Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-3-29
pubmed:abstractText
Protein fold recognition using sequence profile searches frequently allows prediction of the structure and biochemical mechanisms of proteins with an important biological function but unknown biochemical activity. Here we describe such predictions resulting from an analysis of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenases, a class of enzymes that are widespread in eukaryotes and bacteria and catalyze a variety of reactions typically involving the oxidation of an organic substrate using a dioxygen molecule.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10222208, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10455179, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10493868, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10592240, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10611362, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10655615, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10734313, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-10950872, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-3536913, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-7791906, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-7928996, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-7952184, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-7984417, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-8175725, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-8345525, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-8600462, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-8621606, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9096332, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9135134, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9254694, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9395322, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9398335, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9461283, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9504803, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9541544, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9667935, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9723623, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9738467, http://linkedlifedata.com/resource/pubmed/commentcorrection/11276424-9852764
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alkane 1-Monooxygenase, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System, http://linkedlifedata.com/resource/pubmed/chemical/Egl-9 protein, C elegans, http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Iron, http://linkedlifedata.com/resource/pubmed/chemical/Ketoglutaric Acids, http://linkedlifedata.com/resource/pubmed/chemical/LEPRE1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases, http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans, http://linkedlifedata.com/resource/pubmed/chemical/alpha-ketoglutaric acid
pubmed:status
MEDLINE
pubmed:issn
1465-6914
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
RESEARCH0007
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11276424-Alkane 1-Monooxygenase, pubmed-meshheading:11276424-Amino Acid Sequence, pubmed-meshheading:11276424-Animals, pubmed-meshheading:11276424-Caenorhabditis elegans Proteins, pubmed-meshheading:11276424-Computational Biology, pubmed-meshheading:11276424-Conserved Sequence, pubmed-meshheading:11276424-Cytochrome P-450 Enzyme System, pubmed-meshheading:11276424-Databases as Topic, pubmed-meshheading:11276424-Evolution, Molecular, pubmed-meshheading:11276424-Expressed Sequence Tags, pubmed-meshheading:11276424-Helminth Proteins, pubmed-meshheading:11276424-Humans, pubmed-meshheading:11276424-Iron, pubmed-meshheading:11276424-Ketoglutaric Acids, pubmed-meshheading:11276424-Membrane Glycoproteins, pubmed-meshheading:11276424-Mixed Function Oxygenases, pubmed-meshheading:11276424-Models, Molecular, pubmed-meshheading:11276424-Molecular Sequence Data, pubmed-meshheading:11276424-Oxygenases, pubmed-meshheading:11276424-Protein Folding, pubmed-meshheading:11276424-Protein Structure, Secondary, pubmed-meshheading:11276424-Proteoglycans, pubmed-meshheading:11276424-Sequence Alignment, pubmed-meshheading:11276424-Sequence Homology, pubmed-meshheading:11276424-Software
pubmed:year
2001
pubmed:articleTitle
The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases.
pubmed:affiliation
National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA. aravind@ncbi.nlm.nih.gov
pubmed:publicationType
Journal Article