Evidence map›Paper›PMID 28472372›Full record

ArticleNucleic acids research2017

ProteinsPlus: a web portal for structure analysis of macromolecules.

Rainer Fährrolfes, Stefan Bietz, Florian Flachsenberg, Agnes Meyder, Eva Nittinger, Thomas Otto, Andrea Volkamer, Matthias Rarey

Abstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing 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

105 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Pangenomics insights of enterococcus faecium human isolates and identification of novel therapeutic targets by in silico subtractive genomics.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026
    Article
  6. Article
  7. Article
  8. Molecular and Pharmacokinetic Rationale for the Use ofMolecules (Basel, Switzerland) · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Inhibitory Effect ofTheScientificWorldJournal · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Article

45 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

8 authors.

Rainer FährrolfesUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.
Stefan BietzUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.
Florian FlachsenbergUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.
Agnes MeyderUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.
Eva NittingerUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.
Thomas OttoUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.
Andrea VolkamerInstitute of Physiology, Charité-Universitätsmedizin Berlin, Virchowweg 6, 10117 Berlin, Germany.
Matthias RareyUniversität Hamburg, ZBH-Center for Bioinformatics, Bundesstrasse 43, 20146 Hamburg, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

With currently more than 126 000 publicly available structures and an increasing growth rate, the Protein Data Bank constitutes a rich data source for structure-driven research in fields like drug discovery, crop science and biotechnology in general. Typical workflows in these areas involve manifold computational tools for the analysis and prediction of molecular functions. Here, we present the ProteinsPlus web server that offers a unified easy-to-use interface to a broad range of tools for the early phase of structure-based molecular modeling. This includes solutions for commonly required pre-processing tasks like structure quality assessment (EDIA), hydrogen placement (Protoss) and the search for alternative conformations (SIENA). Beyond that, it also addresses frequent problems as the generation of 2D-interaction diagrams (PoseView), protein-protein interface classification (HyPPI) as well as automatic pocket detection and druggablity assessment (DoGSiteScorer). The unified ProteinsPlus interface covering all featured approaches provides various facilities for intuitive input and result visualization, case-specific parameterization and download options for further processing. Moreover, its generalized workflow allows the user a quick familiarization with the different tools. ProteinsPlus also stores the calculated results temporarily for future request and thus facilitates convenient result communication and re-access. The server is freely available at http://proteins.plus.

Indexed as

Protein ConformationSoftwareBinding SitesHydrogenInternetLigandsModels, MolecularProtein Interaction MappingProteinsHydrogenLigandsProteins

Identifiers

PMID28472372
PMCPMC5570178

What OpenQuestion holds

Textmetadata
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.