Evidence map›Paper›PMID 23914800›Full record

ArticleJournal of proteome research2013

Global analysis of protein expression and phosphorylation of three stages of Plasmodium falciparum intraerythrocytic development.

Brittany N Pease, Edward L Huttlin, Mark P Jedrychowski, Eric Talevich, John Harmon, Timothy Dillman, Natarajan Kannan, Christian Doerig, Ratna Chakrabarti, Steven P Gygi and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 2 pooled it
13.7field-weighted citation impact, top 1% 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

103 citing papers in PubMed, 2 syntheses or guidelines pooled it, 179 citations in OpenAlex.

  1. Phosphorylation in theJournal of proteome research · 2024
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  17. mBio · 2023
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43 more citing papers are in PubMed but not listed here.

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

11 authors at 4 institutions in 2 countries.

Brittany N PeaseBurnett School of Biomedical Sciences, University of Central Florida, Orlando, Florida 32826, United States.
Edward L Huttlin
Mark P Jedrychowski
Eric Talevich
John Harmon
Timothy Dillman
Natarajan Kannan
Christian Doerig
Ratna Chakrabarti
Steven P Gygi
Debopam Chakrabarti
University of Central Florida · USHarvard University · USUniversity of Georgia · USMonash University · AU

Funding

New Sample Multiplexing Technologies to Identify Chemical Probes and Illuminate Ubiquitin BiologyR01GM067945 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2003 to 2024
$10.5M
New Technologies for Quantitative Phosphorylation AnalysisR01HG003456 · NHGRI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GYGI, STEVEN P · 2005 to 2011
$2.7M
Chemical Genetics of Plasmodium KinasesR01AI073795 · NIAID · UNIVERSITY OF CENTRAL FLORIDA · PI CHAKRABARTI, DEBOPAM · 2008 to 2010
$1.1M
NHGRI NIH HHS R01 HG003456NIAID NIH HHS AI73795NIAID NIH HHS R01 AI073795NIGMS NIH HHS R01 GM067945
6 · The paper itself

Abstract

During asexual intraerythrocytic development, Plasmodium falciparum diverges from the paradigm of the eukaryotic cell cycles by undergoing multiple rounds of DNA replication and nuclear division without cytokinesis. A better understanding of the molecular switches that coordinate a myriad of events for the progression of the parasite through the intraerythrocytic developmental stages will be of fundamental importance for rational design of intervention strategies. To achieve this goal, we performed isobaric tag-based quantitative proteomics and phosphoproteomics analyses of three developmental stages in the Plasmodium asexual cycle and identified 2767 proteins, 1337 phosphoproteins, and 6293 phosphorylation sites. Approximately 34% of identified proteins and 75% of phosphorylation sites exhibit changes in abundance as the intraerythrocytic cycle progresses. Our study identified 43 distinct phosphorylation motifs and a range of potential MAPK/CDK substrates. Further analysis of phosphorylated kinases identified 30 protein kinases with 126 phosphorylation sites within the kinase domain or in N- or C-terminal tails. Many of these phosphorylations are likely CK2-mediated. We define the constitutive and regulated expression of the Plasmodium proteome during the intraerythrocytic developmental cycle, offering an insight into the dynamics of phosphorylation during asexual cycle progression. Our system-wide comprehensive analysis is a major step toward defining kinase-substrate pairs operative in various signaling networks in the parasite.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceCells, CulturedErythrocytesHumansMolecular Sequence DataPhosphoproteinsPhosphorylationPlasmodium falciparumProtein KinasesProteomeProtozoan ProteinsSignal TransductionStaining and LabelingPhosphoproteinsProtein KinasesProteomeProtozoan Proteins

Identifiers

PMID23914800
PMCPMC5292867
OpenAlexW2017123927

What OpenQuestion holds

Textmetadata
LicenceTDM
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.