Evidence map›Paper›PMID 31257893›Full record

ArticleNano letters2019

Removal of a Conserved Disulfide Bond Does Not Compromise Mechanical Stability of a VHH Antibody Complex.

Haipei Liu, Valentin Schittny, Michael A Nash

Abstract read
In one paragraph

Article in Nano letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Deciphering the crystal structure of a novel nanobody against the NEIL1 DNA glycosylase.Acta crystallographica. Section D, Structural biology · 2024
    Article
  7. Article
  8. Review
  9. Article
  10. NbThermo: a new thermostability database for nanobodies.Database : the journal of biological databases and curation · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
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.

Haipei LiuDepartment of Chemistry , University of Basel , 4058 Basel , Switzerland.
Valentin SchittnyDepartment of Chemistry , University of Basel , 4058 Basel , Switzerland.
Michael A NashDepartment of Chemistry , University of Basel , 4058 Basel , Switzerland.ORCID 0000-0003-3842-1567

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-domain VHH antibodies are promising reagents for medical therapy. A conserved disulfide bond within the VHH framework region is known to be critical for thermal stability, however, no prior studies have investigated its influence on the stability of VHH antibody-antigen complexes under mechanical load. Here, we used single-molecule force spectroscopy to test the influence of a VHH domain's conserved disulfide bond on the mechanical strength of the interaction with its antigen mCherry. We found that although removal of the disulfide bond through cysteine-to-alanine mutagenesis significantly lowered VHH domain denaturation temperature, it had no significant impact on the mechanical strength of the VHH:mCherry interaction with complex rupture occurring at ∼60 pN at 10

Indexed as

AlanineCysteineDisulfidesLuminescent ProteinsModels, MolecularProtein DenaturationProtein DomainsProtein StabilityRed Fluorescent ProteinSingle-Domain AntibodiesTemperatureThermodynamicsAlanineCysteineDisulfidesLuminescent ProteinsRed Fluorescent ProteinSingle-Domain AntibodiesAntibodiesbiophysicsdisulfide bondnanobodysingle-molecule force spectroscopy

Identifiers

PMID31257893
PMCPMC6975629

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.