Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. - Wikidata - wikimedia - TriplyDB

Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases.

Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases.

http://www.wikidata.org/entity/Q45072759

about

Formation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectin The coexistence of an equal amount of Alzheimer's amyloid-β 40 and 42 forms structurally stable and toxic oligomers through a distinct pathway Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy Membrane curvature induction and tubulation are common features of synucleins and apolipoproteins.Fenton chemistry and oxidative stress mediate the toxicity of the beta-amyloid peptide in a Drosophila model of Alzheimer's disease Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates Protein folding: then and now Molecular origin of polyglutamine aggregation in neurodegenerative diseases.The Rationale for Insulin Therapy in Alzheimer's Disease Common mechanisms involved in Alzheimer's disease and type 2 diabetes: a key role of chronic bacterial infection and inflammation Insights into Mechanisms of Chronic Neurodegeneration Molecular Structure, Membrane Interactions, and Toxicity of the Islet Amyloid Polypeptide in Type 2 Diabetes Mellitus Targeting heat shock proteins to modulate α-synuclein toxicity The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models Tangles, Toxicity, and Tau Secretion in AD - New Approaches to a Vexing Problem A window into the heterogeneity of human cerebrospinal fluid Aβ peptides On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism Seeking a mechanism for the toxicity of oligomeric α-synuclein Antidepressants reduce neuroinflammatory responses and astroglial alpha-synuclein accumulation in a transgenic mouse model of multiple system atrophy Protein misfolding and aggregation in Alzheimer's disease and type 2 diabetes mellitus Exploring new biological functions of amyloids: bacteria cell agglutination mediated by host protein aggregation Bisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetes Methylated BSA mimics amyloid-related proteins and triggers inflammation Nanoscale Synaptic Membrane Mimetic Allows Unbiased High Throughput Screen That Targets Binding Sites for Alzheimer's-Associated Aβ Oligomers.Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association.The stability of cylindrin β-barrel amyloid oligomer models-a molecular dynamics study.Amyloid Beta annular protofibrils in cell processes and synapses accumulate with aging and Alzheimer-associated genetic modification Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.Biophysics of α-synuclein membrane interactions.Implications of protein structure instability: from physiological to pathological secondary structure.Membrane interactions of a self-assembling model peptide that mimics the self-association, structure and toxicity of Abeta(1-40).Two disaccharides and trimethylamine N-oxide affect Abeta aggregation differently, but all attenuate oligomer-induced membrane permeability.Structural differences between Abeta(1-40) intermediate oligomers and fibrils elucidated by proteolytic fragmentation and hydrogen/deuterium exchange.Simultaneous monitoring of peptide aggregate distributions, structure, and kinetics using amide hydrogen exchange: application to Abeta(1-40) fibrillogenesis Exploring the mechanism of beta-amyloid toxicity attenuation by multivalent sialic acid polymers through the use of mathematical models.Cytoplasmic prion protein induces forebrain neurotoxicity

P2860

Q21202837-7B398E51-08E6-45A3-A7F4-DC82560F04A9 Q24294387-DF4294CF-C3B9-40E2-B61C-28C490CDAE3D Q24632795-933920B2-C685-40A1-8EAA-70261D57A7D5 Q24633016-1B1FAF63-62E5-44AD-A820-4CBA142EB2E3 Q24633488-9999921D-571A-45B3-9E3F-9F47170917E4 Q24656549-BA68421A-3F59-4C31-8928-96CEEA164AE8 Q24657543-F2F6BB72-FF4D-4500-8E98-746EDB6138CF Q24671711-830E8626-9163-486D-8B2F-144FD1178982 Q24816819-F9084035-AEA0-4AA3-9096-180C92BE0643 Q26744834-FE9626E5-EBB8-4D6A-9865-36397B76B7E9 Q26766681-1CAEFD39-3B82-4232-88CC-584D0FE2788A Q26771732-4FA506BF-A5A3-4B6C-B001-ED4127976ECE Q26774381-99217367-6891-4801-A3F0-C00AF4B857FE Q26827066-1A2EE096-EB34-42F5-8C0E-F73AAB849E1D Q26830682-C78819DB-F8CB-46AB-B03D-03E18D930355 Q26995918-7D378B62-005B-4F3F-9A73-B8224025292C Q27004724-275C9D0F-8ED6-45D8-9AA8-B606CAF580F6 Q27010785-44AD61D9-C609-4299-AE7E-A5D6900773DA Q27022467-1895920C-F2BC-46F0-80DA-7E2990897BC8 Q27315907-57FFBA54-0655-4D24-91B7-320C85785FF6 Q28080551-C3F324F9-91DF-46A5-B64C-0A9BD6838C4C Q28395248-C21A2C46-BADF-4947-B736-3EBA4ABE2A68 Q28397425-9919CBB7-AB9E-4933-9A42-7B59000D0DEC Q28484823-04900CB7-267E-4633-ABC6-98671B4BCBD3 Q28485267-75B5C6F1-880E-4998-8C4C-5EAAA4A4A5BC Q28487451-E76FA5F0-432A-4FE4-8692-886AB7E39F76 Q28546877-02EB39EE-9428-4F3F-86E8-922E3044406F Q30152727-64B2615F-52E4-46A5-9024-A9784EB169F2 Q30152889-4BBD4F03-00AF-4470-A40C-1296B5E65E4F Q30155110-2B03E032-4ABF-453B-8C97-68F5AFCED00E Q30157432-8E2AD37F-CD4B-40E3-9D43-EBD0B8339AA6 Q30157440-75CFC523-ECC2-4237-849E-AF57F1EF8CF2 Q30405705-BD18C680-100B-4C8C-B69B-63B7393AAA1A Q30416896-22FF9C86-7E1F-4BCA-994E-6922FA521E51 Q30419488-CE6D8B26-4F19-4E50-9C12-C93DCDAA7DFC Q30434734-C65D5022-BEAD-4A8A-8C10-9961384AE04E Q30437131-EDF0749E-BCD9-4955-981E-876B367C9675 Q30438164-DA1F4ED2-1FA1-4113-A54F-5FB25AAB0165 Q30481429-3740ABF1-102E-4EC5-B787-219756BFDFF3 Q30488090-66E8F287-B078-40C8-A227-B15208E7B025

P2860

Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases.

http://www.wikidata.org/entity/Q45072759

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

name

Permeabilization of lipid bila ...... n protein misfolding diseases.

@en

Permeabilization of lipid bila ...... n protein misfolding diseases.

@nl

type

label

Permeabilization of lipid bila ...... n protein misfolding diseases.

@en

Permeabilization of lipid bila ...... n protein misfolding diseases.

@nl

prefLabel

Permeabilization of lipid bila ...... n protein misfolding diseases.

@en

Permeabilization of lipid bila ...... n protein misfolding diseases.

@nl

P1433

Q45072759-063FDF40-D956-4EAE-A21E-5DC2BAAEBDE5

P1476

Q45072759-9ED3BF58-BDC2-4691-809F-D57E794C738E

P2093

Q45072759-21791FAF-EE89-4FC6-A565-4C0F5A108BDC

Q45072759-597BA475-B9A3-41CD-B13B-403ADC98AD38

Q45072759-6E22A007-6835-48FA-BA5D-692D0B383C15

Q45072759-9EF0A079-5832-4A0B-9D87-5C5DD9B16A55

Q45072759-A2DA2329-6AC9-4849-91D6-5744C20253C6

Q45072759-AF9271F6-D6E3-4164-94D8-C3546E1529D9

Q45072759-CEB8FCD8-604D-4928-BC9E-4DCB454329C7

P304

Q45072759-B594EFB4-CCE1-49EF-8A66-69A2C3ADF013

P31

Q45072759-AC839821-BC57-4048-99CB-D5A19674E1D9

P356

Q45072759-458A22C1-CF3B-4FD5-BCF9-76B3F7232666

P407

Q45072759-A51F3491-E614-4FAF-8935-D0F8E09D4A91

P433

Q45072759-4B87F389-BA88-4286-A616-995503F1FC8A

P478

Q45072759-676EADE9-9EF7-4F73-B9C1-0203554BC83B

P577

Q45072759-713BD7E3-69F3-47C4-9363-D5EAE320F5A1

P698

Q45072759-85F782C3-FF92-4254-B944-AC0264447BAC

P356

P1433

Journal of Biological Chemistry

P1476

Permeabilization of lipid bila ...... n protein misfolding diseases.

@en

P2093

Brian Edmonds

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

Charles G Glabe

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

James E Hall

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

Rakez Kayed

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

Saskia C Milton

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

Theresa M McIntire

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

Yuri Sokolov

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

P304

46363-46366

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

P31

scholarly article

P356

10.1074/JBC.C400260200

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

P407

P433

45

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

P478

279

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

P577

2004-09-21T00:00:00Z

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

P698

15385542

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