ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transpo
about
Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon proteaseCrystal structure of a heterodimeric ABC transporter in its inward-facing conformationThe hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function.Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS.Hydrogen-bond formation of the residue in H-loop of the nucleotide binding domain 2 with the ATP in this site and/or other residues of multidrug resistance protein MRP1 plays a crucial role during ATP-dependent solute transportInsight in eukaryotic ABC transporter function by mutation analysis.The ATPases of cohesin interface with regulators to modulate cohesin-mediated DNA tethering.Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.Structure and function of ABC transporters.The deviant ATP-binding site of the multidrug efflux pump Pdr5 plays an active role in the transport cycle.NMR and EPR studies of membrane transporters.Identification and characterization of functionally important elements in the multidrug resistance protein 1 COOH-terminal region.Multidrug resistance protein 4 (ABCC4)-mediated ATP hydrolysis: effect of transport substrates and characterization of the post-hydrolysis transition state.Mutation of the aromatic amino acid interacting with adenine moiety of ATP to a polar residue alters the properties of multidrug resistance protein 1.Nucleotides and transported substrates modulate different steps of the ATPase catalytic cycle of MRP1 multidrug transporter.Identification of proline residues in the core cytoplasmic and transmembrane regions of multidrug resistance protein 1 (MRP1/ABCC1) important for transport function, substrate specificity, and nucleotide interactions.Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.Replacement of the positively charged Walker A lysine residue with a hydrophobic leucine residue and conformational alterations caused by this mutation in MRP1 impair ATP binding and hydrolysisNonequivalence of the nucleotide binding domains of the ArsA ATPase.Boosted coupling of ATP hydrolysis to substrate transport upon cooperative estradiol-17-β-D-glucuronide binding in a Drosophila ATP binding cassette type-C transporter.Targeting Nucleotide Binding Domain of Multidrug Resistance-associated Protein-1 (MRP1) for the Reversal of Multi Drug Resistance in Cancer
P2860
Q24644909-E9DC4F36-E914-40AF-A133-53AF6F4292A8Q27678196-98262C8C-F680-43D3-ADDE-29DD526E7ECCQ34201794-F97DF6DF-ED3E-4EDC-A2EE-D12F166EEC05Q35259130-33A2E0B2-B7BC-44FF-8682-4EE4CAE50FB0Q35742010-45F2420E-5F80-41C8-A6B3-1554D58E5A1EQ36379776-10E97483-66A5-4D77-BA3B-4E0C4DE9B118Q36452407-181A27AE-37EC-4948-84B4-A2E248616DD9Q36525551-B9C653FF-7BD9-44BB-9AB3-C36D6E0F242BQ36786255-CFCFCE3E-3605-4ED0-8629-A163CD51ABDFQ37234052-0C912E9B-A64D-4161-BF3A-5D6CB09E3E30Q37488240-8EAD315F-0C51-46F0-A552-C35905313C88Q40508859-AC1B3E1C-A76C-4D1F-8286-78A766B129C0Q40516141-10C2C399-203E-4514-8C15-6D94F9805B7DQ40517912-302F222F-B297-4F02-AC03-29DDA164B20DQ40593645-83EF0F49-E9C6-4385-9876-9C4F447A731EQ40599587-CF1508B6-9E69-4991-9E9C-A23FE5238429Q42156999-851796E1-7558-4820-A8E5-79D26DDEE212Q42407863-00CA31BF-E99E-414F-B5E4-55040F8377E3Q45214719-4AFE2B89-E447-40DB-969C-41211D2EB3C7Q47758944-8EABD7DC-A2BC-4302-9956-9B1E73C8D4A7Q58790849-56390026-1DE7-4D89-A954-8FB9A511BFF6
P2860
ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transpo
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
ATP binding to the first nucle ...... pendent leukotriene C4 transpo
@en
type
label
ATP binding to the first nucle ...... pendent leukotriene C4 transpo
@en
prefLabel
ATP binding to the first nucle ...... pendent leukotriene C4 transpo
@en
P2093
P2860
P356
P1476
ATP binding to the first nucle ...... pendent leukotriene C4 transpo
@en
P2093
John R Riordan
Liying Cui
Runying Yang
Xiu-bao Chang
Yue-xian Hou
P2860
P304
30764-30771
P356
10.1074/JBC.M304118200
P407
P577
2003-06-03T00:00:00Z