Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity

ET Petri, A Ćelić, SD Kennedy… - Proceedings of the …, 2010 - National Acad Sciences
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca2+-permeable channel, is
frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have …

[HTML][HTML] Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity

ET Petri, A Ćelić, SD Kennedy, BE Ehrlich… - Proceedings of the …, 2010 - ncbi.nlm.nih.gov
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca 2+-permeable channel, is
frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have …

Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity

ET Petri, A Ćelić, SD Kennedy… - Proceedings of the …, 2010 - ui.adsabs.harvard.edu
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca 2+-permeable channel, is
frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have …

Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca²⁺-dependent regulation of polycystin-2 channel activity

ET Petri, A Ćelić, SD Kennedy, BE Ehrlich… - Proceedings of the …, 2010 - JSTOR
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca²⁺-permeable channel, is
frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have …

Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity

ET Petri, A Celic, SD Kennedy… - Proceedings of the …, 2010 - pubmed.ncbi.nlm.nih.gov
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca (2+)-permeable channel,
is frequently mutated or truncated in autosomal dominant polycystic kidney disease. We …

[PDF][PDF] Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca 2-dependent regulation of polycystin-2 channel activity

ET Petria, A Ćelića, SD Kennedyb, BE Ehrlicha… - researchgate.net
Results NMR Structure of the C-Terminal EF-Hand Domain of PC2 in the Presence of Ca2+.
Chemical shifts (1H, 13C, and 15N) for Ca2+-bound PC2-EF (N720-P797) were assigned …

Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca 2+ -dependent regulation of polycystin-2 channel activity

ET Petri, A Ćelić, SD Kennedy, BE Ehrlich… - Proceedings of the …, 2010 - cir.nii.ac.jp
抄録< jats: p> The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca< jats: sup>
2+</jats: sup>-permeable channel, is frequently mutated or truncated in autosomal dominant …

Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity.

ET Petri, A Celic, SD Kennedy, BE Ehrlich… - Proceedings of the …, 2010 - europepmc.org
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca 2+-permeable channel, is
frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have …

Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity.

ET Petri, A Celic, SD Kennedy, BE Ehrlich… - Proceedings of the …, 2010 - europepmc.org
The C-terminal cytoplasmic tail of polycystin-2 (PC2/TRPP2), a Ca 2+-permeable channel, is
frequently mutated or truncated in autosomal dominant polycystic kidney disease. We have …

[引用][C] Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca²⁺-dependent regulation of polycystin-2 channel activity

ET Petri, A Ćelić, SD Kennedy, BE Ehrlich, TJ Boggon… - 2010