ライフサイエンスコーパス: peptidylglycine alpha-amidating monooxygenase

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1 irst identified through its interaction with peptidylglycine-alpha-amidating monooxygenase.

2 was converted to DAB389SP by treatment with peptidylglycine-alpha-amidating monooxygenase.

3 l protein identified by its interaction with peptidylglycine alpha-amidating monooxygenase, an enzyme

4 he endogenous peptide-processing enzyme PAM (peptidylglycine alpha-amidating monooxygenase) as tools

5 The bifunctional enzyme peptidylglycine-alpha-amidating monooxygenase mediates t

6 sed as separate domains of a single protein (peptidylglycine alpha-amidating monooxygenase or PAM).

7 Peptidylglycine alpha-amidating monooxygenase (PAM) (EC

8 The luminal domains of membrane peptidylglycine alpha-amidating monooxygenase (PAM) are

9 Peptidylglycine alpha-amidating monooxygenase (PAM) cata

10 Peptidylglycine alpha-amidating monooxygenase (PAM) cata

11 Peptidylglycine alpha-amidating monooxygenase (PAM) cata

12 Peptidylglycine alpha-amidating monooxygenase (PAM) cata

13 olic domain of the peptide processing enzyme peptidylglycine alpha-amidating monooxygenase (PAM) cont

14 tigated the trafficking of integral membrane peptidylglycine alpha-amidating monooxygenase (PAM) in t

15 eady state distribution of membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) in t

16 Peptidylglycine alpha-amidating monooxygenase (PAM) is a

17 Because peptidylglycine alpha-amidating monooxygenase (PAM) is o

18 Peptidylglycine alpha-amidating monooxygenase (PAM), a b

19 7a, a copper-transporting P-type ATPase, and peptidylglycine alpha-amidating monooxygenase (PAM), a c

20 We examined the turnover of peptidylglycine alpha-amidating monooxygenase (PAM), a m

21 The two catalytic domains of peptidylglycine alpha-amidating monooxygenase (PAM), a t

22 des require amidation for full activation by peptidylglycine alpha-amidating monooxygenase (PAM), a t

23 dy we used pharmacological tools to identify peptidylglycine alpha-amidating monooxygenase (PAM), a t

24 We recently identified peptidylglycine alpha-amidating monooxygenase (PAM), an

25 Peptidylglycine alpha-amidating monooxygenase (PAM), an

26 Peptidylglycine alpha-amidating monooxygenase (PAM), an

27 Peptidylglycine alpha-amidating monooxygenase (PAM), an

28 Peptidylglycine alpha-amidating monooxygenase (PAM), an

29 lability on the synthesis and trafficking of peptidylglycine alpha-amidating monooxygenase (PAM), an

30 and in situ hybridization, we find that both peptidylglycine alpha-amidating monooxygenase (PAM), the

31 ctions, catalyzed by acyl-CoA synthetase and peptidylglycine alpha-amidating monooxygenase (PAM).

32 cytoplasmic domain of the amidating enzyme, peptidylglycine alpha-amidating monooxygenase (PAM).

33 lyase activities of the bifunctional enzyme, peptidylglycine alpha-amidating monooxygenase (PAM).

34 erminal amidation by the bifunctional enzyme peptidylglycine alpha-amidating monooxygenase (PAM).

35 g with the cytosolic routing determinants of peptidylglycine alpha-amidating monooxygenase (PAM).

36 posttranslational processing is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM).

37 peptide-processing integral membrane protein peptidylglycine alpha-amidating monooxygenase (PAM; EC 1

38 ha-N bond in N-benzoylglycine (hippurate) by peptidylglycine alpha-amidating monooxygenase to again y

39 lycine alpha-amidating lyase (PAL) domain of peptidylglycine alpha-amidating monooxygenase was invest

40 cesses PACAP's precursor to the mature form, peptidylglycine alpha-amidating monooxygenase, were upre

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