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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
6 sed as separate domains of a single protein (peptidylglycine alpha-amidating monooxygenase or PAM).
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
20 7a, a copper-transporting P-type ATPase, and peptidylglycine alpha-amidating monooxygenase (PAM), a c
22 dy we used pharmacological tools to identify peptidylglycine alpha-amidating monooxygenase (PAM), a t
24 des require amidation for full activation by peptidylglycine alpha-amidating monooxygenase (PAM), a t
25 major membrane protein in atrial granules is peptidylglycine alpha-amidating monooxygenase (PAM), an
27 lability on the synthesis and trafficking of peptidylglycine alpha-amidating monooxygenase (PAM), an
32 many neuropeptides requires a single enzyme, peptidylglycine alpha-amidating monooxygenase (PAM), and
33 ted release of the peptide amidating enzyme, peptidylglycine alpha-amidating monooxygenase (PAM), and
34 and in situ hybridization, we find that both peptidylglycine alpha-amidating monooxygenase (PAM), the
35 ctions, catalyzed by acyl-CoA synthetase and peptidylglycine alpha-amidating monooxygenase (PAM).
37 lyase activities of the bifunctional enzyme, peptidylglycine alpha-amidating monooxygenase (PAM).
38 erminal amidation by the bifunctional enzyme peptidylglycine alpha-amidating monooxygenase (PAM).
39 g with the cytosolic routing determinants of peptidylglycine alpha-amidating monooxygenase (PAM).
40 posttranslational processing is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM).
41 peptide-processing integral membrane protein peptidylglycine alpha-amidating monooxygenase (PAM; EC 1
42 ha-N bond in N-benzoylglycine (hippurate) by peptidylglycine alpha-amidating monooxygenase to again y
43 lycine alpha-amidating lyase (PAL) domain of peptidylglycine alpha-amidating monooxygenase was invest
44 cesses PACAP's precursor to the mature form, peptidylglycine alpha-amidating monooxygenase, were upre