Alternative conformations of amyloidogenic proteins govern their behavior.
about
Fluorescent Proteins as Biomarkers and Biosensors: Throwing Color Lights on Molecular and Cellular ProcessesMolecular chaperone properties of serum amyloid P componentDeficiency of disulfide bonds facilitating fibrillogenesis of endostatinThe pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillizationThe 8 and 5 kDa fragments of plasma gelsolin form amyloid fibrils by a nucleated polymerization mechanism, while the 68 kDa fragment is not amyloidogenicA systematic exploration of the influence of the protein stability on amyloid fibril formation in vitroWhat macromolecular crowding can do to a proteinHuman-murine transthyretin heterotetramers are kinetically stable and non-amyloidogenic. A lesson in the generation of transgenic models of diseases involving oligomeric proteinsInhibiting transthyretin conformational changes that lead to amyloid fibril formationAn amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated beta-sheet structure for amyloidThe roles of turn formation and cross-strand interactions in fibrillization of peptides derived from the OspA single-layer beta-sheetPrediction of Peptide and Protein Propensity for Amyloid FormationSynergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical InvestigationsA quasi-spontaneous amyloid route in a DNA binding gene regulatory domain: The papillomavirus HPV16 E2 protein.Equilibrium unfolding CD studies of bovine beta-lactoglobulin and its 14-52 fragment at acidic pH.Amyloid fibril formation by an SH3 domain.Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow ChemistrySwitch region for pathogenic structural change in conformational disease and its predictionReduction of the C191-C220 disulfide of α-chymotrypsinogen A reduces nucleation barriers for aggregation.Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics.De novo amyloid proteins from designed combinatorial librariesAmyloid-forming peptides selected proteolytically from phage display library.In vivo glycosylation suppresses the aggregation of amyloidogenic hen egg white lysozymes expressed in yeast.Construction and characterization of protein libraries composed of secondary structure modules.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.Amyloid formation from an α-helix peptide bundle is seeded by 3(10)-helix aggregates.Spatial extent of charge repulsion regulates assembly pathways for lysozyme amyloid fibrilsEffects of several quinones on insulin aggregation.Constant pH replica exchange molecular dynamics in biomolecules using a discrete protonation modelConstant pH Molecular Dynamics in Explicit Solvent with Enveloping Distribution Sampling and Hamiltonian ExchangeSupport for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro.The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.Late-onset neurodegenerative diseases--the role of protein insolubility.Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsDetection and characterization of aggregates, prefibrillar amyloidogenic oligomers, and protofibrils using fluorescence spectroscopy.Protein folding: a perspective for biology, medicine and biotechnology.Protein misfolding and disease; protein refolding and therapy.Early events in insulin fibrillization studied by time-lapse atomic force microscopy.Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.
P2860
Q22241334-D0945594-38C4-48FA-A62C-4D71AC414761Q22254102-9EB43345-8FB4-41C1-9265-058F340DF667Q24293595-784CB1AC-949F-405B-AA6B-5094D7CED959Q24308267-00AA53B5-1DEB-4464-8390-0D89A2219518Q24316253-A5088881-7428-4890-B224-7ACEB79AB2E2Q24672760-24A43804-378D-4919-9FC1-ECD0FC3F63B0Q27012942-FD652657-5D39-4737-8F76-FB28473FA43AQ27649069-C22B8E4A-3761-47E4-A8C9-01B189FA660DQ27765742-0D35974C-C89E-4020-84B7-C9826921E077Q28202568-2CA5411E-B20F-4838-9F6C-FAD0C3D00C75Q28359810-E05AA765-7E1F-454B-9B26-87B901A1CBC2Q28546984-AAE45EE2-0493-4EEF-B4E3-222F41CD0549Q28553635-FEB689D8-A3EF-4AE8-B220-12CC9B859658Q30158017-2607D701-6706-4DD1-8BFD-F49AE1840E6DQ30175801-64E03763-16C6-4580-AEC9-2F325E08A58DQ30176202-A4EBC0D1-5C2D-452C-AA79-F15C80B1502AQ30375158-843E8B02-257E-475B-B2CA-EBA26665E176Q30384993-4272D9EA-9939-40C0-AEF9-B27FAB07DA04Q30408748-ABAAB742-6852-4695-B90B-A493D14A28DCQ30457664-5B089934-A735-4169-8689-B2D203D424F7Q30585001-CE2BCA7C-F892-48F4-AA13-D87785C7AF19Q30779135-A38524FC-DB00-44F5-BC1A-76B9B72480CCQ30968152-E5E00E51-9E8C-4ECF-8880-6520914809B6Q32065189-43C52737-3A10-4B61-9813-721BC41FC1F9Q33184872-1F70611D-F4F3-4C72-98EB-DC964CDE0599Q33356197-6E852639-6A02-40DD-BC76-B912DEF13FC3Q33786022-893D17B4-E865-41CA-BF48-A669F9E5C944Q33869235-E17AB0F5-4E92-4CB6-9449-CD12CA305F38Q33876973-14718612-BB4C-4692-A9A6-5CD8A4C236FBQ33880577-EBB73408-D10D-464D-B61A-9A33969AB642Q33893524-D2500D57-ABE1-4A00-BC24-6BFBF8A41E8BQ33949040-66521DE7-DA16-4B12-BC41-ADAD8BB403F6Q33952780-FF5A53D0-16F5-49B5-AA8A-560A78D673D3Q33989372-6BCBAEB2-D986-4403-8343-D76E0197A050Q34184303-4C325E2E-89F3-46F6-99D2-DAA6485622E5Q34190708-18075042-B41F-4438-860E-3C630AFF840CQ34206504-76A96725-5919-4307-8FC3-6DA6BB6F95C2Q34286115-4C04E027-DB35-48A8-BA71-0E14585DC72FQ34353013-29029051-CD39-4975-AE39-85DD98547592Q34443878-82FF57AE-999D-4112-9B99-B0AAF89C715A
P2860
Alternative conformations of amyloidogenic proteins govern their behavior.
description
1996 nî lūn-bûn
@nan
1996 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Alternative conformations of amyloidogenic proteins govern their behavior.
@ast
Alternative conformations of amyloidogenic proteins govern their behavior.
@en
Alternative conformations of amyloidogenic proteins govern their behavior.
@nl
type
label
Alternative conformations of amyloidogenic proteins govern their behavior.
@ast
Alternative conformations of amyloidogenic proteins govern their behavior.
@en
Alternative conformations of amyloidogenic proteins govern their behavior.
@nl
prefLabel
Alternative conformations of amyloidogenic proteins govern their behavior.
@ast
Alternative conformations of amyloidogenic proteins govern their behavior.
@en
Alternative conformations of amyloidogenic proteins govern their behavior.
@nl
P1476
Alternative conformations of amyloidogenic proteins govern their behavior.
@en
P2093
P356
10.1016/S0959-440X(96)80089-3
P577
1996-02-01T00:00:00Z