Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Smitha Padmanabha"'
Publikováno v:
Biochemical and Biophysical Research Communications. 529:425-431
Background: Loss of a-crystallin chaperone function results in the lens protein aggregation leading to cataract. In this study, we evaluated the efficacy of micellar lutein with different fatty acids in modulating a-crystallin chaperone function unde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8bd470983e9b2b70dbffe768944d478
https://doi.org/10.1016/j.bbrc.2020.06.021
https://doi.org/10.1016/j.bbrc.2020.06.021
Publikováno v:
Biochemical and Biophysical Research Communications. 530:611
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82da366015495ef970f59df984398f81
https://doi.org/10.1016/j.bbrc.2020.06.080
https://doi.org/10.1016/j.bbrc.2020.06.080
Autor:
Marcus A. Glomb, Maneesh Mailankot, Ram H. Nagaraj, Smitha Padmanabha, Mikhail Linetsky, Magdalena Staniszewska, Liew Jun Mun
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1804:829-838
Human lens proteins (HLP) become chemically modified by kynurenines and advanced glycation end products (AGEs) during aging and cataractogenesis. We investigated the effects of kynurenines on AGE synthesis in HLP. We found that incubation with 5 mM r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16081af08ce19584b566c2bf9b17efd4
https://doi.org/10.1016/j.bbapap.2009.12.008
https://doi.org/10.1016/j.bbapap.2009.12.008
Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin
Autor:
Ashis Biswas, Ram H. Nagaraj, Puttur Santhoshkumar, Sandip Kumar Nandi, Rooban B. Nahomi, Smitha Padmanabha, Rong Huang, Benlian Wang, Slawomir Filipek
Publikováno v:
Biochemistry. 52(45)
αB-Crystallin is a chaperone and an anti-apoptotic protein that is strongly expressed in many tissues, including the lens, retina, heart, and kidney. In the human lens, several lysine residues in αB-crystallin are acetylated. We have previously sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e590e57177622f80d636b2666a19ca04
https://pubmed.ncbi.nlm.nih.gov/24128140
https://pubmed.ncbi.nlm.nih.gov/24128140
Autor:
Monika Pischetsrieder, Trilok J. Parmar, S.R. Kaid Johar, Ram H. Nagaraj, Smitha Padmanabha, Mikhail Linetsky, Abhay R. Vasavada, Jasmin Meltretter
Dideoxyosones (DDOs) are intermediates in the synthesis of advanced glycation end products (AGEs), such as pentosidine and glucosepane. Although the formation of pentosidine and glucosepane in the human lens has been firmly established, the formation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d2cd8f5f7a11e3ad557119b0d0fc47a
https://europepmc.org/articles/PMC3172345/
https://europepmc.org/articles/PMC3172345/
Autor:
Mikhail Linetsky, Nagarekha Pasupuleti, Rooban B. Nahomi, Alok Kumar Panda, Ashis Biswas, Smitha Padmanabha, Puttur Santhoshkumar, Ram H. Nagaraj, Shilpa Shanthakumar, Benlian Wang
Publikováno v:
Biochimica et biophysica acta. 1822(2)
α-Crystallin is a major protein in the human lens that is perceived to help to maintain the transparency of the lens through its chaperone function. In this study, we demonstrate that many lens proteins including αA-crystallin are acetylated in viv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::778087994999eb3cb9c65dfff04a898a
https://pubmed.ncbi.nlm.nih.gov/22120592
https://pubmed.ncbi.nlm.nih.gov/22120592
Autor:
Smitha Padmanabha, Puttur Santhoshkumar, Ram H. Nagaraj, Mahesha Gangadhariah, Nagarekha Pasupuleti
Publikováno v:
Journal of cellular biochemistry. 110(2)
The small heat shock protein Hsp27 is a molecular chaperone and an anti-apoptotic protein. Human Hsp27 has one cysteine residue at position 137. We investigated the role of this cysteine residue in the chaperone and anti-apoptotic functions of Hsp27
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c2b930e5d6615a29fbf605c7f99522f
https://pubmed.ncbi.nlm.nih.gov/20225272
https://pubmed.ncbi.nlm.nih.gov/20225272
Autor:
Nagarekha Pasupuleti, Ram H. Nagaraj, Smitha Padmanabha, Maneesh Mailankot, Denice L. Major, Scott Howell
Publikováno v:
Biogerontology. 10(6)
Glyoxalase I (GLOI) is the first enzyme of the glyoxalase system that catalyzes the metabolism of reactive dicarbonyls, such as methylglyoxal (MGO). During aging and cataract development, human lens proteins are chemically modified by MGO, which is l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a8746e2f2f2ad28bf9ae6495ceccc97
https://pubmed.ncbi.nlm.nih.gov/19238574
https://pubmed.ncbi.nlm.nih.gov/19238574