Evidence map›Paper›PMID 28647092›Full record

ReviewTrends in cell biology2017

Regulating Secretory Proteostasis through the Unfolded Protein Response: From Function to Therapy.

Lars Plate, R Luke Wiseman

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Inhibition of FicD-mediated AMPylation and deAMPylation by isoprenoid diphosphates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. From Genome to Geroscience: How DNA Damage Shapes Systemic Decline.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Review
  13. Dual roles of UPRJournal of molecular medicine (Berlin, Germany) · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Secretion of functional α1-antitrypsin is cell type dependent: Implications for intramuscular delivery for gene therapy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article
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.

Lars PlateDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA.
R Luke WisemanDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA. Electronic address: wiseman@scripps.edu.

Funding

Establishing Strategies to Ameliorate Amyloid Pathology in Light Chain AmyloidosisR01DK107604 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI WISEMAN, ROCKLAND LUKE · 2016 to 2024
$4.3M
Direct Regulation of Extracellular Proteostasis by the Unfolded Protein ResponseR01NS092829 · NINDS · SCRIPPS RESEARCH INSTITUTE, THE · PI WISEMAN, ROCKLAND LUKE · 2015 to 2019
$2.1M
TARGETING ENDOGENOUS SIGNALING PATHWAYS TO AMELIORATE SYSTEMIC AMYLOIDOSESR01DK102635 · NIDDK · SCRIPPS RESEARCH INSTITUTE, THE · PI MURPHY, GEORGE J, WISEMAN, ROCKLAND LUKE · 2014 to 2017
$823k
NIDDK NIH HHS R01 DK102635NIDDK NIH HHS R01 DK107604NINDS NIH HHS R01 NS092829
6 · The paper itself

Abstract

Imbalances in secretory proteostasis induced by genetic, environmental, or aging-related insults are pathologically associated with etiologically diverse protein misfolding diseases. To protect the secretory proteome from these insults, organisms evolved stress-responsive signaling pathways that regulate the composition and activity of biologic pathways involved in secretory proteostasis maintenance. The most prominent of these is the endoplasmic reticulum (ER) unfolded protein response (UPR), which functions to regulate ER proteostasis in response to ER stress. While the signaling mechanisms involved in UPR activation are well defined, the impact of UPR activation on secretory proteostasis is only now becoming clear. Here, we highlight recent reports defining how activation of select UPR signaling pathways influences proteostasis within the ER and downstream secretory environments. Furthermore, we describe recent evidence that highlights the therapeutic potential for targeting UPR signaling pathways to correct pathologic disruption in secretory proteostasis associated with diverse types of protein misfolding diseases.

Indexed as

Activating Transcription Factor 6AnimalsBiological TransportEndoplasmic Reticulum StressHumansProteomeProteostasisRepressor ProteinsSecretory PathwaySignal TransductionUnfolded Protein ResponseActivating Transcription Factor 6ProteomeRepressor Proteins

Identifiers

PMID28647092
PMCPMC5612838

What OpenQuestion holds

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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.