900193 | pubmed:author | pubmed-author:OpgenorthT... | lld:pubmed |
| pubmed-article:8900193 | pubmed:author | pubmed-author:von... | lld:pubmed |
| pubmed-article:8900193 | pubmed:author | pubmed-author:RarickH MHM | lld:pubmed |
| pubmed-article:8900193 | pubmed:author | pubmed-author:Wu-WongJ RJR | lld:pubmed |
| pubmed-article:8900193 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8900193 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:8900193 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8900193 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8900193 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8900193 | pubmed:pagination | 27039-43 | lld:pubmed |
| pubmed-article:8900193 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
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| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
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| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:meshHeading | pubmed-meshheading:8900193-... | lld:pubmed |
| pubmed-article:8900193 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8900193 | pubmed:articleTitle | An essential myosin light chain peptide induces supramaximal stimulation of cardiac myofibrillar ATPase activity. | lld:pubmed |
| pubmed-article:8900193 | pubmed:affiliation | Department of Physiology and Biophysics, College of Medicine, University of Illinois, Chicago, Illinois 60612-7342, USA. | lld:pubmed |
| pubmed-article:8900193 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8900193 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8900193 | lld:pubmed |
