scispace - formally typeset
D

Diego Acosta-Alvear

Researcher at University of California, Santa Barbara

Publications -  41
Citations -  3815

Diego Acosta-Alvear is an academic researcher from University of California, Santa Barbara. The author has contributed to research in topics: Unfolded protein response & Endoplasmic reticulum. The author has an hindex of 21, co-authored 36 publications receiving 3093 citations. Previous affiliations of Diego Acosta-Alvear include Howard Hughes Medical Institute & University of California, San Francisco.

Papers
More filters
Journal ArticleDOI

XBP1 Controls Diverse Cell Type- and Condition-Specific Transcriptional Regulatory Networks

TL;DR: A core group of genes involved in constitutive maintenance of ER function in all cell types and tissue- and condition-specific targets are identified and a cadre of unexpected targets that link XBP1 to neurodegenerative and myodegenerative diseases, as well as to DNA damage and repair pathways are identified.
Journal ArticleDOI

Opposing unfolded-protein-response signals converge on death receptor 5 to control apoptosis.

TL;DR: It is reported that unmitigated ER stress promoted apoptosis through cell-autonomous, UPR-controlled activation of death receptor 5 (DR5), which integrates opposing UPR signals to couple ER stress and apoptotic cell fate.
Journal ArticleDOI

An initial blueprint for myogenic differentiation

TL;DR: It is found that MRFs play an unexpectedly wide-ranging role in directing the assembly and usage of the neuromuscular junction and these factors also prepare myoblasts to respond to diverse types of stress.
Journal ArticleDOI

The Unfolded Protein Response: Detecting and Responding to Fluctuations in the Protein-Folding Capacity of the Endoplasmic Reticulum

TL;DR: Recent developments in the field that have provided new insights into the ER stress-sensing mechanisms used by UPR sensors and the mechanisms by which they integrate various cellular inputs to adjust the folding capacity of the organelle to accommodate to fluctuations in ER protein-folding demands are reviewed.