Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Monica X. Li"'
Autor:
Monica X. Li, Shorena Gelozia, Gaddafi I. Danmaliki, Yurong Wen, Philip B. Liu, M. Joanne Lemieux, Frederick G. West, Brian D. Sykes, Peter M. Hwang
Publikováno v:
Biochemistry and Biophysics Reports, Vol 16, Iss , Pp 145-151 (2018)
The compound MCI-154 was previously shown to increase the calcium sensitivity of cardiac muscle contraction. Using solution NMR spectroscopy, we demonstrate that MCI-154 interacts with the calcium-sensing subunit of the cardiac troponin complex, card
Externí odkaz:
https://doaj.org/article/7921eb263864415793b07715535b4a6d
Publikováno v:
Journal of Medicinal Chemistry. 64:3026-3034
Troponin regulates the calcium-mediated activation of skeletal muscle. Muscle weakness in diseases such as amyotrophic lateral sclerosis and spinal muscular atrophy occurs from diminished neuromuscular output. The first direct fast skeletal troponin
Autor:
Andres F. Cuesta, Peter J. Reiser, Monica X. Li, Peter M. Hwang, Jonathan P. Davis, Morgan V. Price, Natalya Belevych, Svetlana B. Tikunova, Brandon J. Biesiadecki
Publikováno v:
The Journal of General Physiology
Cardiac troponin activators could be beneficial in systolic heart failure. Tikunova et al. demonstrate that, unlike previously known calcium sensitizers, the small molecule 3-chlorodiphenylamine does not activate isolated cardiac troponin C but inste
Publikováno v:
Journal of medicinal chemistry. 64(6)
Troponin regulates the calcium-mediated activation of skeletal muscle. Muscle weakness in diseases such as amyotrophic lateral sclerosis and spinal muscular atrophy occurs from diminished neuromuscular output. The first direct fast skeletal troponin
Autor:
Peter M. Hwang, Fangze Cai, Frederick G. West, Steffen Lindert, Shorena Gelozia, Sandra E. Pineda-Sanabria, Monica X. Li, Brian D. Sykes
Publikováno v:
Journal of Molecular and Cellular Cardiology. 101:134-144
In cardiac and skeletal muscle, the troponin complex turns muscle contraction on and off in a calcium-dependent manner. Many small molecules are known to bind to the troponin complex to modulate its calcium binding affinity, and this may be useful in
Autor:
Peter M. Hwang, Shorena Gelozia, Gaddafi I. Danmaliki, Frederick G. West, Monica X. Li, Brian D. Sykes, Yurong Wen, Philip B. Liu, M. Joanne Lemieux
Publikováno v:
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 16, Iss, Pp 145-151 (2018)
Biochemistry and Biophysics Reports, Vol 16, Iss, Pp 145-151 (2018)
The compound MCI-154 was previously shown to increase the calcium sensitivity of cardiac muscle contraction. Using solution NMR spectroscopy, we demonstrate that MCI-154 interacts with the calcium-sensing subunit of the cardiac troponin complex, card
Publikováno v:
Metabolomics. 10:1145-1151
As small animal models of disease become more widely used, there is increasing importance and potential for characterizing their metabolomes. However, as the animal becomes smaller, the amounts of biofluids such as urine and cerebral spinal fluid ava
Autor:
Qiang Wang, Monica X. Li, Siew E. Chua, Grainne M. McAlonan, Y. Wang, Wei Deng, P. C. Sham, David A. Collier, Tao Li, Ching-Lung Cheung, Lijun Jiang, Qiyong Gong, Chaohua Huang, X. Ma
Publikováno v:
Psychological Medicine. 43:2301-2309
BackgroundIt is not clear whether the progressive changes in brain microstructural deficits documented in previous longitudinal magnetic resonance imaging (MRI) studies might be due to the disease process or to other factors such as medication. It is
Publikováno v:
Cardiovascular Research. 97:481-489
Aims Ischaemic heart disease is the leading cause of mortality worldwide. Acidosis is the main mediator of ischaemia and shielding against it might be possible. In this study, we characterize the nature of interaction between the regulatory domain of
Autor:
Valerie Daggett, An Yue Tu, Melissa L. Crane, Zhaoxiong Luo, Brian D. Sykes, Ian M. Robertson, Michael Regnier, Monica X. Li, Dan Wang, Michelle E. McCully
Publikováno v:
Biochemistry. 51:4473-4487
Calcium binding to the regulatory domain of cardiac troponin C (cNTnC) causes a conformational change that exposes a hydrophobic surface to which troponin I (cTnI) binds, prompting a series of protein-protein interactions that culminate in muscle con