Evidence map›Paper›PMID 17905885›Full record

ArticleApplied and environmental microbiology2007

Exploration of new geometries in cellulosome-like chimeras.

Florence Mingardon, Angélique Chanal, Chantal Tardif, Edward A Bayer, Henri-Pierre Fierobe

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

31 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Current challenges in designer cellulosome engineering.Applied microbiology and biotechnology · 2023
    Review
  4. Carbohydrate Depolymerization by Intricate Cellulosomal Systems.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  5. Article
  6. Frontiers in microbiology · 2022
    Article
  7. Mechanisms and Effects of Substrate Channelling in Enzymatic Cascades.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  8. Article
  9. Review
  10. Article
  11. Biomimetic strategy for constructingBiotechnology for biofuels · 2018
    Article
  12. Review
  13. Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Integration of bacterial lytic polysaccharide monooxygenases into designer cellulosomes promotes enhanced cellulose degradation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  18. Article
  19. Article
  20. 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 at 3 institutions in 2 countries.

Florence MingardonDepartment of Bioénergétique et Ingénierie des Protéines, CNRS, IBSM, 13402 Marseille, France.
Angélique Chanal
Chantal Tardif
Edward A Bayer
Henri-Pierre Fierobe
Centre National de la Recherche Scientifique · FRBioénergétique et Ingénierie des Protéines · FRWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this study, novel cellulosome chimeras exhibiting atypical geometries and binding modes, wherein the targeting and proximity functions were directly incorporated as integral parts of the enzyme components, were designed. Two pivotal cellulosomal enzymes (family 48 and 9 cellulases) were thus appended with an efficient cellulose-binding module (CBM) and an optional cohesin and/or dockerin. Compared to the parental enzymes, the chimeric cellulases exhibited improved activity on crystalline cellulose as opposed to their reduced activity on amorphous cellulose. Nevertheless, the various complexes assembled using these engineered enzymes were somewhat less active on crystalline cellulose than the conventional designer cellulosomes containing the parental enzymes. The diminished activity appeared to reflect the number of protein-protein interactions within a given complex, which presumably impeded the mobility of their catalytic modules. The presence of numerous CBMs in a given complex, however, also reduced their performance. Furthermore, a "covalent cellulosome" that combines in a single polypeptide chain a CBM, together with family 48 and family 9 catalytic modules, also exhibited reduced activity. This study also revealed that the cohesin-dockerin interaction may be reversible under specific conditions. Taken together, the data demonstrate that cellulosome components can be used to generate higher-order functional composites and suggest that enzyme mobility is a critical parameter for cellulosome efficiency.

Indexed as

Cell Cycle ProteinsCellulasesCelluloseCellulosomesChromosomal Proteins, Non-HistoneCohesinsElectrophoresis, Polyacrylamide GelHydrolysisKineticsModels, BiologicalNuclear ProteinsProtein BindingRecombinant Fusion ProteinsCell Cycle ProteinsCellulasesCelluloseChromosomal Proteins, Non-HistoneCohesinsNuclear ProteinsRecombinant Fusion Proteins

Identifiers

PMID17905885
PMCPMC2168198
OpenAlexW2165978836

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.