English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/173683
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


How novel structures inform understanding of complement function

AuthorsGoicoechea de Jorge, Elena ; Yébenes, Hugo; Serna, Marina; Tortajada, Agustín ; Llorca, Óscar ; Rodríguez de Córdoba, Santiago
Structural biology
C3\C5 convertase
Complement regulators
Factor H
Membrane attack complex
Issue DateJan-2018
CitationSeminars in Immunopathology 40(1) 3-14 (2018)
AbstractDuring the last decade, the complement field has experienced outstanding advancements in the mechanistic understanding of how complement activators are recognized, what C3 activation means, how protein complexes like the C3 convertases and the membrane attack complex are assembled, and how positive and negative complement regulators perform their function. All of this has been made possible mostly because of the contributions of structural biology to the study of the complement components. The wealth of novel structural data has frequently provided support to previously held knowledge, but often has added alternative and unexpected insights into complement function. Here we will review some of these findings focusing in the alternative and terminal complement pathways.
Description33 p.-3 fig.
Publisher version (URL)https://doi.org/10.1007/s00281-017-0643-z
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
How novel structures inform understanding 2017.pdfPostprint463,99 kBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.