Evidence map›Paper›PMID 25833954›Full record

ArticleDatabase : the journal of biological databases and curation2015

CHOPIN: a web resource for the structural and functional proteome of Mycobacterium tuberculosis.

Bernardo Ochoa-Montaño, Nishita Mohan, Tom L Blundell

Open access · goldAbstract readDataset
In one paragraph

Article in Database : the journal of biological databases and curation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  3. Review
  4. A platform for target prediction of phenotypic screening hit molecules.Journal of molecular graphics & modelling · 2020
    Article
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  15. Article
  16. SInCRe-structural interactome computational resource for Mycobacterium tuberculosis.Database : the journal of biological databases and curation · 2015
    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

3 authors at 2 institutions in 2 countries.

Bernardo Ochoa-MontañoDepartment of Biochemistry, University of Cambridge, Sanger Building, 80 Tennis Court Road, Cambridge CB2 1GA, UK and Department of Biotechnology, Indian Institute of Technology Madras, Chennai, Tamil Nadu 600036, India bernardo@cryst.bioc.cam.ac.uk.
Nishita MohanDepartment of Biochemistry, University of Cambridge, Sanger Building, 80 Tennis Court Road, Cambridge CB2 1GA, UK and Department of Biotechnology, Indian Institute of Technology Madras, Chennai, Tamil Nadu 600036, India Department of Biochemistry, University of Cambridge, Sanger Building, 80 Tennis Court Road, Cambridge CB2 1GA, UK and Department of Biotechnology, Indian Institute of Technology Madras, Chennai, Tamil Nadu 600036, India.
Tom L BlundellDepartment of Biochemistry, University of Cambridge, Sanger Building, 80 Tennis Court Road, Cambridge CB2 1GA, UK and Department of Biotechnology, Indian Institute of Technology Madras, Chennai, Tamil Nadu 600036, India.
Indian Institute of Technology Madras · INUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tuberculosis kills more than a million people annually and presents increasingly high levels of resistance against current first line drugs. Structural information about Mycobacterium tuberculosis (Mtb) proteins is a valuable asset for the development of novel drugs and for understanding the biology of the bacterium; however, only about 10% of the ∼4000 proteins have had their structures determined experimentally. The CHOPIN database assigns structural domains and generates homology models for 2911 sequences, corresponding to ∼73% of the proteome. A sophisticated pipeline allows multiple models to be created using conformational states characteristic of different oligomeric states and ligand binding, such that the models reflect various functional states of the proteins. Additionally, CHOPIN includes structural analyses of mutations potentially associated with drug resistance. Results are made available at the web interface, which also serves as an automatically updated repository of all published Mtb experimental structures. Its RESTful interface allows direct and flexible access to structures and metadata via intuitive URLs, enabling easy programmatic use of the models.

Indexed as

Bacterial ProteinsDatabases, GeneticDrug Resistance, BacterialMycobacterium tuberculosisProteomeAnimalsHumansModels, BiologicalProtein Structure, TertiaryTuberculosisBacterial ProteinsProteome

Identifiers

PMID25833954
PMCPMC4381106
OpenAlexW2149949919

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.