Evidence map›Paper›PMID 33710900›Full record

ArticleThe journal of physical chemistry letters2021

Substrates Modulate Charge-Reorganization Allosteric Effects in Protein-Protein Association.

Shirsendu Ghosh, Koyel Banerjee-Ghosh, Dorit Levy, Inbal Riven, Ron Naaman, Gilad Haran

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Chiral Induced Spin Selectivity.Chemical reviews · 2024
    Review
  7. New Perspective on Electron Transfer through Molecules.The journal of physical chemistry letters · 2022
    Article
  8. Control of protein activity by photoinduced spin polarized charge reorganization.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. 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

6 authors at 1 institution in 1 country.

Shirsendu GhoshDepartment of Chemical and Biological Physics, Weizmann Institute, Rehovot 76100, Israel.
Koyel Banerjee-GhoshDepartment of Chemical and Biological Physics, Weizmann Institute, Rehovot 76100, Israel.
Dorit LevyDepartment of Chemical and Biological Physics, Weizmann Institute, Rehovot 76100, Israel.
Inbal RivenDepartment of Chemical and Biological Physics, Weizmann Institute, Rehovot 76100, Israel.
Ron NaamanDepartment of Chemical and Biological Physics, Weizmann Institute, Rehovot 76100, Israel.ORCID http://orcid.org/0000-0003-1910-366X
Gilad HaranDepartment of Chemical and Biological Physics, Weizmann Institute, Rehovot 76100, Israel.ORCID http://orcid.org/0000-0003-1837-9779
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein function may be modulated by an event occurring far away from the functional site, a phenomenon termed allostery. While classically allostery involves conformational changes, we recently observed that charge redistribution within an antibody can also lead to an allosteric effect, modulating the kinetics of binding to target antigen. In the present work, we study the association of a polyhistidine tagged enzyme (phosphoglycerate kinase, PGK) to surface-immobilized anti-His antibodies, finding a significant Charge-Reorganization Allostery (CRA) effect. We further observe that PGK's negatively charged nucleotide substrates modulate CRA substantially, even though they bind far away from the His-tag-antibody interaction interface. In particular, binding of ATP reduces CRA by more than 50%. The results indicate that CRA is affected by the binding of charged molecules to a protein and provide further insight into the significant role that charge redistribution can play in protein function.

Indexed as

Adenosine TriphosphateAllosteric RegulationAntibodiesAntigen-Antibody ReactionsHistidineOligopeptidesPhosphoglycerate KinaseProtein ConformationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityAdenosine TriphosphateAntibodiesHis-His-His-His-His-HisHistidineOligopeptidesPhosphoglycerate KinaseRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID33710900
PMCPMC8041378
OpenAlexW3134434435

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.