Oligomerization of the polycystin-2 C-terminal tail and effects on its Ca2+-binding properties
about
Structural studies of the C-terminal tail of polycystin-2 (PC2) reveal insights into the mechanisms used for the functional regulation of PC2.Extracellular Loops Are Essential for the Assembly and Function of Polycystin Receptor-Ion Channel Complexes.Identification of a Novel EF-Loop in the N-terminus of TRPM2 Channel Involved in Calcium Sensitivity.
P2860
Oligomerization of the polycystin-2 C-terminal tail and effects on its Ca2+-binding properties
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Oligomerization of the polycys ...... on its Ca2+-binding properties
@ast
Oligomerization of the polycys ...... on its Ca2+-binding properties
@en
Oligomerization of the polycys ...... on its Ca2+-binding properties
@nl
type
label
Oligomerization of the polycys ...... on its Ca2+-binding properties
@ast
Oligomerization of the polycys ...... on its Ca2+-binding properties
@en
Oligomerization of the polycys ...... on its Ca2+-binding properties
@nl
prefLabel
Oligomerization of the polycys ...... on its Ca2+-binding properties
@ast
Oligomerization of the polycys ...... on its Ca2+-binding properties
@en
Oligomerization of the polycys ...... on its Ca2+-binding properties
@nl
P2093
P2860
P356
P1476
Oligomerization of the polycys ...... on its Ca2+-binding properties
@en
P2093
Barbara E Ehrlich
Camille Keeler
Michael E Hodsdon
Yifei Yang
P2860
P304
10544-10554
P356
10.1074/JBC.M115.641803
P407
P577
2015-02-25T00:00:00Z