Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs - Wikidata - wikimedia - TriplyDB

Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs

Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs

http://www.wikidata.org/entity/Q28251387

about

Toward the structure of presenilin/γ-secretase and presenilin homologs Making the cut: central roles of intramembrane proteolysis in pathogenic microorganisms Plasmodium falciparum signal peptide peptidase cleaves malaria heat shock protein 101 (HSP101). Implications for gametocytogenesis A C-terminal region of signal peptide peptidase defines a functional domain for intramembrane aspartic protease catalysis Identification of an archaeal presenilin-like intramembrane protease Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors Selective amyloid-beta lowering agents.The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes.γ-Secretase Inhibitors and Modulators Induce Distinct Conformational Changes in the Active Sites of γ-Secretase and Signal Peptide Peptidase Inhibitors of signal peptide peptidase (SPP) affect HSV-1 infectivity in vitro and in vivo.Presenilin is the molecular target of acidic γ-secretase modulators in living cells.Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteases Targeting the ERAD pathway via inhibition of signal peptide peptidase for antiparasitic therapeutic design Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.Experimental detection of proteolytic activity in a signal peptide peptidase of Arabidopsis thaliana.A subset of membrane-altering agents and γ-secretase modulators provoke nonsubstrate cleavage by rhomboid proteases Taking the plunge: integrating structural, enzymatic and computational insights into a unified model for membrane-immersed rhomboid proteolysis Three-dimensional structure of the signal peptide peptidase Phenylpiperidine-type γ-secretase modulators target the transmembrane domain 1 of presenilin 1 Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's Disease Vigilin interacts with signal peptide peptidase.Membrane immersion allows rhomboid proteases to achieve specificity by reading transmembrane segment dynamics.Distinct pharmacological effects of inhibitors of signal peptide peptidase and gamma-secretase.Substrate specificity of gamma-secretase and other intramembrane proteases.Structural and Functional Determinants of gamma-Secretase, an Intramembrane Protease Implicated in Alzheimer's Disease.Intramembrane proteolysis Intramembrane proteolytic cleavage of a membrane-tethered transcription factor by a metalloprotease depends on ATP.Intramembrane proteolysis by signal peptide peptidases: a comparative discussion of GXGD-type aspartyl proteases.The structure and function of Alzheimer's gamma secretase enzyme complex.γ-Secretase inhibitors and modulators for Alzheimer's disease.Structural biology of presenilins and signal peptide peptidases.Development and mechanism of γ-secretase modulators for Alzheimer's disease.Novel γ-secretase enzyme modulators directly target presenilin protein.Signal peptide peptidase (SPP) dimer formation as assessed by fluorescence lifetime imaging microscopy (FLIM) in intact cells.Signal peptide peptidase (SPP) assembles with substrates and misfolded membrane proteins into distinct oligomeric complexes.Intramembrane proteolysis of GXGD-type aspartyl proteases is slowed by a familial Alzheimer disease-like mutation.Signal peptide peptidase and gamma-secretase share equivalent inhibitor binding pharmacology.Binding of HSV-1 glycoprotein K (gK) to signal peptide peptidase (SPP) is required for virus infectivity The intrinsic disorder status of the human hepatitis C virus proteome.A cytosolic STIM2 preprotein created by signal peptide inefficiency activates ORAI1 in a store-independent manner.

P2860

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P2860

Signal peptide peptidase: biochemical properties and modulation by nonsteroidal antiinflammatory drugs

http://www.wikidata.org/entity/Q28251387

description

2006 nî lūn-bûn

@nan

2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

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2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

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name

Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

@ast

Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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type

label

Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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prefLabel

Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Signal peptide peptidase: bioc ...... eroidal antiinflammatory drugs

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Andrew C Nyborg

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

Michael S Wolfe

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Nobuhisa Iwata

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Takaomi C Saido

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

Thekla S Diehl

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

Todd E Golde

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Toru Sato

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8649-56

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scholarly article

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10.1021/BI060597G

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28

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45

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2006-07-18T00:00:00Z

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16834339

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