Evidence map›Paper›PMID 30394618›Full record

ArticleProtein science : a publication of the Protein Society2019

Thermal stability of single-domain antibodies estimated by molecular dynamics simulations.

Gert-Jan Bekker, Benson Ma, Narutoshi Kamiya

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Protein Data Bank Japan: Improved tools for sequence-oriented analysis of protein structures.Protein science : a publication of the Protein Society · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. General Trends of theInternational journal of molecular sciences · 2023
    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.

Gert-Jan BekkerInstitute for Protein Research, Osaka University, Suita, Osaka, Japan.
Benson MaSchool of Computational Science and Engineering, Georgia Institute of Technology, Atlanta, Georgia, 30332.
Narutoshi KamiyaGraduate School of Simulation Studies, University of Hyogo, Kobe, Hyogo, Japan.ORCID 0000-0002-0527-6968

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-domain antibodies (sdAbs) function like regular antibodies, however, consist of only one domain. Because of their low molecular weight, sdAbs have advantages with respect to production and delivery to their targets and for applications such as antibody drugs and biosensors. Thus, sdAbs with high thermal stability are required. In this work, we chose seven sdAbs, which have a wide range of melting temperature (T

Indexed as

Hot TemperatureMolecular Dynamics SimulationProtein StabilitySingle-Domain AntibodiesSingle-Domain Antibodiesmelting temperaturemolecular dynamics simulationpoint mutationssingle-domain antibodythermal stability

Identifiers

PMID30394618
PMCPMC6319760

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.