Author
M. M. Moosa
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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2017-2023 · peak 2/yrCo-Author Collaboration Network
10 top collaborators · 16 mutual co-author links7 papers
Recent·Most cited
- BiophysicsbioRxivPreprintDOI 10.1101/2023.04.12.536623
- BiophysicsbioRxiv
FUS Oncofusion Protein Condensates Recruit mSWI/SNF Chromatin Remodelers via Heterotypic Interactions Between Prion-like Domains
R. B. Davis, T. Kaur, M. M. Moosa, P. R. Banerjee
This study shows FUS-DDIT3 oncofusion protein forms condensates that recruit SWI/SNF chromatin remodelers via PLD-PLD interactions, leading to transcriptional reprogramming.
DOI 10.1002/pro.4127 - BiophysicsbioRxiv
Programmable Viscoelasticity in Protein-RNA Condensates with Disordered Sticker-Spacer Polypeptides
I. Alshareedah, M. M. Moosa, M. Pham…·P. R. Banerjee
The paper investigates the viscoelastic properties of protein-RNA condensates formed by sticker-spacer polypeptides and shows how sequence composition tunes their mechanical behavior.
DOI 10.1038/s41467-021-26733-7 - BiophysicsbioRxiv
Phase Transition of RNA-protein Complexes into Ordered Hollow Condensates
I. Alshareedah, M. M. Moosa, M. Raju…·P. R. Banerjee
This study identifies a new phase of RNA-protein condensates forming hollow vesicles through phase separation, distinct from typical liquid droplets.
DOI 10.1073/pnas.1922365117 - BiophysicsbioRxiv
Interplay Between Short-range Attraction and Long-range Repulsion Controls Reentrant Liquid Condensation of Ribonucleoprotein-RNA Complexes
I. Alshareedah, T. Kaur, J. Ngo…·P. R. Banerjee
The paper investigates the molecular forces driving reentrant liquid condensation in RNP-RNA complexes, showing how short-range attractions and long-range repulsions control phase transitions.
DOI 10.1021/jacs.9b03689 - BiophysicsbioRxiv
Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates
T. Kaur, I. S. Alshareedah, W. Wang…·P. R. R. Banerjee
This study investigates how molecular crowding affects the physical properties of RNP condensates, showing they transition from liquid to gel-like states and that this is independent of LCD charge patterns.
DOI 10.3390/biom9020071 - BiophysicsbioRxiv
The N-terminal domain of ALS-linked TDP-43 assembles without misfolding
P. S. Tsoi, K. J. Choi, P. G. Leonard…·A. C. M. Ferreon
This study shows the N-terminal domain of TDP-43 can oligomerize under physiological conditions, potentially promoting pathological aggregation of the C-terminal domain in neurodegenerative diseases.
DOI 10.1002/anie.201706769