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210168
Source:
http://linkedlifedata.com/resource/pubmed/id/210168
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(
51
)
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Statements in which the resource exists as a subject.
Predicate
Object
rdf:type
pubmed:Citation
lifeskim:mentions
umls-concept:C0005456
,
umls-concept:C0010749
,
umls-concept:C0010760
,
umls-concept:C0024337
,
umls-concept:C0220806
,
umls-concept:C0392747
,
umls-concept:C0443199
,
umls-concept:C1554963
,
umls-concept:C1709915
,
umls-concept:C1880497
,
umls-concept:C1996904
pubmed:issue
17
pubmed:dateCreated
1978-10-27
pubmed:language
eng
pubmed:journal
http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids
,
http://linkedlifedata.com/resource/pubmed/chemical/Anhydrides
,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group
,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV
,
http://linkedlifedata.com/resource/pubmed/chemical/Formaldehyde
,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine
,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed-author:BosshardH RHR
,
pubmed-author:RiederRR
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
253
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6045-53
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed-meshheading:210168-Acetylation
,
pubmed-meshheading:210168-Amino Acids
,
pubmed-meshheading:210168-Anhydrides
,
pubmed-meshheading:210168-Binding Sites
,
pubmed-meshheading:210168-Cytochrome c Group
,
pubmed-meshheading:210168-Electron Transport Complex IV
,
pubmed-meshheading:210168-Formaldehyde
,
pubmed-meshheading:210168-Lysine
,
pubmed-meshheading:210168-Methylation
,
pubmed-meshheading:210168-Oxidation-Reduction
,
pubmed-meshheading:210168-Peptide Fragments
,
pubmed-meshheading:210168-Protein Binding
pubmed:year
1978
pubmed:articleTitle
The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome c.
pubmed:publicationType
Journal Article