Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.
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Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine.Microcanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity.High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .NMR characterizations of an amyloidogenic conformational ensemble of the PI3K SH3 domain.Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersThe core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.Defective protein folding and aggregation as the basis of neurodegenerative diseases: the darker aspect of proteins.Covalent α-synuclein dimers: chemico-physical and aggregation properties.Highly amyloidogenic two-chain peptide fragments are released upon partial digestion of insulin with pepsin.Core sequence of PAPf39 amyloid fibrils and mechanism of pH-dependent fibril formation: the role of monomer conformationNanotools for megaproblems: probing protein misfolding diseases using nanomedicine modus operandiFolding versus aggregation: polypeptide conformations on competing pathwaysDirect characterization of amyloidogenic oligomers by single-molecule fluorescence.Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.Structure-activity relationship of amyloid fibrils.Nuclear inclusion bodies of mutant and wild-type p53 in cancer: a hallmark of p53 inactivation and proteostasis remodelling by p53 aggregation.Mass spectroscopic analysis of Sup35NM prion polymerization.Influence of denatured and intermediate states of folding on protein aggregationOn the nucleation of amyloid beta-protein monomer folding.Self-assembly of bacteriophage-associated hyaluronate lyase (HYLP2) into an enzymatically active fibrillar film.Kinetic and thermodynamic stability of bacterial intracellular aggregates.Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry.Global analysis of protein structural changes in complex proteomes.The synergistic effect between KLVFF and self-assembly chaperones on both disaggregation of beta-amyloid fibrils and reducing consequent toxicity.Inhibition of amyloid aggregation by formation of helical assemblies.Oleuropein aglycone stabilizes the monomeric α-synuclein and favours the growth of non-toxic aggregates.
P2860
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P2860
Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.
description
2003 nî lūn-bûn
@nan
2003 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Protein aggregation and amyloi ...... probed by limited proteolysis.
@ast
Protein aggregation and amyloi ...... probed by limited proteolysis.
@en
type
label
Protein aggregation and amyloi ...... probed by limited proteolysis.
@ast
Protein aggregation and amyloi ...... probed by limited proteolysis.
@en
prefLabel
Protein aggregation and amyloi ...... probed by limited proteolysis.
@ast
Protein aggregation and amyloi ...... probed by limited proteolysis.
@en
P2093
P1476
Protein aggregation and amyloi ...... probed by limited proteolysis.
@en
P2093
Angelo Fontana
Cristina Capanni
Erica Frare
Fabrizio Chiti
Niccolò Taddei
Patrizia Polverino de Laureto
Silvia Costantini
P304
P356
10.1016/J.JMB.2003.09.024
P407
P577
2003-11-01T00:00:00Z