Author
P. M. Seidler
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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2020-2024 · peak 2/yrCo-Author Collaboration Network
10 top collaborators · 36 mutual co-author links6 papers
Recent·Most cited
Selective inhibition of hsp90 paralogs: Uncovering the role of helix 1 in Grp94-selective ligand binding
N. L. S. Que, P. M. Seidler, W. J. Aw, G. Chiosis, D. T. Gewirth
This study investigates how Grp94-selective ligands bind to Grp94 and Hsp90 by analyzing structural changes and identifies helix 1 as a key determinant of selectivity.
bioRxiv · Jul 31, 2023Biochemistry
Improving the solubility of pseudo-hydrophobic Alzheimer's Disease medicinal chemicals through co-crystal formulation
A. Tse, I. Janilkarn-Urena, J. Lin, X. Chang, C. Efthymiou, A. Idrissova, M. Zhang, C. K. Williams, S. D. Magaki, H. V. Vinters, D. L. Davies, T. Gonen, H. Gukasyan, P. M. Seidler
This study shows that forming salts of dihydromyricetin (DHM) improves its solubility and inhibitory activity against Alzheimer's disease tau, suggesting potential for medicinal chemistry applications.
bioRxiv · Apr 25, 2023 · PreprintPharmacology & Toxicology
The SARS-CoV-2 nucleocapsid protein preferentially binds long and structured RNAs
C. E. Tai, E. Tayeb-Fligelman, S. Griner, L. Salwinski, J. T. Bowler, R. Abskharon, X. Cheng, P. M. Seidler, Y. X. Jiang, D. S. Eisenberg, F. Guo
This study investigates how SARS-CoV-2 nucleocapsid protein binds RNA, finding it preferentially interacts with structured and long RNAs, and proposes a mechanism linking packaging to RNA recognition.
bioRxiv · Dec 25, 2021 · PreprintBiochemistry
Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2
E. Tayeb-Fligelman, X. Cheng, C. Tai, J. T. Bowler, S. Griner, M. R. Sawaya, P. M. Seidler, Y. X. Jiang, J. Lu, G. M. Rosenberg, L. Salwinski, R. Abskharon, C.-T. Zee, K. Hou, Y. Li, , D. Eisenberg
The paper identifies amyloid-forming segments in SARS-CoV-2 Nucleoprotein and designs peptide inhibitors based on their atomic structures to target Covid-19.
bioRxiv · Mar 5, 2021 · PreprintBiochemistry
CryoEM reveals how the small molecule EGCG binds to AD brain-derived tau fibrils and initiates fibril disaggregation
P. M. Seidler, D. R. Boyer, M. R. Sawaya, P. Ge, A. Shin, M. A. DeTure, D. W. Dickson, L. Jiang, D. S. Eisenberg
This study uses cryoEM to determine how EGCG binds to AD tau fibrils and initiates their disaggregation by wedging into a cleft and causing charge repulsions.
bioRxiv · May 29, 2020 · PreprintBiochemistry