Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Syrus R. Soltaninassab"'
Publikováno v:
Journal of Cellular Physiology. 182:163-170
Glutathione is an important antioxidant that is involved in numerous cellular activities. gamma-Glutamylcysteine synthetase (gammaGCS) is a key regulatory enzyme in the synthesis of glutathione. It is a heterodimeric zinc metalloprotein that belongs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3fd4c3906fa62deb3eeb7865c2c1138d
https://doi.org/10.1002/(sici)1097-4652(200002)182:2<163::aid-jcp4>3.0.co
https://doi.org/10.1002/(sici)1097-4652(200002)182:2<163::aid-jcp4>3.0.co
Autor:
Konjeti S. Sekhar, Michael L. Freeman, Shelly C. Lu, Michael J. Meredith, Syrus R. Soltaninassab, Carrie L. Cusick
Publikováno v:
Biochemical and Biophysical Research Communications. 248:458-463
Overexpression of Bcl-2 and related anti-apoptotic gene products has been shown to increase the intracellular concentration of the antioxidant tripeptide glutathione in neuronal and hematopoietic cells. A similar examination of HeLa cells that stably
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42ff52a08e69145150a7e46c15c8ee79
https://doi.org/10.1006/bbrc.1998.8998
https://doi.org/10.1006/bbrc.1998.8998
Autor:
Michael J. Meredith, Larry D. Kerr, Douglas R. Spitz, Zhi-Qi Xu, Michael L. Freeman, Konjeti R. Sekhar, Syrus R. Soltaninassab
Publikováno v:
Biochemical and Biophysical Research Communications. 234:588-593
The gene GLCLC encodes the catalytic subunit of gamma-glutamylcysteine synthetase (glutamate-cysteine ligase E.C. 6.3.2.2), the rate limiting enzyme for glutathione synthesis. When HepG2 cells were exposed to the serine/threonine phosphatase inhibito
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4de49a8c9d804918ee6d9e4c6e1d4698
https://doi.org/10.1006/bbrc.1997.6697
https://doi.org/10.1006/bbrc.1997.6697
Publikováno v:
Biochemistry. 35:1212-1222
Proteins C1 and C2 together comprise about one-third the protein mass of mammalian core 40S heterogeneous nuclear ribonucleoprotein particles (40S hnRNP) and exist as heterotetramers of (C1)3C2. On the basis of nonequilibrium binding studies, it has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0bf73b38ad7469cf85660d94f7b1c49
https://doi.org/10.1021/bi951974k
https://doi.org/10.1021/bi951974k
Autor:
Hyun Cheol Shin, Emily K. Reinke, Cara J. Westmark, Pamela R. Westmark, James S. Malter, Syrus R. Soltaninassab
Publikováno v:
Neurobiology of aging. 27(6)
Overproduction of amyloid precursor protein (APP) and beta-amyloid likely contribute to neurodegeneration in Alzheimer's disease (AD). In an effort to understand neuronal APP gene regulation, we identified a 52 base element (52sce) immediately downst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d74fb0ec8852e56985df94d4944a9d4
https://pubmed.ncbi.nlm.nih.gov/16672170
https://pubmed.ncbi.nlm.nih.gov/16672170
Autor:
Michael J. Borrelli, Michael L. Freeman, Zhi-Qi Xu, Syrus R. Soltaninassab, Michael J. Meredith, Konjeti R. Sekhar, Frederick E. Domann
Publikováno v:
Biochemical and biophysical research communications. 270(1)
The majority of short- and long-lived cellular proteins are degraded by the activities of the 26S proteasome, a large multi-catalytic protease. Its unique function places it as a central regulatory activity for many important physiological processes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8481343d09c66ed3b7e9dc92997e34b
https://pubmed.ncbi.nlm.nih.gov/10733945
https://pubmed.ncbi.nlm.nih.gov/10733945
Publikováno v:
The Journal of biological chemistry. 273(33)
Based on UV cross-linking experiments, it has been reported that the C protein tetramer of 40 S heterogeneous nuclear ribonucleoprotein complexes specifically interacts with stem-loop I of U2 small nuclear RNA (snRNA) (Temsamani, J., and Pederson, T.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87f18eb66a559293b6785c0935602430
https://pubmed.ncbi.nlm.nih.gov/9694897
https://pubmed.ncbi.nlm.nih.gov/9694897