Crystal Structure of the Potassium Channel KirBac1.1 in the Closed State

By Anling Kuo, J. Gulbis, Jennifer F. Antcliff, Tahmina Rahman, E. Lowe, J. Zimmer, J. Cuthbertson, Frances M. Ashcroft, T. Ezaki, D. Doyle. Science, 2003

816 citations recorded by the source corpus.

Subfields: Cardiology and Cardiovascular Medicine, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/fd88bad8f1d90b52262791de403e16f22d1ae9ed

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cardiology and Cardiovascular Medicine

1. Adam P. Hill
2. Jamie I. Vandenberg
3. M. Perrin
4. Stefan A. Mann
5. M. Perry
6. Ying Ke

In Molecular Biology

1. B. Suh
2. Adam P. Hill
3. Jamie I. Vandenberg
4. M. Perrin
5. Bertil Hille
6. Stefan A. Mann
7. M. Perry
8. Ying Ke

Citations in the corpus

• hERG K(+) channels: structure, function, and clinical significance. (2012, background): “Subsequently, these models of the pore have been validated by crystal structures of multiple K channel proteins (111, 150, 244, 297, 337, 384, 386, 619, 682), as well as a bacterial voltage-gated Na channel (479).”
• PIP2 is a necessary cofactor for ion channel function: how and why? (2008, background): “1 that is inhibited by PIP2 and PIP3 (35), and structures of cytoplasmic domains of Kir3.”
• Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “1 (404) and a chimera between bacterial KirBac3.”