Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
  Small molecules detected by second-harmonic generation modulate the conformation of monomeric α-synuclein and reduce its aggregation in cell.

Moree, B., Yin, G., Lazaro, D. F., Munari, F., Strohäker, T., Giller, K., et al. (2015). Small molecules detected by second-harmonic generation modulate the conformation of monomeric α-synuclein and reduce its aggregation in cell. Journal of Biological Chemistry, 290(46), 27582-27593. doi:10.1074%2Fjbc.M114.636027.

Item is

Dateien

einblenden: Dateien
ausblenden: Dateien
:
2240344.pdf (Verlagsversion), 3MB
Name:
2240344.pdf
Beschreibung:
-
OA-Status:
Sichtbarkeit:
Öffentlich
MIME-Typ / Prüfsumme:
application/pdf / [MD5]
Technische Metadaten:
Copyright Datum:
-
Copyright Info:
-

Externe Referenzen

einblenden:
ausblenden:
externe Referenz:
http://www.jbc.org/content/290/46/27582.full.pdf+html (Verlagsversion)
Beschreibung:
-
OA-Status:

Urheber

einblenden:
ausblenden:
 Urheber:
Moree, B., Autor
Yin, G., Autor
Lazaro, D. F., Autor
Munari, F.1, Autor           
Strohäker, T.1, Autor           
Giller, K.2, Autor           
Becker, S.2, Autor           
Outeiro, T. F., Autor
Zweckstetter, M.1, Autor           
Salafsky, J., Autor
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR-Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

Inhalt

einblenden:
ausblenden:
Schlagwörter: drug discovery, Parkinson disease, protein aggregation, protein conformation, protein drug interaction
 Zusammenfassung: Proteins are structurally dynamic molecules that perform specialized functions through unique conformational changes accessible in physiological environments. An ability to specifically and selectively control protein function via conformational modulation is an important goal for development of novel therapeutics and studies of protein mechanism in biological networks and disease. Here we applied a second-harmonic generation-based technique for studying protein conformation in solution and in real time to the intrinsically disordered, Parkinson disease related protein α-synuclein. From a fragment library, we identified small molecule modulators that bind to monomeric α-synuclein in vitro and significantly reduce α-synuclein aggregation in a neuronal cell culture model. Our results indicate that the conformation of α-synuclein is linked to the aggregation of protein in cells. They also provide support for a therapeutic strategy of targeting specific conformations of the protein to suppress or control its aggregation.

Details

einblenden:
ausblenden:
Sprache(n): eng - English
 Datum: 2015-09-222015-11-13
 Publikationsstatus: Online veröffentlicht
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1074%2Fjbc.M114.636027
 Art des Abschluß: -

Veranstaltung

einblenden:

Entscheidung

einblenden:

Projektinformation

einblenden:

Quelle 1

einblenden:
ausblenden:
Titel: Journal of Biological Chemistry
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 290 (46) Artikelnummer: - Start- / Endseite: 27582 - 27593 Identifikator: -