Remodeling of the fibrillation pathway of α-synuclein by interaction with antimicrobial peptide LL-III
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: R. Oliva, S. K. Mukherjee, L. Ostermeier, L. A. Pazurek, S. Kriegler, V. Bader, D. Prumbaum, S. Raunser, K. F. Winklhofer, J. Tatzelt, R. Winter, Chem. Eur. J. 2021, 27, 11845.
- Klassifikation
-
Chemie
- Ereignis
-
Veröffentlichung
- (wo)
-
Dortmund
- (wer)
-
Universitätsbibliothek Dortmund
- (wann)
-
2021
- Urheber
-
Oliva, Rosario
Mukherjee, Sanjib K.
Ostermeier, Lena
Pazurek, Lilli A.
Kriegler, Simon
Bader, Verian
Prumbaum, Daniel
Raunser, Stefan
Winklhofer, Konstanze
Tatzelt, Jörg
Winter, Roland
- Handle
-
2003/40820
- URN
-
urn:nbn:de:101:1-2022032502432316709690
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:35 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
- Oliva, Rosario
- Mukherjee, Sanjib K.
- Ostermeier, Lena
- Pazurek, Lilli A.
- Kriegler, Simon
- Bader, Verian
- Prumbaum, Daniel
- Raunser, Stefan
- Winklhofer, Konstanze
- Tatzelt, Jörg
- Winter, Roland
- Universitätsbibliothek Dortmund
Entstanden
- 2021
Ähnliche Objekte (12)
Remodeling of the Fibrillation Pathway of α‐Synuclein by Interaction with Antimicrobial Peptide LL‐III
Direct Visualization of Model Membrane Remodeling by α‐Synuclein Fibrillization
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Unravelling the inhibitory activity of Chlamydomonas reinhardtii sulfated polysaccharides against α-Synuclein fibrillation
Functionalization of α-synuclein fibrils
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro
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
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
Remodeling of the Fibrillation Pathway of α‐Synuclein by Interaction with Antimicrobial Peptide LL‐III
Direct Visualization of Model Membrane Remodeling by α‐Synuclein Fibrillization
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Unravelling the inhibitory activity of Chlamydomonas reinhardtii sulfated polysaccharides against α-Synuclein fibrillation
Functionalization of α-synuclein fibrils
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro
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
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
Remodeling of the Fibrillation Pathway of α‐Synuclein by Interaction with Antimicrobial Peptide LL‐III
Direct Visualization of Model Membrane Remodeling by α‐Synuclein Fibrillization
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Unravelling the inhibitory activity of Chlamydomonas reinhardtii sulfated polysaccharides against α-Synuclein fibrillation
Functionalization of α-synuclein fibrils
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Calbindin-D28K acts as a calcium-dependent chaperone suppressing α-synuclein fibrillation in vitro
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