Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration. - Wikidata - awgldk - TriplyDB

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration.

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration.

http://www.wikidata.org/entity/Q35826425

about

The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy Amyloid-β Receptors: The Good, the Bad, and the Prion Protein Molecular Structure of Aggregated Amyloid-β: Insights from Solid-State Nuclear Magnetic Resonance PMEL Amyloid Fibril Formation: The Bright Steps of Pigmentation Pre-amyloid oligomers of the proteotoxic RepA-WH1 prionoid assemble at the bacterial nucleoid X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17-36 β-Hairpin.What amyloid ligands can tell us about molecular polymorphism and disease.Effective anti-Alzheimer Aβ therapy involves depletion of specific Aβ oligomer subtypes.A Decentralized Approach to the Formulation of Hypotheses: A Hierarchical Structural Model for a Prion Self-Assembled System Quantitative Comparison of Dense-Core Amyloid Plaque Accumulation in Amyloid-β Protein Precursor Transgenic Mice Alzheimer's Toxic Amyloid Beta Oligomers: Unwelcome Visitors to the Na/K ATPase alpha3 Docking Station.Non-canonical soluble amyloid-beta aggregates and plaque buffering: controversies and future directions for target discovery in Alzheimer's disease.Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.Oligomeropathies and pathogenesis of Alzheimer and Parkinson's diseases.Phosphorylation of the amyloid β-peptide at Ser26 stabilizes oligomeric assembly and increases neurotoxicity.Potential mechanisms and implications for the formation of tau oligomeric strains.Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases.Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.Ganglioside-Dependent Neural Stem Cell Proliferation in Alzheimer's Disease Model Mice.Deficiency of TYROBP, an adapter protein for TREM2 and CR3 receptors, is neuroprotective in a mouse model of early Alzheimer's pathology.Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS).Nanoscale Dynamics of Amyloid β-42 Oligomers As Revealed by High-Speed Atomic Force Microscopy.Discrete pools of oligomeric amyloid-β track with spatial learning deficits in a mouse model of Alzheimer amyloidosis.Amyloid-β and tau complexity - towards improved biomarkers and targeted therapies.Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.A human scFv antibody that targets and neutralizes high molecular weight pathogenic amyloid-β oligomers.Selective lowering of synapsins induced by oligomeric α-synuclein exacerbates memory deficits.The amyloid-β oligomer Aβ*56 induces specific alterations in neuronal signaling that lead to tau phosphorylation and aggregation.Humanin Specifically Interacts with Amyloid-β Oligomers and Counteracts Their in vivo Toxicity.Self-assembly of the full-length amyloid Aβ42 protein in dimers.Non-Fibrillar Oligomeric Amyloid-β within Synapses.Soluble Oligomers Require a Ganglioside to Trigger Neuronal Calcium Overload.Aβ seeding potency peaks in the early stages of cerebral β-amyloidosis.Toward peptide-based inhibitors as therapies for Parkinson's disease.Combination anti-Aβ treatment maximizes cognitive recovery and rebalances mTOR signaling in APP mice.The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade.Origin of metastable oligomers and their effects on amyloid fibril self-assembly Shear-Induced Amyloid Formation in the Brain: III. The Roles of Shear Energy and Seeding in a Proposed Shear Model

P2860

Q26747107-052A2355-FD14-4E05-9B15-A7A486B7E8DB Q26771532-E70682B4-9EF4-4EAB-A648-85102BD2BD05 Q28066391-755B9F25-821B-4B83-8329-AFD76070F6F7 Q28076932-04610C86-9F5B-4F15-8070-320C1E7BF971 Q36109803-383F2F07-9460-4BB0-9EF6-64025897F1B6 Q36797995-15CDE80D-40FA-4A66-A36A-62C72426ED06 Q36871202-2382047C-8CD8-42B3-9130-DF3253EC013A Q36894417-8E80615A-93BD-451A-9E01-5A4018D3F16E Q37134269-D2EDF99A-2C4D-4E9C-AD81-BCA43E2C05B7 Q37610732-35428BCB-86FC-42BF-B937-74C6838A6DE0 Q37724402-AC4EC285-7202-4B01-A588-BFAB7ED35F92 Q38619618-8A822D4F-69AA-4671-A316-6C580F852F44 Q38777380-0A733BC7-9E1B-42A4-B33E-3EB3892081ED Q38794219-229EFD75-A90A-4812-ADF9-6C29ED4B5C4B Q38959054-AD6A1ED4-568F-4117-B5A5-318B45D43D4B Q38960046-48DF12DF-B4AA-4942-9492-FCD7F82420FC Q41074727-AD361710-F261-4DE3-B7F4-E8F21A673671 Q41702344-B42CB965-EDB6-411F-97FB-4F24F51AB771 Q41871137-1957C26A-2B65-46D4-BFA3-5C34C455DD5F Q42683481-FEB7673B-1BBC-4EAE-9218-3D023E30E893 Q45953477-8860FD6C-5A66-44F9-A648-E4E8771F6809 Q46024871-9536D9AE-1B5F-42D5-B692-C7257BBEFD5C Q46238269-951D543D-A7FC-47A0-9CDF-FC129EEA3A85 Q46240783-22687125-5572-4110-BBBD-D86B81DBB4CE Q46316131-A63FA1D5-36A1-4E7A-92B3-C56D1405EDE4 Q46341580-3516CBC7-EEF6-484E-B39C-EF8B8EE77154 Q46362244-D394BA1C-EDF3-4094-AF32-F710D644144B Q46368794-019225A5-886E-4F83-87C8-48986E1D5BA2 Q46405748-44AD4B9C-783F-4C67-87FA-271C82B84615 Q46523542-1FB8EE6B-F80C-4305-92DE-6E80722E09F5 Q46538110-FAED367F-5CAF-45C2-B8B6-636B8BDEFC82 Q47785630-F45832E7-D19B-44B7-944C-3BBABDB98911 Q48137001-DEAEFF27-AEF7-4BDA-8436-AD86D392EAE0 Q48340201-66581E0B-BE91-4B75-9AA3-4471F8BD27F9 Q53416393-2F74C599-A89A-4645-A27D-F5CD771B80A4 Q54977832-5B12A18A-7D4E-4B28-94B2-D2964418486C Q57273364-F859083B-7873-4E73-A164-56DB260D0966 Q58797396-6CE11219-07E4-43BF-B49E-123FB7D2E871

P2860

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration.

http://www.wikidata.org/entity/Q35826425

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@ast

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en-gb

type

label

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@ast

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en-gb

prefLabel

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@ast

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en-gb

P1433

Q35826425-DEF8D8A7-24AC-4DC2-B0F0-0CD60D0A1854

P1476

Q35826425-A3DCF77A-DB56-4820-A64E-32D1474DAD1A

P2093

Q35826425-01A04D42-6922-4865-B233-497E0F7E2DF2

Q35826425-10955C9A-DB89-4BD7-9B16-DACF7F4BDE3A

Q35826425-1EC502EA-67EB-4F00-8408-6E61FD0B14A5

Q35826425-27C59467-74BF-474A-BE34-5DD124CFB0FB

Q35826425-7481BFED-B654-495B-8772-DD1C1C5D10C2

Q35826425-87B48B0B-31B3-4593-865B-DF38D7FB073D

Q35826425-9C827E5C-E718-4F53-B18C-C464A17BD994

Q35826425-A4C877D0-01FB-4B10-98D4-9F71811AF4DD

Q35826425-A6DCD63A-4885-43F2-B5EA-9BB3B0E8865E

Q35826425-B1F8A801-EA4D-41ED-97FF-2E4BBF9E7147

P2860

Q35826425-0B050949-0C26-4CEC-ACFD-63DD472C1257

Q35826425-0E8CE51C-6558-4472-8663-A97D538EB56A

Q35826425-0FEB66B5-C851-4079-A6A9-E5DD1989AC35

Q35826425-10CDDC4E-63E3-4B96-811D-3AF4B58BE572

Q35826425-110667A2-93C6-4A18-B369-93DB76494E1F

Q35826425-1AC0CFB1-D983-44AB-AD46-97AB5FFD3408

Q35826425-243B524A-3FB5-4481-8DD8-E64D46A2EF08

Q35826425-2CEB7C91-2623-4F76-809B-E84B53F2E14F

Q35826425-3463DA33-033E-4D62-9C3C-93B0A8FEE3B8

Q35826425-3BECE65F-6E10-4D3C-8ECF-38C05BD0F26C

P304

Q35826425-3BC94E05-D7EA-4055-8C9D-51B4F121EBDB

P31

Q35826425-66009DE6-22EF-497A-9190-7814552E92D4

P356

Q35826425-E33C3B73-6EC4-41C7-BF8A-009383FE6996

P433

Q35826425-3F0B1CE2-2A01-424D-90BC-CE5DC6E4567D

P478

Q35826425-92134F72-7883-42E7-B98A-D1383D43E6A6

P50

Q35826425-0ED03F10-15BD-407E-A4B9-1E9F0EF4E10B

P577

Q35826425-25067819-1C32-4E0C-BE16-1DD6B21305AC

P5875

Q35826425-C2D83368-C4FA-470E-83B9-3B9A80F90A0A

P698

Q35826425-E5329223-E41A-4857-B079-565B611BC4FD

P932

Q35826425-334388EE-F4A6-43CA-8108-4D416A68F048

P356

J.CELREP.2015.05.021

P1433

P1476

Quaternary Structure Defines a ...... Neutralized by Sequestration.

@en

P2093

Angie C A Chiang

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

Colleen L Forster

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

James P Cleary

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

Joanna L Jankowsky

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

John H Reichl

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

Karen H Ashe

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

Kathleen R Zahs

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

Linda A Kotilinek

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

Marianne K O Grant

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

Miranda N Reed

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

P2860

Persistent amyloidosis following suppression of Abeta production in a transgenic model of Alzheimer disease

Correlative Memory Deficits, Abeta Elevation, and Amyloid Plaques in Transgenic Mice

Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Neuropathological alterations in Alzheimer disease

Out-of-register -sheets suggest a pathway to toxic amyloid aggregates

Antiparallel -sheet architecture in Iowa-mutant -amyloid fibrils

Atomic View of a Toxic Amyloid Small Oligomer

Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue

Modeling an in-register, parallel "iowa" aβ fibril structure using solid-state NMR data from labeled samples with rosetta

A specific amyloid-beta protein assembly in the brain impairs memory

P304

1760-1771

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

P31

scholarly article

P356

10.1016/J.CELREP.2015.05.021

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

P433

11

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

P478

11

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

P50

Carrie M Wilmot

P577

2015-06-04T00:00:00Z

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

P5875

277893980

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

P698

26051935

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

P932

4494129

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