Author

B. A. Nguyen

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Research Focus:protein folding & dynamics· 2 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1

Frequent Co-Authors

L. Saelices· 2 shared P. Singh· 2 shared R. Pedretti· 2 shared S. Afrin· 2 shared V. Singh· 2 shared A. Javed· 1 shared A. Lemoff· 1 shared A. T. Balana· 1 shared

Activity by Year

2022-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 39 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 papersBiophysics

L. Saelices

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Cryo-EM confirms a common fibril fold in the heart of four patients with ATTRwt amyloidosis

B. A. Nguyen, V. Singh, S. Afrin, P. Singh, M. Pekala, Y. Ahmed, R. Pedretti, J. Canepa, A. Lemoff, B. Kluve-Beckerman, P. Wydorski, F. Chhapra, L. Saelices

The paper uses cryo-EM to show that cardiac ATTRwt amyloid fibrils from four patients are structurally identical, supporting their consistent clinical presentation.

bioRxiv · Mar 8, 2024Biophysics

O-GlcNAc modification forces the formation of an α-Synuclein amyloid-strain with notably diminished seeding activity and pathology

A. T. Balana, A.-L. Mahul-Mellier, B. A. Nguyen, M. Horvath, A. Javed, E. R. Hard, Y. Jasiqi, P. Singh, S. Afrin, R. Pedretti, V. Singh, V. M.-Y. Lee, K. C. Luk, L. Saelices, H. A. Lashuel, M. R. Pratt

This study shows that O-GlcNAc modification of α-Synuclein leads to amyloid fibrils with reduced seeding activity and pathology in Parkinson's disease models.

bioRxiv · Mar 7, 2023 · PreprintBiochemistry

Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation

R. Abskharon, M. R. Sawaya, D. R. Boyer, Q. Cao, B. A. Nguyen, D. Cascio, D. S. Eisenberg

The paper presents a cryo-EM structure of RNA-bound tau fibrils, revealing a small C-terminal core that may nucleate fibril formation and is essential for fibril integrity.

bioRxiv · Jan 28, 2022Biophysics