Evidence map›Paper›PMID 34163600›Full record

ArticleChemical science2020

Anion binding to ubiquitin and its relevance to the Hofmeister effects.

Wei Yao, Kaiyu Wang, Aide Wu, Wayne F Reed, Bruce C Gibb

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Assessing Weak Anion Binding to Small Peptides.The journal of physical chemistry. B · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Biophysical andChemical communications (Cambridge, England) · 2022
    Article
  11. Article
  12. 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

5 authors at 1 institution in 1 country.

Wei YaoDepartment of Chemistry, Tulane University New Orleans LA 70118 USA bgibb@tulane.edu.ORCID https://orcid.org/0000-0002-4229-0486
Kaiyu WangDepartment of Chemistry, Tulane University New Orleans LA 70118 USA bgibb@tulane.edu.ORCID https://orcid.org/0000-0003-2464-2828
Aide WuDepartment of Physics and Engineering Physics, Tulane University New Orleans LA 70118 USA.ORCID https://orcid.org/0000-0002-8006-1254
Wayne F ReedDepartment of Physics and Engineering Physics, Tulane University New Orleans LA 70118 USA.
Bruce C GibbDepartment of Chemistry, Tulane University New Orleans LA 70118 USA bgibb@tulane.edu.ORCID https://orcid.org/0000-0002-4478-4084
Tulane University · US

Funding

Ion-Ion Interactions and the Reverse Hofmeister EffectR01GM125690 · NIGMS · TULANE UNIVERSITY OF LOUISIANA · PI GIBB, BRUCE C · 2018 to 2021
$1.7M
NIGMS NIH HHS R01 GM125690
6 · The paper itself

Abstract

Although the non-covalent interactions between proteins and salts contributing to the Hofmeister effects have been generally mapped, there are many questions regarding the specifics of these interactions. We report here studies involving the small protein ubiquitin and salts of polarizable anions. These studies reveal a complex interplay between the reverse Hofmeister effect at low pH, the salting-in Hofmeister effect at higher pH, and six anion binding sites in ubiquitin at the root of these phenomena. These sites are all located at protuberances of preorganized secondary structure, and although stronger at low pH, are still apparent when ubiquitin possesses no net charge. These results demonstrate the traceability of these Hofmeister phenomena and suggest new strategies for understanding the supramolecular properties of proteins.

Identifiers

PMID34163600
PMCPMC8178748
OpenAlexW3094845984

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.