about
Binding of epigallocatechin-3-gallate to transthyretin modulates its amyloidogenicityIn vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)Human metallothioneins 2 and 3 differentially affect amyloid-beta binding by transthyretinSynergy of combined doxycycline/TUDCA treatment in lowering Transthyretin deposition and associated biomarkers: studies in FAP mouse modelsDeposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregatesTransthyretin and Alzheimer's disease: where in the brain?Transthyretin protects against A-beta peptide toxicity by proteolytic cleavage of the peptide: a mechanism sensitive to the Kunitz protease inhibitor.Stability of the transthyretin molecule as a key factor in the interaction with a-beta peptide--relevance in Alzheimer's disease.Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.Transthyretin participates in beta-amyloid transport from the brain to the liver--involvement of the low-density lipoprotein receptor-related protein 1?Resveratrol administration increases Transthyretin protein levels ameliorating AD features - importance of transthyretin tetrameric stability.Transthyretin neuroprotection in Alzheimer's disease is dependent on proteolysis.Targeting a rare amyloidotic disease through rationally designed polymer conjugates.Polymer-doxycycline conjugates as fibril disrupters: an approach towards the treatment of a rare amyloidotic disease.Comparative in vitro and ex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design.S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation.Testing the therapeutic potential of doxycycline in a Drosophila melanogaster model of Alzheimer disease.Controlling amyloid-beta peptide(1-42) oligomerization and toxicity by fluorinated nanoparticles.Randomization of amyloid-β-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity.Design and biological activity of beta-sheet breaker peptide conjugates.Amyloidogenic properties of transthyretin-like protein (TLP) from Escherichia coli.Transthyretin binding to A-Beta peptide--impact on A-Beta fibrillogenesis and toxicity.Activation of ERK1/2 MAP kinases in familial amyloidotic polyneuropathy.4'-iodo-4'-deoxydoxorubicin and tetracyclines disrupt transthyretin amyloid fibrils in vitro producing noncytotoxic species: screening for TTR fibril disrupters.Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?4'-Iodo-4'-deoxydoxorubicin disrupts the fibrillar structure of transthyretin amyloid.Small molecules present in the cerebrospinal fluid metabolome influence superoxide dismutase 1 aggregationSelective binding to transthyretin and tetramer stabilization in serum from patients with familial amyloidotic polyneuropathy by an iodinated diflunisal derivative.X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization.Aprotinin binding to amyloid fibrils.Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.Insights on the Interaction between Transthyretin and Aβ in Solution. A Saturation Transfer Difference (STD) NMR Analysis of the Role of Iododiflunisal.Transthyretin stability is critical in assisting beta amyloid clearance- Relevance of transthyretin stabilization in Alzheimer's disease.Transthyretin stabilization by iododiflunisal promotes amyloid-β peptide clearance, decreases its deposition, and ameliorates cognitive deficits in an Alzheimer's disease mouse model.Gender-dependent transthyretin modulation of brain amyloid-β levels: evidence from a mouse model of Alzheimer's disease.Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model.Dual ligand immunoliposomes for drug delivery to the brain.Transthyretin decrease in plasma of MCI and AD patients: investigation of mechanisms for disease modulation.The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants
P50
Q24311309-5F6C70A4-813D-49DE-B363-9917136382CFQ24337632-DC6333A9-F755-4B6F-AA15-9D137E159B10Q24339434-71DC0497-CAF2-419F-A178-3E1D4DA80EA0Q24631610-B7165AC4-1DE6-4E5B-86E9-31A9EFCC1794Q24685634-7AD4E4C5-88EE-4332-9A90-98E69B5C3CD2Q33243335-60958632-F5FD-4CBF-B059-54974EDFAD6FQ33358106-7BD82AAA-DAE9-4B73-A699-2CACDE2AD2E7Q34428889-4D5B6128-9F77-47C3-9E7A-895F11B26693Q35009596-64BAC274-081E-4C69-B550-A1194E9B6770Q36536181-3DFDE807-317D-4FEE-BD6B-766E13FA858DQ37370545-FA731A52-6627-4DD8-9AE3-F327D907FC04Q38638835-970BC208-316F-47E7-A597-FABFBD4AA286Q39028309-0960BD4B-69DA-407D-8C12-20E392F38E27Q39081517-94A64B30-4A38-44F4-B4FD-B28828511859Q39254356-D232653E-27E7-47E0-B826-435AF2546B5EQ39257498-BC79999E-B58B-4FCA-A9F7-25A9F195477BQ39458294-01D6A6B4-D4B5-4F77-9084-D77A182AA1F3Q39675329-A76C88DC-0AEA-4A2D-AB83-12BC4B79F569Q39702813-F72B4C13-70F8-4006-A894-3FE86EDBDDEFQ39878701-A7DFE1F2-0415-4DA1-9672-82D0C7542176Q39957230-F0810418-9689-41BA-BBAA-75E46B92489BQ40009615-DDE471E3-414C-497E-A215-584130206CF2Q40309149-8B2A4545-370B-4F85-8461-ECDFD784463EQ40651115-70DD37DD-2886-4AB7-A47D-BFA28C7BA1A9Q41955617-67300552-4559-43FD-957A-98347CB5152DQ42048697-43B78FF4-1406-4A4F-9525-4B43E64F6BD2Q42664185-B7789FC9-7F92-470A-9C20-3524E2C55953Q42806704-FBE57088-A99D-4AD4-922F-86505C83EAC8Q44285399-F8BE8CDC-C80C-420F-92EA-E166C27FB2C8Q46305215-AC95B5A2-72F7-4AB0-9279-7363B69F6124Q46791114-DA9E532F-7EF5-44E4-AAAC-6E16CDDE04FFQ48319785-690C2949-D7BB-45A9-BE7F-5F5FC66625CCQ48344282-BC62F0E5-5120-4909-9500-7C22DA570A4AQ48906790-0334C16F-FFCC-4701-8175-0C21A1335909Q48949588-8A3CA00F-0D7A-4659-A8FD-60DD2DCBAFC9Q50743781-F8938EF4-F055-4C5B-9FE1-2A7C8237977AQ51836873-BFFAEECD-8745-44FE-937E-1205416F0D09Q53329503-42D80BB3-CD5A-4B8D-A86C-4AA52FA65667Q55418035-ABD7F0E4-B1A2-492B-89CA-35C39A36F0E1Q57665571-D01473D3-4BAC-476E-922E-BC3F7B12DC1C
P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Isabel Cardoso
@ast
Isabel Cardoso
@en
Isabel Cardoso
@es
Isabel Cardoso
@nl
Isabel Cardoso
@sl
type
label
Isabel Cardoso
@ast
Isabel Cardoso
@en
Isabel Cardoso
@es
Isabel Cardoso
@nl
Isabel Cardoso
@sl
prefLabel
Isabel Cardoso
@ast
Isabel Cardoso
@en
Isabel Cardoso
@es
Isabel Cardoso
@nl
Isabel Cardoso
@sl
P1053
K-3903-2013
P106
P1153
6701390815
P21
P31
P3829
P496
0000-0003-2472-7055