Molecular mechanisms for protein-encoded inheritance - Test2 - elhamkhani - TriplyDB

Molecular mechanisms for protein-encoded inheritance

Molecular mechanisms for protein-encoded inheritance

http://www.wikidata.org/entity/Q27657037

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Prion strains and amyloid polymorphism influence phenotypic variation Ubiquitous amyloids Synthetic prions with novel strain-specified properties Mapping the conformational dynamics and pathways of spontaneous steric zipper Peptide oligomerization Minimalist design of water-soluble cross-beta architecture.Crystallographic Studies of Prion Protein (PrP) Segments Suggest How Structural Changes Encoded by Polymorphism at Residue 129 Modulate Susceptibility to Human Prion Disease β2-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages Atomic Structures Suggest Determinants of Transmission Barriers in Mammalian Prion Disease Structures of segments of α-synuclein fused to maltose-binding protein suggest intermediate states during amyloid formation Characteristics of Amyloid-Related Oligomers Revealed by Crystal Structures of Macrocyclic β-Sheet Mimics Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation Towards a Pharmacophore for Amyloid Molecular basis for amyloid- polymorphism Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation Structure and dynamics of amyloid-β segmental polymorphisms Common features at the start of the neurodegeneration cascade Defining the conformational features of anchorless, poorly neuroinvasive prions The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins Inter-species cross-seeding: stability and assembly of rat-human amylin aggregates Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril Recent progress in understanding Alzheimer's β-amyloid structures.Glutamine and Asparagine Side Chain Hyperconjugation-Induced Structurally Sensitive Vibrations.Protein structure along the order-disorder continuum Considering protonation as a posttranslational modification regulating protein structure and function.Polymorphism of β2-microglobulin amyloid fibrils manifested by ultrasonication-enhanced fibril formation in trifluoroethanol Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion Selenomethionine incorporation into amyloid sequences regulates fibrillogenesis and toxicity Two amyloid States of the prion protein display significantly different folding patterns Human prion protein sequence elements impede cross-species chronic wasting disease transmission.The Surprising Role of Amyloid Fibrils in HIV Infection Distinct prion strains are defined by amyloid core structure and chaperone binding site dynamics.Identifying the amylome, proteins capable of forming amyloid-like fibrils Principles governing oligomer formation in amyloidogenic peptides.Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation.Amyloid structure: conformational diversity and consequences.Interactions between amyloid-β and Tau fragments promote aberrant aggregates: implications for amyloid toxicity The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesis

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P2860

Molecular mechanisms for protein-encoded inheritance

http://www.wikidata.org/entity/Q27657037

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին 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

Molecular mechanisms for protein-encoded inheritance

@ast

Molecular mechanisms for protein-encoded inheritance

@en

Molecular mechanisms for protein-encoded inheritance

@nl

type

label

Molecular mechanisms for protein-encoded inheritance

@ast

Molecular mechanisms for protein-encoded inheritance

@en

Molecular mechanisms for protein-encoded inheritance

@nl

prefLabel

Molecular mechanisms for protein-encoded inheritance

@ast

Molecular mechanisms for protein-encoded inheritance

@en

Molecular mechanisms for protein-encoded inheritance

@nl

P1433

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P1433

Nature Structural & Molecular Biology

P1476

Molecular mechanisms for protein-encoded inheritance

@en

P2093

Angela B Soriaga

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

Jed J W Wiltzius

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

Kanagalaghatta Rajashankar

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

Lukasz Goldschmidt

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

Marcin I Apostol

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

Rebecca Nelson

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

P2860

Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism

The 3D profile method for identifying fibril-forming segments of proteins

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

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

RosettaDesign server for protein design

Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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

Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)

Molecular structural basis for polymorphism in Alzheimer's -amyloid fibrils

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P304

973-8

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scholarly article

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10.1038/NSMB.1643

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9

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16

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David Eisenberg

Michael R Sawaya

P577

2009-09-01T00:00:00Z

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26745778

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1051653779

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P698

19684598

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structural biology

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3640378

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