Zobrazeno 1 - 10
of 10
pro vyhledávání: '"John E. Rubin"'
Autor:
John E. Rubin, Vanessa Ng, Justin Chung, Nicolas Salvatierra, Brady Rippon, Diana Khatib, Natalia I. Girardi, Kane O. Pryor, Roniel Y. Weinberg, Silis Jiang, Sherif Khairallah, Stephanie L. Mick, Tiffany R. Tedore
Publikováno v:
BJA Open, Vol 11, Iss , Pp 100288- (2024)
Background: Sternal pain after cardiac surgery results in considerable discomfort. Single-injection parasternal fascial plane blocks have been shown to reduce pain scores and opioid consumption during the first 24 h after surgery, but the efficacy of
Externí odkaz:
https://doaj.org/article/f68fdc1aa2d348b6a5be8d7a8af229e8
Publikováno v:
Interventional Pain Medicine. 2:100180
Publikováno v:
Surgery. 170:1591-1592
Autor:
Cindy A. Cheung, June M. Chan, John E. Rubin, Rohan Jotwani, Eric D. Brumberger, Jimmy Y. Lin, Kane O. Pryor, Marguerite M. Hoyler, Matthew D. Perlstein
Publikováno v:
British Journal of Anaesthesia
BJA: British Journal of Anaesthesia
BJA: British Journal of Anaesthesia
Publikováno v:
JAMA Cardiology. 5:723
We have used fluorescence spectroscopy, molecular modeling, and limited proteolysis to examine structural dynamics of the sarcoplasmic reticulum Ca-ATPase (SERCA). The Ca-ATPase in sarcoplasmic reticulum vesicles from fast twitch muscle (SERCA1a isof
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cd702f72adaadfd803be86271094c51
https://europepmc.org/articles/PMC3493948/
https://europepmc.org/articles/PMC3493948/
Publikováno v:
Biophysical Journal. 102(3)
We have detected structural dynamics in the nucleotide-binding domain of the Ca-ATPase (SERCA) using fluorescence spectroscopy and molecular modeling. SERCA in sarcoplasmic reticulum (SR) vesicles was selectively labeled with fluorescein isothiocyana
Autor:
John E. Rubin, Bengt Svensson, David D. Thomas, Seth L. Robia, Kurt C. Peterson, Joseph M. Autry
Publikováno v:
Biophysical Journal. 108:423a
We have used fluorescence microscopy to detect interactions of sarcolipin (SLN), phospholamban (PLB), and the SR Ca-ATPase (SERCA1a isoform). SLN and PLB individually regulate SERCA activity through protein-protein interactions controlled by phosphor
Publikováno v:
Biophysical Journal. (3):466a
We have monitored molecular interactions of sarcolipin (SLN) and the sarcoplasmic reticulum Ca- ATPase (SERCA) by measuring Forster resonance energy transfer (FRET) between fusion proteins labeled with cyan fluorescent protein (donor) and yellow fluo
Publikováno v:
Biophysical Journal. (3):170a
We have monitored molecular interactions of sarcolipin (SLN) and the sarcoplasmic reticulum Ca-ATPase (SERCA) by measuring Forster resonance energy transfer (FRET) between fusion proteins labeled with cyan fluorescent protein (CFP) and yellow fluores