Conformational ensemble of human α-synuclein physiological form predicted by molecular simulations
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: Physical chemistry, chemical physics 18(8), Seiten/Artikel-Nr.:5702-5706; 10.1039/C5CP04549E
- Klassifikation
-
Biowissenschaften, Biologie
- Ereignis
-
Veröffentlichung
- (wo)
-
Aachen
- (wer)
-
Universitätsbibliothek der RWTH Aachen
- (wann)
-
2016
- Urheber
-
Rossetti, Giulia
Musiani, F.
Abad, E.
Dibenedetto, Domenica
Mouhib, Halima
Fernandez, C. O.
Carloni, Paolo
- DOI
-
10.18154/RWTH-2016-01620
- URN
-
urn:nbn:de:101:1-201804202389
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:49 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Rossetti, Giulia
- Musiani, F.
- Abad, E.
- Dibenedetto, Domenica
- Mouhib, Halima
- Fernandez, C. O.
- Carloni, Paolo
- Universitätsbibliothek der RWTH Aachen
Entstanden
- 2016
Ähnliche Objekte (12)
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](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
Predicting conformational ensembles of the intrinsically disordered protein α-synuclein [alpha-synuclein] via molecular simulation
Immunoregulation of microglial polarization: an unrecognized physiological function of α-synuclein
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
α-Synuclein and neuronal cell death
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
Immunoregulation of microglial polarization: an unrecognized physiological function of α-synuclein
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
α-Synuclein and neuronal cell death
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
Immunoregulation of microglial polarization: an unrecognized physiological function of α-synuclein
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