Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Earl Homsher"'
Autor:
James R. Sellers, Attila Nagy, Aibing Wang, Yasuharu Takagi, Neil Billington, Davin K.T. Hong, Earl Homsher, Sara A. Sun
Publikováno v:
Journal of Biological Chemistry. 288:709-722
Nonmuscle myosin IIB (NMIIB) is a cytoplasmic myosin, which plays an important role in cell motility by maintaining cortical tension. It forms bipolar thick filaments with ~14 myosin molecule dimers on each side of the bare zone. Our previous studies
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3bf199b1d3b904e7132993edd565335
https://doi.org/10.1074/jbc.m112.424671
https://doi.org/10.1074/jbc.m112.424671
Autor:
Earl Homsher
Publikováno v:
Biophysical Journal. 112:205-206
The second phase of the biphasic force decay upon release of phosphate from caged phosphate was previously interpreted as a signature of kinetics of the force-generating step in the cross-bridge cycle. To test this hypothesis without using caged comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b5be154db1807a7bcbcc98a3e74071f
https://doi.org/10.1016/j.bpj.2016.12.028
https://doi.org/10.1016/j.bpj.2016.12.028
Autor:
Mary L. Garcia-Cazarin, C. Amelia Sumandea, Marius P. Sumandea, Jon Staidle, Earl Homsher, Susan Vahebi
Publikováno v:
Biochemistry. 48:7722-7731
Cardiac troponin T (cTnT) is a phosphoprotein that modulates cardiac muscle contraction through its extensive and diverse interactions with neighboring thin filament proteins. Its N-terminal half is the "glue" that anchors the troponin complex to tro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a625f3fcd2035de29f1f76af3e79a59
https://doi.org/10.1021/bi900516n
https://doi.org/10.1021/bi900516n
Publikováno v:
Biophysical Journal. 90(4):1295-1307
The mechanical load borne by a molecular motor affects its force, sliding distance, and its rate of energy transduction. The control of ATPase activity by the mechanical load on a muscle tunes its efficiency to the immediate task, increasing ATP hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01d9913a437fa45f2de99cfd7e015b5e
Publikováno v:
Journal of Biological Chemistry. 278:41742-41748
The relationship between tropomyosin thermal stability and thin filament activation was explored using two N-domain mutants of alpha-striated muscle tropomyosin, A63V and K70T, each previously implicated in familial hypertrophic cardiomyopathy. Both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::758f64b7eb3c7c5c250158ee5192ff1b
https://doi.org/10.1074/jbc.m303408200
https://doi.org/10.1074/jbc.m303408200
Publikováno v:
Frontiers in Physiology, Vol 5 (2014)
Frontiers in Physiology
Frontiers in Physiology
Striated muscle is an elegant system for study at many levels. Much has been learned about the mechanism of contraction from studying the mechanical properties of intact and permeabilized (or skinned) muscle fibers. Structural studies using electron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::472c9a6d0c61606f1997865cf4b3831c
https://doi.org/10.3389/fphys.2014.00090
https://doi.org/10.3389/fphys.2014.00090
Publikováno v:
Physiology. 16:49-55
Changes in thin filament structure induced by Ca2+ binding to troponin and subsequent strong cross-bridge binding regulate additional strong cross-bridge attachment, force development, and dependence of force on sarcomere length in skeletal and cardi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54b01bf5d50de7e7a900e8f5d281750b
https://doi.org/10.1152/physiologyonline.2001.16.2.49
https://doi.org/10.1152/physiologyonline.2001.16.2.49
Autor:
Marion L. Greaser, Mahta Nili, Earl Homsher, Richard L. Moss, Dimitry Pavlov, José A.A. Sant'Ana Pereira
Publikováno v:
Journal of Biological Chemistry. 276:4409-4415
The kinetics of nucleotide turnover vary considerably among isoforms of vertebrate type II myosin, possibly due to differences in the rate of ADP release from the nucleotide binding pocket. Current ideas about likely mechanisms by which ADP release i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7f501b04fab914da7040d15386c40d5
https://doi.org/10.1074/jbc.m006441200
https://doi.org/10.1074/jbc.m006441200
Autor:
James Strand, Larry S. Tobacman, Lameh Fananapazir, Carol A. Butters, Andrew E. Arai, Nick Back, Anne Ortiz, Linda L. Bachinski, Robert Roberts, Earl Homsher, Akihiko Karibe
Publikováno v:
Circulation. 103:65-71
Background —We report hypertrophic cardiomyopathy (HCM) in a Spanish-American family caused by a novel α-tropomyosin ( TPM1) mutation and examine the pathogenesis of the clinical disease by characterizing functional defects in the purified mutant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79ea5abd484fc5b228b25432390d1ecf
https://doi.org/10.1161/01.cir.103.1.65
https://doi.org/10.1161/01.cir.103.1.65
Publikováno v:
Journal of Biological Chemistry. 276:20245-20251
Calcium controls the level of muscle activation via interactions with the troponin complex. Replacement of the native, skeletal calcium-binding subunit of troponin, troponin C, with mixtures of functional cardiac and mutant cardiac troponin C insensi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::375bcf05b7d16468425aad03814e8dcd
https://doi.org/10.1074/jbc.m007371200
https://doi.org/10.1074/jbc.m007371200