K. Almquist

Publications29
h-index20
Citations5,772
Highly Influential Citations267
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Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line.
TLDR
Reversion to drug sensitivity was associated with loss of gene amplification and a marked decrease in mRNA expression, and the mRNA encodes a member of the ATP-binding cassette transmembrane transporter superfamily.
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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.
TLDR
Evidence is provided of the ability of MRP to transport cysteinyl leukotriene C4 in membrane vesicles from MRP-transfected HeLa cells (T14), as well as drug-selected H69AR lung cancer cells which express high levels of MRp.
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Overexpression of multidrug resistance-associated protein (MRP) increases resistance to natural product drugs.
TLDR
It is demonstrated that MRP overexpression confers a multidrug resistance phenotype similar to that formerly associated exclusively with elevated levels of P-glycoprotein.
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ATP-dependent 17-Estradiol 17-(-D-Glucuronide) Transport by Multidrug Resistance Protein (MRP)
TLDR
MRP is identified as a potential transporter of cholestatic conjugated estrogens and site-specific requirements for glucuronidation of the steroid nucleus are demonstrated.
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Comparison of the Functional Characteristics of the Nucleotide Binding Domains of Multidrug Resistance Protein 1*
TLDR
This work has used a baculovirus dual expression vector encoding both halves of MRP1 to reconstitute an active transporter and compared the ability of each NBD to be photoaffinity-labeled with 8-azido-[32P]ATP and to trap 8-razido-ADP in the presence of orthovanadate.
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Multidrug Resistance Protein (MRP)-mediated Transport of Leukotriene C and Chemotherapeutic Agents in Membrane Vesicles
TLDR
The identification of an MRP-specific mAb that inhibits LTC transport and prevents photolabeling of MRP by LTC, provides conclusive evidence of the ability of MRp to transport cysteinyl leukotrienes and it is demonstrated that MRP is capable of mediating ATP-dependent transport of vincristine and that transport is GSH-dependent.
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Membrane Topology of the Multidrug Resistance Protein (MRP)
TLDR
N-Glycosylation of Asn19 and Asn23 provides the first direct experimental evidence that MRP has an extracytosolic NH2 terminus, and strongly suggests that the NH2-terminal MSD of MRP contains an odd number of transmembrane helices.
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Characterization of the Mr 190,000 Multidrug Resistance Protein (MRP) in Drug-selected and Transfected Human Tumor Cells
TLDR
Comparisons of MRP post-translational modification, stability, processing, and subcellular distribution in the HeLa transfectants and in the drug-selected H69AR cells establish that MRP in both the transfected and selected cells is an ATP-binding, integral membrane glycophosphoprotein with an apparent molecular weight of 190,000.
Location of a protease-hypersensitive region in the multidrug resistance protein (MRP) by mapping of the epitope of MRP-specific monoclonal antibody QCRL-1.
TLDR
The epitope of MAb QCRL-1, a panel of MRP-specific monoclonal antibodies which detect distinct epitopes in the MRP molecule, is identified and confirmed that this epitope has a cytoplasmic location consistent with the topology of MRp predicted from hydrophobicity analyses.
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ATP-dependent 17 beta-estradiol 17-(beta-D-glucuronide) transport by multidrug resistance protein (MRP). Inhibition by cholestatic steroids.
TLDR
Data identify MRP as a potential transporter of cholestatic conjugated estrogens and demonstrate site-specific requirements for glucuronidation of the steroid nucleus.
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