Evidence map›Paper›PMID 38676806›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Analysis of Protein Interactions in Patient-Derived Xenografts Using Immunoprecipitation.

Hozaifa Metwally, Maha M Elbrashy

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. 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. 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

2 authors.

Hozaifa MetwallyLaboratory of Immune Regulation, Immunology Frontier Research Center, Osaka University, Osaka, Japan. hozaifa1@ifrec.osaka-u.ac.jp.ORCID 0000-0002-8664-096X
Maha M ElbrashyLaboratory of Immune Regulation, Immunology Frontier Research Center, Osaka University, Osaka, Japan.ORCID 0000-0002-3167-8653

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are large, complex molecules that regulate multiple functions within the cell. The protein rarely functions as a single molecule, but rather interacts with one or more other proteins forming a dynamic network. Protein-protein interactions are critical for regulating the cell's response toward various stimuli from outside and inside the cell. Identification of protein-protein interactions enhanced our understanding of various biological processes in the living cell. Immunoprecipitation (IP) has been one of the standard and most commonly used biochemical methods to identify and confirm protein-protein interactions. IP uses a target protein-specific antibody conjugated with protein A/G affinity beads to identify molecules interacting with the target protein. Here, we describe the principle, procedure and challenges of the IP assay.

Indexed as

ImmunoprecipitationProtein Interaction MappingAnimalsHeterograftsHumansMiceProtein BindingProteinsProteinsImmunoprecipitationInteractionProtein

What OpenQuestion holds

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Registered trials

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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.