Evidence map›Paper›PMID 33998133›Full record

ArticleEMBO reports2021

Ubiquitination by a Mycobacterium protein that mimics E1 and E3 activities.

Lei Song, Zhao-Qing Luo

Abstract readNewsComment
In one paragraph

Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Lei SongDepartment of Respiratory Medicine and Center of Infection and Immunity, Key Laboratory of Organ Regeneration and Transplantation of the Ministry of Education, The First Hospital, Jilin University, Changchun, China.ORCID 0000-0002-4115-065X
Zhao-Qing LuoDepartment of Respiratory Medicine and Center of Infection and Immunity, Key Laboratory of Organ Regeneration and Transplantation of the Ministry of Education, The First Hospital, Jilin University, Changchun, China.ORCID 0000-0001-8890-6621

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacterium tuberculosis (Mtb) has evolved various strategies to co-opt the host ubiquitin network to facilitate its proliferation. In the current issue of EMBO Reports, Liu and colleagues (Wang et al, 2021) demonstrate that the Mtb kinase PknG catalyzes ubiquitination by an unprecedented mechanism wherein the reaction starts by ATP hydrolysis occurring at the α-phosphate position, leading to covalent attachment of the modifier to Lys82 of the E2 conjugation enzyme UbcH7. Ubiquitin is then delivered to host proteins important for immunity by a putative peptidase activity also embedded in PknG. This novel activity of PknG expands our understanding of protein ubiquitination mechanisms, which may be harnessed to identify potential therapeutics for fighting Mtb infection.

Indexed as

Mycobacterium tuberculosisCyclic GMP-Dependent Protein KinasesUbiquitinUbiquitinationUbiquitin-Conjugating EnzymesCyclic GMP-Dependent Protein KinasesUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID33998133
PMCPMC8183397

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.