A predicted alpha -helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway.
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Functional and structural characterization of a dense core secretory granule sorting domain from the PC1/3 proteaseA prohormone convertase cleavage site within a predicted alpha-helix mediates sorting of the neuronal and endocrine polypeptide VGF into the regulated secretory pathwayTwo dipolar α-helices within hormone-encoding regions of proglucagon are sorting signals to the regulated secretory pathway.FCRL, a novel member of the leukocyte Fc receptor family possesses unique structural features.Modulation of PC1/3 activity by self-interaction and substrate binding.The transmembrane domain of the prohormone convertase PC3: a key motif for targeting to the regulated secretory pathway.Sorting of the neuroendocrine secretory protein Secretogranin II into the regulated secretory pathway: role of N- and C-terminal alpha-helical domains.Sending proteins to dense core secretory granules: still a lot to sort out.Exploring the membrane topology of prohormone convertase 1 in AtT20 Cells: in situ analysis by immunofluorescence microscopyRole of loop structures of neuropsin in the activity of serine protease and regulated secretion.PC1/3, PC2 and PC5/6A are targeted to dense core secretory granules by a common mechanism.The C-terminal region of the proprotein convertase 1/3 (PC1/3) exerts a bimodal regulation of the enzyme activity in vitro.Prohormone-convertase 1 processing enhances post-Golgi sorting of prothyrotropin-releasing hormone-derived peptides.Modulation of secretory granule-targeting efficiency by cis and trans compounding of sorting signals.A conserved alpha-helix at the amino terminus of prosomatostatin serves as a sorting signal for the regulated secretory pathway.Progastrin is directed to the regulated secretory pathway by synergistically acting basic and acidic motifs.Evidence for proprotein convertase activity in the endoplasmic reticulum/early Golgi.A Hydrophobic Patch in a Charged α-Helix Is Sufficient to Target Proteins to Dense Core Secretory Granules
P2860
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P2860
A predicted alpha -helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway.
description
2000 nî lūn-bûn
@nan
2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
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@zh-mo
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@wuu
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name
A predicted alpha -helix media ...... e regulated secretory pathway.
@en
type
label
A predicted alpha -helix media ...... e regulated secretory pathway.
@en
prefLabel
A predicted alpha -helix media ...... e regulated secretory pathway.
@en
P2860
P356
P1476
A predicted alpha -helix media ...... e regulated secretory pathway.
@en
P2093
T L Reudelhuber
P2860
P304
40337-40343
P356
10.1074/JBC.M004757200
P407
P577
2000-12-01T00:00:00Z