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20695994
Source:
http://linkedlifedata.com/resource/pubmed/id/20695994
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rdf:type
pubmed:Citation
lifeskim:mentions
umls-concept:C0022202
,
umls-concept:C0024742
,
umls-concept:C0038592
,
umls-concept:C1621532
pubmed:issue
3
pubmed:dateCreated
2010-8-18
pubmed:abstractText
Characterization of substrate specificity of a D-lyxose isomerase from Serratia proteamaculans and application of the enzyme in the production of D-lyxose and D-mannose.
pubmed:language
eng
pubmed:journal
http://linkedlifedata.com/resource/pubmed/journal/8510094
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aldose-Ketose Isomerases
,
http://linkedlifedata.com/resource/pubmed/chemical/D-lyxose ketol-isomerase
,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial
,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose
,
http://linkedlifedata.com/resource/pubmed/chemical/Pentoses
,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
,
http://linkedlifedata.com/resource/pubmed/chemical/lyxose
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1472-765X
pubmed:author
pubmed-author:ENGEE
,
pubmed-author:KimY-SYS
,
pubmed-author:ParkC-SCS
,
pubmed-author:RoeR TRT
,
pubmed-author:YeomS-JSJ
pubmed:issnType
Electronic
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
343-50
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:20695994-Aldose-Ketose Isomerases
,
pubmed-meshheading:20695994-DNA, Bacterial
,
pubmed-meshheading:20695994-Enzyme Stability
,
pubmed-meshheading:20695994-Hydrogen-Ion Concentration
,
pubmed-meshheading:20695994-Kinetics
,
pubmed-meshheading:20695994-Mannose
,
pubmed-meshheading:20695994-Molecular Sequence Data
,
pubmed-meshheading:20695994-Molecular Weight
,
pubmed-meshheading:20695994-Pentoses
,
pubmed-meshheading:20695994-Protein Multimerization
,
pubmed-meshheading:20695994-Recombinant Proteins
,
pubmed-meshheading:20695994-Sequence Analysis, DNA
,
pubmed-meshheading:20695994-Serratia
,
pubmed-meshheading:20695994-Substrate Specificity
,
pubmed-meshheading:20695994-Temperature
pubmed:year
2010
pubmed:articleTitle
Substrate specificity of a recombinant D-lyxose isomerase from Serratia proteamaculans that produces D-lyxose and D-mannose.
pubmed:affiliation
Department of Bioscience and Biotechnology, Konkuk University, Seoul, Korea.
pubmed:publicationType
Journal Article
,
Research Support, Non-U.S. Gov't