A glimpse of a possible amyloidogenic intermediate of transthyretin.
about
Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid diseaseMechanisms of amyloid formation revealed by solution NMRChemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosisAmyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSESA Substructure Combination Strategy To Create Potent and Selective Transthyretin Kinetic Stabilizers That Prevent Amyloidogenesis and CytotoxicityChemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasmaNovel Zn2+-binding Sites in Human Transthyretin: IMPLICATIONS FOR AMYLOIDOGENESIS AND RETINOL-BINDING PROTEIN RECOGNITIONConformational Conversion during Amyloid Formation at Atomic ResolutionTafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascadeThe rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosisThe structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicityNMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo.A kinetic study of beta-lactoglobulin amyloid fibril formation promoted by urea.Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Rapid generation of amyloid from native proteins in vitro.Progress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis.The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.Initial conformational changes of human transthyretin under partially denaturing conditionsDistinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrilsSequence-dependent denaturation energetics: A major determinant in amyloid disease diversity.A competition assay to identify amyloidogenesis inhibitors by monitoring the fluorescence emitted by the covalent attachment of a stilbene derivative to transthyretin.Therapeutic strategies for human amyloid diseases.Amyloid-fibril formation. Proposed mechanisms and relevance to conformational disease.Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions.Cysteine 10 is a key residue in amyloidogenesis of human transthyretin Val30Met.Binding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.Why is Leu55-->Pro55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomersTransthyretin slowly exchanges subunits under physiological conditions: A convenient chromatographic method to study subunit exchange in oligomeric proteins.Localized structural fluctuations promote amyloidogenic conformations in transthyretin.Substoichiometric inhibition of transthyretin misfolding by immune-targeting sparsely populated misfolding intermediates: a potential diagnostic and therapeutic for TTR amyloidoses.Structural Changes Associated with Transthyretin Misfolding and Amyloid Formation Revealed by Solution and Solid-State NMR.NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.Quantification of the thermodynamically linked quaternary and tertiary structural stabilities of transthyretin and its disease-associated variants: the relationship between stability and amyloidosis.Solid-State NMR Studies Reveal Native-like β-Sheet Structures in Transthyretin Amyloid.Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils.Understanding the complex mechanisms of β2-microglobulin amyloid assembly.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.Considerably Unfolded Transthyretin Monomers Preceed and Exchange with Dynamically Structured Amyloid Protofibrils.The pH-dependent stability of wild-type and mutant transthyretin oligomers.
P2860
Q24564070-D90897BF-FA89-4FF0-A25F-079C30467305Q26797492-A360A352-E93F-4318-A469-6A74A40A01CFQ27004511-BA785BBC-25D4-46E2-B234-7CC73116FCA6Q27656412-2B004BE0-C4F8-4045-8A74-5DF7F854BDEEQ27658823-D1C7AD79-4D51-430E-A51D-3090A2B0E3A2Q27659009-04045157-F673-4FA8-9544-B9BC4CE647F9Q27663605-D0078405-2A88-4A0F-BCF0-0C24C51F8342Q27666683-BF6B6D3C-00A3-4454-BDB4-6583E3FD0CB5Q27679360-4EE843ED-D6F5-46CD-9BA6-B6414335EAECQ28287224-5FE54068-1DD7-413A-B0FF-0518CE7111DEQ30157531-A1686F30-CE1E-49B8-AC07-AA3845EDE1D1Q30159629-898E2097-21A6-4D4F-9150-5629389994BEQ30313147-DECBDE1B-CC0A-47AA-8427-95C6309DD5FAQ30849505-AD614FC9-7C9C-45C1-A512-D7D1F6498838Q33516611-E97F1FD5-DD1F-4347-AF38-ABAEA92BC41FQ33709292-029B6191-7879-4220-8441-F8847729DB7DQ33952579-D2C7AA1B-E27C-4B22-AAD0-9F45EDDCD3A7Q33952780-A92A2DE4-6E88-42F2-B513-99C62A30CFAAQ34350522-BE4B0AB4-231A-482F-A29F-208BBC7B643CQ34416296-CC6F80D7-CA57-4906-9148-8485108E181AQ34443897-242EA86D-F361-44CB-ADEE-BF85AC5DBFD4Q34576022-B2D47092-5221-436F-8154-BE840316A749Q34743288-B80AADFF-7EF4-4607-BDF1-F78873CED1ACQ34756441-07B3C4E8-3E50-49A8-B133-17E4BCD21156Q34815754-280B2D15-CCA1-4C2D-B5CE-57FCF57F2F13Q35083244-D2D4A3BF-3E6F-4011-922A-0B0DD0481D7AQ35643865-1A5112CC-8C39-4FD9-8B6A-FFAA79A6EFDFQ36572016-DAC81B98-77AE-47C3-9EC2-6722CB84A7AEQ36640504-E8E47785-5E49-4036-B7E0-A9FEC8440AC2Q36675670-B7B6FEA6-15BF-4836-BB29-B06AD667AEF6Q36845920-262D83DC-EC22-4B8D-9FB0-5F316D7C3903Q36996369-5977DDB7-3C28-4328-B865-DD100F0AC7AFQ37088583-EFA63E7D-F851-4EE1-867B-504D12BB1795Q37153865-DE9F8EE9-FA0C-480C-9029-82A017C36FB7Q37280085-FE8F2A7F-48E2-4924-9569-8A27A1FA4C46Q37626820-2E62770D-6118-4921-A5AF-EB5A5817CE37Q37877295-B63EE153-A7CA-428A-A225-CED3104AAB61Q37975816-177209B2-9309-4DDF-9747-2665EFCEF072Q38991962-A90A47F7-7216-4761-AB5A-A47A6C9816ACQ40234857-BD122026-9C7B-4D2E-8127-E911225DB9F1
P2860
A glimpse of a possible amyloidogenic intermediate of transthyretin.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
A glimpse of a possible amyloidogenic intermediate of transthyretin.
@en
type
label
A glimpse of a possible amyloidogenic intermediate of transthyretin.
@en
prefLabel
A glimpse of a possible amyloidogenic intermediate of transthyretin.
@en
P2093
P356
P1476
A glimpse of a possible amyloidogenic intermediate of transthyretin.
@en
P2093
P2888
P304
P356
10.1038/78980
P577
2000-09-01T00:00:00Z
P5875
P6179
1027074443