Control of the Selectivity of the Aquaporin Water Channel Family by Global Orientational Tuning

By Emad Tajkhorshid, P. Nollert, Morten Ø. Jensen, L. Miercke, J. O’Connell, R. Stroud, Klaus Schulten. Science, 2002

824 citations recorded by the source corpus.

Subfields: Biomedical Engineering, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/9deee981d20b4abd51ad5ed94f01b675dfa806b0

How researchers see this paper

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

In Biomedical Engineering

In Molecular Biology

Citations in the corpus

More than just water channels: unexpected cellular roles of aquaporins (2005, background): “3 nm pore, in which steric and electrostatic factors prevent transport of protons and other small molecules (Tajkhorshid et al., 2002).”
Aquaporin Water Channels (2004, methodology): “These observations permitted molecular dynamics simulations by Bert de Groot and Helmut Grubmüller at the University of Göttingen (2001) and the group of Klaus Schulten at University of Illinois at Urbana-Champaign (Tajkhorshid et al., 2002).”
Scalable molecular dynamics with NAMD (2005, background): “…and function of these channels is a good example of systems that require inclusion of more than 100,000 atoms in the molecular system [112,113,114,115], as one needs to explicitly include a lipid bilayer and water in order to provide a natural environment to the protein and to be able to…”
From structure to disease: the evolving tale of aquaporin biology (2004, background): “Structural studies also revealed that the restriction of AQP1 permeability to water — excluding even hydronium (H 3 O + ) ions — arises from two principal mechanism”
Biological and synthetic membranes: What can be learned from a coarse-grained description? (2006, background): “l to the bilayer normal, which implies that f(x) should be a monotonically decreasing function of its argument. Elliott et al. [ 274] utilize the generic form f(cosΘ) = 2m +1 2 (cos2Θ)m ≈ mexp(−mΘ2), (48) where Θ is the angle between the local chain orientation u and the bilayer normal c. The parame”
Accurate de novo structure prediction of large transmembrane protein domains using fragment-assembly and correlated mutation analysis (2012, background): “Additionally, the two reentrant helices containing the NPA motif, whose asparagine residue plays a vital role in water selectivity (40), are also accurately positioned adjacent to the central channel (2d57A, Fig.”
A glimpse of structural biology through X-ray crystallography. (2014, background): “12 ns MD simulations of the aquaglyceroporin GlpF identified the spatial and temporal probability distribution of a single file of seven to nine water molecules and defined their orientation inside the channel, which mechanistically explained the impermeability of aquaporin to protons (Tajkhorshid e”