Evidence map›Paper›PMID 34309398›Full record

ArticleJournal of bacteriology2021

Modulation of the Enzymatic Activity of the Flagellar Lytic Transglycosylase SltF by Rod Components and the Scaffolding Protein FlgJ in

Mariela García-Ramos, Javier de la Mora, Teresa Ballado, Laura Camarena, Georges Dreyfus

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 26% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Microorganisms · 2021
    Review
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

5 authors at 1 institution in 1 country.

Mariela García-RamosInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, Mexico.
Javier de la MoraInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, Mexico.
Teresa BalladoInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, Mexico.
Laura CamarenaInstituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Mexico City, Mexico.ORCID 0000-0003-0344-6000
Georges DreyfusInstituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City, Mexico.ORCID 0000-0001-9502-5072
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macromolecular cell-envelope-spanning structures such as the bacterial flagellum must traverse the cell wall. Lytic transglycosylase enzymes are capable of enlarging gaps in the peptidoglycan meshwork to allow the efficient assembly of supramolecular complexes. In the periplasmic space, the assembly of the flagellar rod requires the scaffold protein FlgJ, which includes a muramidase domain in the canonical models Salmonella enterica and Escherichia coli. In contrast, in Rhodobacter sphaeroides, FlgJ and the dedicated flagellar lytic transglycosylase SltF are separate entities that interact in the periplasm. In this study, we show that

Indexed as

Bacterial ProteinsFlagellaGene Expression Regulation, BacterialRhodobacter sphaeroidesBacterial Proteinsflagellar biogenesisflagellar rodlytic transglycosylaseRhodobacter sphaeroidesSltF

Identifiers

PMID34309398
PMCPMC8459770
OpenAlexW3185982437

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.