Evidence map›Paper›PMID 37668979›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Exploring the Binding Interaction Between Phosphotyrosine Peptides and SH2 Domains by Proximal Crosslinking.

Rui Wang, Yishu Bao, Jiang Xia

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Rui Wang *Department of Chemistry, The Chinese University of Hong Kong, Hong Kong, SAR, China.
Yishu Bao *Department of Chemistry, The Chinese University of Hong Kong, Hong Kong, SAR, China.
Jiang XiaDepartment of Chemistry, The Chinese University of Hong Kong, Hong Kong, SAR, China. jiangxia@cuhk.edu.hk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proximal crosslinking refers to the site-specific conjugation reaction between a synthetic ligand with a bioorthogonal reactive group incorporated at a particular site and a protein of interest (POI). The binding interaction positions a reactive group of a native amino acid of the POI to the proximity of the reactive group in the ligand. The covalent conjugation increases the molecular weight of the POI, shows an upshift in the polyacrylamide gel, and gives a fluorescent band if the ligand is fluorescently labeled. Here, we summarize a method to covalently conjugate phosphotyrosine peptides and SH2 domains that contain cysteine residues. This method yields covalent peptide blockers for a set of SH2 proteins and elucidates the binding interaction between phosphotyrosine peptides and SH2 domains.

Indexed as

Peptidessrc Homology DomainsAmino AcidsLigandsPhosphotyrosineAmino AcidsLigandsPeptidesPhosphotyrosinePhosphotyrosine peptidesProximal crosslinkingSite-specific conjugationSrc homology 2

Identifiers

PMID37668979

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.