Evidence map›Paper›PMID 28581033›Full record

ReviewThe New phytologist2018

Life and death of proteins after protease cleavage: protein degradation by the N-end rule pathway.

Nico Dissmeyer, Susana Rivas, Emmanuelle Graciet

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in The New phytologist, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
22.8field-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

44 citing papers in PubMed, 92 citations in OpenAlex.

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  10. Frontiers in molecular biosciences · 2023
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  13. Label-Free Quantitative Proteomics Reveal the Involvement of PRT6 inInternational journal of molecular sciences · 2022
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 3 institutions in 3 countries.

Nico DissmeyerIndependent Junior Research Group on Protein Recognition and Degradation, Leibniz Institute of Plant Biochemistry (IPB), Weinberg 3, Halle (Saale), D-06120, Germany.ORCID 0000-0002-4156-3761
Susana RivasLIPM, Université de Toulouse, INRA, CNRS, Castanet-Tolosan, 31 326, France.
Emmanuelle GracietDepartment of Biology, Maynooth University, Maynooth, Co. Kildare, Ireland.ORCID 0000-0003-3548-8213
Centre National de la Recherche Scientifique · FRLeibniz Institute of Plant Biochemistry · DENational University of Ireland, Maynooth · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Contents Summary 929 I.

introductionconservation and diversity of N-end rule pathways 929 II. Defensive functions of the N-end rule pathway in plants 930 III. Proteases and degradation by the N-end rule pathway 930 IV. New proteomics approaches for the identification of N-end rule substrates 932 V. Concluding remarks 932 Acknowledgements 934 References 934 SUMMARY: The N-end rule relates the stability of a protein to the identity of its N-terminal residue and some of its modifications. Since its discovery in the 1980s, the repertoire of N-terminal degradation signals has expanded, leading to a diversity of N-end rule pathways. Although some of these newly discovered N-end rule pathways remain largely unexplored in plants, recent discoveries have highlighted roles of N-end rule-mediated protein degradation in plant defense against pathogens and in cell proliferation during organ growth. Despite this progress, a bottleneck remains the proteome-wide identification of N-end rule substrates due to the prerequisite for endoproteolytic cleavage and technical limitations. Here, we discuss the recent diversification of N-end rule pathways and their newly discovered functions in plant defenses, stressing the role of proteases. We expect that novel proteomics techniques (N-terminomics) will be essential for substrate identification. We review these methods, their limitations and future developments.

Indexed as

ProteolysisEndopeptidasesPlant ProteinsPlantsProteomicsSubstrate SpecificityEndopeptidasesPlant Proteinsarginylationcysteine oxidationN-degronN-end rule pathwayN-recogninsN-terminomicsproteasesubiquitin-proteasome system

Identifiers

PMID28581033
OpenAlexW2624375602

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.