Evidence map›Paper›PMID 32887796›Full record

ReviewThe Journal of biological chemistry2020

Small molecule strategies to harness the unfolded protein response: where do we go from here?

Julia M D Grandjean, R Luke Wiseman

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
7.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

76 citing papers in PubMed, 145 citations in OpenAlex.

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  18. SON-dependent nuclear speckle rehabilitation alleviates proteinopathies.bioRxiv : the preprint server for biology · 2025
    Article
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Julia M D GrandjeanDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, California, USA.
R Luke WisemanDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, California, USA. Electronic address: wiseman@scripps.edu.
Scripps Research Institute · US

Funding

Discovering small molecules activators of stress responsive signalingR01AG046495 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI JEFFERY W KELLY, Rockland Luke Wiseman · 2013 to 2026
$6.0M
Discovering Small Molecule Activators of Stress-Responsive SignalingRF1AG046495 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W, WISEMAN, ROCKLAND LUKE · 2023 to 2025
$2.8M
Adapting Secretory Proteostasis through Pharmacologic IRE1 ActivationF31AG063489 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI GRANDJEAN, JULIA MARIE DENDLE · 2019 to 2020
$54k
NIA NIH HHS F31 AG063489NIA NIH HHS R01 AG046495NIA NIH HHS RF1 AG046495
6 · The paper itself

Abstract

The unfolded protein response (UPR) plays a central role in regulating endoplasmic reticulum (ER) and global cellular physiology in response to pathologic ER stress. The UPR is comprised of three signaling pathways activated downstream of the ER membrane proteins IRE1, ATF6, and PERK. Once activated, these proteins initiate transcriptional and translational signaling that functions to alleviate ER stress, adapt cellular physiology, and dictate cell fate. Imbalances in UPR signaling are implicated in the pathogenesis of numerous, etiologically-diverse diseases, including many neurodegenerative diseases, protein misfolding diseases, diabetes, ischemic disorders, and cancer. This has led to significant interest in establishing pharmacologic strategies to selectively modulate IRE1, ATF6, or PERK signaling to both ameliorate pathologic imbalances in UPR signaling implicated in these different diseases and define the importance of the UPR in diverse cellular and organismal contexts. Recently, there has been significant progress in the identification and characterization of UPR modulating compounds, providing new opportunities to probe the pathologic and potentially therapeutic implications of UPR signaling in human disease. Here, we describe currently available UPR modulating compounds, specifically highlighting the strategies used for their discovery and specific advantages and disadvantages in their application for probing UPR function. Furthermore, we discuss lessons learned from the application of these compounds in cellular and

Indexed as

Allosteric RegulationeIF-2 KinaseEndoplasmic ReticulumEndoribonucleasesHumansProtein Kinase InhibitorsProtein Serine-Threonine KinasesSignal TransductionSmall Molecule LibrariesUnfolded Protein ResponseeIF-2 KinaseEndoribonucleasesERN1 protein, humanProtein Kinase InhibitorsProtein Serine-Threonine KinasesSmall Molecule Librariesendoplasmic reticulum (ER)endoplasmic reticulum stress (ER stress)high-throughput screening (HTS)modulationproteostasissmall moleculestress responseunfolded protein response (UPR)

Identifiers

PMID32887796
PMCPMC7667976
OpenAlexW3083466538

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.