Zobrazeno 1 - 10
of 116
pro vyhledávání: '"Herbert C. Cheung"'
Publikováno v:
PLoS ONE, Vol 9, Iss 2, p e87135 (2014)
Cardiac troponin (cTn) is the Ca(2+)-sensitive molecular switch that controls cardiac muscle activation and relaxation. However, the molecular detail of the switching mechanism and how the Ca(2+) signal received at cardiac troponin C (cTnC) is commun
Externí odkaz:
https://doaj.org/article/c066a69b554b4ac9b5a5965bcaee941d
Publikováno v:
Protein Science. 9:280-289
The distance between Ca2+-binding site III in the C-terminal domain and Cys35 in the N-terminal domain in cardiac muscle troponin C (cTnC) was determined with a single-tryptophan mutant using bound Tb3+ as the energy donor and iodoacetamidotetramethy
Autor:
Vladimir V. Veselovsky, Sergei D. Maltsev, Ejvis Lamani, Natalia Ya. Grigorieva, R. Brandon Mewbourne, Leonid L. Danilov, Vladimir N. Shibaev, Damona S. Fletcher, Mark J. Jedrzejas, W. Thomas Forsee, O. A. Pinsker, John S. Schutzbach, Antonina V. Lozanova, Jun Xing, Herbert C. Cheung
Publikováno v:
Glycobiology. 16:666-678
Dolichyl-phosphate-mannose (Dol-P-Man) synthase catalyzes the reversible formation of a key intermediate that is involved as a mannosyl donor in at least three different pathways for the synthesis of glycoconjugates important for eukaryotic developme
Autor:
Herbert C. Cheung, Christie G. Brouillette, Marjorie Ray, Zhengrong W. Yang, Irina I. Protasevich, Wen-Ji Dong, Jeffrey A. Engler
Publikováno v:
Biochemistry. 44:16413-16425
Apolipoprotein (apo) A-I mutants were constructed for FRET studies to distinguish between two possible lipid-free conformers, a globular helix bundle and an elongated helical hairpin. Mutants containing a single Trp at position 50 were prepared by re
Publikováno v:
Journal of Molecular Biology. 340:295-305
The principal task of the Ca(2+) activation of striated muscle is the release of the troponin I (TnI) inhibitory region (TnI-I) from actin. TnI-I release facilitates the repositioning of tropomyosin across the actin surface and the formation of stron
Publikováno v:
Biochemistry. 43:5996-6004
In experiments reported here, we compared tension and thin filament Ca 2 + signaling in preparations containing either wild-type cardiac troponin I (cTnl) or a mutant cTnl with an R146G mutation [cTnI(146G)] linked to familial hypertrophic cardiomyop
Publikováno v:
Journal of Biological Chemistry. 278:42394-42402
Upon Ca2+ activation of cardiac muscle, several structural changes occur in the troponin subunits. These changes include the opening of the cardiac troponin C (cTnC) N-domain, the change of secondary structure of the inhibitory region of cardiac trop
Publikováno v:
Biochemistry. 42:5877-5884
The skeletal myosin cross-bridge in dynamic association with actin is the unitary energy transducer in muscle, converting free energy from ATP hydrolysis into contractile force. Myosin's conserved ATP-sensitive tryptophan (AST) is an energy transduct
Publikováno v:
Biophysical Journal. 84(2):1057-1064
The contiguous inhibitory and regulatory regions of troponin I in the heterotrimeric troponin complex play a critical role in Ca2+ activation of striated muscle. Knowledge of the structure of this critical region within the complex will enhance effor
Publikováno v:
Journal of Molecular Biology. 322:1065-1088
We have formulated a three-compartment model of muscle activation that includes both strong cross-bridge (XB) and Ca 2+ -activated regulatory-unit (RU) mediated nearest-neighbor cooperative influences. The model is based on the tight coupling premise