Multiple Membrane-associated Tryptophan Residues Contribute to the Transport Activity and Substrate Specificity of the Human Multidrug Resistance Protein, MRP1
Open Access
- 1 December 2002
- journal article
- Published by Elsevier
- Vol. 277 (51), 49495-49503
- https://doi.org/10.1074/jbc.m206896200
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Charged Amino Acids in the Sixth Transmembrane Helix of Multidrug Resistance Protein 1 (MRP1/ABCC1) Are Critical Determinants of Transport ActivityPublished by Elsevier ,2002
- GSH-dependent Photolabeling of Multidrug Resistance Protein MRP1 (ABCC1) by [125I]LY475776Published by Elsevier ,2002
- Glutathione-dependent Binding of a Photoaffinity Analog of Agosterol A to the C-terminal Half of Human Multidrug Resistance ProteinJournal of Biological Chemistry, 2001
- The Structure of the Multidrug Resistance Protein 1 (MRP1/ABCC1)Published by Elsevier ,2001
- Structure–Activity Studies of Verapamil Analogs That Modulate Transport of Leukotriene C4 and Reduced Glutathione by Multidrug Resistance Protein MRP1Biochemical and Biophysical Research Communications, 2000
- Helical Membrane Protein Folding, Stability, and EvolutionAnnual Review of Biochemistry, 2000
- Domain–domain interface packing at conserved Trp-20 in class α glutathione transferase impacts on protein stabilityBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
- Channel-Lining Residues in the M3 Membrane-Spanning Segment of the Cystic Fibrosis Transmembrane Conductance RegulatorBiochemistry, 1998
- Helix packing in membrane proteinsJournal of Molecular Biology, 1997
- A Model Recognition Approach to the Prediction of All-Helical Membrane Protein Structure and TopologyBiochemistry, 1994