Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides. - Wikidata - awgldk - TriplyDB

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

http://www.wikidata.org/entity/Q30319086

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Immunotherapy targeting pyroglutamate-3 Aβ: prospects and challenges Structural and functional analyses of a glutaminyl cyclase from Ixodes scapularis reveal metal-independent catalysis and inhibitor binding Brain pyroglutamate amyloid-β is produced by cathepsin B and is reduced by the cysteine protease inhibitor E64d, representing a potential Alzheimer's disease therapeutic Structural Analysis and Aggregation Propensity of Pyroglutamate Aβ(3-40) in Aqueous Trifluoroethanol Glutaminyl cyclase activity correlates with levels of Aβ peptides and mediators of angiogenesis in cerebrospinal fluid of Alzheimer's disease patients.Enhanced Fibril Fragmentation of N-Terminally Truncated and Pyroglutamyl-Modified Aβ Peptides.Characterizing Aging, Mild Cognitive Impairment, and Dementia with Blood-Based Biomarkers and Neuropsychology.An anti-pyroglutamate-3 Aβ vaccine reduces plaques and improves cognition in APPswe/PS1ΔE9 mice A quantitative analysis of spontaneous isoaspartate formation from N-terminal asparaginyl and aspartyl residues.Probing secondary glutaminyl cyclase (QC) inhibitor interactions applying an in silico-modeling/site-directed mutagenesis approach: implications for drug development.Glutaminyl cyclase knock-out mice exhibit slight hypothyroidism but no hypogonadism: implications for enzyme function and drug development Prion-like behaviour and tau-dependent cytotoxicity of pyroglutamylated amyloid-β.Glutaminyl cyclase-mediated toxicity of pyroglutamate-beta amyloid induces striatal neurodegeneration Pyroglutamate amyloid β (Aβ) aggravates behavioral deficits in transgenic amyloid mouse model for Alzheimer disease.Focusing the amyloid cascade hypothesis on N-truncated Abeta peptides as drug targets against Alzheimer's disease Distinct glutaminyl cyclase expression in Edinger-Westphal nucleus, locus coeruleus and nucleus basalis Meynert contributes to pGlu-Abeta pathology in Alzheimer's disease.Pyroglutamate-amyloid-β and glutaminyl cyclase are colocalized with amyloid-β in secretory vesicles and undergo activity-dependent, regulated secretion.PYROGLUTAMATE FORMATION AT THE N-TERMINI OF ABRI MOLECULES IN FAMILIAL BRITISH DEMENTIA IS NOT RESTRICTED TO THE CENTRAL NERVOUS SYSTEM.Recombinant production of isotope-labeled peptides and spontaneous cyclization of amino-terminal glutamine into pyroglutamic acid.Disturbed Ca2+ homeostasis increases glutaminyl cyclase expression; connecting two early pathogenic events in Alzheimer's disease in vitro.Role of the fast kinetics of pyroglutamate-modified amyloid-β oligomers in membrane binding and membrane permeability.Characterization of a single-chain variable fragment recognizing a linear epitope of aβ: a biotechnical tool for studies on Alzheimer's disease?Glutaminyl cyclase contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Aβ deposits in hippocampus via distinct cellular mechanisms Isoglutaminyl cyclase contributes to CCL2-driven neuroinflammation in Alzheimer's disease.Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease.Pyroglutamyl-N-terminal prion protein fragments in sheep brain following the development of transmissible spongiform encephalopathies.Mitochondrial dysfunction induced by a post-translationally modified amyloid linked to a familial mutation in an alternative model of neurodegeneration.Impact of amyloid β aggregate maturation on antibody treatment in APP23 mice Lessons from a Rare Familial Dementia: Amyloid and Beyond.Alzheimer's amyloid-β A2T variant and its N-terminal peptides inhibit amyloid-β fibrillization and rescue the induced cytotoxicity.Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.Oxidative stress and mitochondria-mediated cell death mechanisms triggered by the familial Danish dementia ADan amyloid Abundant pyroglutamate-modified ABri and ADan peptides in extracellular and vascular amyloid deposits in familial British and Danish dementias.Amyloid-β Peptide Aβ3pE-42 Induces Lipid Peroxidation, Membrane Permeabilization, and Calcium Influx in Neurons.Pyroglutamate-3 amyloid-β deposition in the brains of humans, non-human primates, canines, and Alzheimer disease-like transgenic mouse models Amyloid-β 1-24 C-terminal truncated fragment promotes amyloid-β 1-42 aggregate formation in the healthy brain.A modification-specific peptide-based immunization approach using CRM197 carrier protein: Development of a selective vaccine against pyroglutamate Aβ peptides.Alzheimer's disease, β-amyloid, glutamate, NMDA receptors and memantine--searching for the connections Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer's disease.

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P2860

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

http://www.wikidata.org/entity/Q30319086

description

2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2009年の論文

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2009年論文

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2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

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2009年论文

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name

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

@ast

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

@en

type

label

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

@ast

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

@en

prefLabel

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

@ast

Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

@en

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Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides.

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Dagmar Schlenzig

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Gerd Hause

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Hans-Ulrich Demuth

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Martin Kleinschmidt

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Stephan Schilling

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Susanne Aileen Funke

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Susanne Manhart

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Yeliz Cinar

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7072-7078

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scholarly article

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10.1021/BI900818A

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29

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48

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Dieter Willbold

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2009-07-01T00:00:00Z

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19518051

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