Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Venkata Pulla Rao, Vendra"'
Autor:
Venkata Pulla Rao Vendra, Christian Ostrowski, Rebecca Clark, Marzena Dyba, Sergey G. Tarasov, J. Fielding Hejtmancik
Publikováno v:
Biochemistry.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::047782d446680235ad7b951c4bd0b0a8
https://doi.org/10.1021/acs.biochem.2c00628
https://doi.org/10.1021/acs.biochem.2c00628
Autor:
Venkata Pulla Rao Vendra
Publikováno v:
Journal of Biosciences. 48
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::823365eecd2ecc8f05bdf094c579571b
https://doi.org/10.1007/s12038-023-00330-w
https://doi.org/10.1007/s12038-023-00330-w
Autor:
Venkata Pulla Rao Vendra, Garima Agarwal, Sushil Chandani, Venu Talla, Narayanaswamy Srinivasan, Dorairajan Balasubramanian
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e70336 (2013)
BACKGROUND: We highlight an unrecognized physiological role for the Greek key motif, an evolutionarily conserved super-secondary structural topology of the βγ-crystallins. These proteins constitute the bulk of the human eye lens, packed at very hig
Externí odkaz:
https://doaj.org/article/b9675a72f016481694a7f0eba7b1cdd6
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e51401 (2012)
BACKGROUND: Human γS-crystallin is an important component of the human eye lens nucleus and cortex. The mutation V42M in the molecule causes severe congenital cataract in children. We compare the structure of the mutant protein with that of the wild
Externí odkaz:
https://doaj.org/article/7f98499d3c2e40968368c8514a6d3c4e
Autor:
Venkata Pulla Rao Vendra, Ismail Khan, Sushil Chandani, Anbukkarasi Muniyandi, Dorairajan Balasubramanian
Publikováno v:
Biochimica et biophysica acta. 1860(1 Pt)
Background Protein crystallins co me in three types (α, β and γ) and are found predominantly in the eye, and particularly in the lens, where they are packed into a compact, plastic, elastic, and transparent globule of proper refractive power range
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c55110ea01b8890bd87974dd1592e8ec
https://pubmed.ncbi.nlm.nih.gov/26116913
https://pubmed.ncbi.nlm.nih.gov/26116913
Publikováno v:
Cornea. 34(6)
PURPOSE To investigate the effect of mutations in SLC4A11 on cellular localization of the protein, mitochondrial function, and apoptosis due to oxidative stress. Mutations in SLC4A11 have been associated with 2 different forms of corneal endothelial
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::347189f2fb199188d4e41d0eb4b1bcf5
https://pubmed.ncbi.nlm.nih.gov/25811729
https://pubmed.ncbi.nlm.nih.gov/25811729
Autor:
Srinivasu, Karri, Ramesh Babu, Kasetti, Venkata Pulla Rao, Vendra, Sushil, Chandani, Dorairajan, Balasubramanian
Publikováno v:
Molecular Vision
Purpose To analyze the protein structural features responsible for the aggregation properties of the mutant protein D26G human γS-crystallin (HGSC) associated with congenital Coppock-type cataract. Methods cDNAs of wild-type (WT) and D26G mutant HGS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fa71f81c7ca757b24f19dfe48f5e8c8d
https://pubmed.ncbi.nlm.nih.gov/23761725
https://pubmed.ncbi.nlm.nih.gov/23761725
Autor:
Narayanaswamy Srinivasan, Garima Agarwal, Dorairajan Balasubramanian, Venu Talla, Sushil Chandani, Venkata Pulla Rao Vendra
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e70336 (2013)
PLoS ONE
PLoS ONE
Background: We highlight an unrecognized physiological role for the Greek key motif, an evolutionarily conserved super-secondary structural topology of the beta gamma-crystallins. These proteins constitute the bulk of the human eye lens, packed at ve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da759235a34bde27ae634db9efc8c7b1
http://eprints.iisc.ernet.in/47520/
http://eprints.iisc.ernet.in/47520/
