Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin. - Test2 - elhamkhani - TriplyDB

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

http://www.wikidata.org/entity/Q37519267

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Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.Anti-Amyloid-β Monoclonal Antibodies for Alzheimer's Disease: Pitfalls and Promise.Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies.Alzheimer's disease hypothesis and related therapies.ABBY: A phase 2 randomized trial of crenezumab in mild to moderate Alzheimer disease.Structural and kinetic basis for the selectivity of aducanumab for aggregated forms of amyloid-β.Adherence/Retention Alzheimer's Prevention Initiative Colombia Plan Computational Analysis for the Rational Design of Anti-Amyloid Beta (Aβ) Antibodies Amyloid positron emission tomography and cerebrospinal fluid results from a crenezumab anti-amyloid-beta antibody double-blind, placebo-controlled, randomized phase II study in mild-to-moderate Alzheimer's disease (BLAZE)

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Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

http://www.wikidata.org/entity/Q37519267

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 20 December 2016

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

@en

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

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type

label

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

@en

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

@nl

prefLabel

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

@en

Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

@nl

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Scientific Reports

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Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin.

@en

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Andrea Pfeifer

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

Andreas Muhs

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

Bing Li

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

Charles Eigenbrot

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

Germaine Fuh

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

James A Ernst

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

Jasvinder K Atwal

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

Maria Pihlgren

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

Mark Ultsch

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

Mary Mathieu

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

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

Processing of X-ray diffraction data collected in oscillation mode

Amyloid-beta-anti-amyloid-beta complex structure reveals an extended conformation in the immunodominant B-cell epitope

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

A therapeutic antibody targeting BACE1 inhibits amyloid-β production in vivo

Gantenerumab: a novel human anti-Aβ antibody demonstrates sustained cerebral amyloid-β binding and elicits cell-mediated removal of human amyloid-β

Structural basis of C-terminal β-amyloid peptide binding by the antibody ponezumab for the treatment of Alzheimer's disease

Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

Phasercrystallographic software

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39374

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scholarly article

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10.1038/SREP39374

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6

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2016-12-20T00:00:00Z

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1015448910

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27996029

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5171940

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