Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Arthur S. Rovner"'
Autor:
Arthur S. Rovner, Susan Lowey, James Gulick, Leanne M. Lesko, Robert B. Low, Sheryl L. White, Mercedes Rincon, Alex R. Hodges, Jeffrey Robbins
Publikováno v:
Journal of Biological Chemistry. 283:20579-20589
The R403Q mutation in the beta-myosin heavy chain (MHC) was the first mutation to be linked to familial hypertrophic cardiomyopathy (FHC), a primary disease of heart muscle. The initial studies with R403Q myosin, isolated from biopsies of patients, s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::769c613f40c8e4797d624bfe70cd6944
https://doi.org/10.1074/jbc.m800554200
https://doi.org/10.1074/jbc.m800554200
Autor:
Arthur S. Rovner, Amy S. Miner, Paul H. Ratz, Daniel P. Meer, Thomas J. Eddinger, Joel T. Meehl
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 320:865-870
Blebbistatin is reported to be a selective and specific small molecule inhibitor of the myosin II isoforms expressed by striated muscles and nonmuscle (IC(50) = 0.5-5 microM) but is a poor inhibitor of purified turkey smooth muscle myosin II (IC(50)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b33e860f0aa6d9d10ce4a9e23267ad6
https://doi.org/10.1124/jpet.106.109363
https://doi.org/10.1124/jpet.106.109363
Publikováno v:
Biochemistry. 45:5280-5289
Regulatory light chain (RLC) phosphorylation activates smooth and non-muscle myosin II, but it has not been established if phosphorylation of one head turns on the whole molecule. Baculovirus expression and affinity chromatography were used to isolat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::702b159db18047154d65023f415db965
https://doi.org/10.1021/bi060154c
https://doi.org/10.1021/bi060154c
Autor:
David M. Warshaw, Arthur S. Rovner, Peteranne B. Joel, Neil M. Kad, Guy G. Kennedy, Kathleen M. Trybus, Joseph B. Patlak, Patricia M. Fagnant
Publikováno v:
The Journal of Cell Biology
Each of the heads of the motor protein myosin II is capable of supporting motion. A previous report showed that double-headed myosin generates twice the displacement of single-headed myosin (Tyska, M.J., D.E. Dupuis, W.H. Guilford, J.B. Patlak, G.S.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::347548ce8d471fc7c21749eac28f4009
https://doi.org/10.1083/jcb.200304023
https://doi.org/10.1083/jcb.200304023
Publikováno v:
Journal of Biological Chemistry. 278:26938-26945
The interaction between the two heads of myosin II during motion and force production is poorly understood. To examine this issue, we developed an expression and purification strategy to isolate homogeneous populations of heterodimeric smooth muscle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42679b2bb4630d93d6de5d3cd9291745
https://doi.org/10.1074/jbc.m303122200
https://doi.org/10.1074/jbc.m303122200
Publikováno v:
Journal of Biological Chemistry. 275:25481-25487
To examine the structural basis of the intrinsic fluorescence changes that occur during the MgATPase cycle of myosin, we generated three mutants of smooth muscle myosin motor domain essential light chain (MDE) containing a single conserved tryptophan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a56dde3999b50d3c5097ddcc979189c
https://doi.org/10.1074/jbc.m002910200
https://doi.org/10.1074/jbc.m002910200
Autor:
Arthur S. Rovner
Publikováno v:
Journal of Biological Chemistry. 273:27939-27944
Chimeric substitution of the weak actin-binding loop (ABL) from chicken skeletal muscle myosin for that of gizzard smooth muscle heavy meromyosin (HMM) causes activation of the dephosphorylated mutant (SABL HMM; Rovner, A. S., Freyzon, Y., and Trybus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f5d7b30bb1228f588fdcd595f12f034
https://doi.org/10.1074/jbc.273.43.27939
https://doi.org/10.1074/jbc.273.43.27939
Autor:
David M. Warshaw, Yelena Freyzon, Arthur S. Rovner, Matthew J. Tyska, Anne-Marie Lauzon, Kathleen M. Trybus
Publikováno v:
Journal of Muscle Research & Cell Motility. 19:825-837
Two smooth muscle myosin heavy chain isoforms differ by a 7-amino- acid insert in a flexible surface loop located near the nucleotide binding site. The non-inserted isoform is predominantly found in tonic muscle, while the inserted isoform is mainly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f4ec96ce4a992fe2b80b1ce952d4c320
https://doi.org/10.1023/a:1005489501357
https://doi.org/10.1023/a:1005489501357
Publikováno v:
Journal of Muscle Research and Cell Motility. 18:103-110
Smooth muscle myosin isoforms of the heavy chain and the essential light chain have been hypothesized to contribute to the different shortening velocities of phasic and tonic smooth muscles, and to their different affinities for MgADP. We used the ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e3cd327d39ad813cba58bb7e8cddbed
https://doi.org/10.1023/a:1018689102122
https://doi.org/10.1023/a:1018689102122
Publikováno v:
Journal of Biological Chemistry. 270:30260-30263
Regulatory light chain (RLC) phosphorylation is necessary to activate smooth muscle myosin, unlike constitutively active striated muscle myosins. Here we show that an actin-binding surface loop located at the 50/20-kDa junction contributes to this fu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96170be364788ac6395c89f4ceefeb36
https://doi.org/10.1074/jbc.270.51.30260
https://doi.org/10.1074/jbc.270.51.30260