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WormBase Tree Display for Paper: WBPaper00006483

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Name Class

WBPaper00006483Namecgc6483
doi10.1074/jbc.M401514200
AGRKB:101000000619603
DB_infoDatabaseMEDLINEPMID14985345
StatusValid
ReferenceTitleCollagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in Km values for peptide substrates with increasing chain length: mutation of one of the two catalytic sites in the tetramer inactivates the enzyme by more than half.
JournalJ Biol Chem
Page18656-61
Volume279
Publication_date2004-04-30
AuthorKukkola LPersonWBPerson7827
Koivunen P
Pakkanen O
Page APPersonWBPerson466
Myllyharju JPersonWBPerson7832
PersonWBPerson466
WBPerson7827
WBPerson7832
Brief_citationKukkola L et al. (2004) J Biol Chem "Collagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in ...."
AbstractWBPaper00006483
TypeJournal_articlePerson_evidenceWBPerson10877
Refers_toGeneWBGene00001077Curator_confirmedWBPerson627
WBGene00003963Curator_confirmedWBPerson627
WBGene00004025Curator_confirmedWBPerson627
SpeciesCaenorhabditis elegans
AntibodyWBAntibody00000539