- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2045-2322
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Cryo-EM analysis of homodimeric full-length LRRK2 and LRRK1 protein complexes ; volume:7 ; number:1 ; day:17 ; month:8 ; year:2017 ; pages:1-12 ; date:12.2017
Scientific reports ; 7, Heft 1 (17.8.2017), 1-12, 12.2017
- Classification
-
Biowissenschaften, Biologie
- Creator
-
Sejwal, Kushal
Chami, Mohamed
Rémigy, Hervé
Vancraenenbroeck, Renée
Sibran, William
Sütterlin, Rosmarie
Baumgartner, Paul
McLeod, Robert
Chartier-Harlin, Marie-Christine
Baekelandt, Veerle
Stahlberg, Henning
Taymans, Jean-Marc
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41598-017-09126-z
- URN
-
urn:nbn:de:101:1-2019102014453788598444
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:32 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Sejwal, Kushal
- Chami, Mohamed
- Rémigy, Hervé
- Vancraenenbroeck, Renée
- Sibran, William
- Sütterlin, Rosmarie
- Baumgartner, Paul
- McLeod, Robert
- Chartier-Harlin, Marie-Christine
- Baekelandt, Veerle
- Stahlberg, Henning
- Taymans, Jean-Marc
- SpringerLink (Online service)
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Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
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Author Correction: Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Statistical Inference of cryo-EM Maps
Manifold methods for cryo-EM image denoising
Invariants for multireference alignment and cryo-EM
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Cryo-EM structure of the full-length hnRNPA1 amyloid fibril
Cryo-EM structures of the full-length human KCC2 and KCC3 cation-chloride cotransporters
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion
Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Estimating loop length from CryoEM images at medium resolutions
Author Correction: Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Statistical Inference of cryo-EM Maps
Manifold methods for cryo-EM image denoising
Invariants for multireference alignment and cryo-EM
CryoEM at IUCRJ: a new era
New Approaches to Cryo-EM Image Processing
Cryo-EM structure of the full-length hnRNPA1 amyloid fibril
Cryo-EM structures of the full-length human KCC2 and KCC3 cation-chloride cotransporters
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel
Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion
Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Estimating loop length from CryoEM images at medium resolutions
Author Correction: Pharmacology of LRRK2 with type I and II kinase inhibitors revealed by cryo-EM
Statistical Inference of cryo-EM Maps
Manifold methods for cryo-EM image denoising
Invariants for multireference alignment and cryo-EM
CryoEM at IUCRJ: a new era