Evidence map›Paper›PMID 18450811›Full record

ArticleBioinformatics (Oxford, England)2008

Characterization and prediction of residues determining protein functional specificity.

John A Capra, Mona Singh

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed.

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  13. Predicting susceptibility to SARS-CoV-2 infection based on structural differences in ACE2 across species.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
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9 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

2 authors.

John A CapraDepartment of Computer Science, Lewis-Sigler Institute for Integrative Genomics, Princeton University, Princeton, NJ 08540, USA.
Mona Singh

Funding

Spatial Patterning During DevelopmentP50GM071508 · NIGMS · PRINCETON UNIVERSITY · PI POWELL, SUSAN M · 2004 to 2013
$30.6M
Quantitavie and Computational Biology Graduate ProgramT32HG003284 · NHGRI · PRINCETON UNIVERSITY · PI Joshua Michael Akey, Stanislav Y. Shvartsman · 2004 to 2026
$9.9M
VIRAL AND CELLULAR ONCOGENES--MECHANISM OF ACTIONP01CA041086 · NCI · PRINCETON UNIVERSITY · PI WIESCHAUS, ERIC F · 1986 to 2005
$9.4M
Predicting and analyzing variation in cellular interactomesR01GM076275 · NIGMS · PRINCETON UNIVERSITY · PI SINGH, MONA · 2006 to 2022
$4.0M
NCI NIH HHS CA041086NCI NIH HHS P01 CA041086NHGRI NIH HHS T32 HG003284NIGMS NIH HHS GM076275NIGMS NIH HHS P50 GM071508NIGMS NIH HHS R01 GM076275
6 · The paper itself

Abstract

motivationWithin a homologous protein family, proteins may be grouped into subtypes that share specific functions that are not common to the entire family. Often, the amino acids present in a small number of sequence positions determine each protein's particular functional specificity. Knowledge of these specificity determining positions (SDPs) aids in protein function prediction, drug design and experimental analysis. A number of sequence-based computational methods have been introduced for identifying SDPs; however, their further development and evaluation have been hindered by the limited number of known experimentally determined SDPs.

resultsWe combine several bioinformatics resources to automate a process, typically undertaken manually, to build a dataset of SDPs. The resulting large dataset, which consists of SDPs in enzymes, enables us to characterize SDPs in terms of their physicochemical and evolutionary properties. It also facilitates the large-scale evaluation of sequence-based SDP prediction methods. We present a simple sequence-based SDP prediction method, GroupSim, and show that, surprisingly, it is competitive with a representative set of current methods. We also describe ConsWin, a heuristic that considers sequence conservation of neighboring amino acids, and demonstrate that it improves the performance of all methods tested on our large dataset of enzyme SDPs. AVAILABILITY: Datasets and GroupSim code are available online at http://compbio.cs.princeton.edu/specificity/. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

Indexed as

AlgorithmsAmino Acid SequenceMolecular Sequence DataPattern Recognition, AutomatedProteinsSequence AlignmentSequence Analysis, ProteinProteins

Identifiers

PMID18450811
PMCPMC2718669

What OpenQuestion holds

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LicenceCC BY-NC
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.