Publications

Featured

1. Brindhavanam PT, Sahu I*. Decoding the ubiquitin landscape by cutting-edge ubiquitinomic approaches. Biochemical Society Transactions. Apr 2024; 52(2):627-637. [* Corresponding Author]. See publication

2. Sahoo M.P#, Levi T#, Cohen N, Sahu I, Kleifeld O*. Activity-Guided Proteomic Profiling of Proteasomes Uncovers a Variety of Active (and Inactive) Proteasome species. Molecular & Cellular Proteomics. March 2024, Vol. 23 (3), 100728. See publication

3. Sahu I, Zhu He, Buhrlage Sara*, Marto Jarrod A*. Proteomic approaches to study ubiquitinomics. Biochimica et Biophysica Acta - Gene Regulatory Mechanisms. June 2023, Vol.1866 (2), 194940. See publication

4. Sahu I#*, Bajorek M#, Osmulski P, Krutauz D, Reis N, Gaczynska M, Glickman M.H*. A unique role for the N-terminus of the alpha-2 subunit in aiding substrate translocation into the catalytic core of the proteasome. Biomolecules. 2023, 3(3), 480. [* Corresponding Author, # Equal Contribution]. See publication

5. Sahu I*, Sahoo M.P, Kleifeld O*, Glickman M.H*. Isolation of Proteasome-Trapped Peptides (PTPs) for degradome analysis. Methods in Molecular Biology. 2023, 2602: 229–241. [* Corresponding Author]. See publication

6. Sahu I, Mali S.M, Sulkshane P, Morag R, Xu C, Rozenberg A, Sahoo M.P, Singh S.K, Ding Z, Wang Y, Day S, Cong Y, Kleifeld O*, Brik A*, Glickman M.H*. The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag. Nature Communications 2021, 12, 6173. See publication.Featured article on Editors’ Highlights webpage https://www.nature.com/collections/hhfigaahch

7. Sahu I* and Glickman M.H*. “Proteasome in action” – Substrate degradation by the 26S proteasome. Biochemical Society Transactions 2021, 49 (2): 629–644. [* Corresponding Author]. See publication

8. Sahu I* and Glickman, M.H*. Structural insights into substrate recognition and processing by the 20S Proteasome. Biomolecules 2021, 11(2), 148. [* Corresponding Author]. See publication

9. Tiwari R, Ganguli N, Alam H, Sahu I, Vadivel C, Sinha S, Patel S, Jamghare S, Bane S, Thorat R, Manjumdar, Vaidya M.M*. Generation of tissue specific transgenic model for K8 phosphomutants: A tool to investigate the role of K8 phosphorylation during skin carcinogenesis in vivo. Cell Biol Int. 2021, 45 (8), 1720-1732. See publication

10. Sahu I, Nanaware Padma, Mane M, Mulla W.S, Roy S, and Venkatraman P*. Role of a 19S Proteasome Subunit-      PSMD10/Gankyrin in Neurogenesis of human Neural Progenitor Cells. International Journal of Stem cells. (2019) Vol. 12, (3), 463-473. See publication

11. Ding Z, Xu C, Sahu I, Wang Y, Fu Z, Huang M, Wong C. C. L, Glickman M.H*, Cong Y*. Structural snapshots of 26S proteasome reveal tetraubiquitin-induced conformations. Molecular Cell. (2019) Vol. 73 (6), 1150-1161. See publication

12. Tiwari R, Sahu I, Soni B, Sathe G.J, Thapa P, Patel P, Sinha S, Vadivel C.K, Patel S, Oak S, Thorat R, Gowda H, and Vaidya M.M*. Depletion of Keratin 8/18 modulate oncogenic potential of A431 cells by governing multiple signaling pathways. FEBS J. (2018) Vol. 285(7):1251-1276. See publication

13. Tiwari R, Sahu I, Soni B, Sathe G.J, Datta K.K, Thapa P, Dhaka B, Sinha S, Gowda H, and Vaidya M.M*. Quantitative phosphoproteomic analysis reveals system-wide signaling pathways regulated by site-specific phosphorylation on Keratin-8 in skin squamous cell carcinoma derived cell line. Proteomics. (2017) Vol. 17, Issue 7. See publication. [Inside Front Cover: See front cover]

14. Sahu I#, Singh S.K#, Mali S.M, Hemantha H.P, Kleifeld O, Glickman M.H*, and Brik A*. Synthetic uncleavable ubiquitinated proteins dissect proteasome deubiquitination and degradation and highlight distinctive fate of tetraubiquitin. J. Am. Chem. Soc. (2016) Vol. 138, 16004−16015. [# Equal Contribution]. See publication

15. Hjerpe R, Bett J.S, Keuss M.J, Solovyova A, McWilliams T.G, Johnson C, Sahu I, Varghese J, Wood N, Wightman M, Osbourne G, Bates G.P, Glickman M.H, Trost M, Knebel A, Marchesi F, and Kurz T*. UBQLN2 connects the proteasome with the HSP70 system to promote autophagy-independent protein aggregate clearance. Cell. (2016) Vol. 166 (4), 935-949. See publication

16. Sahu I, Sangith N, Ramteke M, Gadre R, Venkatrama P*. A novel role for the proteasomal chaperone PSMD9 and hnRNPA1 in enhancing IκBα degradation and NF-κB activation – functional relevance of predicted PDZ domain–motif interaction. FEBS J. (2014) Vol. 281 (11), 2688-2709. See publication

17. Sangith N, Srinivasaraghavan K, Sahu I, Desai A, Medipally S, Somavarappu A.K, Verma C, Venkatraman P*. Discovery of novel interacting partners of PSMD9, a proteasomal chaperone: Role of an Atypical and versatile PDZ-domain motif interaction and identification of putative functional modules. FEBS Openbio. (2014) Vol. 4, 571–583. See publication