Author

Nadya I. Tarasova

National Cancer InstituteORCID 0000-0002-4949-0069Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Organism:human· 2 Research Focus:drug response / drug discovery· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:proteomics· 1

Frequent Co-Authors

Kylie J. WaltersiD· 2 shared Raj ChariiD· 2 shared Sergey G. TarasoviD· 2 shared Xiang CheniD· 2 shared Þorkell AndréssoniD· 2 shared Bao Quoc TraniD· 1 shared Caroline FromontiD· 1 shared Charles D. SchwietersiD· 1 shared

Activity by Year

2020-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 41 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

2 shared papersMolecular Biology

Kylie J. WaltersORCID

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma

Xiuxiu Lu, Venkata R. Sabbasani, Vasty Osei Amponsa, Christine N. Evans, Julianna C. King, Sergey G. Tarasov, Marzena Dyba, Sudipto Das, King C. Chan, Charles D. Schwieters, Sulbha Choudhari, Caroline Fromont, Yongmei Zhao, Bao Quoc Tran, Xiang Chen, , Kylie J. Walters

The paper identifies a chemical scaffold targeting hRpn13, revealing a DEUBAD-lacking isoform upregulated in multiple myeloma and demonstrating its potential as a therapeutic target.

Nature Communications · Dec 16, 2021Peer-reviewedMolecular Biology

Structure of E3 ligase E6AP with a novel proteasome-binding site provided by substrate receptor hRpn10

Gwen R. Buel, Xiang Chen, Raj Chari, Maura J. O’Neill, Danielle L. Ebelle, Conor Jenkins, Vinidhra Sridharan, Sergey G. Tarasov, Nadya I. Tarasova, Þorkell Andrésson, Kylie J. Walters

The paper identifies a novel proteasome-binding site in E6AP mediated by hRpn10, showing E6AP's unique interaction with the proteasome for substrate ubiquitination.

Nature Communications · Mar 10, 2020Peer-reviewedMolecular Biology