Modulation of the conformational space of SARS-CoV-2 RNA quadruplex RG-1 by cellular components and the amyloidogenic peptides α-Synuclein and hIAPP

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Chemistry - a European journal ; 28(9)

Classification: Chemie

Event: Veröffentlichung

(where): Dortmund

(who): Universitätsbibliothek Dortmund

(when): 2021

Creator: Mukherjee, Sanjib K.
Knop, Jim-Marcel
Winter, Roland

Handle: 2003/40762

URN: urn:nbn:de:101:1-2022031102440985081744

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:34 AM CEST

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Associated

Mukherjee, Sanjib K.
Knop, Jim-Marcel
Winter, Roland
Universitätsbibliothek Dortmund

Time of origin

2021

Other Objects (12)

Modulation of the Conformational Space of SARS‐CoV‐2 RNA Quadruplex RG‐1 by Cellular Components and the Amyloidogenic Peptides α‐Synuclein and hIAPP

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Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

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Modulation of the Conformational Space of SARS‐CoV‐2 RNA Quadruplex RG‐1 by Cellular Components and the Amyloidogenic Peptides α‐Synuclein and hIAPP

Conformational templating of α-synuclein aggregates in neuronal-glial cultures

Hochschulschrift

Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Overexpression-Induced α-Synuclein Brain Spreading

Modulation of the Conformational Space of SARS‐CoV‐2 RNA Quadruplex RG‐1 by Cellular Components and the Amyloidogenic Peptides α‐Synuclein and hIAPP

Conformational templating of α-synuclein aggregates in neuronal-glial cultures

Hochschulschrift

Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Overexpression-Induced α-Synuclein Brain Spreading

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Modulation of the conformational space of SARS-CoV-2 RNA quadruplex RG-1 by cellular components and the amyloidogenic peptides α-Synuclein and hIAPP

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Other Objects (12)

Modulation of the Conformational Space of SARS‐CoV‐2 RNA Quadruplex RG‐1 by Cellular Components and the Amyloidogenic Peptides α‐Synuclein and hIAPP

Conformational templating of α-synuclein aggregates in neuronal-glial cultures

Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Overexpression-Induced α-Synuclein Brain Spreading

Modulation of the Conformational Space of SARS‐CoV‐2 RNA Quadruplex RG‐1 by Cellular Components and the Amyloidogenic Peptides α‐Synuclein and hIAPP

Conformational templating of α-synuclein aggregates in neuronal-glial cultures

Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Overexpression-Induced α-Synuclein Brain Spreading

Modulation of the Conformational Space of SARS‐CoV‐2 RNA Quadruplex RG‐1 by Cellular Components and the Amyloidogenic Peptides α‐Synuclein and hIAPP

Conformational templating of α-synuclein aggregates in neuronal-glial cultures

Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation

Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

Direct Observation “Elongated” Conformational States in α‐Synuclein upon Liquid‐Liquid Phase Separation

α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice

Functionalization of α-synuclein fibrils

Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity

Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein

Overexpression-Induced α-Synuclein Brain Spreading

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