Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events.
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Biosynthetic processing and quaternary interactions of proprotein convertase SPC4 (PACE4)Mutations within the propeptide, the primary cleavage site or the catalytic site, or deletion of C-terminal sequences, prevents secretion of proPC2 from transfected COS-7 cellsProcessing of prothyrotropin-releasing hormone by the family of prohormone convertasesNeuroendocrine secretory protein 7B2: structure, expression and functionsIsolation of the human PC6 gene encoding the putative host protease for HIV-1 gp160 processing in CD4+ T lymphocytes7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activityMechanism of the facilitation of PC2 maturation by 7B2: involvement in ProPC2 transport and activation but not foldingA subtilisin-like protein in secretory organelles of Plasmodium falciparum merozoitesLeSBT1, a subtilase from tomato plants. Overexpression in insect cells, purification, and characterization.Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro.The transmembrane domain of the prohormone convertase PC3: a key motif for targeting to the regulated secretory pathway.Prohormone convertase 2 activity is increased in the hippocampus of Wfs1 knockout mice.SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis.Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2.Stochastic rotational catalysis of proton pumping F-ATPaseExploring the membrane topology of prohormone convertase 1 in AtT20 Cells: in situ analysis by immunofluorescence microscopyInternal cleavage of the inhibitory 7B2 carboxyl-terminal peptide by PC2: a potential mechanism for its inactivation.Mutations in the catalytic domain of prohormone convertase 2 result in decreased binding to 7B2 and loss of inhibition with 7B2 C-terminal peptide.Single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme.Activation of the kexin from Schizosaccharomyces pombe requires internal cleavage of its initially cleaved prosequence.Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells.A predicted alpha -helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway.Sorting and storage during secretory granule biogenesis: looking backward and looking forward.Involvement of the membrane lipid bilayer in sorting prohormone convertase 2 into the regulated secretory pathway.Activation and routing of membrane-tethered prohormone convertases 1 and 2.pH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules.Identification of a transferable sorting domain for the regulated pathway in the prohormone convertase PC2.Characterization of the endopeptidase PC2 activity towards secretogranin II in stably transfected PC12 cells.The dynamic plasticity of insulin production in β-cells.Endoplasmic reticulum Ca2+ is important for the proteolytic processing and intracellular transport of proinsulin in the pancreatic beta-cell.Prosomatostatin processing in permeabilized cells. Calcium is required for prohormone cleavage but not formation of nascent secretory vesicles.PACE4: a subtilisin-like endoprotease with unique properties.Differences in the autocatalytic cleavage of pro-PC2 and pro-PC3 can be attributed to sequences within the propeptide and Asp310 of pro-PC2.In vitro characterization of the novel proprotein convertase PC7.Molecular determinants for subcellular trafficking of the malarial sheddase PfSUB2.Maturation and specificity of Plasmodium falciparum subtilisin-like protease-1, a malaria merozoite subtilisin-like serine protease.Dissociation of the complex between the neuroendocrine chaperone 7B2 and prohormone convertase PC2 is not associated with proPC2 maturation.Localization of metallocarboxypeptidase D in AtT-20 cells. Potential role in prohormone processing.Inhibition of the vacuolar H+-ATPase perturbs the transport, sorting, processing and release of regulated secretory proteins
P2860
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P2860
Differences in pH optima and calcium requirements for maturation of the prohormone convertases PC2 and PC3 indicates different intracellular locations for these events.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh-hant
name
Differences in pH optima and c ...... ar locations for these events.
@en
Differences in pH optima and c ...... ar locations for these events.
@nl
type
label
Differences in pH optima and c ...... ar locations for these events.
@en
Differences in pH optima and c ...... ar locations for these events.
@nl
prefLabel
Differences in pH optima and c ...... ar locations for these events.
@en
Differences in pH optima and c ...... ar locations for these events.
@nl
P2093
P2860
P356
P1476
Differences in pH optima and c ...... ar locations for these events.
@en
P2093
G Matthews
J L Jermany
K I Shennan
N A Taylor
P2860
P304
P356
10.1074/JBC.270.3.1402
P407
P577
1995-01-01T00:00:00Z