about
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EASDifferential effects of glycation on protein aggregation and amyloid formation.Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicityThe chaperone domain BRICHOS prevents CNS toxicity of amyloid-β peptide in Drosophila melanogasterStabilization of neurotoxic Alzheimer amyloid-beta oligomers by protein engineeringAmyloid structure: conformational diversity and consequences.Molecular interpretation of ACTH-β-endorphin coaggregation: relevance to secretory granule biogenesisTowards revealing the structure of bacterial inclusion bodies.Regulation and aggregation of intrinsically disordered peptidesA dynamic study of protein secretion and aggregation in the secretory pathway.Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptideRole of β-hairpin formation in aggregation: the self-assembly of the amyloid-β(25-35) peptide.Influence of the valine zipper region on the structure and aggregation of the basic leucine zipper (bZIP) domain of activating transcription factor 5 (ATF5).Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granulesInitiation of assembly of tau(273-284) and its ΔK280 mutant: an experimental and computational study.Nephila clavipes Flagelliform silk-like GGX motifs contribute to extensibility and spacer motifs contribute to strength in synthetic spider silk fibers.Therapeutic applications of antibodies in non-infectious neurodegenerative diseasesProtein engineering to stabilize soluble amyloid β-protein aggregates for structural and functional studies.Nanomaterials: amyloids reflect their brighter side.Lipopolysaccharide-binding protein (LBP) reverses the amyloid state of fibrin seen in plasma of type 2 diabetics with cardiovascular co-morbidities.Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid β-protein aggregation and toxicity.BRICHOS domains efficiently delay fibrillation of amyloid β-peptide.Early aggregation preceding the nucleation of insulin amyloid fibrils as monitored by small angle X-ray scattering.Polymorphism in bovine serum albumin fibrils: morphology and statistical analysis.p53 amyloid formation leading to its loss of function: implications in cancer pathogenesis.Controlled Exposure of Bioactive Growth Factor in 3D Amyloid Hydrogel for Stem Cells Differentiation.Influence of amino acid specificities on the molecular and supramolecular organization of glycine-rich elastin-like polypeptides in water.Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides.Human lysozyme inhibits the in vitro aggregation of Aβ peptides, which in vivo are associated with Alzheimer's disease.Lipopolysaccharide-binding protein (LBP) can reverse the amyloid state of fibrin seen or induced in Parkinson's disease.No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases.Structural Insight of Amyloidogenic Intermediates of Human Insulin.Adhesion of Human Mesenchymal Stem Cells and Differentiation of SH-SY5Y Cells on Amyloid Fibrils
P2860
Q27677102-6A28BECA-81C8-4E0F-B594-2D83FB5ED4C0Q30374807-227D4AE8-8ACF-4200-901F-0559F305ADEDQ30472712-45FBA06E-3107-4492-AC42-5F0D15ACA713Q33677217-F5A9C56B-97A2-469D-8D61-A983D558A7F7Q34100591-A8C0EBB2-53E6-40B2-9B35-2508DBF3D112Q34175001-37F249E9-D960-43BF-8C58-10A6D76AD63DQ34189316-5B85A6AE-9588-47DA-8F5C-74BA41996F58Q34612503-96844358-1054-46D4-B6BF-6EDB77BE3BE4Q35157010-92B9719E-0F0D-4B20-BEA9-90DF77C690FFQ35298457-7F3BBC40-ADF4-46AA-A638-1AA687FD8744Q35585206-B46513A1-2985-4DC2-8024-35749AA26D43Q36150710-E477BBFE-85EE-4861-8D06-2C01C280174AQ36502656-59A65E6A-240B-433C-A6C3-DB438297D365Q36650385-ABF731B2-1609-43A6-AA80-56C52BC6C12FQ36719261-9C8C0BCE-7040-4879-B5B6-8BE31D570AF4Q36874806-0856F725-B4BB-4C81-A4DD-E53ECE32C687Q37593235-6BE584AC-9A6D-4229-A521-09179572ADFAQ37862785-D8C5F485-4F96-483B-B584-F146FEBC5363Q37913546-DC5407D7-6870-49DD-A52A-3D97CB7C731EQ37960007-EB3B2A67-599B-4B8A-BCE2-6AE041876F2FQ38603046-FFCF24E7-2F17-435F-91AA-98444A850A25Q39342506-BC22F4B2-CDF8-457A-922A-845A6EA2EFA4Q41856638-5C3EE767-D8AF-4279-93F8-B518F57F1207Q43201255-DEA606D8-8FDF-46F1-A71D-AE6025E0FC60Q44072190-A73FCB74-98E6-4549-AC79-9C0867B009CCQ46345550-8BDE5996-58F2-4D6D-A332-BC43AEDB1DADQ47889447-F9D8FC36-E8CD-4DAD-A275-1B23F79B85C6Q50539465-F0BB36AC-0DA1-4CF9-B6DD-C9D8DFF2E914Q50796594-E6500DB8-562D-4A8A-9AE6-3BF348371BCDQ50909964-D52625D2-F4FD-48E8-A494-99895110A388Q52679530-341BEB8D-C47B-405A-AE04-E91AEFE6FE72Q53698735-BA7FA1A0-6826-4EAD-BB8C-FF24EF48198EQ55715578-15A6FE5F-7549-4300-831F-6C807F746C57Q57747734-F8822FE5-5806-4F93-A2FE-6D5D29E9D1A5
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 14 July 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Structure-activity relationship of amyloid fibrils.
@en
Structure-activity relationship of amyloid fibrils.
@nl
type
label
Structure-activity relationship of amyloid fibrils.
@en
Structure-activity relationship of amyloid fibrils.
@nl
prefLabel
Structure-activity relationship of amyloid fibrils.
@en
Structure-activity relationship of amyloid fibrils.
@nl
P2093
P2860
P1433
P1476
Structure-activity relationship of amyloid fibrils
@en
P2093
Jason Greenwald
Roland Riek
P2860
P304
P356
10.1016/J.FEBSLET.2009.07.003
P407
P50
P577
2009-07-14T00:00:00Z