A causative link between the structure of aberrant protein oligomers and their toxicity. - Wikidata - wikimedia - TriplyDB

A causative link between the structure of aberrant protein oligomers and their toxicity.

A causative link between the structure of aberrant protein oligomers and their toxicity.

http://www.wikidata.org/entity/Q39750915

about

Amyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta pores The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy Mechanisms of amyloid formation revealed by solution NMR Protein Folding and Mechanisms of Proteostasis Assessing the causes and consequences of co-polymerization in amyloid formation Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease Exploring the accessible conformations of N-terminal acetylated α-synuclein Ubiquitous amyloids RepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerization Out-of-register -sheets suggest a pathway to toxic amyloid aggregates Seeking a mechanism for the toxicity of oligomeric α-synuclein Brain intraventricular injection of amyloid-β in zebrafish embryo impairs cognition and increases tau phosphorylation, effects reversed by lithium Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide Two-Step Amyloid Aggregation: Sequential Lag Phase Intermediates Mapping the structure of amyloid nucleation precursors by protein engineering kinetic analysis.Modulation of the stability of amyloidogenic precursors by anion binding strongly influences the rate of amyloid nucleation.Monoclonal antibodies against Aβ42 fibrils distinguish multiple aggregation state polymorphisms in vitro and in Alzheimer disease brain.Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living Cells Single molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Multi-dimensional super-resolution imaging enables surface hydrophobicity mapping.A FRET sensor for non-invasive imaging of amyloid formation in vivo.Identification of oligomers at early stages of tau aggregation in Alzheimer's disease.Effect of tetracyclines on the dynamics of formation and destructuration of beta2-microglobulin amyloid fibrils.Direct observations of amyloid β self-assembly in live cells provide insights into differences in the kinetics of Aβ(1-40) and Aβ(1-42) aggregation.A major role for side-chain polyglutamine hydrogen bonding in irreversible ataxin-3 aggregation.Amyloid oligomer formation probed by water proton magnetic resonance spectroscopy.Heparin induces harmless fibril formation in amyloidogenic W7FW14F apomyoglobin and amyloid aggregation in wild-type protein in vitro.Inversion of the balance between hydrophobic and hydrogen bonding interactions in protein folding and aggregation N-terminal domain of prion protein directs its oligomeric association.Direct observation of the interconversion of normal and toxic forms of α-synuclein Oligomeric forms of insulin amyloid aggregation disrupt outgrowth and complexity of neuron-like PC12 cells.Elevation of proteasomal substrate levels sensitizes cells to apoptosis induced by inhibition of proteasomal deubiquitinases.Probing the nucleus model for oligomer formation during insulin amyloid fibrillogenesis Perturbed amelogenin secondary structure leads to uncontrolled aggregation in amelogenesis imperfecta mutant proteins.Multivariate analyses of amyloid-beta oligomer populations indicate a connection between pore formation and cytotoxicity Direct three-dimensional visualization of membrane disruption by amyloid fibrils The relationship between aggregation and toxicity of polyglutamine-containing ataxin-3 in the intracellular environment of Escherichia coli.Resveratrol inhibits the formation of multiple-layered β-sheet oligomers of the human islet amyloid polypeptide segment 22-27

P2860

Q26738355-A3951993-1D33-49F5-BFFC-3F97BD8F076F Q26747107-A4407A67-9927-43F7-B664-04DFB06E54F6 Q26797492-D62F8CD8-550A-4F39-9C38-93C358A035EE Q26801512-44FBAEE0-A129-4C53-8F80-BAAF6967467A Q26824195-7AE3330F-40C6-4ECD-8CC3-059CAC936A18 Q26827421-B3D772CB-5664-4DA3-AE1A-2B19D9BF1689 Q26852660-249790CC-078B-4154-9375-30E8F97F0540 Q27016014-7F5A4A14-F047-4BB2-92BB-561743107039 Q27332087-7854670A-7518-4772-92C0-3E740AFD7653 Q27346272-5E428D19-19CE-4978-BFD9-A2FF18542D35 Q27675366-32C12D62-96D7-416E-80EC-D1F3A4A48EC2 Q28080551-B6B51242-C1C9-4755-9FDE-F5C2408C0111 Q28542815-AB897293-E6E3-4854-A546-F516496D3F79 Q28821551-836B919F-99E7-455E-B8AB-7BE00102167D Q30008795-019FD6C8-ACEE-49ED-A863-FA91DB428C1C Q30009502-C84C4381-AFF2-42FF-B970-DA22BE7A797A Q30009585-7A7C7DF8-BE06-4942-9C82-B4B346E69D1D Q30153325-24F5A917-3627-4CC2-BE5D-B78F114D9E56 Q30359467-6DFA3E79-8A69-4153-A0AD-B18B8F7CBF5A Q30420104-7967EF53-CA02-4397-996C-979A87C7C6B2 Q30533868-7EE2E8F0-E216-47A6-9A95-F43C20A76C87 Q30831874-42E0777D-D129-484B-9C85-85D862F4E016 Q33596287-2B1E84F7-F377-4F90-B422-93A7816494C8 Q33713341-BEE31E85-C36A-4601-8C99-A960F0053197 Q33743772-C062E06C-BFE5-4EAD-9513-4BEB716FF4BF Q33795294-E269571C-4570-493B-AEC2-D0709C517425 Q33886685-1AE33BE5-FB91-4157-B4CA-C3A8EA0E4A8D Q33888735-64842669-33B3-42F1-BE46-3771209627A3 Q33968252-4CE8B30E-3890-4785-B7C3-849320F7A055 Q34055197-9DFA5370-370D-44B4-AFBA-7AC355691BF3 Q34170632-6D48C7B0-5CC8-4D55-9D76-AE60F558AE41 Q34277399-F914C32B-31D9-4E0D-98BC-480456688AB2 Q34291460-68723502-078A-480A-ACF5-B5195D6E003F Q34294233-22838A70-F66D-426D-ADF6-C36500F6BF0A Q34398432-DC3AB762-472C-4B33-AE94-46086D605B5F Q34412585-8DC04D2B-1732-418C-831F-6D5D6752D905 Q34450675-60C64DCA-2D4C-4727-B585-16AFDAB241F8 Q34489472-67D0FC8C-5FE0-4ABD-A48B-880BF32F2DEB Q34517343-65886F24-E9CD-43E7-9320-290CA3756706 Q34688893-33505446-2EE5-4CA1-9105-3ED9CF84D07E

P2860

A causative link between the structure of aberrant protein oligomers and their toxicity.

http://www.wikidata.org/entity/Q39750915

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年学术文章

@wuu

2010年学术文章

@zh-cn

2010年学术文章

@zh-hans

2010年学术文章

@zh-my

2010年学术文章

@zh-sg

2010年學術文章

@yue

2010年學術文章

@zh

2010年學術文章

@zh-hant

name

A causative link between the structure of aberrant protein oligomers and their toxicity.

@en

A causative link between the structure of aberrant protein oligomers and their toxicity.

@nl

type

label

A causative link between the structure of aberrant protein oligomers and their toxicity.

@en

A causative link between the structure of aberrant protein oligomers and their toxicity.

@nl

prefLabel

A causative link between the structure of aberrant protein oligomers and their toxicity.

@en

A causative link between the structure of aberrant protein oligomers and their toxicity.

@nl

P1433

Q39750915-1E678CAE-B73E-4174-9F5D-01D85CB80F96

P1476

Q39750915-6E338925-CA59-4A6F-BB80-52F34BB1DE94

P2093

Q39750915-04E911EB-E47E-4D80-90CF-BEF2BABFC936

Q39750915-07CB0F66-4ADD-4439-886B-F72A6CCE1AD1

Q39750915-0F4D221B-512E-462E-A18E-78999B861A14

Q39750915-5418A692-75F9-45EC-96C4-E5A4F0C793FF

Q39750915-71E82713-C79F-4E9C-B928-89C740604865

Q39750915-DAFE45BC-855B-49FB-99AE-191A2D0BB818

Q39750915-DC8CD3F8-9A0A-43FE-9F1B-E6784F8EE3C0

Q39750915-EDE7A700-0333-455C-9E4B-B4FA0E2550FA

Q39750915-FB775DA3-BCA4-43FE-8B15-F98541D02F52

P2860

Q39750915-824F70D1-A0BE-4312-BCC7-FFF846C5943D

Q39750915-A17DAD1E-46F2-4742-8741-42AA21801B81

Q39750915-BB9E4B8C-068B-4216-84E8-2615143867DA

Q39750915-E970EA61-51DC-40C1-A836-36378469AF0B

P2888

Q39750915-8C9DC14A-2172-4F13-96FE-C3BBB7B5317B

P304

Q39750915-5F24119B-844A-4E41-A169-42EBB3451C56

P31

Q39750915-44FC27D2-72F8-46B7-91E1-81D3F192422E

P356

Q39750915-A37BE6A3-064E-462D-8A11-AB537491590A

P433

Q39750915-7046FAA8-70B0-4115-B1B1-B49BC2B16A5E

P478

Q39750915-80495A6A-DCAA-4924-8140-C699FD0DE78A

P50

Q39750915-02E5B205-807B-4743-957B-7F36E92440CD

Q39750915-4A8341B2-65D7-4137-8E87-8994B5FA9A8A

P577

Q39750915-8CB02431-26C5-4E67-AF85-D9DC8ED6E8B8

P5875

Q39750915-692DB234-D641-45FC-89CC-58AB693C1640

P698

Q39750915-A05B1501-83CE-4B66-BE90-00C8862E409B

P921

Q39750915-C3F2B536-09AD-46DA-BDAF-47504A1A2AC7

P356

P1433

Nature Chemical Biology

P1476

A causative link between the structure of aberrant protein oligomers and their toxicity

@en

P2093

Anna Pensalfini

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

Annalisa Relini

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

Benedetta Mannini

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

Christopher M Dobson

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

Claudia Parrini

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

Elisa Evangelisti

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

Fabrizio Chiti

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

Mariagioia Zampagni

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

Silvia Campioni

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

P2860

Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain

Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.

Spectrofluorimetric assessment of the surface hydrophobicity of proteins.

Comparative analysis of the cytotoxicity of homopolymeric amino acids.

P2888

P304

140-147

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

P31

scholarly article

P356

10.1038/NCHEMBIO.283

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

P433

2

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

P478

6

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

P50

Massimo Stefani

Cristina Cecchi

P577

2010-01-10T00:00:00Z

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

P5875

41041482

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

P698

20081829

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

P921

protein structure