Evidence map›Paper›PMID 27382059›Full record

ArticleThe Journal of biological chemistry2016

Identification of Components of the SUMOylation Machinery in Candida glabrata: ROLE OF THE DESUMOYLATION PEPTIDASE CgUlp2 IN VIRULENCE.

Rahul Gujjula, Sangeetha Veeraiah, Kundan Kumar, Suman S Thakur, Krishnaveni Mishra, Rupinder Kaur

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Solo or in Concert: SUMOylation in Pathogenic Fungi.The plant pathology journal · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. SUMOylation in fungi: A potential target for intervention.Computational and structural biotechnology journal · 2020
    Review
  11. Article
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.

Rahul GujjulaFrom the Centre for DNA Fingerprinting and Diagnostics, Building 7, Gruhakalpa, 5-4-399/B, Nampally, Hyderabad 500001.
Sangeetha Veeraiahthe Department of Biochemistry, School of Life Science, University of Hyderabad, Prof. C. R. Rao Road, Gachibowli, Hyderabad 500046.
Kundan KumarFrom the Centre for DNA Fingerprinting and Diagnostics, Building 7, Gruhakalpa, 5-4-399/B, Nampally, Hyderabad 500001, the Graduate Studies Program, Manipal University, Manipal, Karnataka 576104, and.
Suman S Thakurthe Centre for Cellular and Molecular Biology, Habsiguda, Uppal Road, Hyderabad 500007, India.
Krishnaveni Mishrathe Department of Biochemistry, School of Life Science, University of Hyderabad, Prof. C. R. Rao Road, Gachibowli, Hyderabad 500046, krishnaveni.mishra@gmail.com.
Rupinder KaurFrom the Centre for DNA Fingerprinting and Diagnostics, Building 7, Gruhakalpa, 5-4-399/B, Nampally, Hyderabad 500001, rkaur@cdfd.org.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regulation of protein function by reversible post-translational modification, SUMOylation, is widely conserved in the eukaryotic kingdom. SUMOylation is essential for cell growth, division, and adaptation to stress in most organisms, including fungi. As these are key factors in determination of fungal virulence, in this study, we have investigated the importance of SUMOylation in the human pathogen, Candida glabrata We identified the enzymes involved in small ubiquitin-like modifier conjugation and show that there is strong conservation between Saccharomyces cerevisiae and C. glabrata We demonstrate that SUMOylation is an essential process and that adaptation to stress involves changes in global SUMOylation in C. glabrata Importantly, loss of the deSUMOylating enzyme CgUlp2 leads to highly reduced small ubiquitin-like modifier protein levels, and impaired growth, sensitivity to multiple stress conditions, reduced adherence to epithelial cells, and poor colonization of specific tissues in mice. Our study thus demonstrates a key role for protein SUMOylation in the life cycle and pathobiology of C. glabrata.

Indexed as

SumoylationAnimalsCandida glabrataCandidiasisCell Line, TumorEndopeptidasesFemaleFungal ProteinsHumansMiceMice, Inbred BALB CVirulence FactorsEndopeptidasesFungal ProteinsVirulence FactorsadhesionbiofilmC. glabrataEpa adhesinsfungal pathogenesismicrobial pathogenesissmall ubiquitin-like modifier (SUMO)SUMO ligaseSUMO peptidasesumoylation

Identifiers

PMID27382059
PMCPMC5016692

What OpenQuestion holds

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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.