about
The RIP1/RIP3 necrosome forms a functional amyloid signaling complex required for programmed necrosisHsp90-Tau complex reveals molecular basis for specificity in chaperone actionAltered ribostasis: RNA-protein granules in degenerative disordersAmyloid-beta Alzheimer targets - protein processing, lipid rafts, and amyloid-beta poresTargeting innate immunity for neurodegenerative disorders of the central nervous systemMolecular chaperones: guardians of the proteome in normal and disease statesInsights into Mechanisms of Chronic NeurodegenerationPredominant Role of Plasmacytoid Dendritic Cells in Stimulating Systemic AutoimmunityChaperones in NeurodegenerationTechniques to elucidate the conformation of prionsDisaggregases, molecular chaperones that resolubilize protein aggregatesMechanisms of amyloid formation revealed by solution NMRProtein Folding and Mechanisms of ProteostasisAssessing the causes and consequences of co-polymerization in amyloid formationPrion strains and amyloid polymorphism influence phenotypic variationSelf-propagation of pathogenic protein aggregates in neurodegenerative diseasesFeatures of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinityNeurodegenerative diseases: expanding the prion conceptChaperone machines for protein folding, unfolding and disaggregationA switchable self-assembling and disassembling chiral system based on a porphyrin-substituted phenylalanine-phenylalanine motifRepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Nature and nurture: environmental influences on a genetic rat model of depression.Out-of-register -sheets suggest a pathway to toxic amyloid aggregatesAtomic structure and hierarchical assembly of a cross- amyloid fibrilClass I Major Histocompatibility Complex, the Trojan Horse for Secretion of Amyloidogenic β 2 -MicroglobulinThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityAtomic Resolution Structure of Monomorphic Aβ42 Amyloid FibrilsATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure.Engineering enhanced protein disaggregases for neurodegenerative diseaseLegal but lethal: functional protein aggregation at the verge of toxicityAxin cancer mutants form nanoaggregates to rewire the Wnt signaling networkStructure and dynamics of amyloid-β segmental polymorphismsAggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast modelShaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrilsβ2-Microglobulin amyloid fibril-induced membrane disruption is enhanced by endosomal lipids and acidic pHDrug Development in Conformational Diseases: A Novel Family of Chemical Chaperones that Bind and Stabilise Several Polymorphic Amyloid StructuresPhase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillizationRational design of fiber forming supramolecular structuresAn Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.The stability of cylindrin β-barrel amyloid oligomer models-a molecular dynamics study.
P2860
Q24293754-095D145F-58AC-4377-97DF-2B613BA7D160Q24338439-00B47D57-46CF-484F-B9E6-5DD75C66CD18Q24604643-9B972FDB-55AB-4790-9339-738F1CC71511Q26738355-EF30C8CB-F8B5-458F-BA17-40EC41A0BE1DQ26744219-0294D5F5-EC0F-4551-97CB-07D18FBC69E1Q26766168-23979C41-9C76-4231-8882-455FFBB9DB60Q26771732-48DD24E8-D040-4EC6-BB4C-E59372CDABEAQ26777199-9F5029F4-0215-4B79-B0D4-E609EA28B46AQ26782943-81268B18-FFDC-40DF-9C8F-907AD728C783Q26795754-637F07F6-B574-43E7-A108-3218E730D380Q26796603-4F538194-91C3-4CF7-9873-2A4D490FB0EBQ26797492-C7A8ECD6-2DEB-4E69-A0E5-8A372B3F7F9FQ26801512-73D61AC6-073D-44A7-8EF6-77BEC351471EQ26824195-9D7CE628-0826-4DB2-81AE-022804523ABDQ26827209-D7DC9D72-BD01-4EF9-81C1-F693367A5FE8Q26996441-574DBE18-7E04-431D-9CDA-D936AD24C52DQ26996645-C6C09561-0BB4-4ED6-A146-9B665060F2F5Q27011744-56FDF35D-126C-4BEE-8E35-6953D2E936D5Q27026110-BC426EAB-51C7-461B-9648-80132FF85BD7Q27330000-B7E6CEF5-504A-489F-894D-083C450D7109Q27332087-DD4183BA-6825-45AA-B3E1-356A06432BCFQ27339187-0F05DB83-7CF4-4401-B6A9-347091A8BB14Q27675366-6FCF6DE7-9DEC-478A-9611-7AE5B3D4ED47Q27676898-EB00E224-739F-41FE-92F5-20F15A479315Q27680885-96443F34-8271-48D7-A4BE-FDCBB950966CQ27683083-B2A0AB23-8326-4882-86F9-7A2A42C6E971Q27714742-779A94EB-2F10-421E-BC3A-7599664B59AEQ27936710-6FB94590-4F09-45DA-BA5F-D4526230D2D2Q28083809-25905ABE-D822-4CB2-8566-AB480AA56BEBQ28084859-298732E3-932B-4AA3-8450-EA83E7C24E40Q28274105-F1969127-0936-4651-8E19-DA1954BB568AQ28481479-B6AB3B90-2CD4-4575-94B8-CC82583122FCQ28487681-455FF38D-FBC2-4B4E-BD79-65AF56EEC3D3Q28539309-D94BD33A-238B-4FC8-A718-15D2DE22EBE8Q28541669-7B763A60-8A32-48D0-A6E4-1F5AB6A75A1CQ28547692-28ED2C1F-A224-4BE2-8167-8997B38F8728Q28588090-3D450019-5334-4436-BA43-74C823B86519Q28829633-70558B55-34D0-4FD8-AA3F-95A832DBF99DQ30152729-9BE9DED3-C772-45BE-BEE4-EA527644955DQ30155110-34FEB4AB-3470-497A-B15B-2B9C52685710
P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
The amyloid state of proteins in human diseases.
@en
The amyloid state of proteins in human diseases.
@nl
type
label
The amyloid state of proteins in human diseases.
@en
The amyloid state of proteins in human diseases.
@nl
prefLabel
The amyloid state of proteins in human diseases.
@en
The amyloid state of proteins in human diseases.
@nl
P2860
P1433
P1476
The amyloid state of proteins in human diseases.
@en
P2093
David Eisenberg
P2860
P304
P356
10.1016/J.CELL.2012.02.022
P407
P577
2012-03-01T00:00:00Z