Evidence map›Paper›PMID 23339312›Full record

ReviewCurrent topics in medicinal chemistry2012

Protein homeostasis as a therapeutic target for diseases of protein conformation.

Barbara Calamini, Richard I Morimoto

Abstract readReview
In one paragraph

Review in Current topics in medicinal chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Human Protein-l-isoaspartateBiochemistry · 2022
    Article
  8. Review
  9. CSPα in neurodegenerative diseases.Frontiers in aging neuroscience · 2022
    Review
  10. Review
  11. Article
  12. Heat Shock Protein 70 as a Sex-Skewed Regulator of α-Synucleinopathy.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2021
    Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. 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 at 1 institution in 1 country.

Barbara CalaminiDepartment of Neurobiology and Center for Drug Discovery, Duke University, Durham, NC, USA.
Richard I Morimoto
Duke University · US

Funding

REGULATION AND EXPRESSION OF THE HSP70 GENE FAMILYR37GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2000 to 2009
$5.6M
REGULATION AND EXPRESSION OF THE HUMAN HSP70 GENE FAMILYR01GM038109 · NIGMS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 1987 to 2013
$2.2M
C. Elegans Model for Neurodegenerative Diseases of AgingR01AG026647 · NIA · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I · 2005 to 2009
$2.0M
Small Molecule Screen for Novel Regulators of Chaperone ExpressionR21NS056337 · NINDS · NORTHWESTERN UNIVERSITY · PI MORIMOTO, RICHARD I. · 2006 to 2007
$363k
NIA NIH HHS R01 AG026647NIGMS NIH HHS R01 GM038109NIGMS NIH HHS R37 GM038109NINDS NIH HHS R21 NS056337
6 · The paper itself

Abstract

Protein misfolding and aggregation are widely implicated in an increasing number of human diseases providing for new therapeutic opportunities targeting protein homeostasis (proteostasis). The cellular response to proteotoxicity is highly regulated by stress signaling pathways, molecular chaperones, transport and clearance machineries that function as a proteostasis network (PN) to protect the stability and functional properties of the proteome. Consequently, the PN is essential at the cellular and organismal level for development and lifespan. However, when challenged during aging, stress, and disease, the folding and clearance machineries can become compromised leading to both gain-of-function and loss-of-function proteinopathies. Here, we assess the role of small molecules that activate the heat shock response, the unfolded protein response, and clearance mechanisms to increase PN capacity and protect cellular proteostasis against proteotoxicity. We propose that this strategy to enhance cell stress pathways and chaperone activity establishes a cytoprotective state against misfolding and/or aggregation and represents a promising therapeutic avenue to prevent the cellular damage associated with the variety of protein conformational diseases.

Indexed as

Heat-Shock ResponseProtein ConformationAutophagyHistone Deacetylase InhibitorsHomeostasisHumansMolecular ChaperonesMolecular Targeted TherapyProteasome InhibitorsProtein FoldingProteinsProteostasis DeficienciesHistone Deacetylase InhibitorsMolecular ChaperonesProteasome InhibitorsProteins

Identifiers

PMID23339312
PMCPMC3955168
OpenAlexW1978324338

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.