Evidence map›Paper›PMID 26497286›Full record

ReviewCurrent opinion in structural biology2015

Protein stability: computation, sequence statistics, and new experimental methods.

Thomas J Magliery

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing 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

71 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Towards routine accurate electron-density studies of biological macromolecules.Acta crystallographica. Section D, Structural biology · 2026
    Article
  5. Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.Angewandte Chemie (International ed. in English) · 2026
    Article
  6. Exploring the Blueprint of Life: The Innovation in Antibody and Protein Design.Combinatorial chemistry & high throughput screening · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Improving Protein Expression, Stability, and Function with ProteinMPNN.Journal of the American Chemical Society · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Forensic Proteomics for the Discovery of NewInternational journal of molecular sciences · 2023
    Article
  17. Article
  18. Article
  19. Article
  20. Review

11 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

1 author.

Thomas J MaglieryDepartment of Chemistry & Biochemistry, The Ohio State University, 100 W. 18(th) Ave., Columbus, OH 43210, USA. Electronic address: magliery.1@osu.edu.

Funding

Training and Education CoreU54NS058183 · NINDS · U.S. ARMY MEDICAL RESEARCH INST CHEM DEF · PI CERASOLI, DOUGLAS MARK, MAGLIERY, THOMAS J · 2006 to 2013
$20.6M
Combinatorial biophysics: Understanding protein stability with library approachesR01GM083114 · NIGMS · OHIO STATE UNIVERSITY · PI MAGLIERY, THOMAS J · 2008 to 2017
$2.9M
NIGMS NIH HHS R01 GM083114NIGMS NIH HHS R01GM083114NINDS NIH HHS U54 NS058183
6 · The paper itself

Abstract

Calculating protein stability and predicting stabilizing mutations remain exceedingly difficult tasks, largely due to the inadequacy of potential functions, the difficulty of modeling entropy and the unfolded state, and challenges of sampling, particularly of backbone conformations. Yet, computational design has produced some remarkably stable proteins in recent years, apparently owing to near ideality in structure and sequence features. With caveats, computational prediction of stability can be used to guide mutation, and mutations derived from consensus sequence analysis, especially improved by recent co-variation filters, are very likely to stabilize without sacrificing function. The combination of computational and statistical approaches with library approaches, including new technologies such as deep sequencing and high throughput stability measurements, point to a very exciting near term future for stability engineering, even with difficult computational issues remaining.

Indexed as

Computational BiologyProtein StabilityModels, MolecularMutationProtein ConformationProteinsProteins

Identifiers

PMID26497286
PMCPMC4858314

What OpenQuestion holds

Textmetadata
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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.