Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. - Wikidata - awgldk - TriplyDB

Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.

Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.

http://www.wikidata.org/entity/Q42062269

about

Mechanisms of amyloid formation revealed by solution NMR Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation Energy landscapes of functional proteins are inherently risky.pH-induced molecular shedding drives the formation of amyloid fibril-derived oligomers Bacterial Chaperones CsgE and CsgC Differentially Modulate Human α-Synuclein Amyloid Formation via Transient Contacts Decoding the Structural Bases of D76N ß2-Microglobulin High Amyloidogenicity through Crystallography and Asn-Scan Mutagenesis.Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.Distinguishing closely related amyloid precursors using an RNA aptamer.The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.(S)Pinning down protein interactions by NMR.An Internal Disulfide Locks a Misfolded Aggregation-prone Intermediate in Cataract-linked Mutants of Human γD-Crystallin.A covalent homodimer probing early oligomers along amyloid aggregation.An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation.Selection of DNA Aptamer That Blocks the Fibrillogenesis of a Proteolytic Amyloidogenic Fragment of β2 m.Layers of structure and function in protein aggregation.Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity.Dynamic disulfide exchange in a crystallin protein in the human eye lens promotes cataract-associated aggregation

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P2860

Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly.

http://www.wikidata.org/entity/Q42062269

description

2014 nî lūn-bûn

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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2014年论文

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2014年论文

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name

Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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Visualization of transient pro ...... e or inhibit amyloid assembly.

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P2860

Electrostatics of nanosystems: application to microtubules and the ribosome

The mechanism of prion inhibition by HET-S

Assessing the causes and consequences of co-polymerization in amyloid formation

A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme

A peptide that antagonizes TCR-mediated reactions with both syngeneic and allogeneic agonists: functional and structural aspects

Stabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formation

Conformational Conversion during Amyloid Formation at Atomic Resolution

Atomic structure and hierarchical assembly of a cross- amyloid fibril

Structure of an intermediate state in protein folding and aggregation

Adapting proteostasis for disease intervention

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