Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Judith A. Heiny"'
Publikováno v:
PLoS ONE, Vol 17, Iss 4 (2022)
The highly conserved, cardiotonic steroid binding site (also termed ouabain binding site) on the primary α subunit of Na,K-ATPase plays a receptor signaling role in a range of vital cell processes and is a therapeutic target for human disease. Mouse
Externí odkaz:
https://doaj.org/article/5d004eb2aead474c8098ef4046d756e9
Autor:
Palanikumar Manoharan, Taejeong Song, Tatiana L. Radzyukevich, Sakthivel Sadayappan, Jerry B Lingrel, Judith A. Heiny
Publikováno v:
iScience, Vol 17, Iss , Pp 334-346 (2019)
Summary: Skeletal muscle repair and regeneration after injury requires coordinated interactions between the innate immune system and the injured muscle. Myeloid cells predominate in these interactions. This study examined the role of KLF2, a zinc-fin
Externí odkaz:
https://doaj.org/article/249991ea0d8248549a05af65d1f5d32f
Autor:
Taejeong Song, Palanikumar Manoharan, Douglas P. Millay, Sheryl E. Koch, Jack Rubinstein, Judith A. Heiny, Sakthivel Sadayappan
Publikováno v:
Skeletal Muscle, Vol 9, Iss 1, Pp 1-12 (2019)
Abstract Background Skeletal muscle myopathy and exercise intolerance are diagnostic hallmarks of heart failure (HF). However, the molecular adaptations of skeletal muscles during dilated cardiomyopathy (DCM)-mediated HF are not completely understood
Externí odkaz:
https://doaj.org/article/44a1821af2a34b7dbcfd9f06b9b56e03
Autor:
Hesamedin Hakimjavadi, Cory A. Stiner, Tatiana L. Radzyukevich, Jerry B. Lingrel, Natalie Norman, Julio A. Landero Figueroa, Judith A. Heiny
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 9, p 2725 (2018)
The potassium affinities of Na,K-ATPase isozymes are important determinants of their physiological roles in skeletal muscle. This study measured the apparent K+ and Rb+ affinities of the Na,K-ATPase α1 and α2 isozymes in intact, dissociated myofibe
Externí odkaz:
https://doaj.org/article/8eee196a30264ce4a28115322362b087
Autor:
Peter Wladyslaw Chomczynski, Kianna M Vires, Michal Rymaszewski, Judith Ann Heiny, Piotr Chomczynski
We conducted a pilot study to determine if the BinaxNOW rapid antigen test can detect SARS-CoV-2 antigen in saliva, in place of the specified nasal (Nares) swab sample. A nasal swab may not provide an optimal sample for detecting Omicron, now the pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::818f63054ab42cf0dcf2a1ecd2bdd2dc
https://doi.org/10.21203/rs.3.rs-1634124/v1
https://doi.org/10.21203/rs.3.rs-1634124/v1
The highly conserved, cardiotonic steroid binding site (also termed ouabain binding site) on the primary α subunit of Na,K-ATPase plays a receptor signaling role in a range of vital cell processes and is a therapeutic target for human disease. Mouse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e847ef4373c2e56ea30da804d814158
https://doi.org/10.17504/protocols.io.b63frgjn
https://doi.org/10.17504/protocols.io.b63frgjn
Publikováno v:
SSRN Electronic Journal.
We developed a sensitive, ratiometric method to measure simultaneously 13C-labeled glucose and rubidium in biological samples using ICP-MS. The method uses probe-assisted ultra-sonication with water to extract 13C-[6C]-labeled-D-glucose and other pol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62449876627047ac941022cf55fc57bc
https://doi.org/10.1101/2021.10.14.454503
https://doi.org/10.1101/2021.10.14.454503
Publikováno v:
Journal of General Physiology. 151:1146-1155
Ion movements across biological membranes, driven by electrochemical gradients or active transport mechanisms, control essential cell functions. Membrane ion movements can manifest as electrogenic currents or electroneutral fluxes, and either process
Autor:
Sakthivel Sadayappan, Thomas C. Irving, Lisa A. Martin, Jose R. Pinto, Maicon Landim-Vieira, Roger Craig, Judith A. Heiny, James W. McNamara, Taejeong Song, John N. Lorenz, Kyounghwan Lee, Weikang Ma
Publikováno v:
Proc Natl Acad Sci U S A
Fast skeletal myosin-binding protein-C (fMyBP-C) is one of three MyBP-C paralogs and is predominantly expressed in fast skeletal muscle. Mutations in the gene that encodes fMyBP-C, MYBPC2, are associated with distal arthrogryposis, while loss of fMyB