Author

V. Mullapudi

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Assay:proteomics· 4 Organism:human· 3 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Approach:comparative / phylogenetic analysis· 1 Organism:mouse· 1 Approach:statistical model· 1

Frequent Co-Authors

L. A. Joachimiak· 4 shared A. JoachimiakiD· 1 shared A. Wosztyl· 1 shared B. Nguyen· 1 shared B. T. Lanham· 1 shared C. Tesar· 1 shared D. Chen· 1 shared D. Fushman· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 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

4 shared papersBiophysics

L. A. Joachimiak

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Disease-associated patterns of acetylation stabilize tau fibril formation

L. Li, B. Nguyen, V. Mullapudi, L. Saelices, L. A. Joachimiak

This study identifies acetylation patterns that drive tau fibril formation and shows their structural and functional role in tauopathies.

bioRxiv · Jan 10, 2023Biophysics

FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

D. Chen, A. Wosztyl, V. Mullapudi, S. Bali, J. Vacquer-Alicea, S. Melhem, H. Seelaar, J. Van Swieten, M. I. Diamond, L. A. Joachimiak

This study investigates how the FTD-tau S320F mutation stabilizes local structure and promotes amyloid motif-dependent aggregation through allosteric effects.

bioRxiv · Aug 11, 2022 · PreprintBiophysics

Development of a new DHFR-based destabilizing domain with enhanced basal turnover and applicability in mammalian systems

E. Nakahara, V. Mullapudi, L. A. Joachimiak, J. D. Hulleman

The paper develops a new destabilizing domain (C12) with reduced basal levels and improved dynamic range, demonstrating its utility in regulating stress-responsive proteins.

bioRxiv · Jun 21, 2022Biochemistry

Dual domain recognition determines SARS-CoV-2 PLpro selectivity for human ISG15 and K48-linked di-ubiquitin

P. M. Wydorski, J. Osipiuk, B. T. Lanham, C. Tesar, M. Endres, E. Engle, R. Jedrzejczak, V. Mullapudi, K. Michalska, K. Fidelis, D. Fushman, A. Joachimiak, L. A. Joachimiak

This study identifies how SARS-CoV-2 PLpro selectively binds human ISG15 and K48-linked di-ubiquitin through dual domain recognition, revealing potential drug targets.

bioRxiv · Sep 15, 2021 · PreprintBiophysics