rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
8
|
pubmed:dateCreated |
2007-7-11
|
pubmed:abstractText |
We have shown that cytochrome b5 (cyt b5), along with its reductase, NADH cytochrome b5 reductase (b5R), is capable of direct xenobiotic biotransformation. We hypothesized that functionally significant genetic variability in cyt b5 could be found in healthy individuals.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
1744-6872
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
17
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
597-603
|
pubmed:dateRevised |
2007-12-3
|
pubmed:meshHeading |
pubmed-meshheading:17622936-Amino Acid Substitution,
pubmed-meshheading:17622936-Cytochromes b5,
pubmed-meshheading:17622936-DNA Mutational Analysis,
pubmed-meshheading:17622936-Escherichia coli,
pubmed-meshheading:17622936-Gene Expression Regulation,
pubmed-meshheading:17622936-HeLa Cells,
pubmed-meshheading:17622936-Humans,
pubmed-meshheading:17622936-Hydroxylamine,
pubmed-meshheading:17622936-Kinetics,
pubmed-meshheading:17622936-Mutant Proteins,
pubmed-meshheading:17622936-Oxidation-Reduction,
pubmed-meshheading:17622936-Protein Biosynthesis,
pubmed-meshheading:17622936-Protein Processing, Post-Translational,
pubmed-meshheading:17622936-RNA, Messenger
|
pubmed:year |
2007
|
pubmed:articleTitle |
Discovery and characterization of a cytochrome b5 variant in humans with impaired hydroxylamine reduction capacity.
|
pubmed:affiliation |
Department of Medical Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI 53706, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|