Inhibitory potency and specificity of subtilase-like pro-protein convertase (SPC) prodomains. - Wikidata - awgldk - TriplyDB

Inhibitory potency and specificity of subtilase-like pro-protein convertase (SPC) prodomains.

Inhibitory potency and specificity of subtilase-like pro-protein convertase (SPC) prodomains.

http://www.wikidata.org/entity/Q30769503

about

Identification and characterization of three members of the human metallocarboxypeptidase gene family Molecular identification of a malaria merozoite surface sheddase Furin Processing and Proteolytic Activation of Semliki Forest Virus Microneme Protein 5 Regulates the Activity of Toxoplasma Subtilisin 1 by Mimicking a Subtilisin Prodomain Stepwise proteolytic activation of type I procollagen to collagen within the secretory pathway of tendon fibroblasts in situ.Targeting host cell furin proprotein convertases as a therapeutic strategy against bacterial toxins and viral pathogens Functional characterization of the propeptide of Plasmodium falciparum subtilisin-like protease-1 Optimization of protease-inhibitor interactions by randomizing adventitious contacts Inhibition of furin/proprotein convertase-catalyzed surface and intracellular processing by small molecules.Autocatalytic activation of the furin zymogen requires removal of the emerging enzyme's N-terminus from the active site.A femtomol range FRET biosensor reports exceedingly low levels of cell surface furin: implications for the processing of anthrax protective antigen Functional analysis of the cucumisin propeptide as a potent inhibitor of its mature enzyme.An atypical proprotein convertase in Giardia lamblia differentiation.Proteolytic processing of angiopoietin-like protein 4 by proprotein convertases modulates its inhibitory effects on lipoprotein lipase activity.Furin is the major processing enzyme of the cardiac-specific growth factor bone morphogenetic protein 10.Inhibition of prohormone convertases PC1/3 and PC2 by 2,5-dideoxystreptamine derivatives.Loss of endothelial furin leads to cardiac malformation and early postnatal death.Proprotein convertase subtilisin/kexin type 4 in mammalian fertility: a review.Inflammatory proprotein convertase-matrix metalloproteinase proteolytic pathway in antigen-presenting cells as a step to autoimmune multiple sclerosis.Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets.On the cutting edge of proprotein convertase pharmacology: from molecular concepts to clinical applications.Therapeutic uses of furin and its inhibitors: a patent review.Single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme.Development of protein-based inhibitors of the proprotein of convertase SKI-1/S1P: processing of SREBP-2, ATF6, and a viral glycoprotein.Structure-function analysis of the prosegment of the proprotein convertase PC5A.Propeptides as modulators of functional activity of proteases.Posttranslational processing of FGF23 in osteocytes during the osteoblast to osteocyte transition.PACE4 inhibitors and their peptidomimetic analogs block prostate cancer tumor progression through quiescence induction, increased apoptosis and impaired neovascularisation.A novel subtilase inhibitor in plants shows structural and functional similarities to protease propeptides.PACE4-based molecular targeting of prostate cancer using an engineered ⁶⁴Cu-radiolabeled peptide inhibitor.Processing of human toll-like receptor 7 by furin-like proprotein convertases is required for its accumulation and activity in endosomes.The Multi-Leu peptide inhibitor discriminates between PACE4 and furin and exhibits antiproliferative effects on prostate cancer cells.Selective and potent furin inhibitors protect cells from anthrax without significant toxicity Proteolysis of the membrane type-1 matrix metalloproteinase prodomain: implications for a two-step proteolytic processing and activation.Identification of furin pro-region determinants involved in folding and activation.TACE/ADAM-17 maturation and activation of sheddase activity require proprotein convertase activity.Substrate cleavage analysis of furin and related proprotein convertases. A comparative study.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 Processing and trafficking of a prohormone convertase 2 active site mutant

P2860

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P2860

Inhibitory potency and specificity of subtilase-like pro-protein convertase (SPC) prodomains.

http://www.wikidata.org/entity/Q30769503

description

2001 nî lūn-bûn

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2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2001 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2001年の論文

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年学术文章

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2001年學術文章

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name

Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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P1433

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P1433

Journal of Biological Chemistry

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Inhibitory potency and specifi ...... n convertase (SPC) prodomains.

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P2093

Frédéric Gagnon

http://www.w3.org/2001/XMLSchema#string

Klaus Klarskov

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Martin Fugère

http://www.w3.org/2001/XMLSchema#string

Pierre Lavigne

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Polizois C Limperis

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Richard Leduc

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Robert Day

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Véronique Beaulieu-Audy

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P2860

The prosegments of furin and PC7 as potent inhibitors of proprotein convertases. In vitro and ex vivo assessment of their efficacy and selectivity

Prohormone convertase PC5 is a candidate processing enzyme for prorenin in the human adrenal cortex

Biosynthesis, distinct post-translational modifications, and functional characterization of lymphoma proprotein convertase

Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins

Regulation of membrane type-1 matrix metalloproteinase activation by proprotein convertases

Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction

The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions

The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of prohormone convertase PC2

Regulatory roles of the P domain of the subtilisin-like prohormone convertases

Activation of the furin endoprotease is a multiple-step process: requirements for acidification and internal propeptide cleavage

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7648-7656

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scholarly article

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10.1074/JBC.M107467200

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P433

10

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277

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2001-11-26T00:00:00Z

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11723118

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