Evidence map›Paper›PMID 35507259›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Three-dimensional Structure Databases of Biological Macromolecules.

Vaishali P Waman, Christine Orengo, Gerard J Kleywegt, Arthur M Lesk

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. PhiSiCal-Checkup: A Bayesian framework to validate amino acid conformations within experimental protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Chimera X Interface to Enhance Understanding in Biochemistry and Immunology.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology
    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.

Vaishali P WamanInstitute of Structural and Molecular Biology, University College London, London, UK.
Christine OrengoInstitute of Structural and Molecular Biology, University College London, London, UK.
Gerard J KleywegtEuropean Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Cambridge, UK.
Arthur M LeskDepartment of Biochemistry and Molecular Biology and Center for Computational Biology and Bioinformatics, The Pennsylvania State University, University Park, PA, USA. aml25@psu.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Databases of three-dimensional structures of proteins (and their associated molecules) provide: (a) Curated repositories of coordinates of experimentally determined structures, including extensive metadata; for instance information about provenance, details about data collection and interpretation, and validation of results. (b) Information-retrieval tools to allow searching to identify entries of interest and provide access to them. (c) Links among databases, especially to databases of amino-acid and genetic sequences, and of protein function; and links to software for analysis of amino-acid sequence and protein structure, and for structure prediction. (d) Collections of predicted three-dimensional structures of proteins. These will become more and more important after the breakthrough in structure prediction achieved by AlphaFold2. The single global archive of experimentally determined biomacromolecular structures is the Protein Data Bank (PDB). It is managed by wwPDB, a consortium of five partner institutions: the Protein Data Bank in Europe (PDBe), the Research Collaboratory for Structural Bioinformatics (RCSB), the Protein Data Bank Japan (PDBj), the BioMagResBank (BMRB), and the Electron Microscopy Data Bank (EMDB). In addition to jointly managing the PDB repository, the individual wwPDB partners offer many tools for analysis of protein and nucleic acid structures and their complexes, including providing computer-graphic representations. Their collective and individual websites serve as hubs of the community of structural biologists, offering newsletters, reports from Task Forces, training courses, and "helpdesks," as well as links to external software.Many specialized projects are based on the information contained in the PDB. Especially important are SCOP, CATH, and ECOD, which present classifications of protein domains.

Indexed as

ProteinsSoftwareComputational BiologyDatabases, ProteinProtein ConformationProteinsData archivingDomain analysisFold classificationProtein Data BankProtein structureStructural biology

Identifiers

PMID35507259

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.