Evidence map›Paper›PMID 36823715›Full record

ArticleProtein science : a publication of the Protein Society2023

Multiplex measurement of protein-peptide dissociation constants using dialysis and mass spectrometry.

Yu Zhao, Gevorg Grigoryan

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Yu ZhaoDepartment of Computer Science, Dartmouth College, Hanover, New Hampshire, USA.ORCID 0000-0001-5008-0836
Gevorg GrigoryanDepartment of Computer Science, Dartmouth College, Hanover, New Hampshire, USA.

Funding

Computational design of novel protein binders based on structure mining and learning from dataR01GM132117 · NIGMS · DARTMOUTH COLLEGE · PI GRIGORYAN, GEVORG, KEATING, AMY E · 2020 to 2023
$1.5M
NIGMS NIH HHS R01 GM132117NIH HHS R01GM132117
6 · The paper itself

Abstract

We propose a high-throughput method for quantitatively measuring hundreds of protein-peptide binding affinities in parallel. In this assay, a solution of protein is dialyzed into a buffer containing a pool of potential binding peptides, such that upon equilibration the relative abundance of a peptide species is mathematically related to that peptide's dissociation constant, K

Indexed as

PeptidesRenal DialysisMass SpectrometryPeptide LibraryProteinsPeptide LibraryPeptidesProteinsaffinity measuringdialysishigh-throughputmass spectrometryPDZ domainprotein-peptide interaction

Identifiers

PMID36823715
PMCPMC10031237

What Socratic 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 Socratic graph.