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1 the conversion of glutamyl residues to gamma-carboxyglutamate.
2 certain protein glutamate residues to gamma-carboxyglutamate.
3 sttranslationally modified amino acid, gamma-carboxyglutamate.
4 its vitamin K-dependent substrates to gamma-carboxyglutamate.
9 12 (F12), is composed of an N-terminal gamma-carboxyglutamate domain (Gla) followed by two kringles (
10 r3) contains 19 amino acids with three gamma-carboxyglutamate (Gla) residues, a post-translationally
12 he Ca2+-loaded conantokin-T (con-T), a gamma-carboxyglutamate (Gla)-containing 21-residue peptide (NH
13 il Conus geographus is a 17-amino acid gamma-carboxyglutamate (Gla)-containing peptide that inhibits
14 evidence that conantokin-G (con-G), a gamma-carboxyglutamate (Gla)-rich neuroactive peptide from a v
15 are short (17-27 amino acid residues), gamma-carboxyglutamate (Gla)-rich peptide components of the ve
16 a family of small, naturally occurring gamma-carboxyglutamate (Gla)-rich peptides that specifically a
20 ll-length prothrombin variants lacking gamma-carboxyglutamate modifications (desGla) with impaired me
22 osphoprotein 1 (osteopontin), and bone gamma-carboxyglutamate protein (osteocalcin) are increased by
23 the amino terminus of both connexins, gamma-carboxyglutamate residues in the cytoplasmic loop of bot
26 clotting cascade bind, via their GLA (gamma-carboxyglutamate-rich) domains, to membranes containing
27 ; and au5a, FCCPFIRYCCW (where gamma = gamma-carboxyglutamate, W(+) = bromotryptophan, O = hydroxypro
28 nt gamma-carboxylation of glutamate to gamma-carboxyglutamate was originally well characterized in th
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