Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation.
about
New Class of Inhibitors of Amyloid-beta Fibril Formation. IMPLICATIONS FOR THE MECHANISM OF PATHOGENESIS IN ALZHEIMER'S DISEASEA Substructure Combination Strategy To Create Potent and Selective Transthyretin Kinetic Stabilizers That Prevent Amyloidogenesis and CytotoxicityTrapping of palindromic ligands within native transthyretin prevents amyloid formationStilbene Vinyl Sulfonamides as Fluorogenic Sensors of and Traceless Covalent Kinetic Stabilizers of Transthyretin That Prevent AmyloidogenesisThe preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic stateTransthyretin variants with improved inhibition of β-amyloid aggregation.Serum transthyretin monomer in patients with familial amyloid polyneuropathy.Identification of S-sulfonation and S-thiolation of a novel transthyretin Phe33Cys variant from a patient diagnosed with familial transthyretin amyloidosisFourier transform infrared spectroscopy provides a fingerprint for the tetramer and for the aggregates of transthyretin.Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease.Inflammatory state exists in familial amyloid polyneuropathy that may be triggered by mutated transthyretin.Amyloid diseases: abnormal protein aggregation in neurodegenerationProgress in transthyretin fibrillogenesis research strengthens the amyloid hypothesis.Effect of surfaces on amyloid fibril formation.Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosisAmyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins.Characterization of the interaction of β-amyloid with transthyretin monomers and tetramers.Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometryA mechanistic model for amorphous protein aggregation of immunoglobulin-like domains.Initial conformational changes of human transthyretin under partially denaturing conditionsStability of the transthyretin molecule as a key factor in the interaction with a-beta peptide--relevance in Alzheimer's disease.Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversionA 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.Cooperative stabilization of transthyretin by clusterin and diflunisal.Cysteine 10 is a key residue in amyloidogenesis of human transthyretin Val30Met.Thermodynamic study of transthyretin association (wild-type and senile forms) with heparan sulfate proteoglycan: pH effect and implication of the reactive histidine residue.Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.Involvement of Macrophages in the Pathogenesis of Familial Amyloid Polyneuropathy and Efficacy of Human iPS Cell-Derived Macrophages in Its TreatmentA novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis.Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution.Amyloid fibrils trigger the release of neutrophil extracellular traps (NETs), causing fibril fragmentation by NET-associated elastase.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.A current pharmacologic agent versus the promise of next generation therapeutics to ameliorate protein misfolding and/or aggregation diseases.Gd-nanoparticles functionalization with specific peptides for ß-amyloid plaques targetingDifferential modification of Cys10 alters transthyretin's effect on beta-amyloid aggregation and toxicity.Induced pluripotent stem cell modeling of multisystemic, hereditary transthyretin amyloidosis.The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.
P2860
Q22248067-5BA1ADEF-A87C-4B5D-B3D7-6A66E80119D1Q27658823-30E1A09C-72C5-4483-985D-0EEF977EB4D6Q27665687-070FBDE7-5107-49FB-9D1C-36CBAB6AD2C8Q27680500-392DBB9A-193E-4732-AB1C-074121F9F779Q28118516-3BC51969-75C5-4E18-85AC-E9526A5949BCQ30757280-391F687B-3D2C-4FAC-A68C-DEBA002EB1CDQ30797299-CEAEAA69-C7F5-4D1B-8226-DD94F3CB8FB8Q30968181-8097B841-3F2B-4B43-A7DE-99D6B5D5D6A7Q33435248-C630BF4A-5D9D-4D25-A329-DB513D81887BQ33546211-129927A1-CDC8-41EF-A081-83F21A80EB6CQ33685899-BA087094-577A-4D4F-A21A-E14613AC5F5AQ33723502-CBEFFD1A-863D-47FA-8CA1-227278011FE7Q33952579-973DE532-8C25-47C1-BA38-F497F0C73D11Q34053378-A959735C-9C49-4552-9FC6-C935891CDF66Q34078348-5AA656ED-76F3-47A8-8160-ADC82A02FB56Q34083143-F30D084F-D2F5-4DE7-A5D0-BF6AE6844E0DQ34146589-9AB27318-E6E3-4CEF-9963-897C0C1CCF56Q34173720-0039A472-0AF9-493C-B1C2-820D6D30B14BQ34334001-42A27481-55AD-4391-AD37-BDB4B16A38A3Q34350522-7FCC21AE-8128-4116-A3AD-AB237D21AC60Q34428889-4CF138CB-6092-4436-BE71-3662ED0A4423Q34561167-BEA1ABCF-7494-4E9F-AF21-5244227C8FA9Q34576022-CDD5D97E-8C8C-4D5D-9D0D-B1613998A906Q34743288-A7B161F1-38BA-40AF-A6B9-2D0FF270315AQ35001154-60F7CC63-00AE-410F-B9EF-B19B125E52A0Q35083244-643FD526-4AD9-4A2E-8266-5C0305D18817Q35254474-4F1D2013-49C3-481A-95F9-01ED07993E0FQ35813797-610CD8AA-4737-4637-BBA1-46938738482CQ36151383-0D711766-CBDF-4DE4-A2E9-AB3CACBDD089Q36159473-DD4FE3FE-4AF0-47E6-B50A-494303B0C6BCQ36281902-9500B5EF-75D8-4934-8793-F0433AD2A66BQ36347798-EE04CC11-CC85-447F-9B78-FCDF17F6856AQ36572016-C5B2932E-9D4E-4CEC-BE2D-BFC3E1F49D24Q36640504-C83EA461-2C30-42AF-8F02-DE39E195E769Q36675670-1A9EEB2F-4E9C-444F-A2EB-27360C146B25Q37004163-35CAC494-0075-4593-AD90-832D6E811D94Q37126036-93A4C104-C50F-413D-944D-C59988C8E1F8Q37285491-5F365EBC-C7F1-4F2F-833D-995597E654D1Q37344629-6FF879DE-C7D2-439C-8B7F-90157B2712A6Q37975816-1FBEEA6A-87C6-4850-998B-F0F45EC53D0D
P2860
Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Characterization of the transt ...... L55P amyloid fibril formation.
@en
Characterization of the transt ...... L55P amyloid fibril formation.
@nl
type
label
Characterization of the transt ...... L55P amyloid fibril formation.
@en
Characterization of the transt ...... L55P amyloid fibril formation.
@nl
prefLabel
Characterization of the transt ...... L55P amyloid fibril formation.
@en
Characterization of the transt ...... L55P amyloid fibril formation.
@nl
P356
P1433
P1476
Characterization of the transt ...... L55P amyloid fibril formation.
@en
P304
17851-17864
P356
10.1021/BI981876+
P407
P577
1998-12-01T00:00:00Z