K
Kurt C. Almquist
Researcher at Queen's University
Publications - 10
Citations - 5288
Kurt C. Almquist is an academic researcher from Queen's University. The author has contributed to research in topics: Multidrug Resistance Protein 1 & ATP-binding cassette transporter. The author has an hindex of 10, co-authored 10 publications receiving 5210 citations.
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Journal ArticleDOI
Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line
Susan P.C. Cole,Gabu Bhardwaj,James H. Gerlach,J. E. Mackie,Caroline E. Grant,Kurt C. Almquist,Alistair J. Stewart,Ebba U. Kurz,A. M. V. Duncan,Roger G. Deeley +9 more
TL;DR: 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.
Journal Article
Overexpression of multidrug resistance-associated protein (MRP) increases resistance to natural product drugs.
Caroline E. Grant,Gunnar Valdimarsson,David R. Hipfner,Kurt C. Almquist,Susan P.C. Cole,Roger G. Deeley +5 more
TL;DR: It is demonstrated that MRP overexpression confers a multidrug resistance phenotype similar to that formerly associated exclusively with elevated levels of P-glycoprotein.
Journal ArticleDOI
Multidrug resistance protein (MRP)-mediated transport of leukotriene C4 and chemotherapeutic agents in membrane vesicles. Demonstration of glutathione-dependent vincristine transport
TL;DR: 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.
Journal ArticleDOI
ATP-dependent 17β-Estradiol 17-(β-D-Glucuronide) Transport by Multidrug Resistance Protein (MRP): INHIBITION BY CHOLESTATIC STEROIDS
TL;DR: MRP is identified as a potential transporter of cholestatic conjugated estrogens and site-specific requirements for glucuronidation of the steroid nucleus are demonstrated.
Journal ArticleDOI
Membrane Topology of the Multidrug Resistance Protein (MRP) A STUDY OF GLYCOSYLATION-SITE MUTANTS REVEALS AN EXTRACYTOSOLIC NH2 TERMINUS
David R. Hipfner,Kurt C. Almquist,Elaine M. Leslie,James H. Gerlach,Caroline E. Grant,Roger G. Deeley,Susan P.C. Cole +6 more
TL;DR: In this article, the authors identify which of the 14 N-glycosylation sequons in multidrug resistance protein (MRP) are utilized to aid in determining the topology most likely to be correct, which may have important implications for the further understanding of the interaction of drugs with MRP.