Evidence map›Paper›PMID 31114592›Full record

ArticleFrontiers in plant science2019

Proteases Underground: Analysis of the Maize Root Apoplast Identifies Organ Specific Papain-Like Cysteine Protease Activity.

Jan Schulze Hüynck, Farnusch Kaschani, Karina van der Linde, Sebastian Ziemann, André N Müller, Thomas Colby, Markus Kaiser, Johana C Misas Villamil, Gunther Doehlemann

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

9 citing papers in PubMed, 20 citations in OpenAlex.

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  9. The Apoplast: A Key Player in Plant Survival.Antioxidants (Basel, Switzerland) · 2020
    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

9 authors at 5 institutions in 1 country.

Jan Schulze HüynckCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, Germany.
Farnusch KaschaniMax Planck Institute for Plant Breeding Research, Cologne, Germany.
Karina van der LindeMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Sebastian ZiemannCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, Germany.
André N MüllerMax Planck Institute for Terrestrial Microbiology, Marburg, Germany.
Thomas ColbyMax Planck Institute for Plant Breeding Research, Cologne, Germany.
Markus KaiserInstitute of Chemical Biology, University of Duisburg-Essen, Essen, Germany.
Johana C Misas VillamilCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, Germany.
Gunther DoehlemannCenter of Excellence on Plant Sciences (CEPLAS), Botanical Institute, University of Cologne, Cologne, Germany.
Cluster of Excellence on Plant Sciences · DEMax Planck Institute for Plant Breeding Research · DEMax Planck Institute for Terrestrial Microbiology · DEUniversity of Cologne · DEUniversity of Duisburg-Essen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant proteases are key regulators of plant cell processes such as seed development, immune responses, senescence and programmed cell death (PCD). Apoplastic papain-like cysteine proteases (PL) are hubs in plant-microbe interactions and play an important role during abiotic stresses. The apoplast is a crucial interface for the interaction between plant and microbes. So far, apoplastic maize PL and their function have been mostly described for aerial parts. In this study, we focused on apoplastic PLCPs in the roots of maize plants. We have analyzed the phylogeny of maize PLCPs and investigated their protein abundance after salicylic acid (SA) treatment. Using activity-based protein profiling (ABPP) we have identified a novel root-specific PLCP belonging to the RD21-like subfamily, as well as three SA activated PLCPs. The root specific PLCP CP1C shares sequence and structural similarities to known CP1-like proteases. Biochemical analysis of recombinant CP1C revealed different substrate specificities and inhibitor affinities compared to the related proteases. This study characterized a root-specific PLCP and identifies differences between the SA-dependent activation of PLCPs in roots and leaves.

Indexed as

apoplastorgan specificPLCProotsalicylic acid

Identifiers

PMID31114592
PMCPMC6503450
OpenAlexW2943500866

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.