Evidence map›Paper›PMID 18535787›Full record

ArticlePlant molecular biology2008

Identification of ubiquitinated proteins in Arabidopsis.

Concepción Manzano, Zamira Abraham, Gema López-Torrejón, Juan C Del Pozo

Abstract read
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In one paragraph

Article in Plant molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 104 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Root Membrane Ubiquitinome under Short-Term Osmotic Stress.International journal of molecular sciences · 2022
    Article
  6. Journal of fungi (Basel, Switzerland) · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. TheFrontiers in plant science · 2019
    Article
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  13. 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

4 authors at 1 institution in 1 country.

Concepción ManzanoCentro de Biotecnología y Genómica de Plantas, Campus de Montegancedo s/n. Boadilla del Monte, Madrid, Spain.
Zamira Abraham
Gema López-Torrejón
Juan C Del Pozo
Centre for Plant Biotechnology and Genomics · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin (Ub) is a small peptide that is covalently attached to proteins in a posttranslational reaction. Ubiquitination is a precise regulatory system that is present in all eukaryotic organisms and regulates the stability, the activity, the localization and the transport of proteins. Ubiquitination involves different enzymatic activities, in which the E3 ligases catalyze the last step recruiting of the target for labelling with ubiquitin. Genomic analyses have shown that the ubiquitin-proteasome system involves a large number of proteins in plants, as approximately 5% of the total protein belongs to this pathway. In contrast to the high number of E3 ligases of ubiquitin identified, very few proteins regulated by ubiquitination have been described. To solve this, we have undertaken a new proteomic approach aimed to identify proteins modified with ubiquitin. This is based on affinity purification and identification for ubiquitinated proteins using the ubiquitin binding domain (UBA) polypeptide of the P62 protein attached to agarose beads. This P62-agarose matrix is capable of specifically binding ubiquitinated proteins. These bound proteins were digested with trypsin and the peptides separated by HPLC chromatography, spotted directly onto a MALDI target and analyzed by MALDI-TOF/TOF off-line coupled LC/MALDI-MS/MS. A total of 200 putative ubiquitinated proteins were identified. From these we found that several of the putative targets were already described in plants, as well as in other organisms, as ubiquitinated proteins. In addition, we have found that some of these proteins were indeed modified with ubiquitin in vivo. Taken together, we have shown that this approach is useful for identifying ubiquitinated protein in plants.

Indexed as

ArabidopsisArabidopsis ProteinsChromatography, AffinityChromatography, High Pressure LiquidImmunoprecipitationProtein BindingSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationUbiquitinationArabidopsis Proteins

Identifiers

PMID18535787
OpenAlexW2052460311

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.