Structures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties.
about
Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum.Trypanosoma cruzi Evades the Complement System as an Efficient Strategy to Survive in the Mammalian Host: The Specific Roles of Host/Parasite Molecules and Trypanosoma cruzi Calreticulin.Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function.
P2860
Structures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties.
description
2016 nî lūn-bûn
@nan
2016 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
name
Structures of parasite calreti ...... te/peptide-binding properties.
@ast
Structures of parasite calreti ...... te/peptide-binding properties.
@en
type
label
Structures of parasite calreti ...... te/peptide-binding properties.
@ast
Structures of parasite calreti ...... te/peptide-binding properties.
@en
prefLabel
Structures of parasite calreti ...... te/peptide-binding properties.
@ast
Structures of parasite calreti ...... te/peptide-binding properties.
@en
P2093
P2860
P1433
P1476
Structures of parasite calreti ...... ate/peptide-binding properties
@en
P2093
Anne Chouquet
Arturo Ferreira
Christine Gaboriaud
Christophe Moreau
Emmanuelle Laffly
Gianluca Cioci
Marina Iannello
P2860
P304
P356
10.1107/S2052252516012847
P577
2016-09-14T00:00:00Z