Structure and mechanism of ABC transporter proteins.
By K. Hollenstein, R. Dawson, K. Locher. Current Opinion in Structural Biology, 2007
651 citations recorded by the source corpus.
Subfields: Infectious Diseases, Nutrition and Dietetics, Oncology
View Paper: https://www.semanticscholar.org/paper/b0ac5f4de6da2145e411fbecc1932868afafe6a9
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In Infectious Diseases
In Nutrition and Dietetics
In Oncology
Citations in the corpus
- An overview of the main pathways of metabolic resistance in insects (2016, background): “membrane proteins that belong to the ATP binding cassette (ABC) superfamily, which utilise the energy derived from ATP hydrolysis to translocate a variety of different metabolites and xenobiotics across cellular membranes (Hollenstein et al., 2007).”
- Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “In all ABC proteins studied so far, NBD1 and NBD2 sandwich Mg-ATP in the dimer (276).”
- Efflux-Mediated Drug Resistance in Bacteria: an Update (2009, background): “The inward-facing conformation is promoted by dissociation of the hydrolysis products adenosine diphosphate (ADP) and phosphate, and shows the substrate-binding site accessible from the cell interior.([98,100]) Similar outward/inwardfacing conformations are also shared by the RND transporter AcrB.”