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Suparna Sanyal

Showing results (1-10 of 75) with videos related to

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Cancers|August 29, 2018
p53 Isoforms and Their Implications in CancerMaximilian Vieler, Suparna Sanyal
Viruses|October 25, 2014
Protein folding activity of the ribosome (PFAR) -- a target for antiprion compoundsDebapriya Banerjee, Suparna Sanyal
The Journal of Biological Chemistry|July 27, 2017
R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteria <i>Escherichia coli</i>Gürkan Korkmaz, Suparna Sanyal
Quarterly Reviews of Biophysics|March 27, 2019
The enigmatic ribosomal stalkAnders Liljas, Suparna Sanyal
Cancers|July 9, 2022
p53 Isoforms as Cancer Biomarkers and Therapeutic TargetsLiuqun Zhao, Suparna Sanyal
International Journal of Molecular Sciences|September 5, 2020
Ribosomal RNA Modulates Aggregation of the <i>Podospora</i> Prion Protein HET-sYanhong Pang, Petar Kovachev, Suparna Sanyal
The Journal of Biological Chemistry|April 22, 2021
GGQ methylation enhances both speed and accuracy of stop codon recognition by bacterial class-I release factorsShreya Pundir, Xueliang Ge, Suparna Sanyal
Elife|July 21, 2025
Δ133p53α and Δ160p53α isoforms of the tumor suppressor protein p53 exert dominant-negative effect primarily by co-aggregationLiuqun Zhao, Tanel Punga, Suparna Sanyal
Journal of Molecular Biology|April 14, 2010
The ribosomal stalk plays a key role in IF2-mediated association of the ribosomal subunitsChenhui Huang, Chandra Sekhar Mandava, Suparna Sanyal
The Journal of Biological Chemistry|September 14, 2014
Comprehensive analysis of stop codon usage in bacteria and its correlation with release factor abundanceGürkan Korkmaz, Mikael Holm, Tobias Wiens, et al.
Pageof 8

Showing results (1-10 of 75) with videos related to

Sort By:
Pageof 8
Cancers|August 29, 2018
p53 Isoforms and Their Implications in CancerMaximilian Vieler, Suparna Sanyal
Viruses|October 25, 2014
Protein folding activity of the ribosome (PFAR) -- a target for antiprion compoundsDebapriya Banerjee, Suparna Sanyal
The Journal of Biological Chemistry|July 27, 2017
R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteria <i>Escherichia coli</i>Gürkan Korkmaz, Suparna Sanyal
Quarterly Reviews of Biophysics|March 27, 2019
The enigmatic ribosomal stalkAnders Liljas, Suparna Sanyal
Cancers|July 9, 2022
p53 Isoforms as Cancer Biomarkers and Therapeutic TargetsLiuqun Zhao, Suparna Sanyal
International Journal of Molecular Sciences|September 5, 2020
Ribosomal RNA Modulates Aggregation of the <i>Podospora</i> Prion Protein HET-sYanhong Pang, Petar Kovachev, Suparna Sanyal
The Journal of Biological Chemistry|April 22, 2021
GGQ methylation enhances both speed and accuracy of stop codon recognition by bacterial class-I release factorsShreya Pundir, Xueliang Ge, Suparna Sanyal
Elife|July 21, 2025
Δ133p53α and Δ160p53α isoforms of the tumor suppressor protein p53 exert dominant-negative effect primarily by co-aggregationLiuqun Zhao, Tanel Punga, Suparna Sanyal
Journal of Molecular Biology|April 14, 2010
The ribosomal stalk plays a key role in IF2-mediated association of the ribosomal subunitsChenhui Huang, Chandra Sekhar Mandava, Suparna Sanyal
The Journal of Biological Chemistry|September 14, 2014
Comprehensive analysis of stop codon usage in bacteria and its correlation with release factor abundanceGürkan Korkmaz, Mikael Holm, Tobias Wiens, et al.
Pageof 8