Evidence map›Paper›PMID 35883484›Full record

ReviewBiomolecules2022

Emerging Link between Tsc1 and FNIP Co-Chaperones of Hsp90 and Cancer.

Sarah J Backe, Rebecca A Sager, Katherine A Meluni, Mark R Woodford, Dimitra Bourboulia, Mehdi Mollapour

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

6 authors at 1 institution in 1 country.

Sarah J BackeDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Rebecca A SagerDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Katherine A MeluniDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Mark R WoodfordDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.ORCID 0000-0002-6737-2832
Dimitra BourbouliaDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.ORCID 0000-0002-8567-2775
Mehdi MollapourDepartment of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.ORCID 0000-0002-2144-1361
SUNY Upstate Medical University · US

Funding

Regulatory mechanisms of the Hsp90 chaperone machinery.R35GM139584 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI MOLLAPOUR, MEHDI · 2021 to 2025
$2.2M
Crosstalk between post-translational regulations of the FNIP co-chaperones and their impact on Hsp90 chaperone function and drug bindingR01GM124256 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI MOLLAPOUR, MEHDI · 2017 to 2020
$1.3M
NIGMS NIH HHS R01 GM124256NIGMS NIH HHS R35 GM139584NIGMS NIH HHS R35GM139584
6 · The paper itself

Abstract

Heat shock protein-90 (Hsp90) is an ATP-dependent molecular chaperone that is tightly regulated by a group of proteins termed co-chaperones. This chaperone system is essential for the stabilization and activation of many key signaling proteins. Recent identification of the co-chaperones FNIP1, FNIP2, and Tsc1 has broadened the spectrum of Hsp90 regulators. These new co-chaperones mediate the stability of critical tumor suppressors FLCN and Tsc2 as well as the various classes of Hsp90 kinase and non-kinase clients. Many early observations of the roles of FNIP1, FNIP2, and Tsc1 suggested functions independent of FLCN and Tsc2 but have not been fully delineated. Given the broad cellular impact of Hsp90-dependent signaling, it is possible to explain the cellular activities of these new co-chaperones by their influence on Hsp90 function. Here, we review the literature on FNIP1, FNIP2, and Tsc1 as co-chaperones and discuss the potential downstream impact of this regulation on normal cellular function and in human diseases.

Indexed as

Tuberous SclerosisTumor Suppressor ProteinsHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesTuberous Sclerosis Complex 1 ProteinHSP90 Heat-Shock ProteinsMolecular ChaperonesTSC1 protein, humanTuberous Sclerosis Complex 1 ProteinTumor Suppressor Proteinscancerco-chaperonesFNIP1FNIP2heat shock protein 90 (Hsp90)kidney cancerrenal cell carcinomaTsc1 (hamartin)Tsc2 (tuberin)tuberous sclerosis complex (TSC)

Identifiers

PMID35883484
PMCPMC9312812
OpenAlexW4283775652

What OpenQuestion 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 OpenQuestion graph.