Evidence map›Paper›PMID 21045122›Full record

ArticlePlant physiology2011

Proteasome activity imaging and profiling characterizes bacterial effector syringolin A.

Izabella Kolodziejek, Johana C Misas-Villamil, Farnusch Kaschani, Jérôme Clerc, Christian Gu, Daniel Krahn, Sherry Niessen, Martijn Verdoes, Lianne I Willems, Hermen S Overkleeft and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 66 citations in OpenAlex.

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  15. Broad-range glycosidase activity profiling.Molecular & cellular proteomics : MCP · 2014
    Article
  16. Article
  17. Activity-based imaging probes of the proteasome.Cell biochemistry and biophysics · 2013
    Review
  18. Article
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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

12 authors at 4 institutions in 4 countries.

Izabella KolodziejekPlant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.
Johana C Misas-Villamil
Farnusch Kaschani
Jérôme Clerc
Christian Gu
Daniel Krahn
Sherry Niessen
Martijn Verdoes
Lianne I Willems
Hermen S Overkleeft
Markus Kaiser
Renier A L van der Hoorn
Max Planck Society · DEChemical Genomics Centre · DEUniversity of Warsaw · PLLeiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Syringolin A (SylA) is a nonribosomal cyclic peptide produced by the bacterial pathogen Pseudomonas syringae pv syringae that can inhibit the eukaryotic proteasome. The proteasome is a multisubunit proteolytic complex that resides in the nucleus and cytoplasm and contains three subunits with different catalytic activities: β1, β2, and β5. Here, we studied how SylA targets the plant proteasome in living cells using activity-based profiling and imaging. We further developed this technology by introducing new, more selective probes and establishing procedures of noninvasive imaging in living Arabidopsis (Arabidopsis thaliana) cells. These studies showed that SylA preferentially targets β2 and β5 of the plant proteasome in vitro and in vivo. Structure-activity analysis revealed that the dipeptide tail of SylA contributes to β2 specificity and identified a nonreactive SylA derivative that proved essential for imaging experiments. Interestingly, subcellular imaging with probes based on epoxomicin and SylA showed that SylA accumulates in the nucleus of the plant cell and suggests that SylA targets the nuclear proteasome. Furthermore, subcellular fractionation studies showed that SylA labels nuclear and cytoplasmic proteasomes. The selectivity of SylA for the catalytic subunits and subcellular compartments is discussed, and the subunit selectivity is explained by crystallographic data.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCell NucleusCrystallography, X-RayFluorescenceImaging, Three-DimensionalMolecular ProbesMolecular Sequence DataOligopeptidesPeptides, CyclicProteasome Endopeptidase ComplexProteasome InhibitorsProtein SubunitsPseudomonas syringaeReproducibility of ResultsArabidopsis ProteinsepoxomicinMolecular ProbesOligopeptidesPeptides, CyclicProteasome Endopeptidase ComplexProteasome InhibitorsProtein Subunitssyringolin A

Identifiers

PMID21045122
PMCPMC3075764
OpenAlexW2123942875

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.