The circularization of amyloid fibrils formed by apolipoprotein C-II.
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Structural basis for the recognition and cross-linking of amyloid fibrils by human apolipoprotein EUltrasonic force microscopy for nanomechanical characterization of early and late-stage amyloid-β peptide aggregation.Amyloid triangles, squares, and loops of apolipoprotein C-III.Phospholipids enhance nucleation but not elongation of apolipoprotein C-II amyloid fibrilsAn equilibrium model for linear and closed-loop amyloid fibril formation."Janus" cyclic peptides: a new approach to amyloid fibril inhibition?A kinetic study of ovalbumin fibril formation: the importance of fragmentation and end-joiningCalcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domainSedimentation coefficient distributions of large particles.Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrilsApolipoproteins and amyloid fibril formation in atherosclerosis.Nanomaterials: amyloids reflect their brighter side.Candida albicans Als adhesins have conserved amyloid-forming sequences.Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Detection of populations of amyloid-like protofibrils with different physical properties.Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy.Fibrillar amyloid protein present in atheroma activates CD36 signal transduction.Existence of different structural intermediates on the fibrillation pathway of human serum albumin.Molecular modeling and dynamic simulations of agglutinin-like family members from Candida albicans: New insights into potential targets for the treatment of candidiasis.Non-fibrillar components of amyloid deposits mediate the self-association and tangling of amyloid fibrils.Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization.Collagen plays an active role in the aggregation of beta2-microglobulin under physiopathological conditions of dialysis-related amyloidosisScaling and dimensionality in the chemical kinetics of protein filament formationKinetic theory of protein filament growth: Self-consistent methods and perturbative techniques
P2860
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P2860
The circularization of amyloid fibrils formed by apolipoprotein C-II.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին 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
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@ast
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@en
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@nl
type
label
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@ast
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@en
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@nl
prefLabel
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@ast
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@en
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@nl
P2093
P2860
P50
P1433
P1476
The circularization of amyloid fibrils formed by apolipoprotein C-II.
@en
P2093
Geoffrey J Howlett
Jason J Davis
Neil H Thomson
Rob Daniels
Walraj S Gosal
P2860
P304
P356
10.1016/S0006-3495(03)74812-7
P407
P577
2003-12-01T00:00:00Z