about
The pentapeptide LQVVR plays a pivotal role in human cystatin C fibrillizationThe extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrilsThe 3D profile method for identifying fibril-forming segments of proteinsStructure of the cross-beta spine of amyloid-like fibrilsMolecular basis for insulin fibril assemblyA systematic survey identifies prions and illuminates sequence features of prionogenic proteinsSequence determinants of protein aggregation: tools to increase protein solubility.SNPeffect: a database mapping molecular phenotypic effects of human non-synonymous coding SNPsMapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerizationHydrophobic Surface Burial Is the Major Stability Determinant of a Flat, Single-layer β-SheetMinimalist design of water-soluble cross-beta architecture.Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicityProtein folding pathology in domestic animals.Cooperative transition between open and closed conformations in potassium channelsBeta-strand interfaces of non-dimeric protein oligomers are characterized by scattered charged residue patternsPrediction of Peptide and Protein Propensity for Amyloid FormationAMYPdb: a database dedicated to amyloid precursor proteinsShort amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.PROTDES: CHARMM toolbox for computational protein design.Intrinsic fibrillation of fast-acting insulin analogs.Distinct aggregation mechanisms of monoclonal antibody under thermal and freeze-thaw stresses revealed by hydrogen exchange.Using simple artificial intelligence methods for predicting amyloidogenesis in antibodiesThe model of amyloid aggregation of Escherichia coli RNA polymerase σ70 subunit based on AFM data and in vitro assays.A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.CPAD, Curated Protein Aggregation Database: A Repository of Manually Curated Experimental Data on Protein and Peptide Aggregation.Prediction of amyloidogenic and disordered regions in protein chainsStructural elements regulating amyloidogenesis: a cholinesterase model system.Prediction of amyloid fibril-forming segments based on a support vector machineAmyloidogenic determinants are usually not buriedMolecular basis for amyloid fibril formation and stability.PASTA 2.0: an improved server for protein aggregation prediction.Conformational transition of amyloid beta-peptide.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.The amyloid stretch hypothesis: recruiting proteins toward the dark sideExploiting heterogeneous features to improve in silico prediction of peptide status - amyloidogenic or non-amyloidogenic.Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubilityFibril-forming motifs are essential and sufficient for the fibrillization of human Tau.Impact of sequence on the molecular assembly of short amyloid peptides.Prediction and analysis of antibody amyloidogenesis from sequences.A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins.
P2860
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P2860
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
Sequence determinants of amyloid fibril formation
@ast
Sequence determinants of amyloid fibril formation
@en
type
label
Sequence determinants of amyloid fibril formation
@ast
Sequence determinants of amyloid fibril formation
@en
prefLabel
Sequence determinants of amyloid fibril formation
@ast
Sequence determinants of amyloid fibril formation
@en
P2860
P356
P1476
Sequence determinants of amyloid fibril formation
@en
P2093
Luis Serrano
Manuela López de la Paz
P2860
P356
10.1073/PNAS.2634884100
P407
P577
2003-12-22T00:00:00Z