Structural insights into functional and pathological amyloid. - Wikidata - wikimedia - TriplyDB

Structural insights into functional and pathological amyloid.

Structural insights into functional and pathological amyloid.

http://www.wikidata.org/entity/Q34947293

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Expression of Fap amyloids in Pseudomonas aeruginosa, P. fluorescens, and P. putida results in aggregation and increased biofilm formation Microbial amyloids--functions and interactions within the host The [RNQ+] prion: a model of both functional and pathological amyloid Amyloid cannot resist identification Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS Functional capabilities of the earliest peptides and the emergence of life Structural basis for host membrane remodeling induced by protein 2B of hepatitis A virus Adhesion mechanisms of curli subunit CsgA to abiotic surfaces Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicity A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins.Strengthening relationships: amyloids create adhesion nanodomains in yeasts.Amyloid triangles, squares, and loops of apolipoprotein C-III.Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.Self-assembly of MinE on the membrane underlies formation of the MinE ring to sustain function of the Escherichia coli Min system.Immunoprecipitation of amyloid fibrils by the use of an antibody that recognizes a generic epitope common to amyloid fibrils.Molecular origin of pH-dependent fibril formation of a functional amyloid Simulation of the β- to α-sheet transition results in a twisted sheet for antiparallel and an α-nanotube for parallel strands: implications for amyloid formation.An amyloid organelle, solid-state NMR evidence for cross-β assembly of gas vesicles The AgrD N-terminal leader peptide of Staphylococcus aureus has cytolytic and amyloidogenic properties.Physical and structural basis for polymorphism in amyloid fibrils Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.Molecular dynamics study of Zn(aβ) and Zn(aβ)2 The bacterial curli system possesses a potent and selective inhibitor of amyloid formation.Functional amyloids keep quorum-sensing molecules in check Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.Amyloid properties of the mouse egg zona pellucida Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.A Monte Carlo Study of the Early Steps of Functional Amyloid Formation Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation.microRNA-34a-Mediated Down-Regulation of the Microglial-Enriched Triggering Receptor and Phagocytosis-Sensor TREM2 in Age-Related Macular Degeneration Role of prion protein aggregation in neurotoxicity.Unzipping a functional microbial amyloid.Sex, prions, and plasmids in yeast.Can infections cause Alzheimer's disease?The Human Disease-Associated Aβ Amyloid Core Sequence Forms Functional Amyloids in a Fungal Adhesin Computational modeling of the relationship between amyloid and disease.Amyloidogenic peptides of yeast cell wall glucantransferase Bgl2p as a model for the investigation of its pH-dependent fibril formation Non-targeted identification of prions and amyloid-forming proteins from yeast and mammalian cells.

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Structural insights into functional and pathological amyloid.

http://www.wikidata.org/entity/Q34947293

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Structural insights into functional and pathological amyloid.

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Structural insights into functional and pathological amyloid.

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Structural insights into functional and pathological amyloid.

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type

label

Structural insights into functional and pathological amyloid.

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Structural insights into functional and pathological amyloid.

@en

Structural insights into functional and pathological amyloid.

@nl

prefLabel

Structural insights into functional and pathological amyloid.

@ast

Structural insights into functional and pathological amyloid.

@en

Structural insights into functional and pathological amyloid.

@nl

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JBC.R111.227108

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Journal of Biological Chemistry

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Structural insights into functional and pathological amyloid.

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Frank Shewmaker

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Ryan P McGlinchey

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P2860

Amyloid aggregates of the HET-s prion protein are infectious.

Structure of the cross-beta spine of amyloid-like fibrils

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

A systematic survey identifies prions and illuminates sequence features of prionogenic proteins

Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure

Structural basis of chaperone function and pilus biogenesis

A domain-swapped RNase A dimer with implications for amyloid formation

Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping

Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily.

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

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16533-16540

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scholarly article

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10.1074/JBC.R111.227108

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19

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286

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2011-03-25T00:00:00Z

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