scispace - formally typeset
F

Francisca E. Reyes-Turcu

Researcher at Emory University

Publications -  14
Citations -  3432

Francisca E. Reyes-Turcu is an academic researcher from Emory University. The author has contributed to research in topics: Deubiquitinating enzyme & Ubiquitin. The author has an hindex of 13, co-authored 14 publications receiving 3117 citations. Previous affiliations of Francisca E. Reyes-Turcu include National Institutes of Health.

Papers
More filters
Journal ArticleDOI

Regulation and Cellular Roles of Ubiquitin-Specific Deubiquitinating Enzymes

TL;DR: A review of recent studies of the regulation of DUB activity and their roles in various cellular processes can be found in this paper, where the authors discuss ubiquitin-specific DUBs and some of the generalizations emerging from recent studies.
Journal ArticleDOI

Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains

TL;DR: Crystallized Lys 63‐linked and linear ubiquitin dimers are revealed, revealing that both adopt equivalent open conformations, forming no contacts between Ubiquitin molecules and thereby differing significantly from Lys 48‐linked ubiquitIn chains.
Journal ArticleDOI

The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin.

TL;DR: The crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitIn are reported, suggesting that binding the Ubiquitin C terminus may be necessary for the function of other proteins.
Journal ArticleDOI

RNA Elimination Machinery Targeting Meiotic mRNAs Promotes Facultative Heterochromatin Formation

TL;DR: These analyses uncover unexpected regulatory roles for mRNA-processing factors that assemble dynamic heterochromatin to modulate gene expression and show that their formation at meiotic genes requires factors that eliminate meiotic messenger RNAs (mRNAs) during vegetative growth.
Journal ArticleDOI

Mtr4-like protein coordinates nuclear RNA processing for heterochromatin assembly and for telomere maintenance.

TL;DR: A nuclear RNA-processing network in fission yeast with a core module comprising the Mtr4-like protein, Mtl1, and the zinc-finger protein, Red1 is described, revealing unique cellular strategies for recognizing regulatory RNAs and coordinating their functions in response to developmental and environmental cues.