The ATP switch model for ABC transporters

By C. Higgins, K. Linton. Nature Structural &Molecular Biology, 2004

758 citations recorded by the source corpus.

Subfields: Molecular Biology, Nutrition and Dietetics, Oncology

View Paper: https://www.semanticscholar.org/paper/86b344d8d58ec69395de4ea2edb0de473109f6ae

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In Molecular Biology

1. Debashish Chowdhury
2. F. Sharom

In Nutrition and Dietetics

1. Debashish Chowdhury
2. F. Sharom

In Oncology

1. S. Cole
2. Debashish Chowdhury
3. R. Deeley
4. F. Sharom
5. Christopher J Westlake

Citations in the corpus

• Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. (2006, background): “However, recent studies, including those of ABCC proteins, have provided strong evidence that it is ATP binding rather than hydrolysis that converts the protein from a high- to low-affinity substrate binding state (173, 328, 329, 386, 424).”
• Human multidrug resistance ABCB and ABCG transporters: participation in a chemoimmunity defense system. (2006, background): “Higgins and Linton (120) also observed an increase in ATP binding affinity of MDR1/Pgp in the presence of vinblastine.”
• Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “Some of the fundamental questions specifically related to the mechanisms of ABC transporters are as follows: (i) why do these machines need two ATPbinding domains although it consumes only one molecule of ATP for transporting one ligand? (ii) Do the two NBDs act in alternating fashion, like a two-cy”
• ABC multidrug transporters: structure, function and role in chemoresistance. (2008, background): “There is an ongoing debate about whether the energy for drug transport is provided by ATP hydrolysis (for a review see [60]) or ATP binding (the ATP switch model [62]).”
• Implications of Abscisic Acid in the Drought Stress Tolerance of Plants (2020, background): “The ABC transporter contains two transmembrane domains to recognize the substrate for translocation, and two nucleotide-binding domains responsible for the hydrolysis of ATP [127].”