H
Herbert C. Cheung
Researcher at University of Alabama at Birmingham
Publications - 98
Citations - 3002
Herbert C. Cheung is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Troponin C & Troponin I. The author has an hindex of 36, co-authored 98 publications receiving 2957 citations. Previous affiliations of Herbert C. Cheung include University of Cincinnati Academic Health Center.
Papers
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Journal ArticleDOI
Conformation of the regulatory domain of cardiac muscle troponin C in its complex with cardiac troponin I.
Wen-Ji Dong,Jun Xing,Matteo Villain,Matthew Hellinger,John M. Robinson,Murali Chandra,R. John Solaro,Patrick K. Umeda,Herbert C. Cheung +8 more
TL;DR: The binding of cardiac TnI to cTnC is a prerequisite to achieve a Ca2+-induced open N-domain similar to that previously observed in fsTNC with no bound fsTnI.
Journal ArticleDOI
NMR analysis of cardiac troponin C-troponin I complexes: effects of phosphorylation
Natosha Finley,M. Bret Abbott,Ekram Abusamhadneh,Vadim Gaponenko,Wen-Ji Dong,Genevieve Gasmi-Seabrook,Jack W. Howarth,Mark Rance,R. John Solaro,Herbert C. Cheung,Paul R. Rosevear +10 more
TL;DR: The non‐phosphorylated cardiac specific amino‐terminus, cardiac troponin I(1–80), was found to make additional interactions with the N‐terminal domain of cardiac trop onin C, which has been demonstrated to reduce the Ca2+ affinity of the cardiac Troponin C regulatory site.
Journal ArticleDOI
Distance distributions in proteins recovered by using frequency-domain fluorometry. Applications to troponin I and its complex with troponin C.
Joseph R. Lakowicz,Ignacy Gryczynski,Herbert C. Cheung,Chien Kao Wang,Michael L. Johnson,Nanda Joshi +5 more
TL;DR: The results demonstrate that distance distributions can be recovered with good accuracy, to the extent of revealing modest changes due to binding of other components, and should have widespread applications in studies of protein folding.
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Effects of protein kinase A phosphorylation on signaling between cardiac troponin I and the N-terminal domain of cardiac troponin C.
TL;DR: The findings indicate that the transduction of PKA-induced phosphorylation signal from cTnI to the regulatory site of cTtnC involves a global change in cTNI structure.