Evidence map›Paper›PMID 17209020›Full record

ArticleJournal of bacteriology2007

Enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum explored by two-dimensional analysis: identification of seven genes encoding new dockerin-containing proteins.

Jean-Charles Blouzard, Caroline Bourgeois, Pascale de Philip, Odile Valette, Anne Bélaïch, Chantal Tardif, Jean-Pierre Bélaïch, Sandrine Pagès

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

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  12. Exploration of new geometries in cellulosome-like chimeras.Applied and environmental microbiology · 2007
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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

8 authors at 2 institutions in 2 countries.

Jean-Charles BlouzardLaboratoire de Bioénergétique et Ingénierie des Protéines, IBSM, Centre National de la Recherche Scientifique and Université de Provence, Marseille, France.
Caroline Bourgeois
Pascale de Philip
Odile Valette
Anne Bélaïch
Chantal Tardif
Jean-Pierre Bélaïch
Sandrine Pagès
Centre National pour la Recherche Scientifique et Technique (CNRST) · MABioénergétique et Ingénierie des Protéines · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme diversity of the cellulolytic system produced by Clostridium cellulolyticum grown on crystalline cellulose as a sole carbon and energy source was explored by two-dimensional electrophoresis. The cellulolytic system of C. cellulolyticum is composed of at least 30 dockerin-containing proteins (designated cellulosomal proteins) and 30 noncellulosomal components. Most of the known cellulosomal proteins, including CipC, Cel48F, Cel8C, Cel9G, Cel9E, Man5K, Cel9M, and Cel5A, were identified by using two-dimensional Western blot analysis with specific antibodies, whereas Cel5N, Cel9J, and Cel44O were identified by using N-terminal sequencing. Unknown enzymes having carboxymethyl cellulase or xylanase activities were detected by zymogram analysis of two-dimensional gels. Some of these enzymes were identified by N-terminal sequencing as homologs of proteins listed in the NCBI database. Using Trap-Dock PCR and DNA walking, seven genes encoding new dockerin-containing proteins were cloned and sequenced. Some of these genes are clustered. Enzymes encoded by these genes belong to glycoside hydrolase families GH2, GH9, GH10, GH26, GH27, and GH59. Except for members of family GH9, which contains only cellulases, the new modular glycoside hydrolases discovered in this work could be involved in the degradation of different hemicellulosic substrates, such as xylan or galactomannan.

Indexed as

Amino Acid SequenceBacterial ProteinsCellulaseCellulasesCelluloseChromosome WalkingElectrophoresis, Gel, Two-DimensionalGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicGlycoside HydrolasesMolecular Sequence DataMultienzyme ComplexesPolymerase Chain ReactionRuminiclostridium cellulolyticumSequence Analysis, DNABacterial ProteinsCellulaseCellulasesCellulosecellulosome, ClostridiumGlycoside HydrolasesMultienzyme Complexes

Identifiers

PMID17209020
PMCPMC1899368
OpenAlexW2108187350

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.