Mutation of proline residues in the NH(2)-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function (Q44568811)

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scientific article published in September 2003

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English	Mutation of proline residues in the NH(2)-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function	scientific article published in September 2003

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scholarly article

1 reference

Europe PubMed Central

4 December 2017

Mutation of proline residues in the NH(2)-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function (English)

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Europe PubMed Central

4 December 2017

multiple drug resistance

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based on heuristic

inferred from title

Susan P.C. Cole

4

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Europe PubMed Central

4 December 2017

author name string

Ken-ichi Ito

1

1 reference

Europe PubMed Central

4 December 2017

Kevin E Weigl

2

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Europe PubMed Central

4 December 2017

Roger G Deeley

3

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Europe PubMed Central

4 December 2017

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publication date

1 September 2003

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Europe PubMed Central

4 December 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

4 December 2017

1615

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Europe PubMed Central

4 December 2017

1-2

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Europe PubMed Central

4 December 2017

103-114

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Europe PubMed Central

4 December 2017

An inventory of the human ABC proteins

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Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line

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Structural, mechanistic and clinical aspects of MRP1.

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Toxicological relevance of the multidrug resistance protein 1, MRP1 (ABCC1) and related transporters.

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Biochemical, cellular, and pharmacological aspects of the multidrug transporter

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Mammalian ABC transporters in health and disease

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Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus.

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Membrane topology of the amino-terminal region of the sulfonylurea receptor

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Multidrug resistance protein. Identification of regions required for active transport of leukotriene C4.

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Functional multidrug resistance protein (MRP1) lacking the N-terminal transmembrane domain

1 reference

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Hypothesis about the function of membrane-buried proline residues in transport proteins

1 reference

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Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function

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Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport

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Multiple membrane-associated tryptophan residues contribute to the transport activity and substrate specificity of the human multidrug resistance protein, MRP1.

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Monoclonal antibodies that inhibit the transport function of the 190-kDa multidrug resistance protein, MRP. Localization of their epitopes to the nucleotide-binding domains of the protein.

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Epitope mapping of monoclonal antibodies specific for the 190-kDa multidrug resistance protein (MRP).

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Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport

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Breaking the camel's back: proline-induced turns in a model transmembrane helix

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Dopamine transporter proline mutations influence dopamine uptake, cocaine analog recognition, and expression.

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Proline residues in transmembrane helices of channel and transport proteins: a molecular modelling study

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Proline-induced distortions of transmembrane helices.

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Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1).

1 reference

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7 January 2021

Structural and functional consequences of mutating cysteine residues in the amino terminus of human multidrug resistance-associated protein 1.

1 reference

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7 January 2021

Characterization of binding of leukotriene C4 by human multidrug resistance protein 1: evidence of differential interactions with NH2- and COOH-proximal halves of the protein.

1 reference

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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

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7 January 2021

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10.1016/S0005-2736(03)00228-1

1 reference

Europe PubMed Central

4 December 2017

1 reference

Europe PubMed Central

4 December 2017

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