Evidence map›Paper›PMID 28752383›Full record

ArticleGlycoconjugate journal2017

Construction and functional characterization of truncated versions of recombinant keratanase II from Bacillus circulans.

Haisheng Wang, Wenqin He, Peixia Jiang, Yanlei Yu, Lei Lin, Xiaojun Sun, Mattheos Koffas, Fuming Zhang, Robert J Linhardt

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 2017. 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
1.2field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 13 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

9 authors at 2 institutions in 2 countries.

Haisheng WangGraduate School of Chinese Academy of Agricultural Sciences, People's Republic of China, Beijing, 100081, China.
Wenqin HeDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Peixia JiangDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Yanlei YuDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Lei LinDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Xiaojun SunDepartment of Chemistry and Chemical Biology, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Mattheos KoffasDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA.
Fuming ZhangDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. zhangf2@rpi.edu.
Robert J LinhardtDepartment of Chemical and Biological Engineering, Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, 12180, USA. linhar@rpi.edu.
Rensselaer Polytechnic Institute · USChinese Academy of Agricultural Sciences · CN

Funding

In vitro synthesis of recombinant heparan sulfateR01HL094463 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI LIU, JIAN, PAWLINSKI, RAFAL L · 2009 to 2021
$5.2M
NHLBI NIH HHS HL094463NIH HHS HL125371NIH HHS HL136271
6 · The paper itself

Abstract

There is a need for degradative enzymes in the study of glycosaminoglycans. Many of these enzymes are currently available either in their natural or recombinant forms. Unfortunately, progress in structure-activity studies of keratan sulfate (KS) have been impeded by the lack of a commercially available endo-β-N-acetylglucosaminidase, keratantase II. The current study uses a recently published sequence of a highly thermostable keratanase II identified in Bacillus circulans to clone and express a series of truncation mutants in Escherichia coli BL21. The resulting truncated forms of keratanase II exhibit activity and excellent storage and thermal stability making these useful tools for glycobiology research.

Indexed as

AcetylglucosaminidaseAmino Acid SequenceBacillusBacterial ProteinsCloning, MolecularEnzyme StabilityEscherichia coliGene ExpressionHydrolysisIsoenzymesKeratan SulfateKineticsPlasmidsProtein EngineeringRecombinant ProteinsStructure-Activity RelationshipAcetylglucosaminidaseBacterial ProteinsIsoenzymeskeratanase IIKeratan SulfateRecombinant ProteinsHydrolaseKeratanase IIKeratan sulfate, glycosaminoglycanMass spectrometryProtein engineering

Identifiers

PMID28752383
OpenAlexW2739483527

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.