Voltage Sensor of Kv1.2: Structural Basis of Electromechanical Coupling

By S. Long, E. Campbell, R. MacKinnon. Science, 2005

999 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Cardiology and Cardiovascular Medicine, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/f4fcfd431477683764a0574efdde20352cdf9bf9

How researchers see this paper

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

In Atomic and Molecular Physics, and Optics

1. Andrei L. Lomize
2. Irina D. Pogozheva
3. Mikhail A. Lomize
4. Henry I. Mosberg

In Cardiology and Cardiovascular Medicine

1. Jie Zheng
2. Adam P. Hill
3. Jamie I. Vandenberg
4. M. Perrin
5. Geoffrey W. Abbott
6. Stefan A. Mann
7. M. Perry
8. Ying Ke

In Molecular Biology

1. Mikhail A. Lomize
2. Henry I. Mosberg
3. Andrei L. Lomize
4. Irina D. Pogozheva
5. Vincenzo Carnevale
6. Jie Zheng
7. Cristian Micheletti
8. Adam P. Hill

Citations in the corpus

• Patterns of coevolving amino acids unveil structural and dynamical domains (2017, background): “In fact, it agrees with the strong mechanical coupling between the pore region and S4 (75–77).”
• Biology of the KCNQ1 Potassium Channel (2014, background): “channel gating is electromechanically coupled to membrane potential (Figure 1(e)) [12].”
• Positioning of proteins in membranes: A computational approach (2006, background): “A small hydrophobic thickness (23 Å) of the KvAP tetramers (1orq) is probably related to the non-native arrangement of its three N-terminal helices in the crystal (Cuello et al. 2004; MacKinnon 2004; Long et al. 2005).”
• hERG K(+) channels: structure, function, and clinical significance. (2012, background): “The voltage-dependent rearrangements of the voltage-sensing domain are transmitted to the activation gate via a physical interaction of the S4S5 linkers with the cytoplasmic terminals of the S6 helices (385, 642).”
• Voltage-gated Potassium Channels as Therapeutic Drug Targets (2009, neutral): “The four S1–S4 segments, each containing four positively charged arginine residues in the S4 helix, act as voltage sensor domains and 'gate' the pore by 'pulling' on the S4–S5 linke”
• DDT, pyrethrins, pyrethroids and insect sodium channels (2007, background): “2 potassium channel crystal structure ( 37, 38 ).”
• Handbook of ion channels (2015, background): “The prevalent notion of electromechanical coupling is that the movement of the S4 helix exerts a force on the S4–S5 linker, which is propagated to the channel gates through the interface between the S4–S5 linker and the S6 helix (102).”