The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity.
about
Molecular cloning of a preprohormone from sea anemones containing numerous copies of a metamorphosis-inducing neuropeptide: a likely role for dipeptidyl aminopeptidase in neuropeptide precursor processing.Insight into the molecular and functional diversity of cnidarian neuropeptides.Three different prohormones yield a variety of Hydra-RFamide (Arg-Phe-NH2) neuropeptides in Hydra magnipapillataStructure of neuropeptide precursors in cnidaria.
P2860
The primary structure of the Pol-RFamide neuropeptide precursor protein from the hydromedusa Polyorchis penicillatus indicates a novel processing proteinase activity.
description
1994 nî lūn-bûn
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1994年の論文
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name
The primary structure of the P ...... rocessing proteinase activity.
@ast
The primary structure of the P ...... rocessing proteinase activity.
@en
type
label
The primary structure of the P ...... rocessing proteinase activity.
@ast
The primary structure of the P ...... rocessing proteinase activity.
@en
prefLabel
The primary structure of the P ...... rocessing proteinase activity.
@ast
The primary structure of the P ...... rocessing proteinase activity.
@en
P2093
P2860
P356
P1433
P1476
The primary structure of the P ...... rocessing proteinase activity.
@en
P2093
Diekhoff D
Grimmelikhuijzen CJ
Schmutzler C
P2860
P304
P356
10.1042/BJ2990431
P407
P478
299 ( Pt 2)
P577
1994-04-01T00:00:00Z