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1 lyzes the conversion of glutamyl residues to gamma-carboxyglutamate.
2 ion of certain protein glutamate residues to gamma-carboxyglutamate.
3 y a posttranslationally modified amino acid, gamma-carboxyglutamate.
4 ues of its vitamin K-dependent substrates to gamma-carboxyglutamate.
5 roglutamic acid, Hyp = hydroxyproline, Gla = gamma-carboxyglutamate, and Trp* = L-6-bromotryptophan.
9 gment 12 (F12), is composed of an N-terminal gamma-carboxyglutamate domain (Gla) followed by two krin
10 and -Pr3) contains 19 amino acids with three gamma-carboxyglutamate (Gla) residues, a post-translatio
12 e of the Ca2+-loaded conantokin-T (con-T), a gamma-carboxyglutamate (Gla)-containing 21-residue pepti
13 ne snail Conus geographus is a 17-amino acid gamma-carboxyglutamate (Gla)-containing peptide that inh
14 ovides evidence that conantokin-G (con-G), a gamma-carboxyglutamate (Gla)-rich neuroactive peptide fr
15 okins are short (17-27 amino acid residues), gamma-carboxyglutamate (Gla)-rich peptide components of
16 s are a family of small, naturally occurring gamma-carboxyglutamate (Gla)-rich peptides that specific
20 on full-length prothrombin variants lacking gamma-carboxyglutamate modifications (desGla) with impai
22 ted phosphoprotein 1 (osteopontin), and bone gamma-carboxyglutamate protein (osteocalcin) are increas
23 significantly increased, including Sp7, bone gamma-carboxyglutamate protein, COL1A1, bone sialoprotei
24 s of sex-determining region Y box 9 and bone gamma-carboxyglutamate protein, key mediators of male se
25 n near the amino terminus of both connexins, gamma-carboxyglutamate residues in the cytoplasmic loop
27 ne to convert specific glutamate residues to gamma-carboxyglutamate residues in VK-dependent proteins
30 docks into FVIIa's active site, whereas the gamma-carboxyglutamate-rich (GLA) domain binds to the TF
31 blood clotting cascade bind, via their GLA (gamma-carboxyglutamate-rich) domains, to membranes conta
32 gn)AAO; and au5a, FCCPFIRYCCW (where gamma = gamma-carboxyglutamate, W(+) = bromotryptophan, O = hydr
33 ependent gamma-carboxylation of glutamate to gamma-carboxyglutamate was originally well characterized