Water transporters: How so fast yet so selective?

Current Biology

Volumn 12, Issue 7, 2002, Pages

  Law, Richard J ^a   Sansom, Mark S P ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; AQUAPORIN 1; ESCHERICHIA COLI PROTEIN; GLPF PROTEIN, E COLI; WATER;

CHEMICAL STRUCTURE; CHEMISTRY; PROTEIN TERTIARY STRUCTURE; REVIEW;

AQUAPORIN 1; AQUAPORINS; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; WATER;

EID: 0037007052     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(02)00784-4     Document Type: Review

References (16)

1. A phylogenetic framework for the aquaporin family in eukaryotes
2. Reconstitution and functional comparison of purified GIpF and AqpZ, the glycerol and water channels from Escherichia coli
3. Structure of a glycerol-conducting channel and the basis of its selectivity
4. Structural determinants of water permeation through aquaporin-1
5. Three-dimensional fold of the human AQP1 water channel determined at 4 angstrom resolution by electron crystallography of two-dimensional crystals embedded in ice
6. Aquaporins - Channels without ions
7. Structural basis of water-specific transport through the AQP1 water channel
8. Water permeation across biological membranes: Mechanism and dynamics of aquaporin-1 and GIpF
9. The mechanism of glycerol conduction in aquaglyceroporins
10. Molecular dynamics study of aquaporin-1 water channel in a lipid bilayer
11. Dynamic mechanisms of the membrane water channel aquaporin-1 (AQP1)
12. Ion channels: Frozen motion
13. Water conduction through the hydrophobic channel of a carbon nanotube
14. Resonant activation over a fluctuating barrier
15. + channel: Electrostatic stabilization of monovalent cations
16. X-ray structure of a CIC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity