Evidence map›Paper›PMID 37668966›Full record

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

Methods for Structure Determination of SH2 Domain-Phosphopeptide Complexes by NMR.

Vittoria Nanna, Michelangelo Marasco, John P Kirkpatrick, Teresa Carlomagno

Abstract read
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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. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 23% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Synthesis of aChembiochem : a European journal of chemical biology · 2025
    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

4 authors at 3 institutions in 3 countries.

Vittoria NannaBMWZ and Institute of Organic Chemistry, Leibniz University Hannover, Hannover, Germany.
Michelangelo MarascoMolecular Pharmacology Program, Sloan Kettering Institute for Cancer Research, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
John P KirkpatrickSchool of Biosciences, University of Birmingham, Birmingham, UK.
Teresa CarlomagnoSchool of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Birmingham, UK. t.carlomagno@bham.ac.uk.
University of Birmingham · GBLeibniz University Hannover · DEMemorial Sloan Kettering Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique to solve the structure of biomolecular complexes at atomic resolution in solution. Small proteins such as Src-homology 2 (SH2) domains have fast tumbling rates and long-lived NMR signals, making them particularly suited to be studied by standard NMR methods. SH2 domains are modular proteins whose function is the recognition of sequences containing phosphotyrosines. In this chapter, we describe the application of NMR to assess the interaction between SH2 domains and phosphopeptides and determine the structure of the resulting complexes.

Indexed as

Phosphopeptidessrc Homology DomainsMagnetic Resonance ImagingMagnetic Resonance SpectroscopyPhosphotyrosinePhosphopeptidesPhosphotyrosineIntermolecular interactionsNuclear magnetic resonance (NMR) spectroscopyPhosphopeptidesPhosphotyrosineSrc-homology 2 (SH2) domainStructure determination

Identifiers

PMID37668966
OpenAlexW4386438991

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.