Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis
about
Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structureDiversity, biogenesis and function of microbial amyloidsProbing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusionsThe TDP-43 N-terminal domain structure at high resolutionStructural insights into functional amyloid inhibition in Gram -ve bacteriaBacterial amyloid formation: structural insights into curli biogensisFunctional amyloids composed of phenol soluble modulins stabilize Staphylococcus aureus biofilmsSpecific chaperones and regulatory domains in control of amyloid formation.Quantifying prefibrillar amyloids in vitro by using a "thioflavin-like" spectroscopic method.The AgrD N-terminal leader peptide of Staphylococcus aureus has cytolytic and amyloidogenic properties.Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau.Strong underwater adhesives made by self-assembling multi-protein nanofibresCurli biogenesis: order out of disorder.Modulation of curli assembly and pellicle biofilm formation by chemical and protein chaperones.The bacterial curli system possesses a potent and selective inhibitor of amyloid formation.A Monte Carlo Study of the Early Steps of Functional Amyloid FormationStructure, Function, and Assembly of Adhesive Organelles by Uropathogenic BacteriaPromiscuous cross-seeding between bacterial amyloids promotes interspecies biofilms.Characterization of curli A production on living bacterial surfaces by scanning probe microscopy.Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formationExperimental manipulation of the microbial functional amyloid called curli.E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly.Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2/B1 introduce potent steric zippers that drive excess RNP granule assembly.Bacterial amyloids.Microbial manipulation of the amyloid fold.Protein folding, misfolding, aggregation and their implications in human diseases: discovering therapeutic ways to amyloid-associated diseases.RepA-WH1 prionoid: a synthetic amyloid proteinopathy in a minimalist hostStructural and functional diversity among amyloid proteins: Agents of disease, building blocks of biology, and implications for molecular engineering.Functional amyloid: turning swords into plowsharesIdentification of Key Amino Acid Residues Modulating Intracellular and In vitro Microcin E492 Amyloid FormationThe C-terminal repeating units of CsgB direct bacterial functional amyloid nucleation.AmyPro: a database of proteins with validated amyloidogenic regions.Amyloid peptides derived from CsgA and FapC modify the viscoelastic properties of biofilm model matrices.The role of microbial amyloid in neurodegeneration.Deamidation Slows Curli Amyloid-Protein Aggregation.Amyloid by Design: Intrinsic Regulation of Microbial Amyloid AssemblyFunctional Amyloids in Bacteria
P2860
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P2860
Gatekeeper residues in the major curlin subunit modulate bacterial amyloid fiber biogenesis
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@ast
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@en
type
label
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@ast
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@en
prefLabel
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@ast
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@en
P2860
P50
P356
P1476
Gatekeeper residues in the maj ...... erial amyloid fiber biogenesis
@en
P2093
Juan-Jie Ren
Yizhou Zhou
P2860
P304
P356
10.1073/PNAS.0908714107
P407
P577
2009-12-04T00:00:00Z