Evidence map›Paper›PMID 21081274›Full record

ReviewCurrent opinion in structural biology2011

Taming the complexity of protein folding.

Gregory R Bowman, Vincent A Voelz, Vijay S Pande

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing 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

79 citing papers in PubMed.

  1. Article
  2. Article
  3. Bridging Scales: Coarse-Grained Protein Models in Computational Biology.Advances in experimental medicine and biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. A Stochastic Landscape Approach for Protein Folding State Classification.Journal of chemical theory and computation · 2024
    Article
  9. On the role of native contact cooperativity in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Photoacid Generators for Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

19 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

3 authors.

Gregory R BowmanDepartment of Chemistry, Stanford University, Stanford, CA 94305, USA.
Vincent A Voelz
Vijay S Pande

Funding

Topology, nucleation, and the protein folding barrierR01GM062868 · NIGMS · STANFORD UNIVERSITY · PI PANDE, VIJAY S · 2002 to 2018
$5.5M
NIGMS NIH HHS R01 GM062868NIGMS NIH HHS R01-GM062868
6 · The paper itself

Abstract

Protein folding is an important problem in structural biology with significant medical implications, particularly for misfolding disorders like Alzheimer's disease. Solving the folding problem will ultimately require a combination of theory and experiment, with theoretical models providing a comprehensive view of folding and experiments grounding these models in reality. Here we review progress towards this goal over the past decade, with an emphasis on recent theoretical advances that are empowering chemically detailed models of folding and the new results these technologies are providing. In particular, we discuss new insights made possible by Markov state models (MSMs), including the role of non-native contacts and the hub-like character of protein folded states.

Indexed as

Protein FoldingComputational BiologyHumansModels, MolecularProteinsProteins

Identifiers

PMID21081274
PMCPMC3042729

What OpenQuestion holds

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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.