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Aishwarya Kanchi Ranganath
Researcher at Rutgers University
Publications - 4
Citations - 237
Aishwarya Kanchi Ranganath is an academic researcher from Rutgers University. The author has contributed to research in topics: Intrinsically disordered proteins & Protein domain. The author has an hindex of 3, co-authored 3 publications receiving 95 citations.
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Journal ArticleDOI
Identifying sequence perturbations to an intrinsically disordered protein that determine its phase-separation behavior
Benjamin S. Schuster,Gregory L. Dignon,Gregory L. Dignon,Wai Shing Tang,Fleurie M. Kelley,Aishwarya Kanchi Ranganath,Craig N. Jahnke,Alison G. Simpkins,Roshan Mammen Regy,Daniel A. Hammer,Matthew C. Good,Jeetain Mittal +11 more
TL;DR: This work explores a model protein, the disordered N-terminal domain of LAF-1, and highlights how three key features of the sequence control the protein’s propensity to phase-separate, and identifies a region of the RGG domain that has high contact probability and is highly conserved between species; deletion of this region significantly disrupts phase separation in vitro and in vivo.
Posted ContentDOI
Identifying Sequence Perturbations to an Intrinsically Disordered Protein that Determine Its Phase Separation Behavior
Benjamin S. Schuster,Benjamin S. Schuster,Gregory L. Dignon,Gregory L. Dignon,Wai Shing Tang,Fleurie M. Kelley,Aishwarya Kanchi Ranganath,Craig N. Jahnke,Alison G. Simpkins,Roshan Mammen Regy,Daniel A. Hammer,Matthew C. Good,Jeetain Mittal +12 more
TL;DR: A model protein, the disordered N-terminal domain of LAF-1, is explored, and it is found that phase behavior of this model IDP is dictated by the presence of a short conserved domain, charge patterning, and arginine-tyrosine interactions.
Journal ArticleDOI
Biomolecular Condensates: Sequence Determinants of Phase Separation, Microstructural Organization, Enzymatic Activity, and Material Properties
Benjamin S. Schuster,Roshan Mammen Regy,Elliott M Dolan,Aishwarya Kanchi Ranganath,Nina Jovic,Sagar D. Khare,Zheng Shi,Jeetain Mittal +7 more
TL;DR: A recent perspective article as mentioned in this paper highlights recent progress and emerging challenges in understanding the formation and function of membraneless organelles (MLOs) and provides many examples to highlight the richness of the observed behavior and potential research directions for improving mechanistic understanding.
Posted ContentDOI
Heterotypic interactions in the dilute phase can drive co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex
TL;DR: In this paper , disordered low-complexity domains of multiple SWI/SNF subunits are shown to be prion-like with a strong propensity to undergo intracellular phase separation.