Evidence map›Paper›PMID 16245324›Full record

ArticleProteins2005

Structural characterization of proteins using residue environments.

Sean D Mooney, Mike Hsin-Ping Liang, Rob DeConde, Russ B Altman

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Graphlet kernels for prediction of functional residues in protein structures.Journal of computational biology : a journal of computational molecular cell biology · 2010
    Article
  9. Article
  10. Distance matrix-based approach to protein structure prediction.Journal of structural and functional genomics · 2009
    Article
  11. Article
  12. Article
  13. Evaluation of features for catalytic residue prediction in novel folds.Protein science : a publication of the Protein Society · 2007
    Article
  14. 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

4 authors at 1 institution in 1 country.

Sean D MooneyDepartment of Genetics, Stanford University, Stanford, California, USA. sdmooney@iupui.edu
Mike Hsin-Ping Liang
Rob DeConde
Russ B Altman
Stanford University · US

Funding

POSTDOCTORAL TRAINING IN MEDICAL INFORMATION SCIENCEST15LM007033 · NLM · STANFORD UNIVERSITY · PI SYLVIA KATINA PLEVRITIS · 1985 to 2026
$25.5M
Text Mining for High-fidelity Curation and Discovery of Gene-drug-phenotype RelationshipsR01LM005652 · NLM · STANFORD UNIVERSITY · PI ALTMAN, RUSS BIAGIO · 2000 to 2018
$6.2M
Predoctoral Training Bioinformatics/Computational Biol.T32GM063495 · NIGMS · STANFORD UNIVERSITY · PI ALTMAN, RUSS BIAGIO · 2001 to 2009
$1.7M
REPRESENTING BIOLOGICAL DATA FOR MOLECULAR MODELINGR01LM006244 · NLM · STANFORD UNIVERSITY · PI ALTMAN, RUSS BIAGIO · 1996 to 2000
$333k
MODELING AND COMPUTING WITH UNCERTAIN STRUCTURESR29LM005652 · NLM · STANFORD UNIVERSITY · PI ALTMAN, RUSS BIAGIO · 1994 to 1998
–
NIGMS NIH HHS GM-63495NIGMS NIH HHS T32 GM063495NLM NIH HHS LM-05652NLM NIH HHS LM06244NLM NIH HHS LM-07033NLM NIH HHS R01 LM005652NLM NIH HHS T15 LM007033
6 · The paper itself

Abstract

A primary challenge for structural genomics is the automated functional characterization of protein structures. We have developed a sequence-independent method called S-BLEST (Structure-Based Local Environment Search Tool) for the annotation of previously uncharacterized protein structures. S-BLEST encodes the local environment of an amino acid as a vector of structural property values. It has been applied to all amino acids in a nonredundant database of protein structures to generate a searchable structural resource. Given a query amino acid from an experimentally determined or modeled structure, S-BLEST quickly identifies similar amino acid environments using a K-nearest neighbor search. In addition, the method gives an estimation of the statistical significance of each result. We validated S-BLEST on X-ray crystal structures from the ASTRAL 40 nonredundant dataset. We then applied it to 86 crystallographically determined proteins in the protein data bank (PDB) with unknown function and with no significant sequence neighbors in the PDB. S-BLEST was able to associate 20 proteins with at least one local structural neighbor and identify the amino acid environments that are most similar between those neighbors.

Indexed as

Amino AcidsComputational BiologyDatabases, ProteinKineticsModels, MolecularMolecular StructureProtein ConformationProteinsProtein Structure, SecondaryAmino AcidsProteins

Identifiers

PMID16245324
PMCPMC2483305
OpenAlexW2009528611

What OpenQuestion holds

Textmetadata
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.