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of 4
pro vyhledávání: '"Jaydip Ghosh"'
Autor:
Dibyendu Samanta, Anindita Das, Jaydip Ghosh, Debasis Das, Arpita Bhattacharya, Chanchal Das Gupta
Publikováno v:
Journal of Biological Chemistry. 286:43771-43781
The peptidyl transferase center of the domain V of large ribosomal RNA in the prokaryotic and eukaryotic cytosolic ribosomes acts as general protein folding modulator. We showed earlier that one part of the domain V (RNA1 containing the peptidyl tran
Autor:
Debasis Das, Chanchal DasGupta, Anindita Das, Jaydip Ghosh, Dibyendu Samanta, Debashis Mukhopadhyay, Saheli Chowdhury, Arunima Basu, Saumen Pal, Arpita Bhattacharya
Publikováno v:
Journal of Bacteriology. 190:3344-3352
The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to
Autor:
Chanchal Das Gupta, Anindita Das, Arpita Bhattacharya, Dibyendu Samanta, Debasis Das, Arunima Basu, Jaydip Ghosh, Abhijit Chakrabarti
Publikováno v:
PLoS ONE, Vol 12, Iss 1, p e0170333 (2017)
PLoS ONE
PLoS ONE
Each cycle of translation initiation in bacterial cell requires free 50S and 30S ribosomal subunits originating from the post-translational dissociation of 70S ribosome from the previous cycle. Literature shows stable dissociation of 70S from model p
Autor:
Jaydip, Ghosh, Arunima, Basu, Saumen, Pal, Saheli, Chowdhuri, Arpita, Bhattacharya, Debashis, Pal, Dhruba K, Chattoraj, Chanchal, DasGupta
Publikováno v:
Molecular microbiology. 48(6)
Bacterial ribosomes or their 50S subunit can refold many unfolded proteins. The folding activity resides in domain V of 23S RNA of the 50S subunit. Here we show that ribosomes can also refold a denatured chaperone, DnaK, in vitro, and the activity ma