Evidence map›Paper›PMID 15980586›Full record

ArticleNucleic acids research2005

ProTarget: automatic prediction of protein structure novelty.

Ori Sasson, Michal Linial

Abstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Ori SassonSchool of Computer Science and Engineering, Institute of Life Sciences, Hebrew University of Jerusalem, 91904 Israel.
Michal Linial

Funding

Discovering Motifs From Orthologous SequencesR01HG002602 · NHGRI · UNIVERSITY OF WASHINGTON · PI TOMPA, MARTIN · 2002 to 2004
$981k
NHGRI NIH HHS HG 02602-01NHGRI NIH HHS R01 HG002602
6 · The paper itself

Abstract

ProTarget is a Web-based tool for the automatic prediction of fold novelty. It offers the structural genomics community a method for target selection by providing an online analysis of any new or pre-existing sequence for its relationship to any previously solved three-dimensional structure. ProTarget takes as input an amino acid sequence. Regions of this sequence that exhibit high similarity to an existing PDB (Protein Data Bank) sequence are removed, leaving one or more subsequences. Each of these subsequences is then analyzed against a clustering of the protein space to determine the likelihood of its representing a new structural superfamily. This likelihood is derived from the distance in the clustering between the (sub)sequence and sequences that have known structures. The output of ProTarget is a graphical visualization of the protein of interest together with the likelihood that a protein sequence represents a novel structural superfamily. ProTarget is updated regularly and currently covers over 160 000 protein sequences from the SwissProt and PDB databases. ProTarget is available at http://www.protarget.cs.huji.ac.il.

Indexed as

Protein ConformationSoftwareAlgorithmsDatabases, ProteinInternetModels, MolecularProtein Folding

Identifiers

PMID15980586
PMCPMC1160150

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.