Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques (Q33784435)

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English	Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques	scientific article

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scholarly article

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Europe PubMed Central

29 July 2017

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Europe PubMed Central

Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine-scanning mutagenesis and thiol-modification techniques (English)

1 reference

Europe PubMed Central

29 July 2017

multiple drug resistance

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based on heuristic

inferred from title

author name string

T W Loo

1

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Europe PubMed Central

29 July 2017

D M Clarke

2

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Europe PubMed Central

29 July 2017

language of work or name

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publication date

1 December 1999

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Europe PubMed Central

29 July 2017

number of pages

11

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Biochimica et Biophysica Acta

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Europe PubMed Central

29 July 2017

1461

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Europe PubMed Central

29 July 2017

2

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Europe PubMed Central

29 July 2017

315-325

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Europe PubMed Central

29 July 2017

A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants

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Diagnosis and reversal of multidrug resistance in paediatric cancers

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P-glycoprotein and multidrug resistance

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The P-glycoprotein efflux pump: how does it transport drugs?

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The tissue dependent expression of hamster P-glycoprotein genes.

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The three mouse multidrug resistance (mdr) genes are expressed in a tissue-specific manner in normal mouse tissues

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The physiological function of drug-transporting P-glycoproteins

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Cellular localization of the multidrug-resistance gene product P-glycoprotein in normal human tissues

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Multidrug-resistance gene (P-glycoprotein) is expressed by endothelial cells at blood-brain barrier sites

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Disruption of the mouse mdr1a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs

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P-glycoprotein in the blood-brain barrier of mice influences the brain penetration and pharmacological activity of many drugs

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The drug transporter P-glycoprotein limits oral absorption and brain entry of HIV-1 protease inhibitors

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HIV-1 protease inhibitors are substrates for the MDR1 multidrug transporter.

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The ABC of channel regulation

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Homology between P-glycoprotein and a bacterial haemolysin transport protein suggests a model for multidrug resistance

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Mammalian multidrug resistance gene: complete cDNA sequence indicates strong homology to bacterial transport proteins

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Isolation and expression of a complementary DNA that confers multidrug resistance

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Internal duplication and homology with bacterial transport proteins in the mdr1 (P-glycoprotein) gene from multidrug-resistant human cells.

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Membrane topology of a cysteine-less mutant of human P-glycoprotein

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Monoclonal antibodies to the Ca2+ + Mg2+-dependent ATPase of sarcoplasmic reticulum identify polymorphic forms of the enzyme and indicate the presence in the enzyme of a classical high-affinity Ca2+ binding site

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Rapid purification of human P-glycoprotein mutants expressed transiently in HEK 293 cells by nickel-chelate chromatography and characterization of their drug-stimulated ATPase activities.

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Human P-glycoprotein exhibits reduced affinity for substrates during a catalytic transition state

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Site-directed mutagenesis of the yeast PMA1 H(+)-ATPase. Structural and functional role of cysteine residues

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P-glycoprotein. Associations between domains and between domains and molecular chaperones

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Correction of Defective Protein Kinesis of Human P-glycoprotein Mutants by Substrates and Modulators

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Superfolding of the partially unfolded core-glycosylated intermediate of human P-glycoprotein into the mature enzyme is promoted by substrate-induced transmembrane domain interactions.

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Both P-glycoprotein Nucleotide-binding Sites Are Catalytically Active

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Covalent modification of human P-glycoprotein mutants containing a single cysteine in either nucleotide-binding fold abolishes drug-stimulated ATPase activity

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The catalytic cycle of P-glycoprotein

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Membrane topology of P-glycoprotein as determined by epitope insertion: transmembrane organization of the N-terminal domain of mdr3

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Transmembrane organization of mouse P-glycoprotein determined by epitope insertion and immunofluorescence

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Multidrug resistance protein (Mdr)-alkaline phosphatase hybrids in Escherichia coli suggest a major revision in the topology of the C-terminal half of Mdr.

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Topological folding and proteolysis profile of P-glycoprotein in membranes of multidrug-resistant cells: implications for the drug-transport mechanism.

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The glycosylation and orientation in the membrane of the third cytoplasmic loop of human P-glycoprotein is affected by mutations and substrates.

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Transmembrane topography of subunit a in the Escherichia coli F1F0 ATP synthase.

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Membrane topology of subunit a of the F1F0 ATP synthase as determined by labeling of unique cysteine residues.

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Functional evidence that transmembrane 12 and the loop between transmembrane 11 and 12 form part of the drug-binding domain in P-glycoprotein encoded by MDR1.

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A single amino acid substitution strongly modulates the activity and substrate specificity of the mouse mdr1 and mdr3 drug efflux pumps

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Functional analysis of P-glycoprotein mutants identifies predicted transmembrane domain 11 as a putative drug binding site.

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Mutations to amino acids located in predicted transmembrane segment 6 (TM6) modulate the activity and substrate specificity of human P-glycoprotein

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Contribution to substrate specificity and transport of nonconserved residues in transmembrane domain 12 of human P-glycoprotein

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Characterization of the human multidrug resistance protein containing mutations in the ATP-binding cassette signature region

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An altered pattern of cross-resistance in multidrug-resistant human cells results from spontaneous mutations in the mdr1 (P-glycoprotein) gene

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P-glycoprotein gene (MDR1) cDNA from human adrenal: normal P-glycoprotein carries Gly185 with an altered pattern of multidrug resistance.

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Inhibition of Oxidative Cross-linking between Engineered Cysteine Residues at Positions 332 in Predicted Transmembrane Segments (TM) 6 and 975 in Predicted TM12 of Human P-glycoprotein by Drug Substrates

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10.1016/S0005-2736(99)00165-0

1 reference

Europe PubMed Central

29 July 2017

1 reference

Europe PubMed Central

29 July 2017

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