Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants
about
Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicityTissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue cultureDeposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregatesMisfolding and amyloid aggregation of apomyoglobinIodine Atoms: A New Molecular Feature for the Design of Potent Transthyretin Fibrillogenesis InhibitorsAmyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSESCold denaturation of a protein dimer monitored at atomic resolutionBeyond genetic factors in familial amyloidotic polyneuropathy: protein glycation and the loss of fibrinogen's chaperone activityEpigallocatechin-3-gallate as a potential therapeutic drug for TTR-related amyloidosis: "in vivo" evidence from FAP mice modelsTransthyretin Amyloidosis: Chaperone Concentration Changes and Increased Proteolysis in the Pathway to DiseaseModifications of the 7-Hydroxyl Group of the Transthyretin Ligand Luteolin Provide Mechanistic Insights into Its Binding Properties and High Plasma SpecificityDifferential effects of glycation on protein aggregation and amyloid formation.The sour side of neurodegenerative disorders: the effects of protein glycation.Simulation of pH-dependent edge strand rearrangement in human beta-2 microglobulin.Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.Physiological IgM class catalytic antibodies selective for transthyretin amyloid.Proteomic analysis of peritoneal fluid of patients treated by peritoneal dialysis: effect of glucose concentration.Differential expression of Cathepsin E in transthyretin amyloidosis: from neuropathology to the immune system.The relative amounts of plasma transthyretin forms in familial transthyretin amyloidosis: a quantitative analysis by Fourier transform ion-cyclotron resonance mass spectrometry.Composition and proteolytic processing of corneal deposits associated with mutations in the TGFBI geneInterleukin-1 signaling pathway as a therapeutic target in transthyretin amyloidosis.Argpyrimidine, a methylglyoxal-derived advanced glycation end-product in familial amyloidotic polyneuropathy.An overview of drugs currently under investigation for the treatment of transthyretin-related hereditary amyloidosis.Maternal serum protein profile and immune response protein subunits as markers for non-invasive prenatal diagnosis of trisomy 21, 18, and 13.The modulation of transthyretin tetramer stability by cysteine 10 adducts and the drug diflunisal. Direct analysis by fluorescence-detected analytical ultracentrifugationGlial cells in familial amyloidotic polyneuropathyCooperative stabilization of transthyretin by clusterin and diflunisal.Structure-based analysis of A19D, a variant of transthyretin involved in familial amyloid cardiomyopathy.Structural and kinetic mapping of side-chain exposure onto the protein energy landscapeThe effect of tafamidis on the QTc interval in healthy subjects.Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways.Transthyretin deposition in articular cartilage: a novel mechanism in the pathogenesis of osteoarthritis.Biomarkers in the assessment of therapies for familial amyloidotic polyneuropathy.A New Folding Kinetic Mechanism for Human Transthyretin and the Influence of the Amyloidogenic V30M Mutation.Uncovering the Mechanism of Aggregation of Human Transthyretin.Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils.Identification of beta-amyloid-binding sites on transthyretin.Why is Leu55-->Pro55 transthyretin variant the most amyloidogenic: insights from molecular dynamics simulations of transthyretin monomersRepositioning tolcapone as a potent inhibitor of transthyretin amyloidogenesis and associated cellular toxicity.Localized structural fluctuations promote amyloidogenic conformations in transthyretin.
P2860
Q24311309-6896F93C-98E1-437F-BA2E-7C7EDA54CE24Q24626477-CD90101E-E1F2-4D5A-9731-9DD5B062E892Q24685634-22C2F10F-E4FB-46A4-AA50-FC9DC93A84BBQ26830356-FF7FD110-721A-475B-BDBC-E946B2B21D50Q27653350-3DCA720B-F35D-46C5-9F5D-B0BAA2432DA0Q27656412-EF5489F4-1AD9-4D80-A88B-19CD6347A70AQ27683967-1881FE6A-02DB-43B0-BA83-1529CA4522DDQ28477682-A0C42D35-6444-496C-967B-6397C8D6F2B5Q28478763-58CCAEB1-9EA6-4ADA-908C-274FAD307537Q28546193-EC816AA7-6678-4E4C-BFD4-32A0636A5E1BQ28551199-978A2AA7-4E12-4F59-8019-4A408C147F05Q30374807-EE9CAC32-3829-4783-BCEC-BBD105FD9A57Q30386079-E824CAE9-64A9-48C1-AB6A-B9D196B93BF9Q31022562-1C30A18E-EE94-4D89-8171-1ECC93FA2215Q33516611-1DC0987E-3A3C-4D71-88A6-CF259BC2E61DQ33676625-1F9DC48E-5E3D-4F8E-AA5B-503BB22B941EQ33747370-3E0514B8-D6BB-49B7-847D-AE8210DC7803Q33768132-08B7E897-A80B-4124-8CF6-F846DD359D3CQ34073701-EA4B5337-F68E-4219-8C77-FE9D1502AF33Q34095791-2554B6B4-07B1-4AC3-AAE7-F7D1C78B6F51Q34336131-1153EC58-26DD-44F5-B3E7-D2F1328D6958Q34336978-368EE4A7-635C-42A5-8F8A-8BC7977E7BFBQ34428314-1D915489-FFF8-48AA-A6BD-CFE5F6562716Q34570581-672EB7D3-FA69-4D1D-B009-F7A6B18B3EE1Q34759704-50C9D7D0-B7C4-48C7-8B5D-45FF23128524Q34793765-AE8EEFC7-8E10-4FA6-B3E9-F0547D377E05Q35001154-3F112C2D-CF6B-49BE-B066-67972567B874Q35072784-D9652AF7-C346-47BC-BB13-F13C4A206D76Q35081718-9E24843E-753F-458D-ACE0-F2563E3E066FQ35684808-783D1346-82F3-42D3-9FC4-CD4ED08011E5Q35763674-D1180A5F-ED7F-488E-8BF8-16A3E1F51CD4Q35901035-55617C13-47A7-4AE0-A62A-7DDFBE2075F6Q36057473-4A84DD64-034C-4B62-9A71-1F3CC83F5A12Q36121846-626D53D5-13EC-4F8F-98C0-D96DD8A34753Q36323485-ECC07528-6306-4B48-9BB6-F939B9344388Q36420250-55B86D41-4092-412F-ABA1-DC782B3284C0Q36488937-D9DC8A11-AB6D-4C6F-8485-A9DB0D4CD4D6Q36572016-38C366C5-96DE-4593-8C86-FA51CC9FB5EAQ36615637-16241BC1-422F-43A6-B254-923E3AF1E54CQ36675670-F64D560F-C40B-4344-8997-9A00F8CF31B7
P2860
Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im April 2001 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована у квітні 2001
@uk
name
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@en
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@nl
type
label
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@en
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@nl
prefLabel
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@en
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@nl
P2860
P50
P356
P1476
Tetramer Dissociation and Mono ...... dogenic Transthyretin Variants
@en
P2093
Maria João M. Saraiva
P2860
P304
27207-27213
P356
10.1074/JBC.M101024200
P407
P577
2001-04-16T00:00:00Z