Evidence map›Paper›PMID 19731377›Full record

ArticleProteins2010

Comparison of structure-based and threading-based approaches to protein functional annotation.

Michal Brylinski, Jeffrey Skolnick

Abstract readComparative Study
In one paragraph

Article in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
–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

24 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. An informatic workflow for the enhanced annotation of excretory/secretory proteins ofComputational and structural biotechnology journal · 2023
    Article
  3. Review
  4. Computational and Experimental Studies of ADP-Ribosylation.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  5. Article
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  9. Interplay of physics and evolution in the likely origin of protein biochemical function.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Article
  11. Review
  12. IMPORTANCE OF EXCLUDED VOLUME AND HYDRODYNAMIC INTERACTIONS ON MACROMOLECULAR DIFFUSIONQuantum bio-informatics V : proceedings of the quantum bio-informatics 2011, Tokyo University of Science, Japan, 7-12 March 2011. Quantum Bio-Informatics (Conference) (5th : 2011 : Tokyo, Japan) · 2013
    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

2 authors.

Michal BrylinskiCenter for the Study of Systems Biology, School of Biology, Georgia Institute of Technology, Atlanta, GA 30318, USA.
Jeffrey Skolnick

Funding

Interaction Pattern Based Predictor of Protein StruturesR01GM048835 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SKOLNICK, JEFFREY · 1994 to 2015
$4.0M
THEORY OF FOLDING TRANSITIONS IN A-HELICAL PROTEINSR01GM037408 · NIGMS · WASHINGTON UNIVERSITY · PI SKOLNICK, JEFFREY · 1987 to 2014
$3.9M
NIGMS NIH HHS GM-48835NIGMS NIH HHS R01 GM037408NIGMS NIH HHS R01 GM048835
6 · The paper itself

Abstract

To exploit the vast amount of sequence information provided by the Genomic revolution, the biological function of these sequences must be identified. As a practical matter, this is often accomplished by functional inference. Purely sequence-based approaches, particularly in the "twilight zone" of low sequence similarity levels, are complicated by many factors. For proteins, structure-based techniques aim to overcome these problems; however, most require high-quality crystal structures and suffer from complex and equivocal relations between protein fold and function. In this study, in extensive benchmarking, we consider a number of aspects of structure-based functional annotation: binding pocket detection, molecular function assignment and ligand-based virtual screening. We demonstrate that protein threading driven by a strong sequence profile component greatly improves the quality of purely structure-based functional annotation in the "twilight zone." By detecting evolutionarily related proteins, it considerably reduces the high false positive rate of function inference derived on the basis of global structure similarity alone. Combined evolution/structure-based function assignment emerges as a powerful technique that can make a significant contribution to comprehensive proteome annotation.

Indexed as

Binding SitesDatabases, ProteinLigandsModels, BiologicalProtein BindingProtein ConformationProteinsSoftwareStructure-Activity RelationshipLigandsProteins

Identifiers

PMID19731377
PMCPMC2804779

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.