Evidence map›Paper›PMID 32808224›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

Simultaneous, Quantitative Characterization of Protein ADP-Ribosylation and Protein Phosphorylation in Macrophages.

Casey M Daniels, Arthur Nuccio, Pauline R Kaplan, Aleksandra Nita-Lazar

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. 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
0.5field-weighted citation impact, top 27% 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, 2 citations in OpenAlex.

  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 at 2 institutions in 1 country.

Casey M DanielsFunctional Cellular Networks Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Arthur NuccioFunctional Cellular Networks Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Pauline R KaplanFunctional Cellular Networks Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA.
Aleksandra Nita-LazarFunctional Cellular Networks Section, Laboratory of Immune System Biology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, USA. nitalazarau@niaid.nih.gov.
National Institute of Allergy and Infectious Diseases · USNational Institutes of Health · US

Funding

Protein Modifications Involved in Cell SignalingZIAAI001084 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI NITA-LAZAR, ALEKSANDRA · 2009 to 2025
$11.4M
Intramural NIH HHS ZIA AI001084
6 · The paper itself

Abstract

The posttranslational modifications (PTMs) ADP-ribosylation and phosphorylation are important regulators of cellular pathways, and while mass spectrometry (MS)-based methods for the study of protein phosphorylation are well developed, protein ADP-ribosylation methodologies are still in a rapidly developing stage. The method described in this chapter uses immobilized metal affinity chromatography (IMAC), a phosphoenrichment matrix, to enrich ADP-ribosylated peptides which have been cleaved down to their phosphoribose attachment sites by a phosphodiesterase, thus isolating the ADP-ribosylated and phosphorylated proteomes simultaneously. To achieve the robust, relative quantification of PTM-level changes we have incorporated dimethyl labeling, a straightforward and economical choice which can be used on lysate from any cell type, including primary tissue. The entire pipeline has been optimized to work in ADP-ribosylation-compatible buffers and with protease-laden lysate from macrophage cells.

Indexed as

Adenosine Diphosphate RiboseADP-RibosylationAnimalsCell LineHumansMacrophagesMicePeptidesPhosphoric Diester HydrolasesPhosphorylationProtein Processing, Post-TranslationalProteomeProteomicsRabbitsRAW 264.7 CellsTandem Mass SpectrometryAdenosine Diphosphate RibosePeptidesPhosphoric Diester HydrolasesProteomeADP-ribosylationDimethyl labelingIMACLC-MS/MSMass spectrometryMono(ADP-ribose)PhosphodiesterasePhosphoenrichmentPhosphoribosylationPhosphorylationPoly(ADP-ribose)Posttranslational modificationsProteomicsSVP

Identifiers

PMID32808224
PMCPMC13577242
OpenAlexW3058817922

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.