Evidence map›Paper›PMID 35326427›Full record

ReviewCells2022

Hsp90 in Human Diseases: Molecular Mechanisms to Therapeutic Approaches.

Mamta P Sumi, Arnab Ghosh

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 2 pooled it
3.0field-weighted citation impact, top 8% 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, 2 syntheses or guidelines pooled it, 37 citations in OpenAlex.

  1. Ferroptosis and Senescence: A Systematic Review.International journal of molecular sciences · 2023
    Pooled it
  2. Pooled it
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
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  10. Review
  11. Article
  12. Article
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  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. The Emerging Role of Heat Shock Factor 1 (HSF1) and Heat Shock Proteins (HSPs) in Ferroptosis.Pathophysiology : the official journal of the International Society for Pathophysiology · 2023
    Review
  20. Review
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.

Mamta P SumiDepartment of Inflammation and Immunity, Lerner Research Institute, The Cleveland Clinic, Cleveland, OH 44195, USA.
Arnab GhoshDepartment of Inflammation and Immunity, Lerner Research Institute, The Cleveland Clinic, Cleveland, OH 44195, USA.ORCID 0000-0002-7498-1994
Cleveland Clinic Lerner College of Medicine · US

Funding

Nitric oxide induced soluble guanylate cyclase dysfunction or activation: Implications as a disease indicator or in therapyR01HL150049 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI GHOSH, ARNAB · 2020 to 2023
$1.7M
Nitric oxide induced soluble guanylate cyclase dysfunction or activation: Implications as disease biomarkers or in therapyR56HL139564 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI GHOSH, ARNAB · 2019 to 2019
$414k
NHLBI NIH HHS R01 HL150049NHLBI NIH HHS R56 HL139564
6 · The paper itself

Abstract

The maturation of hemeprotein dictates that they incorporate heme and become active, but knowledge of this essential cellular process remains incomplete. Studies on chaperon Hsp90 has revealed that it drives functional heme maturation of inducible nitric oxide synthase (iNOS), soluble guanylate cyclase (sGC) hemoglobin (Hb) and myoglobin (Mb) along with other proteins including GAPDH, while globin heme maturations also need an active sGC. In all these cases, Hsp90 interacts with the heme-free or apo-protein and then drives the heme maturation by an ATP dependent process before dissociating from the heme-replete proteins, suggesting that it is a key player in such heme-insertion processes. As the studies on globin maturation also need an active sGC, it connects the globin maturation to the NO-sGC (Nitric oxide-sGC) signal pathway, thereby constituting a novel NO-sGC-Globin axis. Since many aggressive cancer cells make Hbβ/Mb to survive, the dependence of the globin maturation of cancer cells places the NO-sGC signal pathway in a new light for therapeutic intervention. Given the ATPase function of Hsp90 in heme-maturation of client hemeproteins, Hsp90 inhibitors often cause serious side effects and this can encourage the alternate use of sGC activators/stimulators in combination with specific Hsp90 inhibitors for better therapeutic intervention.

Indexed as

HemeHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesMyoglobinNitric OxideSoluble Guanylyl CyclaseHemeHSP90 Heat-Shock ProteinsMolecular ChaperonesMyoglobinNitric OxideSoluble Guanylyl Cyclaseangiogenesishemeheme-freehemeproteinmetastasisoncoproteins

Identifiers

PMID35326427
PMCPMC8946885
OpenAlexW4220752468

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.