Partha P. Datta
Indian Institute of Science Education and Research, Kolkata
35 Papers
137 Citations
Partha P. Datta is an academic researcher from Indian Institute of Science Education and Research, Kolkata. The author has contributed to research in topics: Translation (biology) & Initiation factor. The author has an hindex of 16, co-authored 35 publications. Previous affiliations of Partha P. Datta include Wadsworth Center & Indian Institute of Chemical Biology.
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Papers
Does Linezolid Cause Lactic Acidosis by Inhibiting Mitochondrial Protein Synthesis
Lluis Palenzuela,Noah M. Hahn,Robert Nelson,Janet N. Arno,Carol Schobert,Robert Bethel,Lisa A. Ostrowski,Manjuli R. Sharma,Partha P. Datta,Rajendra K. Agrawal,Jennifer E. Schwartz,Michio Hirano +11 more
TL;DR: Linezolid, an oxazolidinone antibiotic, inhibits bacterial protein synthesis by binding to 23S ribosomal RNA (rRNA) and genetic polymorphisms may have contributed to the toxicity in 2 patients.
A Single Mammalian Mitochondrial Translation Initiation Factor Functionally Replaces Two Bacterial Factors
Rahul Gaur,Domenick Grasso,Partha P. Datta,P. D. V. Krishna,Gautam Das,Angela C. Spencer,Rajendra K. Agrawal,Rajendra K. Agrawal,Linda L. Spremulli,Umesh Varshney +9 more
TL;DR: It is shown that bovine mitochondrial IF2 (IF2(mt)) complements E. coli containing a deletion of the IF2 gene (E. coli DeltainfB) and provides strong evidence that a single factor in mammalian mitochondria performs the functions of two eubacterial factors, IF1 and IF2.
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Interaction of the G' domain of elongation factor G and the C-terminal domain of ribosomal protein L7/L12 during translocation as revealed by cryo-EM.
Partha P. Datta,Manjuli R. Sharma,Li Qi,Li Qi,Joachim Frank,Joachim Frank,Rajendra K. Agrawal,Rajendra K. Agrawal +7 more
TL;DR: Molecular analyses of the cryo-EM maps show that three structural components participate in formation of the ALC, and that both EF-G and the ribosomal protein L7/L12 undergo large conformational changes to form the A LC.
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Insertion domain within mammalian mitochondrial translation initiation factor 2 serves the role of eubacterial initiation factor 1.
Aymen S. Yassin,Md. Emdadul Haque,Partha P. Datta,Partha P. Datta,K. Elmore,Nilesh K. Banavali,Nilesh K. Banavali,Linda L. Spremulli,Rajendra K. Agrawal,Rajendra K. Agrawal +9 more
TL;DR: The finding suggests that the insertion domain of IF2mt mimics the function of eubacterial IF1, by blocking the ribosomal aminoacyl-tRNA binding site (A site) at the initiation step.
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Cold Shock Response and Major Cold Shock Proteins of Vibrio cholerae
Partha P. Datta,Rupak K. Bhadra +1 more
TL;DR: The results suggest that V. cholerae may use an alternative pathway for regulation of gene expression during cold shock, and this promoter is an exception compared to other promoters of cold shock-inducible genes of different organisms, including Escherichia coli.
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