Evidence map›Paper›PMID 28449074›Full record

ArticleNucleic acids research2017

FireProt: web server for automated design of thermostable proteins.

Milos Musil, Jan Stourac, Jaroslav Bendl, Jan Brezovsky, Zbynek Prokop, Jaroslav Zendulka, Tomas Martinek, David Bednar, Jiri Damborsky

Open access · goldAbstract 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 62 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed, 1 pooled it
8.4field-weighted citation impact, top 2% 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

62 citing papers in PubMed, 1 synthesis or guideline pooled it, 207 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. SPIN-guided engineering of a novel (Synthetic and systems biotechnology · 2026
    Article
  6. Article
  7. Article
  8. Optimizing Stability in Dynamic Small-Molecule Binding Proteins.Journal of the American Chemical Society · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Insight into Protein Engineering: FromCurrent pharmaceutical design · 2025
    Review
  17. Circular Engineered Sortase for Interrogating Histone H3 in Chromatin.Journal of the American Chemical Society · 2024
    Article
  18. Article
  19. Review
  20. Article

2 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

9 authors at 2 institutions in 1 country.

Milos MusilLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Jan StouracLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Jaroslav BendlLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Jan BrezovskyLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Zbynek ProkopLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Jaroslav ZendulkaDepartment of Information Systems, Faculty of Information Technology, Brno University of Technology, Brno, Czech Republic.
Tomas MartinekLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
David BednarLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Jiri DamborskyLoschmidt Laboratories, Department of Experimental Biology, Masaryk University, Brno, Czech Republic.
Masaryk University · CZVSB - Technical University of Ostrava · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is a continuous interest in increasing proteins stability to enhance their usability in numerous biomedical and biotechnological applications. A number of in silico tools for the prediction of the effect of mutations on protein stability have been developed recently. However, only single-point mutations with a small effect on protein stability are typically predicted with the existing tools and have to be followed by laborious protein expression, purification, and characterization. Here, we present FireProt, a web server for the automated design of multiple-point thermostable mutant proteins that combines structural and evolutionary information in its calculation core. FireProt utilizes sixteen tools and three protein engineering strategies for making reliable protein designs. The server is complemented with interactive, easy-to-use interface that allows users to directly analyze and optionally modify designed thermostable mutants. FireProt is freely available at http://loschmidt.chemi.muni.cz/fireprot.

Indexed as

MutationUser-Computer InterfaceBacteriaDatabases, ProteinHumansHydrolasesInternetModels, MolecularProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein EngineeringProtein Interaction Domains and MotifsProtein StabilityStructure-Activity RelationshipThermodynamicshaloalkane dehalogenaseHydrolases

Identifiers

PMID28449074
PMCPMC5570187
OpenAlexW2607570365

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.