ライフサイエンスコーパス: gamma-carboxyglutamate

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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.

6 haracteristic of conotoxins (hydroxyproline, gamma-carboxyglutamate) are present.

7 Conantokin-R (con-R), a gamma-carboxyglutamate-containing 27-residue peptide, is

8 We have purified two novel gamma-carboxyglutamate-containing conotoxins, Gla-TxX an

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

11 c" peptide has 27 amino acids, including two gamma-carboxyglutamate (Gla) residues.

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

17 ng glutamate residues in certain proteins to gamma-carboxyglutamate (Gla).

18 ationally modified amino acids, particularly gamma-carboxyglutamate (Gla).

19 gamma-Carboxyglutamate has also been found in a number o

20 on full-length prothrombin variants lacking gamma-carboxyglutamate modifications (desGla) with impai

21 alady caused by functional defects of matrix gamma-carboxyglutamate protein (MGP).

22 ted phosphoprotein 1 (osteopontin), and bone gamma-carboxyglutamate protein (osteocalcin) are increas

23 n near the amino terminus of both connexins, gamma-carboxyglutamate residues in the cytoplasmic loop

24 tide region, consistent with the presence of gamma-carboxyglutamate residues in this peptide.

25 etween two distinct conformers, and has four gamma-carboxyglutamate residues.

26 blood clotting cascade bind, via their GLA (gamma-carboxyglutamate-rich) domains, to membranes conta

27 gn)AAO; and au5a, FCCPFIRYCCW (where gamma = gamma-carboxyglutamate, W(+) = bromotryptophan, O = hydr

28 ependent gamma-carboxylation of glutamate to gamma-carboxyglutamate was originally well characterized

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