Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Puttur Santhoshkumar"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The G98R mutation in αA-crystallin is associated with presenile cataract development in humans. Previous studies have indicated that mutant proteins altered structure, decreased stability, increased oligomeric size, loss of chaperone-like activity,
Externí odkaz:
https://doaj.org/article/51bfb1b74cb84572bf38e90d6c2d0c07
Publikováno v:
PLoS ONE, Vol 8, Iss 6, p e65610 (2013)
Cataract is characterized by progressive protein aggregation and loss of vision. α-Crystallins are the major proteins in the lens responsible for maintaining transparency. They exist in the lens as highly polydisperse oligomers with variable numbers
Externí odkaz:
https://doaj.org/article/d2d668099d0140d8a7dae8283047cebd
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e44077 (2012)
A substitution mutation in human αA-crystallin (αAG98R) is associated with autosomal dominant cataract. The recombinant mutant αAG98R protein exhibits altered structure, substrate-dependent chaperone activity, impaired oligomer stability and aggre
Externí odkaz:
https://doaj.org/article/6bf238bc46ec4602bc167495e5d5d10b
Autor:
Ram H Nagaraj, Alok Kumar Panda, Shilpa Shanthakumar, Puttur Santhoshkumar, NagaRekha Pasupuleti, Benlian Wang, Ashis Biswas
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e30257 (2012)
Methylglyoxal (MGO) is an α-dicarbonyl compound present ubiquitously in the human body. MGO reacts with arginine residues in proteins and forms adducts such as hydroimidazolone and argpyrimidine in vivo. Previously, we showed that MGO-mediated modif
Externí odkaz:
https://doaj.org/article/2435bbd880f34e0daada30c99aa26019
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e19291 (2011)
The eye lens is composed of fiber cells that are filled with α-, β- and γ-crystallins. The primary function of crystallins is to maintain the clarity of the lens through ordered interactions as well as through the chaperone-like function of α-cry
Externí odkaz:
https://doaj.org/article/d49a9ed3fed243f59df069aff4435310
Autor:
Sundararajan Mahalingam, Goutham Shankar, Brian P. Mooney, Kamal Singh, Puttur Santhoshkumar, Krishna K. Sharma
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 1099, p 1099 (2022)
International Journal of Molecular Sciences; Volume 23; Issue 3; Pages: 1099
International Journal of Molecular Sciences; Volume 23; Issue 3; Pages: 1099
Smaller oligomeric chaperones of α-crystallins (αA- and αB-) have received increasing attention due to their improved therapeutic potential in preventing protein aggregating diseases. Our previous study suggested that deleting 54–61 residues fro
Publikováno v:
Biochemistry
The G98R mutation in αA-crystallin is associated with the onset of pre-senile cataract and is characterized biochemically by an increased oligomeric mass, altered chaperone function, and loss of structural stability over time. Thus far, it is not kn
Autor:
K. Krishna Sharma, Peter F. Kador, Ashutosh S. Phadte, Marjorie F. Lou, Puttur Santhoshkumar, Damian M. Daszynski, Haizhen A. Zhong
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports
Scientific Reports
The paradigm that cataracts are irreversible and that vision from cataracts can only be restored through surgery has recently been challenged by reports that oxysterols such as lanosterol and 25-hydroxycholesterol can restore vision by binding to αB
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 19
International Journal of Molecular Sciences, Vol 22, Iss 10771, p 10771 (2021)
Volume 22
Issue 19
International Journal of Molecular Sciences, Vol 22, Iss 10771, p 10771 (2021)
Previously, we showed that the removal of the 54–61 residues from αB-crystallin (αBΔ54–61) results in a fifty percent reduction in the oligomeric mass and a ten-fold increase in chaperone-like activity. In this study, we investigated the oligo
Publikováno v:
Molecular Vision
Purpose The G98R mutant of αA-crystallin is associated with the development of presenile cataracts. In vitro, the recombinant mutant protein exhibits altered structural and functional characteristics, along with the propensity to aggregate by itself