X-ray structure of a voltage-dependent K+ channel
By Youxing Jiang, Alice Lee, Jiayun Chen, V. Ruta, M. Cadene, Brian T. Chait, R. MacKinnon. Nature, 2003
1,772 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/cf9f8e226c414b1bada3fba81e8e7e8cc4441b5d
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cellular and Molecular Neuroscience
- William A. Catterall
- R. MacKinnon
- F. H. Yu
- T. Scheuer
- Vladimir Yarov-Yarovoy
- K. Konoki
- Sandrine Cestèle
- Alice Lee
In Molecular Biology
- William A. Catterall
- R. MacKinnon
- T. Scheuer
- F. H. Yu
- Anthony G. Lee
- Vladimir Yarov-Yarovoy
- K. Konoki
- Sandrine Cestèle
Citations in the corpus
- RCSB Protein Data Bank: Enabling biomedical research and drug discovery (2019, background): “Rod MacKinnon's pioneering work on the homotetrameric potassium channel KcsA from S. lividans 45 and A. pernix K v AP 46 revealed the mechanistic bases for ion selectivity and gating at the atomic level, but structural information for Na v and Ca v channels, which lack the structural fourfold…”
- Monoclonal versus polyclonal antibodies: distinguishing characteristics, applications, and information resources. (2005, background): “It is thought that the tight structure of the Fab provided a scaffold on which the presumably floppy ion channel could align and form a cocrystal (Jiang et al. 2003; Zhou et al. 2001).”
- Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “The slide helix at the cytoplasmic end of TM1 is a unique structural element of the Kir channel family compared with other K channels (143, 336, 338, 404, 466) (Fig.”
- 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).”
- The principle of gating charge movement in a voltage-dependent K+ channel (2003, background): “Conclusion Here and in an accompanying paper(4), we have shown that (1) the gating charges are carried on voltage-sensor paddles, which are helix–turn–helix structures attached to the channel through flexible S3 loops and S4–S5 linkers; (2) the paddles are located at the channel’s outer perimeter an”
- How lipids affect the activities of integral membrane proteins. (2004, background): “It is interesting that the equivalent residues in the voltage-gated potassium channel from the thermophilic bacterium Aeropyrum pernix [148] are Lys and Asp (Fig.”