Evidence map›Paper›PMID 40601143›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2025

High-Throughput Post-Translational Modification Analyses by Reverse Phase Protein Array.

Zhongcheng Shi, Michael Hoang Nguyen, Yuan Yao, Shixia Huang

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2025. 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

4 authors.

Zhongcheng ShiAdvanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
Michael Hoang NguyenAdvanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
Yuan YaoAdvanced Technology Cores, Baylor College of Medicine, Houston, TX, USA.
Shixia HuangAdvanced Technology Cores, Baylor College of Medicine, Houston, TX, USA. shixiah@bcm.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational modifications play a crucial role in regulating protein functions by chemically modifying amino acids without altering underlying protein sequences. Protein modifications are highly involved in cellular signal transduction pathways that require swift changes between active and inactive states. Various methods, including reverse phase protein array (RPPA), have been developed to comprehensively assess the proteomic profile. RPPA technology, a robust antibody-based platform, can detect not only protein expression but also modifications, such as phosphorylation, methylation, and acetylation. This chapter presents the detailed RPPA protocol for profiling post-translational modifications, including protein phosphorylation using whole cell lysates and histone modifications using purified histones.

Indexed as

High-Throughput Screening AssaysProtein Array AnalysisProtein Processing, Post-TranslationalProteomicsAcetylationHistonesHumansMethylationPhosphorylationHistonesAntibody-based proteomicsHigh throughputHistonePhosphorylationPost-translational modificationReverse phase protein array

Identifiers

PMID40601143

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.