Evidence map›Paper›PMID 24434632›Full record

ReviewCurrent opinion in structural biology2014

Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge.

Karan S Hingorani, Lila M Gierasch

Abstract readComparative StudyReview
In one paragraph

Review in Current opinion in structural biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
–field-weighted citation impact
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

44 citing papers in PubMed.

  1. Article
  2. Engineering an indoleamine 2,3-dioxygenase immunotherapyMolecular systems design & engineering · 2025
    Article
  3. Protein folding: From physics-chemical rules and cellular machineries of protein quality control to AI solutions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  10. Article
  11. A second chance for protein targeting/folding: Ubiquitination and deubiquitination of nascent proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Review
  12. Tissue-specific isoform expression of GNE gene in human tissues.Journal of muscle research and cell motility · 2022
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Lessons from equilibrium statistical physics regarding the assembly of protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  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.

Karan S HingoraniProgram in Molecular and Cellular Biology, University of Massachusetts, Amherst, Amherst, MA 01003, United States; Department of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, Amherst, MA 01003, United States.
Lila M GieraschProgram in Molecular and Cellular Biology, University of Massachusetts, Amherst, Amherst, MA 01003, United States; Department of Biochemistry & Molecular Biology, University of Massachusetts, Amherst, Amherst, MA 01003, United States; Department of Chemistry, University of Massachusetts, Amherst, Amherst, MA 01003, United States. Electronic address: gierasch@biochem.umass.edu.

Funding

PEPTIDE CONFORMATIONS &INTERACTIONS WITH MEMBRANESR01GM027616 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GIERASCH, LILA M · 1985 to 2015
$5.3M
CHEMISTRY-BIOLOGY INTERFACE PREDOCTORAL TRAINING GRANTST32GM008515 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 1995 to 2020
$4.3M
NIH DIRECTOR'S PIONEER AWARDDP1OD000945 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2006 to 2010
$3.9M
Modeling a cellular protein homeostasis networkR01GM101644 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M, POWERS, EVAN THOMAS · 2013 to 2016
$1.6M
NIGMS NIH HHS GM027616NIGMS NIH HHS R01 GM027616NIGMS NIH HHS R01 GM101644NIGMS NIH HHS T32 GM008515NIGMS NIH HHS T32 GM08515NIH HHS DP1 OD000945NIH HHS OD00945
6 · The paper itself

Abstract

In this review, we compare and contrast current knowledge about in vitro and in vivo protein folding. Major advances in understanding fundamental principles underlying protein folding in optimized in vitro conditions have yielded detailed physicochemical principles of folding landscapes for small, single domain proteins. In addition, there has been increased research focusing on the key features of protein folding in the cell that differentiate it from in vitro folding, such as co-translational folding, chaperone-facilitated folding, and folding in crowded conditions with many weak interactions. Yet these two research areas have not been bridged effectively in research carried out to date. This review points to gaps between the two that are ripe for future research. Moreover, we emphasize the biological selection pressures that impact protein folding in vivo and how fitness drives the evolution of protein sequences in ways that may place foldability in tension with other requirements on a given protein. We suggest that viewing the physicochemical process of protein folding through the lens of evolution will unveil new insights and pose novel challenges about in-cell folding landscapes.

Indexed as

Protein FoldingAmino Acid SequenceAnimalsHumansModels, MolecularMolecular Sequence DataProteinsProteins

Identifiers

PMID24434632
PMCPMC3984617

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.