Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Raisa Klevitsky"'
Autor:
Jeffrey Robbins, Alina Maloyan, Hanna Osinska, Atsushi Sanbe, Raisa Klevitsky, J. Scott Pattison
Publikováno v:
Circulation. 117:2743-2751
Background— To determine whether soluble preamyloid oligomers (PAOs) are toxic when expressed internally in the cardiomyocyte, we tested the hypothesis that cardiomyocyte-restricted expression and accumulation of a known PAO is cytotoxic and suffic
Autor:
Natosha L. Finley, Hanna Osinska, Jeffrey Robbins, Paul R. Rosevear, Raisa Klevitsky, Sakthivel Sadayappan, Jack W. Howarth, John N. Lorenz
Publikováno v:
The FASEB Journal. 22:1246-1257
Cardiac troponin I (cTnI) phosphorylation modulates myocardial contractility and relaxation during beta-adrenergic stimulation. cTnI differs from the skeletal isoform in that it has a cardiac specific N' extension of 32 residues (N' extension). The r
Autor:
Sakthivel Sadayappan, Raisa Klevitsky, Hanna Osinska, Jonathan G. Seidman, Jeffrey D. Molkentin, John N. Lorenz, Michelle A. Sargent, Jeffrey M. Robbins, Christine E. Seidman
Publikováno v:
Proceedings of the National Academy of Sciences. 103:16918-16923
Cardiac myosin binding protein C (cMyBP-C) has three phosphorylatable serines at its N terminus (Ser-273, Ser-282, and Ser-302), and the residues' phosphorylation states may alter thick filament structure and function. To examine the effects of cMyBP
Autor:
David Brown, Jeffery D. Molkentin, Timothy E. Hewett, Jian Xu, Samuel N. Breit, John N. Lorenz, Raisa Klevitsky, Asne R. Bauskin, Thomas R. Kimball
Publikováno v:
Circulation Research. 98:342-350
Here we identified growth-differentiation factor 15 (GDF15) (also known as MIC-1), a secreted member of the transforming growth factor (TGF)-β superfamily, as a novel antihypertrophic regulatory factor in the heart. GDF15 is not expressed in the nor
Autor:
Harvey S. Hahn, Hanna Osinska, Christine E. Seidman, Lisa A. Martin, Sakthivel Sadayappan, Gerald W. Dorn, Raisa Klevitsky, Jeffrey M. Robbins, James Gulick, Jonathan G. Seidman
Publikováno v:
Circulation Research. 97:1156-1163
The role of cardiac myosin binding protein-C (cMyBP-C) phosphorylation in cardiac physiology or pathophysiology is unclear. To investigate the status of cMyBP-C phosphorylation in vivo, we determined its phosphorylation state in stressed and unstress
Autor:
Maike Krenz, Jeffrey Robbins, Fred Jones, James Gulick, Raisa Klevitsky, Lisa J. Martin, Jeanne James, Carmen E. Quatman
Publikováno v:
Circulation. 111:2339-2346
Background— The biochemical differences between the 2 mammalian cardiac myosin heavy chains (MHCs), α-MHC and β-MHC, are well described, but the physiological consequences of basal isoform expression and isoform shifts in response to altered card
Autor:
Mariappan Muthuchamy, David C. Zawieja, Jeffrey Robbins, Robert D. Gaffin, Raisa Klevitsky, Carl W. Tong, Timothy E. Hewett
Publikováno v:
The Journal of Physiology. 561:777-791
Two important charge differences between the α- and β-tropomyosin (TM) isoforms are the exchange of a serine residue in the inner-core region at position 229, and a histidine residue at the carboxy-terminal end at position 276, with glutamic acid a
Autor:
Jeffrey Robbins, Raisa Klevitsky, Kuppan Gokulan, Mariappan Muthuchamy, James C. Sacchettini, Robert D. Gaffin, Timothy E. Hewett
Publikováno v:
The Journal of Physiology. 556:531-543
Striated muscle tropomyosin (TM) is an essential thin filament protein that is sterically and allosterically involved in calcium-mediated cardiac contraction. We have previously shown that overexpressing the β-TM isoform in mouse hearts leads to phy
Autor:
Wen Zhao, Arnold Schwartz, Stephen B. Liggett, Su Wang, Evangelia G. Kranias, John N. Lorenz, Anna A. DePaoli-Roach, Margaret V. Westfall, Julian C. Braz, Kimberly N. Gregory, Timothy E. Hewett, Edward G. Lakatta, Ilona Bodi, Thomas F. Kimball, Jeffrey Robbins, Angus C. Nairn, Bogachan Sahin, Anand Pathak, Raisa Klevitsky, James A. Bibb, Jeffery D. Molkentin
Publikováno v:
Nature Medicine. 10:248-254
The protein kinase C (PKC) family of serine/threonine kinases functions downstream of nearly all membrane-associated signal transduction pathways. Here we identify PKC-alpha as a fundamental regulator of cardiac contractility and Ca(2+) handling in m
Autor:
Jeffrey Robbins, Christine Brosseau, Norman R. Alpert, Hanna Osinska, John N. Lorenz, Andrea Federico, David M. Warshaw, Raisa Klevitsky, M. Benjamin Perryman, Maike Krenz, Florence Bouyer-Dalloz, Steve M. Helmke, James Gulick, Timothy E. Hewett, Atsushi Sanbe
Publikováno v:
Journal of Biological Chemistry. 278:17466-17474
Comparison of mammalian cardiac alpha- and beta-myosin heavy chain isoforms reveals 93% identity. To date, genetic methodologies have effected only minor switches in the mammalian cardiac myosin isoforms. Using cardiac-specific transgenesis, we have