Evidence map›Paper›PMID 22183528›Full record

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

Evolutionary trace for prediction and redesign of protein functional sites.

Angela Wilkins, Serkan Erdin, Rhonald Lua, Olivier Lichtarge

Abstract 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 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Article
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  5. Review
  6. Article
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  11. DING Proteins Extend to the Extremophilic World.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Expression and Refolding of the Plant Chitinase FromFrontiers in bioengineering and biotechnology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
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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

4 authors.

Angela WilkinsDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA.
Serkan Erdin
Rhonald Lua
Olivier Lichtarge

Funding

TRAINING PROGRAM IN COMPUTATIONAL BIOLOGY AND MEDICINET15LM007093 · NLM · RICE UNIVERSITY · PI Lydia E. Kavraki · 1992 to 2026
$20.8M
Functional Determinnats in G Protein-coupled ReceptorsR01GM066099 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LICHTARGE, OLIVIER · 2003 to 2022
$7.5M
Comparative genomics of protein structure and functionR01GM079656 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI LICHTARGE, OLIVIER · 2007 to 2019
$4.3M
Training in Biomedical Discovery from Large Scale Data SetsT90DA022885 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI PALZKILL, TIMOTHY · 2006 to 2009
$635k
Training in Biomedical Discovery from Large Scale Data SetsR90DA023418 · NIDA · BAYLOR COLLEGE OF MEDICINE · PI PALZKILL, TIMOTHY · 2006 to 2009
$582k
NIDA NIH HHS R90 DA023418NIDA NIH HHS T90 DA022885NIGMS NIH HHS GM066099NIGMS NIH HHS GM079656NIGMS NIH HHS R01 GM066099NIGMS NIH HHS R01 GM079656NLM NIH HHS 5T15LM07093NLM NIH HHS T15 LM007093
6 · The paper itself

Abstract

The evolutionary trace (ET) is the single most validated approach to identify protein functional determinants and to target mutational analysis, protein engineering and drug design to the most relevant sites of a protein. It applies to the entire proteome; its predictions come with a reliability score; and its results typically reach significance in most protein families with 20 or more sequence homologs. In order to identify functional hot spots, ET scans a multiple sequence alignment for residue variations that correlate with major evolutionary divergences. In case studies this enables the selective separation, recoding, or mimicry of functional sites and, on a large scale, this enables specific function predictions based on motifs built from select ET-identified residues. ET is therefore an accurate, scalable and efficient method to identify the molecular determinants of protein function and to direct their rational perturbation for therapeutic purposes. Public ET servers are located at: http://mammoth.bcm.tmc.edu/.

Indexed as

Evolution, MolecularSoftwareAmino AcidsAmino Acid SequenceAutomationMolecular Sequence DataProtein EngineeringProteinsAmino AcidsProteins

Identifiers

PMID22183528
PMCPMC4892863

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.