Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Valeriy Lukyanenko"'
Autor:
Joaquin Muriel, Valeriy Lukyanenko, Thomas A. Kwiatkowski, Yi Li, Sayak Bhattacharya, Kassidy K. Banford, Daniel Garman, Hannah R. Bulgart, Roger B. Sutton, Noah Weisleder, Robert J. Bloch
Publikováno v:
Molecular Therapy: Methods & Clinical Development, Vol 32, Iss 2, Pp 101257- (2024)
Mutations in the DYSF gene, encoding the protein dysferlin, lead to several forms of muscular dystrophy. In healthy skeletal muscle, dysferlin concentrates in the transverse tubules and is involved in repairing the sarcolemma and stabilizing Ca2+ sig
Externí odkaz:
https://doaj.org/article/a94b4fbba8b74fb29787af068191750d
Publikováno v:
Frontiers in Physiology, Vol 13 (2022)
Dysferlin-null A/J myofibers generate abnormal Ca2+ transients that are slightly reduced in amplitude compared to controls. These are further reduced in amplitude by hypoosmotic shock and often appear as Ca2+ waves (Lukyanenko et al., J. Physiol., 20
Externí odkaz:
https://doaj.org/article/c7a9b4794cba43ffb2b1d6ccbd9e19a2
Autor:
Christian J. Kinney, Andrea O'Neill, Kaila Noland, Weiliang Huang, Joaquin Muriel, Valeriy Lukyanenko, Maureen A. Kane, Christopher W. Ward, Alyssa F. Collier, Joseph A. Roche, John C. McLenithan, Patrick W. Reed, Robert J. Bloch
Publikováno v:
Current Research in Physiology, Vol 4, Iss , Pp 47-59 (2021)
μ-Crystallin, encoded by the CRYM gene, binds the thyroid hormones, T3 and T4. Because T3 and T4 are potent regulators of metabolism and gene expression, and CRYM levels in human skeletal muscle can vary widely, we investigated the effects of overex
Externí odkaz:
https://doaj.org/article/fe77dc97c80848a79bd121d57e3278b7
Autor:
Julie In, Valeriy Lukyanenko, Jennifer Foulke-Abel, Ann L Hubbard, Michael Delannoy, Anne-Marie Hansen, James B Kaper, Nadia Boisen, James P Nataro, Chengru Zhu, Edgar C Boedeker, Jorge A Girón, Olga Kovbasnjuk
Publikováno v:
PLoS ONE, Vol 8, Iss 7, p e69196 (2013)
Life-threatening intestinal and systemic effects of the Shiga toxins produced by enterohemorrhagic Escherichia coli (EHEC) require toxin uptake and transcytosis across intestinal epithelial cells. We have recently demonstrated that EHEC infection of
Externí odkaz:
https://doaj.org/article/bbda392d092543809b3e5c6ebe2ea655
The C2 domains of dysferlin: roles in membrane localization, Ca 2+ signalling and sarcolemmal repair
Autor:
Joaquin Muriel, Valeriy Lukyanenko, Tom Kwiatkowski, Sayak Bhattacharya, Daniel Garman, Noah Weisleder, Robert J. Bloch
Publikováno v:
The Journal of Physiology. 600:1953-1968
Publikováno v:
Frontiers in physiology. 13
Dysferlin-null A/J myofibers generate abnormal Ca
Autor:
Robert J. Bloch, Kaila Noland, Joseph A. Roche, Alyssa F. Collier, Valeriy Lukyanenko, Christopher W. Ward, Maureen A. Kane, Christian J Kinney, Joaquin Muriel, Weiliang Huang, John C. McLenithan, Patrick W. Reed, Andrea O'Neill
Publikováno v:
Current Research in Physiology
Current Research in Physiology, Vol 4, Iss, Pp 47-59 (2021)
Current Research in Physiology, Vol 4, Iss, Pp 47-59 (2021)
μ-Crystallin, encoded by the CRYM gene, binds the thyroid hormones, T3 and T4. Because T3 and T4 are potent regulators of metabolism and gene expression, and CRYM levels in human skeletal muscle can vary widely, we investigated the effects of overex
Autor:
Joaquin, Muriel, Valeriy, Lukyanenko, Tom, Kwiatkowski, Sayak, Bhattacharya, Daniel, Garman, Noah, Weisleder, Robert J, Bloch
Publikováno v:
J Physiol
Dysferlin is an integral membrane protein of the transverse tubules of skeletal muscle that is mutated or absent in Limb Girdle Muscular Dystrophy 2B and Miyoshi Myopathy. Here we examine the role of dysferlin’s seven C2 domains, C2A through C2G, i
Publikováno v:
Biophysical Journal. 120:237a-238a
Publikováno v:
The Journal of Physiology. 595:5191-5207
Key points Dysferlin, the protein missing in limb girdle muscular dystrophy 2B and Miyoshi myopathy, concentrates in transverse tubules of skeletal muscle, where it stabilizes voltage-induced Ca2+ transients against loss after osmotic shock injury (O