Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level - Wikidata - awgldk - TriplyDB

Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level

Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level

http://www.wikidata.org/entity/Q35597175

about

Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains Molecular origin of pH-dependent fibril formation of a functional amyloid Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, pmel17.Classifying prion and prion-like phenomena.Why are Functional Amyloids Non-Toxic in Humans?Reversing the amyloid trend: Mechanism of fibril assembly and dissolution of the repeat domain from a human functional amyloid.Identification of an amyloid fibril forming segment of human Pmel17 repeat domain (RPT domain).A β-solenoid model of the Pmel17 repeat domain: insights to the formation of functional amyloid fibrils.

P2860

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P2860

Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level

http://www.wikidata.org/entity/Q35597175

description

2011 nî lūn-bûn

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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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name

Probing fibril dissolution of ...... microscopic and residue level

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P2093

Attila Nagy

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James M Gruschus

http://www.w3.org/2001/XMLSchema#string

Ryan P McGlinchey

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P2860

Pmel17 initiates premelanosome morphogenesis within multivesicular bodies

Melanosomes--dark organelles enlighten endosomal membrane transport

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

Protein misfolding, functional amyloid, and human disease

Stepwise dynamics of epitaxially growing single amyloid fibrils.

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

Electron tomography of early melanosomes: implications for melanogenesis and the generation of fibrillar amyloid sheets.

Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.

Mysterious oligomerization of the amyloidogenic proteins

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10567-10569

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scholarly article

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10.1021/BI201578H

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49

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50

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2011-11-17T00:00:00Z

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51806030

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22092386

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3232329

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