Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2000-10-5
pubmed:databankReference
pubmed:abstractText
Lesions in the gene for frataxin, a nuclear-encoded mitochondrial protein, cause the recessively inherited condition Friedreich's ataxia. It is thought that the condition arises from disregulation of mitochondrial iron homeostasis, with concomitant oxidative damage leading to neuronal death. Very little is, as yet, known about the biochemical function of frataxin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Iron, http://linkedlifedata.com/resource/pubmed/chemical/Iron-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transferrin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/frataxin
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
695-707
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10903947-Amino Acid Sequence, pubmed-meshheading:10903947-Animals, pubmed-meshheading:10903947-Bacterial Proteins, pubmed-meshheading:10903947-Carrier Proteins, pubmed-meshheading:10903947-Circular Dichroism, pubmed-meshheading:10903947-Evolution, Molecular, pubmed-meshheading:10903947-Friedreich Ataxia, pubmed-meshheading:10903947-Fungal Proteins, pubmed-meshheading:10903947-Helminth Proteins, pubmed-meshheading:10903947-Heterozygote, pubmed-meshheading:10903947-Humans, pubmed-meshheading:10903947-Iron, pubmed-meshheading:10903947-Iron-Binding Proteins, pubmed-meshheading:10903947-Ligands, pubmed-meshheading:10903947-Mice, pubmed-meshheading:10903947-Mitochondria, pubmed-meshheading:10903947-Models, Molecular, pubmed-meshheading:10903947-Molecular Sequence Data, pubmed-meshheading:10903947-Oxidative Stress, pubmed-meshheading:10903947-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:10903947-Plant Proteins, pubmed-meshheading:10903947-Point Mutation, pubmed-meshheading:10903947-Protein Conformation, pubmed-meshheading:10903947-Protein Structure, Secondary, pubmed-meshheading:10903947-Recombinant Fusion Proteins, pubmed-meshheading:10903947-Sequence Alignment, pubmed-meshheading:10903947-Sequence Homology, Amino Acid, pubmed-meshheading:10903947-Species Specificity, pubmed-meshheading:10903947-Structure-Activity Relationship, pubmed-meshheading:10903947-Transferrin-Binding Proteins
pubmed:year
2000
pubmed:articleTitle
Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin.
pubmed:affiliation
NIMR, Mill Hill, NW7 1AA, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't