Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Murugan Selvam"'
Publikováno v:
Environmental Engineering and Management Journal. 22:305-319
Publikováno v:
Energy Sources, Part A: Recovery, Utilization, and Environmental Effects. 44:5508-5526
Biofuels are attracted by many investigators because of its environment friendly nature and contribution in the reduction of global warming. The advent of nanotechnology improved the performance of...
Publikováno v:
Biochimie. 176:85-102
Epigenetic modifications govern gene expression by guiding the human genome on 'what to express and what not to'. DNA methyltransferases (DNMTs) establish methylation patterns on DNA, particularly in CpG islands, and such patterns play a major role i
Autor:
Murugan Selvam, Venkateshwarlu Bandi, Saravanaraman Ponne, Cheemala Ashok, Sudhakar Baluchamy
Publikováno v:
Experimental cell research. 415(1)
The Polycomb Repressive Complex (PRC) proteins, EZH2 and EZH1 regulate many biological processes by generating the repressive H3K27me3 modifications in the chromatin. However, the factors that regulate the EZH1/EZH2 functions are poorly studied. We i
Autor:
Cheemala Ashok, Phani K Parcha, Murugan Selvam, Karuppiah Muruga Poopathi Raja, Sudhakar Baluchamy, Saravanaraman Ponne
Publikováno v:
Medical Oncology. 37
CREB signaling is known for several decades, but how it regulates both positive and negative regulators of cell proliferation is not well understood. On the other hand functions of major epigenetic repressors such as DNMT3B, EZH2 and CUL4B for their
Autor:
Sudhakar Baluchamy, Loudu Srijyothi, Cheemala Ashok, Murugan Selvam, Saravanaraman Ponne, Sheikh Owais
Publikováno v:
Medical Oncology. 36
CUL4A; an E3 ubiquitin ligase is involved in the degradation of negative regulators of cell cycle such as p21, p27, p53, etc., through polyubiquitination-mediated protein degradation. The functional role(s) of CUL4A proteins on their targets are well
Publikováno v:
Molecular and cellular biochemistry. 439(1-2)
In the cell, misfolded proteins are processed by molecular chaperone-mediated refolding or through ubiquitin-mediated proteosome system. Dysregulation of these mechanisms facilitates the aggregation of misfolded proteins and forms aggresomes in the j