Author

A. C. Thwin

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

Biology Disciplines

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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 2 Research Focus:chromatin & epigenetic regulation· 2 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Approach:statistical model· 2 Assay:structural biology· 2

Frequent Co-Authors

D. R. Southworth· 4 shared E. Tse· 3 shared A. Aimon· 1 shared A. Dias· 1 shared A. Douangamath· 1 shared A. E. Cohen· 1 shared A. J. Powell· 1 shared A. L. Lucius· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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4 shared papersBiochemistry

D. R. Southworth

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Author profile →

5 papers

Recent·Most cited

Phosphorylation of a Cleaved Tau Proteoform at a Single Residue Inhibits Binding to the E3 Ubiquitin Ligase, CHIP

C. M. Nadel, K. Wucherer, A. Oehler, A. C. Thwin, K. Basu, M. D. Callahan, D. R. Southworth, D. A. Mordes, C. S. Craik, J. E. Gestwicki

This study identifies phosphorylation at residue S416 on tauC3 as a mechanism that inhibits its degradation by CHIP, contributing to its accumulation in Alzheimer's disease.

bioRxiv · Aug 16, 2023 · PreprintBiochemistry

The p97/VCP adapter UBXD1 drives AAA+ remodeling and ring opening through multi-domain tethered interactions

J. R. Braxton, C. R. Altobelli, M. R. Tucker, E. Tse, A. C. Thwin, M. R. Arkin, D. R. Southworth

This study identifies UBXD1 as a p97 ATPase inhibitor and shows how its domains induce structural remodeling and ring opening of the p97 hexamer.

bioRxiv · May 15, 2023 · PreprintBiochemistry

Structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client-maturation state

K. Lee, A. C. Thwin, E. Tse, S. N. Gates, D. R. Southworth

The paper determines the cryo-EM structure of the Hsp90:FKBP51:p23 complex, revealing how cochaperones recognize Hsp90 during client maturation.

bioRxiv · Jan 21, 2021Biophysics

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry

Conformational Plasticity of the ClpAP AAA+ Protease Couples Protein Unfolding and Proteolysis

K. E. Lopez, A. N. Rizo, E. Tse, J. Lin, N. W. Scull, A. C. Thwin, A. L. Lucius, J. Shorter, D. R. Southworth

This study determines high-resolution structures of E. coli ClpAP complex in substrate-bound states to elucidate the mechanism of protein unfolding and proteolysis coupling.

bioRxiv · Oct 29, 2019Biophysics