Evidence map›Paper›PMID 23463216›Full record

ReviewNature reviews. Molecular cell biology2013

Diversity in the origins of proteostasis networks--a driver for protein function in evolution.

Evan T Powers, William E Balch

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed
12.3field-weighted citation impact, top 1% 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

140 citing papers in PubMed, 252 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. YeastbioRxiv : the preprint server for biology · 2025
    Article
  6. Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Climate change-induced stress in the honey beeFrontiers in physiology · 2025
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Protein homeostasis imprinting across evolution.NAR genomics and bioinformatics · 2024
    Article
  20. Article

80 more citing papers are in PubMed but not listed here.

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.

Evan T PowersDepartment of Chemistry, The Scripps Research Institute, La Jolla, California 92037, USA. epowers@scripps.edu
William E Balch
Scripps Research Institute · US

Funding

TRAFFICKING AND ABETA AGGREGATIONP01AG031097 · NIA · SCRIPPS RESEARCH INSTITUTE, THE · PI KELLY, JEFFERY W · 2009 to 2013
$10.2M
Modulation of Lung Disease by Genetic/Epigenetic ProfilingR01HL095524 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI William Edward Balch · 2010 to 2026
$7.5M
ROLE OF RAB PROTEINS AND CA2+ IN VESICULAR TRANSPORTR01GM042336 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD · 1990 to 2011
$4.8M
Structure and Function of Guanine Nucleotide Dissociation InhibitorR01GM033301 · NIGMS · YALE UNIVERSITY · PI BALCH, WILLIAM EDWARD · 1985 to 2012
$4.6M
Proteomic Profiling of CFTR Protein InteractionR01HL079442 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI BALCH, WILLIAM EDWARD, YATES III, JOHN R · 2005 to 2014
$4.6M
NHLBI NIH HHS HL079442NHLBI NIH HHS HL095524NHLBI NIH HHS R01 HL079442NHLBI NIH HHS R01 HL095524NIA NIH HHS AG03109NIA NIH HHS P01 AG031097NIGMS NIH HHS GM33301NIGMS NIH HHS GM42236NIGMS NIH HHS R01 GM033301NIGMS NIH HHS R01 GM042336
6 · The paper itself

Abstract

Although the sequence of a protein largely determines its function, proteins can adopt different folding states in response to changes in the environment, some of which may be deleterious to the organism. All organisms--Bacteria, Archaea and Eukarya--have evolved a protein homeostasis, or proteostasis, network comprising chaperones and folding factors, degradation components, signalling pathways and specialized compartmentalized modules that manage protein folding in response to environmental stimuli and variation. Surveying the origins of proteostasis networks reveals that they have co-evolved with the proteome to regulate the physiological state of the cell, reflecting the unique stresses that different cells or organisms experience, and that they have a key role in driving evolution by closely managing the link between the phenotype and the genotype.

Indexed as

HomeostasisSignal TransductionAnimalsEvolution, MolecularGenetic VariationHumansProtein FoldingProteinsProteomeSpecies SpecificityProteinsProteome

Identifiers

PMID23463216
PMCPMC3718298
OpenAlexW1981899072

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.