Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
about
Molecular identification of a malaria merozoite surface sheddaseStructural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemiaSolution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparumFunctional consequences of a novel variant of PCSK1Mutational analysis of predicted interactions between the catalytic and P domains of prohormone convertase 3 (PC3/PC1)Novel proteomic approaches for tissue analysis.Autocatalytic activation of the furin zymogen requires removal of the emerging enzyme's N-terminus from the active site.Identification of a pH sensor in the furin propeptide that regulates enzyme activationInsights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furinPropeptides are sufficient to regulate organelle-specific pH-dependent activation of furin and proprotein convertase 1/3.Mechanism of Fine-tuning pH Sensors in Proprotein Convertases: IDENTIFICATION OF A pH-SENSING HISTIDINE PAIR IN THE PROPEPTIDE OF PROPROTEIN CONVERTASE 1/3.The mechanism by which a propeptide-encoded pH sensor regulates spatiotemporal activation of furin.Determination of Histidine pKa Values in the Propeptides of Furin and Proprotein Convertase 1/3 Using Histidine Hydrogen-Deuterium Exchange Mass Spectrometry.Single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme.Structure-function analysis of the prosegment of the proprotein convertase PC5A.A novel subtilase inhibitor in plants shows structural and functional similarities to protease propeptides.Identification of furin pro-region determinants involved in folding and activation.Subtleties among subtilases. The structural biology of Kex2 and furin-related prohormone convertases.Functional Characterization of Propeptides in Plant Subtilases as Intramolecular Chaperones and Inhibitors of the Mature Protease.Synthetic peptides derived from the prosegments of proprotein convertase 1/3 and furin are potent inhibitors of both enzymes
P2860
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P2860
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
description
2002 nî lūn-bûn
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2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
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2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
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name
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@ast
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@en
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@nl
type
label
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@ast
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@en
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@nl
prefLabel
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@ast
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@en
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@nl
P2093
P1476
Solution structure of the pro-hormone convertase 1 pro-domain from Mus musculus
@en
P2093
Michael A Tangrea
Philip N Bryan
P304
P356
10.1016/S0022-2836(02)00543-0
P407
P50
P577
2002-07-19T00:00:00Z