Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Elena S. Dremina"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1865:121-131
An interaction of Bcl-2 with SERCA had been documented in vitro using the SERCA1a isoform isolated from rat skeletal muscle [Dremina, E. S., Sharov, V. S., Kumar, K., Azidi, A., Michaelis, E. K., Schoneich, C. (2004) Biochem. J. 383 (361–370)]. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::762eaec96c3772979a82d77b64971ef7
https://doi.org/10.1016/j.bbapap.2016.09.004
https://doi.org/10.1016/j.bbapap.2016.09.004
Publikováno v:
Apoptosis. 19:42-57
Muscle cell apoptosis accompanies normal muscle development and regeneration, as well as degenerative diseases and aging. C2C12 murine myoblast cells represent a common model to study muscle differentiation. Though it was already shown that myogenic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee899bdadc1aec167f7c1a0cec4a97ae
https://doi.org/10.1007/s10495-013-0922-7
https://doi.org/10.1007/s10495-013-0922-7
Publikováno v:
Free Radical Biology and Medicine. 53:1877-1885
Protein tyrosine nitration is a common biomarker of biological aging and diverse pathologies associated with the excessive formation of reactive oxygen and nitrogen species. Recently, we suggested a novel fluorogenic derivatization procedure for the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bca265fc4d3e6300baa9a687940e6f9
https://doi.org/10.1016/j.freeradbiomed.2012.08.582
https://doi.org/10.1016/j.freeradbiomed.2012.08.582
Autor:
Elena S. Dremina, Christian Schöneich, John F. Stobaugh, Victor S. Sharov, Xiaobao Li, Nadezhda A. Galeva
Publikováno v:
Analytical Biochemistry. 418:184-196
We synthesized and characterized a new tagging reagent, (3R,4S)-1-(4-(aminomethyl)phenylsulfonyl)pyrrolidine-3,4-diol (APPD), for the selective fluorogenic derivatization of 3-nitrotyrosine (3-NT) residues in peptides (after reduction to 3-aminotyros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1918c08f3a96f2ff982cc695b267c29a
https://doi.org/10.1016/j.ab.2011.07.024
https://doi.org/10.1016/j.ab.2011.07.024
Autor:
Victor S. Sharov, Elena S. Dremina, Todd D. Williams, Nadezhda A. Galeva, Christian Schöneich
Publikováno v:
Archives of Biochemistry and Biophysics. 484:155-166
There is increasing evidence that sequence-specific formation of 3-nitrotyrosine (3-NT) may cause functional changes in target proteins. Recently, the nitration of Tyr residues in glycogen phosphorylase b (Ph-b) was implicated in the age-associated d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cf9239fb212e43bb766e027b7daaa5a
https://doi.org/10.1016/j.abb.2008.12.012
https://doi.org/10.1016/j.abb.2008.12.012
Publikováno v:
Journal of Neurochemistry. 93:1262-1271
Protein 3-nitrotyrosine (3-NY) immunoreactivity of rat brain homogenate was localized to a ca. 50 kDa protein band by western blot (WB) analysis. The nitrated proteins were localized to the raft fraction obtained by centrifugation of the homogenate i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4911788536dead85b2813397fc553ba4
https://doi.org/10.1111/j.1471-4159.2005.03115.x
https://doi.org/10.1111/j.1471-4159.2005.03115.x
Autor:
Christian Schöneich, Keshava N. Kumar, Elena S. Dremina, Elias K. Michaelis, Asma Zaidi, Victor S. Sharov
Publikováno v:
Biochemical Journal. 383:361-370
The anti-apoptotic effect of Bcl-2 is well established, but the detailed mechanisms are unknown. In the present study, we show in vitro a direct interaction of Bcl-2 with the rat skeletal muscle SERCA (sarcoplasmic/endoplasmic reticulum Ca2+-ATPase),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fef2d9bee7c280989fc9b2d0a833ec94
https://doi.org/10.1042/bj20040187
https://doi.org/10.1042/bj20040187
Publikováno v:
Free Radical Biology and Medicine. 108:S73
Bcl-2 is an anti-apoptotic protein, which is involved in the interaction with multiple proteins at various cellular locations, including mitochondria and the ER. We show here, that Bcl-2 interacts efficiently with various isoforms of the sarco/endopl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::12b5bb0a279451e0fa1904f560026bd3
https://doi.org/10.1016/j.freeradbiomed.2017.04.248
https://doi.org/10.1016/j.freeradbiomed.2017.04.248
We have demonstrated previously that Bcl-2 and Bcl-2Δ21, a C-terminally truncated Bcl-2 sequence, inactivate SERCA (sarcoplasmic/endoplasmic reticulum Ca2+-ATPase) 1 in isolated SR (sarcoplasmic reticulum), accompanied by a translocation from CRDs (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eed8e67db7b7838c3d02296b9cd1a307
https://europepmc.org/articles/PMC3736812/
https://europepmc.org/articles/PMC3736812/
Autor:
Victor S. Sharov, Rick T. Dobrowsky, Christian Schöneich, Elena S. Dremina, Gary S. Gerstenecker, Xiaobao Li, John F. Stobaugh, Nadezhda A. Galeva
Protein 3-nitrotyrosine (3-NT) has been recognized as an important biomarker of nitroxidative stress associated with inflammatory and degenerative diseases, and biological aging. Analysis of protein-bound 3-NT continues to represent a challenge since
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9ada221cc90c62f96d8955e942d807d
https://europepmc.org/articles/PMC2918916/
https://europepmc.org/articles/PMC2918916/