Evidence map›Paper›PMID 22350905›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2012

Cellular responses to misfolded proteins and protein aggregates.

Scott A Houck, Sangita Singh, Douglas M Cyr

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Myocilin misfolding and glaucoma: A 20-year update.Progress in retinal and eye research · 2023
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Dissecting the Molecular Function ofFrontiers in genetics · 2020
    Article
  15. Molecular switching from ubiquitin-proteasome to autophagy pathways in mice stroke model.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. DNAJs: more than substrate delivery to HSPA.Frontiers in molecular biosciences · 2015
    Review
  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

3 authors at 1 institution in 1 country.

Scott A HouckDepartment of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Sangita Singh
Douglas M Cyr
University of North Carolina at Chapel Hill · US

Funding

Roles for Hsp70 and Hsp40 in Membrane Protein TriageR01GM056981 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CYR, DOUGLAS M · 1998 to 2019
$6.1M
NIGMS NIH HHS R01 GM056981NIGMS NIH HHS R01GM056981
6 · The paper itself

Abstract

Maintenance of the proteome is a major homeostatic task of the cell and disregulation of protein homeostasis can be deadly. The accumulation of different forms of misfolded protein can perturb protein homeostasis and cause extensive cell and tissue damage. The cell has various quality control systems to help prevent the accumulation of misfolded proteins and the complexity of the different mechanisms that have evolved is bewildering. The first order of business for all quality control systems is recognition of misfolded proteins, which is followed by a triage decision. In many cases, modular molecular chaperones function in different assemblies with degradatory or folding co-factors to direct a misfolded protein toward continued life or death. Herein, an overview of quality control mechanisms that triage soluble cytosolic proteins, protein aggregates, and ER-associated proteins is presented.

Indexed as

Protein FoldingHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMolecular ChaperonesProteinsProteostasis DeficienciesUbiquitin-Protein LigasesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsMolecular ChaperonesProteinsUbiquitin-Protein Ligases

Identifiers

PMID22350905
PMCPMC4445682
OpenAlexW2441242823

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.