Evidence map›Paper›PMID 35861260›Full record

ReviewMedicinal research reviews2022

The biology and inhibition of glucose-regulated protein 94/gp96.

Kyler W Pugh, Marim Alnaed, Christopher M Brackett, Brian S J Blagg

Open access · greenAbstract readReview
In one paragraph

Review in Medicinal research reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  9. Article
  10. GRP94 is indispensable for definitive endoderm specification of human induced pluripotent stem cells.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  11. Review
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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

4 authors at 1 institution in 1 country.

Kyler W PughDepartment of Chemistry and Biochemistry, Warren Family Research Center for Drug Discovery and Development, University of Notre Dame, Notre Dame, Indiana, USA.ORCID 0000-0002-7195-4800
Marim AlnaedDepartment of Chemistry and Biochemistry, Warren Family Research Center for Drug Discovery and Development, University of Notre Dame, Notre Dame, Indiana, USA.ORCID 0000-0002-1600-2858
Christopher M BrackettDepartment of Chemistry and Biochemistry, Warren Family Research Center for Drug Discovery and Development, University of Notre Dame, Notre Dame, Indiana, USA.ORCID 0000-0003-2652-7006
Brian S J BlaggDepartment of Chemistry and Biochemistry, Warren Family Research Center for Drug Discovery and Development, University of Notre Dame, Notre Dame, Indiana, USA.ORCID 0000-0002-6200-3480
University of Notre Dame · US

Funding

New paradigms for Hsp90 inhibitionR01CA213566 · NCI · UNIVERSITY OF NOTRE DAME · PI BLAGG, BRIAN S J · 2017 to 2020
$1.4M
NCI NIH HHS R01 CA213566
6 · The paper itself

Abstract

The 94 kDa molecular chaperone, glucose-regulated protein 94 (Grp94), has garnered interest during the last decade due to its direct association with endoplasmic reticulum (ER) stress and disease. Grp94 belongs to the Hsp90 family of molecular chaperones and is a master regulator of ER homeostasis due to its ability to fold and stabilize proteins/receptors, and to chaperone misfolded proteins for degradation. Multiple studies have demonstrated that Grp94 knockdown or inhibition leads to the degradation of client protein substrates, which leads to disruption of disease-dependent signaling pathways. As a result, small molecule inhibitors of Grp94 have become a promising therapeutic approach to target a variety of disease states. Specifically, Grp94 has proven to be a promising target for cancer, glaucoma, immune-mediated inflammation, and viral infection. Moreover, Grp94-peptide complexes have been utilized effectively as adjuvants for vaccines against a variety of disease states. This work highlights the significance of Grp94 biology and the development of therapeutics that target this molecular chaperone in multiple disease states.

Indexed as

HSP70 Heat-Shock ProteinsMembrane GlycoproteinsBiologyHumansMembrane ProteinsMolecular Chaperonesglucose-regulated proteinsHSP70 Heat-Shock ProteinsMembrane GlycoproteinsMembrane ProteinsMolecular Chaperonescancerchaperonesglaucomagp96Grp94Hsp90immune systeminhibitorsmutant myocilinviruses

Identifiers

PMID35861260
PMCPMC10003671
OpenAlexW4286494105

What OpenQuestion holds

Textmetadata
LicenceTDM
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.