Evidence map›Paper›PMID 29567834›Full record

ArticleThe Journal of biological chemistry2018

The cohesin module is a major determinant of cellulosome mechanical stability.

Albert Galera-Prat, Sarah Moraïs, Yael Vazana, Edward A Bayer, Mariano Carrión-Vázquez

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Current challenges in designer cellulosome engineering.Applied microbiology and biotechnology · 2023
    Review
  3. Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Article
  5. Article
  6. Dynamic interactions of type I cohesin modules fine-tune the structure of the cellulosome ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  7. 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

5 authors.

Albert Galera-PratInstituto Cajal, IC-CSIC, Avenida Doctor Arce 37, 28002 Madrid, Spain; Instituto Madrileño de Estudios Avanzados en Nanociencia, Cantoblanco, 28049 Madrid, Spain.
Sarah MoraïsDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 76100, Israel.
Yael VazanaDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 76100, Israel.
Edward A BayerDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 76100, Israel.
Mariano Carrión-VázquezInstituto Cajal, IC-CSIC, Avenida Doctor Arce 37, 28002 Madrid, Spain; Instituto Madrileño de Estudios Avanzados en Nanociencia, Cantoblanco, 28049 Madrid, Spain. Electronic address: mcarrion@cajal.csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellulosomes are bacterial protein complexes that bind and efficiently degrade lignocellulosic substrates. These are formed by multimodular scaffolding proteins known as scaffoldins, which comprise cohesin modules capable of binding dockerin-bearing enzymes and usually a carbohydrate-binding module that anchors the system to a substrate. It has been suggested that cellulosomes bound to the bacterial cell surface might be exposed to significant mechanical forces. Accordingly, the mechanical properties of these anchored cellulosomes may be important to understand and improve cellulosome function. Here we used single-molecule force spectroscopy to study the mechanical properties of selected cohesin modules from scaffoldins of different cellulosomes. We found that cohesins located in the region connecting the cell and the substrate are more robust than those located outside these two anchoring points. This observation applies to cohesins from primary scaffoldins (

Indexed as

Acetivibrio thermocellusBacterial ProteinsBiomechanical PhenomenaCell Cycle ProteinsCellulosomesChromosomal Proteins, Non-HistoneCohesinsKineticsMembrane ProteinsMicroscopy, Atomic ForceMolecular Dynamics SimulationProtein BindingProtein RefoldingProtein StabilityBacterial ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsMembrane ProteinsSdbA protein, bacteriaatomic force microscopy (AFM)cellulosomedockerinlinkersnanomechanicsprotein stabilityscaffoldinscaffold proteinsingle-molecule biophysicssingle-molecule force spectroscopy

Identifiers

PMID29567834
PMCPMC5950008

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.