Author

S. S. Paul

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Assay:proteomics· 2 Organism:bacteria (other)· 1 Approach:biophysical modeling· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Bracher· 1 shared A. Lyons· 1 shared F. U. Hartl· 1 shared H. Wang· 1 shared J. Sengupta· 1 shared K. Chattopadhyay· 1 shared M. Hayer-Hartl· 1 shared M. T. Woodside· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 14 mutual co-author links

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1 shared paperBiochemistry

A. Bracher

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Author profile →

3 papers

Recent·Most cited

Quantifying oligomer populations in real time during protein aggregation using single-molecule mass photometry

S. S. Paul, A. Lyons, R. Kirchner, M. T. Woodside

This study uses single-molecule mass photometry to track oligomer populations during protein aggregation, revealing kinetic models and rate constants for tau protein aggregation.

bioRxiv · Jun 15, 2022Biophysics

Structure and conformational cycle of a bacteriophage-encoded chaperonin

M. Hayer-Hartl, A. Bracher, S. S. Paul, H. Wang, N. Wischnewski, F. U. Hartl

This study characterizes the structure and conformational cycle of the bacteriophage-encoded chaperonin gp146 (φEL), showing it functions in aggregation prevention without substrate encapsulation.

bioRxiv · Feb 24, 2020Biochemistry

Heme minimizes Parkinson’s disease-associated toxicity by inducing a conformational distortion in the oligomers of alpha-Synuclein

R. Chakraborty, S. Dey, S. S. Paul, P. Sil, J. Sengupta, K. Chattopadhyay

This study shows heme reduces alpha-Synuclein toxicity by altering its oligomer structure, preventing harmful fibril formation.

bioRxiv · May 7, 2019 · PreprintBiophysics