Evidence map›Paper›PMID 22626931›Full record

ReviewMicrobes and infection2012

Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic target.

Nina M Haste, Hana Talabani, Alex Doo, Anais Merckx, Gordon Langsley, Susan S Taylor

Open access · greenAbstract readReview
In one paragraph

Review in Microbes and infection, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
5.0field-weighted citation impact, top 5% 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

20 citing papers in PubMed, 46 citations in OpenAlex.

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  19. Assembly of allosteric macromolecular switches: lessons from PKA.Nature reviews. Molecular cell biology · 2012
    Review
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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

6 authors at 3 institutions in 2 countries.

Nina M HasteSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California-San Diego, La Jolla, CA 92093-0687, USA.
Hana Talabani
Alex Doo
Anais Merckx
Gordon Langsley
Susan S Taylor
University of California San Diego · USCentre National de la Recherche Scientifique · FRDélégation Paris 5 · FR

Funding

Protein Kinase Regulatory Subunit I Directed MutagenesisR01GM034921 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2018
$7.2M
Protein Kinase: Primary Structure and cAMP InteractionsR01GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2013
$3.4M
PROTEIN KINASE: PRIMARY STRUCTURE AND CAMP INTERACTIONR37GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI TAYLOR, SUSAN S · 1995 to 2004
$2.0M
New Antiobiotics Against Drug-Resistant Pathogens from Marine Natural ProductsF31GM090658 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HASTE, NINA MARIE · 2010 to 2011
$57k
Howard Hughes Medical InstituteNIGMS NIH HHS 5F31 GM090658-02NIGMS NIH HHS F31 GM090658NIGMS NIH HHS GM19301NIGMS NIH HHS GM34921NIGMS NIH HHS R01 GM019301NIGMS NIH HHS R01 GM034921NIGMS NIH HHS R37 GM019301
6 · The paper itself

Abstract

One of the prototype mammalian kinases is PKA and various roles have been defined for PKA in malaria pathogenesis. The recently described phospho-proteomes of Plasmodium falciparum introduced a great volume of phospho-peptide data for both basic research and identification of new anti-malaria therapeutic targets. We discuss the importance of phosphorylations detected in vivo at different sites in the parasite R and C subunits of PKA and highlight the inhibitor sites in the parasite R subunit. The N-terminus of the parasite R subunit is predicted to be very flexible and we propose that phosphorylation at multiple sites in this region likely represent docking sites for interactions with other proteins, such as 14-3-3. The most significant observation when the P. falciparum C subunit is compared to mammalian C isoforms is lack of phosphorylation at a key site tail implying that parasite kinase activity is not regulated so tightly as mammalian PKA. Phosphorylation at sites in the activation loop could be mediating a number of processes from regulating parasite kinase activity, to mediating docking of other proteins. The important differences between Plasmodium and mammalian PKA isoforms that indicate the parasite kinase is a valid anti-malaria therapeutic target.

Indexed as

Protein Processing, Post-TranslationalAntimalarialsCyclic AMP-Dependent Protein KinasesEnzyme InhibitorsHumansPhosphorylationPlasmodium falciparumProtozoan ProteinsAntimalarialsCyclic AMP-Dependent Protein KinasesEnzyme InhibitorsProtozoan Proteins

Identifiers

PMID22626931
PMCPMC3967591
OpenAlexW2040619015

What OpenQuestion holds

Textmetadata
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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.