gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site. - Wikidata - wikimedia - TriplyDB

gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site.

gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site.

http://www.wikidata.org/entity/Q34872108

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When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease Toward the structure of presenilin/γ-secretase and presenilin homologs Allosteric regulation of rhomboid intramembrane proteolysis Anthrax lethal toxin induces cell death-independent permeability in zebrafish vasculature Selective amyloid-beta lowering agents.Targeting Abeta and tau in Alzheimer's disease, an early interim report The secretases: enzymes with therapeutic potential in Alzheimer disease.Selective translational control of the Alzheimer amyloid precursor protein transcript by iron regulatory protein-1.Structure, mechanism and inhibition of gamma-secretase and presenilin-like proteases Amyloid precursor protein selective gamma-secretase inhibitors for treatment of Alzheimer's disease.Chronic treatment with a novel γ-secretase modulator, JNJ-40418677, inhibits amyloid plaque formation in a mouse model of Alzheimer's disease.Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease.Independent relationship between amyloid precursor protein (APP) dimerization and γ-secretase processivity.Presenilins and γ-secretase: structure, function, and role in Alzheimer Disease.Cholestenoic acid, an endogenous cholesterol metabolite, is a potent γ-secretase modulator.Parenchymal and vascular Abeta-deposition and its effects on the degeneration of neurons and cognition in Alzheimer's disease.Chemical Biology, Molecular Mechanism and Clinical Perspective of γ-Secretase Modulators in Alzheimer's Disease Impact of amyloid imaging on drug development in Alzheimer's disease.The FDA-approved natural product dihydroergocristine reduces the production of the Alzheimer's disease amyloid-β peptides The role of γ-secretase activating protein (GSAP) and imatinib in the regulation of γ-secretase activity and amyloid-β generation.The role of presenilin and its interacting proteins in the biogenesis of Alzheimer's beta amyloid 100 years and counting: prospects for defeating Alzheimer's disease Novel therapeutic strategies for the treatment of protein-misfolding diseases.Distinct pharmacological effects of inhibitors of signal peptide peptidase and gamma-secretase.Gamma-secretase inhibition and modulation for Alzheimer's disease.Intramembrane proteolysis Sequence analyses of presenilin mutations linked to familial Alzheimer's disease.Inhibition and modulation of gamma-secretase for Alzheimer's disease Possible mechanisms of action of NSAIDs and related compounds that modulate gamma-secretase cleavage.The structure and function of Alzheimer's gamma secretase enzyme complex.Discovery of notch-sparing gamma-secretase inhibitors Regulated intramembrane proteolysis of the AXL receptor kinase generates an intracellular domain that localizes in the nucleus of cancer cells.The recent updates of therapeutic approaches against aβ for the treatment of Alzheimer's disease.γ-Secretase inhibitors and modulators for Alzheimer's disease.Treatment strategies targeting amyloid β-protein.A review: treatment of Alzheimer's disease discovered in repurposed agents.Complex relationships between substrate sequence and sensitivity to alterations in γ-secretase processivity induced by γ-secretase modulators Production of active glycosylation-deficient γ-secretase complex for crystallization studies.Do Cancer Drugs Counteract Neurodegeneration? Repurposing for Alzheimer's Disease.Zinc and Copper Differentially Modulate Amyloid Precursor Protein Processing by γ-Secretase and Amyloid-β Peptide Production.

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P2860

gamma-Secretase substrate selectivity can be modulated directly via interaction with a nucleotide-binding site.

http://www.wikidata.org/entity/Q34872108

description

2005 nî lūn-bûn

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2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

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gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

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gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

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gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

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gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

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gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

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P1433

Journal of Biological Chemistry

P1476

gamma-Secretase substrate sele ...... ith a nucleotide-binding site.

@en

P2093

Beth L Ostaszewski

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

Dennis J Selkoe

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Matthew J LaVoie

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Michael S Wolfe

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Wenjuan Ye

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P2860

Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state

Purification and characterization of the human gamma-secretase complex

Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

Lessons learned from the development of an abl tyrosine kinase inhibitor for chronic myelogenous leukemia

Gleevec inhibits beta-amyloid production but not Notch cleavage

Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)

Structural basis for the autoinhibition of c-Abl tyrosine kinase

Alzheimer's disease: genes, proteins, and therapy

Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells

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41987-41996

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scholarly article

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10.1074/JBC.M501368200

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51

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280

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Patrick C Fraering

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2005-10-19T00:00:00Z

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16236717

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1523323

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