Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Xiaoqiong Dong"'
Autor:
RobynT. Rebbeck, Kenneth S. Ginsburg, Christopher Y. Ko, Anna Fasoli, Katherine Rusch, George F. Cai, Xiaoqiong Dong, David D. Thomas, Donald M. Bers, Razvan L. Cornea
Publikováno v:
Journal of molecular and cellular cardiology. 168
A key therapeutic target for heart failure and arrhythmia is the deleterious leak through sarcoplasmic reticulum (SR) ryanodine receptor 2 (RyR2) calcium release channels. We have previously developed methods to detect the pathologically leaky state
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc39d5c9f5ab90666a709c563f72c8e7
https://pubmed.ncbi.nlm.nih.gov/35405106
https://pubmed.ncbi.nlm.nih.gov/35405106
Autor:
David D. Thomas, Xiaoqiong Dong
Publikováno v:
Biochemical and Biophysical Research Communications. 449:196-201
We have used time-resolved fluorescence resonance energy transfer (TR-FRET) to characterize the interaction between phospholamban (PLB) and the sarcoplasmic reticulum (SR) Ca-ATPase (SERCA) under conditions that relieve SERCA inhibition. Unphosphoryl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9082959050c4cbf092d9b83da0fc28e2
https://doi.org/10.1016/j.bbrc.2014.04.166
https://doi.org/10.1016/j.bbrc.2014.04.166
Autor:
Xiaoqiong Dong, David D. Thomas, Gregory D. Gillispie, Bradley S. Launikonis, Kenneth S. Ginsburg, Robyn T. Rebbeck, Donald M. Bers, Razvan L. Cornea, Daniel P. Singh
Publikováno v:
Biophysical Journal. 114:117a-118a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2281cc2fc6fda8ad21b4f32a643fb3b
https://doi.org/10.1016/j.bpj.2017.11.675
https://doi.org/10.1016/j.bpj.2017.11.675
Autor:
Xiaoqiong Dong, Razvan L. Cornea, Bradley S. Launikonis, Donald M. Bers, Kenneth S. Ginsburg, David D. Thomas, Robyn T. Rebbeck, Daniel P. Singh
Publikováno v:
Biophysical Journal. 116:380a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2cfa4a1e564ceb25468b3e65c89f309
https://doi.org/10.1016/j.bpj.2018.11.2062
https://doi.org/10.1016/j.bpj.2018.11.2062
Autor:
Donald M. Bers, Xiaoqiong Dong, Masafumi Yano, Hitoshi Uchinoumi, Takeshi Yamamoto, Mena Said, Razvan L. Cornea, Xander H.T. Wehrens, Wehrens S.R. Wayne, Ivanita Stefanon
Publikováno v:
Journal of Cardiac Failure. 23:S81
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f9c7f04038f96e56c1927b666e1f062
https://doi.org/10.1016/j.cardfail.2017.08.407
https://doi.org/10.1016/j.cardfail.2017.08.407
Autor:
Mena Said, Xiaoqiong Dong, Rogerio F. Ribeiro, Ivanita Stefanon, Donald M. Bers, Razvan L. Cornea, Robyn T. Rebbeck
Publikováno v:
Biophysical Journal. 112:255a
Mg2+ is a potent inhibitor of RyR channel gating, as demonstrated in lipid bilayer and SR vesicles. Less is known about Mg2+ effects on RyR2 function in the cardiac myocyte environment or how it might alter RyR2 interaction with accessory proteins li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12054231628ce09585910acd16ed67c1
https://doi.org/10.1016/j.bpj.2016.11.1390
https://doi.org/10.1016/j.bpj.2016.11.1390
Autor:
Xiaoqiong Dong, Jianyi Zhang, Zachary M. James, David D. Thomas, Qiang Xiong, Naa Adjeley D. Ablorh, Christine B. Karim
We have studied the differential effects of phospholamban (PLB) phosphorylation states on the activity of the sarcoplasmic reticulum Ca-ATPase (SERCA). It has been shown that unphosphorylated PLB (U-PLB) inhibits SERCA and that phosphorylation of PLB
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eca2b65fc41ef17677ec2598dc170e30
https://europepmc.org/articles/PMC4200288/
https://europepmc.org/articles/PMC4200288/
Autor:
Xiaoqiong Dong, Naa-Adjeley D. Ablorh, David D. Thomas, Holly R. Langer, Zachary M. James, Christine B. Karim
Publikováno v:
Biophysical Journal. 106(2)
We have studied the differential effects of phospholamban (PLB) phosphorylation states on the activity of the sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA). It is known that PLB inhibits SERCA and that PLB phosphorylation at S16 and/or T17 relieves
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4d84d408890e4fc54a5fdc60e351e3d
We have used membrane surface charge to modulate the structural dynamics of an integral membrane protein, phospholamban (PLB), and thereby its functional inhibition of the sarcoplasmic reticulum Ca-ATPase (SERCA). It was previously shown by electron
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bab40f9e69ffab50c5ba95315eccc21
https://europepmc.org/articles/PMC3327772/
https://europepmc.org/articles/PMC3327772/
Publikováno v:
Biophysical Journal. 104:299a-300a
We have used time-resolved fluorescence resonance energy transfer (TR-FRET) to study the structural basis of regulation of sarcoplasmic reticulum Ca2+ ATPase (SERCA) by a single-pass transmembrane protein, phospholamban (PLB). The most prominent feat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e66b274b0a4ac71431db18798431e8fd
https://doi.org/10.1016/j.bpj.2012.11.1668
https://doi.org/10.1016/j.bpj.2012.11.1668