scispace - formally typeset
S

Shanaya Shital Shah

Researcher at University of California, Davis

Publications -  8
Citations -  553

Shanaya Shital Shah is an academic researcher from University of California, Davis. The author has contributed to research in topics: Homologous recombination & DNA repair. The author has an hindex of 4, co-authored 8 publications receiving 373 citations. Previous affiliations of Shanaya Shital Shah include Indian Institute of Science.

Papers
More filters
Journal ArticleDOI

Homologous recombination and the repair of DNA Double-Strand Breaks

TL;DR: The DNA transactions and enzymatic activities required for this elegantly orchestrated process in the context of the repair of DNA double-strand breaks in somatic cells are discussed.
Journal ArticleDOI

Dynamic Processing of Displacement Loops during Recombinational DNA Repair.

TL;DR: A versatile assay for the physical detection of D-loops in vivo is developed, which enabled studying the kinetics of their formation and defining the activities controlling their metabolism, uncovers a layer of quality control of HR relying on nascent D-loop dynamics.
Journal ArticleDOI

Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6

TL;DR: It is demonstrated that Scd6 gets arginine methylated at its RGG-motif and Hmt1 plays an important role in its methylation, and it is proposed that arginin methylation of translation repressors with RGG -motif could be a general modulator of their repression activity.
Journal ArticleDOI

Arginine methylation augments Sbp1 function in translation repression and decapping

TL;DR: It is reported that Sbp1 is arginine‐methylated in an hnRNP methyl transferase (Hmt1)‐dependent manner and that methylation is enhanced upon glucose deprivation and suggested that arginin methylation modulates Sbp 1 role in mRNA fate determination.
Journal ArticleDOI

Rdh54/Tid1 inhibits Rad51-Rad54-mediated D-loop formation and limits D-loop length

TL;DR: It is shown that Rdh54/Tid1 inhibits D-loop formation by Rad51 and Rad54 in an ATPase-independent manner, and uniquely restricts the length of Rad51-Rad54-mediated D-loops.