Evidence map›Paper›PMID 17506724›Full record

ArticleThe Biochemical journal2007

Novel xylan-binding properties of an engineered family 4 carbohydrate-binding module.

Lavinia Cicortas Gunnarsson, Cedric Montanier, Richard B Tunnicliffe, Mike P Williamson, Harry J Gilbert, Eva Nordberg Karlsson, Mats Ohlin

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 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
0.9field-weighted citation impact, top 27% 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, 32 citations in OpenAlex.

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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

7 authors at 1 institution in 1 country.

Lavinia Cicortas GunnarssonDepartment of Immunotechnology, Lund University, BMC D13, SE-221 84 Lund, Sweden.
Cedric Montanier
Richard B Tunnicliffe
Mike P Williamson
Harry J Gilbert
Eva Nordberg Karlsson
Mats Ohlin
Lund University · SE

Funding

Biotechnology and Biological Sciences Research Council BB/C005074/1
6 · The paper itself

Abstract

Molecular engineering of ligand-binding proteins is commonly used for identification of variants that display novel specificities. Using this approach to introduce novel specificities into CBMs (carbohydrate-binding modules) has not been extensively explored. Here, we report the engineering of a CBM, CBM4-2 from the Rhodothermus marinus xylanase Xyn10A, and the identification of the X-2 variant. As compared with the wild-type protein, this engineered module displays higher specificity for the polysaccharide xylan, and a lower preference for binding xylo-oligomers rather than binding the natural decorated polysaccharide. The mode of binding of X-2 differs from other xylan-specific CBMs in that it only has one aromatic residue in the binding site that can make hydrophobic interactions with the sugar rings of the ligand. The evolution of CBM4-2 has thus generated a xylan-binding module with different binding properties to those displayed by CBMs available in Nature.

Indexed as

AmidesAmino Acid Sequencebeta-GlucansEndo-1,4-beta XylanasesLigandsModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiaryRhodothermusSequence AlignmentSequence Homology, Amino AcidSolubilityStructural Homology, ProteinAmidesbeta-GlucansEndo-1,4-beta XylanasesLigandsXylans

Identifiers

PMID17506724
PMCPMC1948960
OpenAlexW1982048030

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.