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Gary D. Kruh

Researcher at Fox Chase Cancer Center

Publications -  81
Citations -  8855

Gary D. Kruh is an academic researcher from Fox Chase Cancer Center. The author has contributed to research in topics: ATP-binding cassette transporter & Efflux. The author has an hindex of 52, co-authored 81 publications receiving 8596 citations. Previous affiliations of Gary D. Kruh include University of Illinois at Chicago.

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The MRP family of drug efflux pumps.

TL;DR: The MRP family is comprised of nine related ABC transporters that are able to transport structurally diverse lipophilic anions and function as drug efflux pumps that describe the biochemical properties, drug resistance activities and potential in vivo functions of these unusual pumps.
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Predicting drug sensitivity and resistance: profiling ABC transporter genes in cancer cells

TL;DR: This work profiled mRNA expression of the 48 known human ABC transporters in 60 diverse cancer cell lines used by the National Cancer Institute and found and validated compounds whose activity is potentiated, rather than antagonized, by the MDR1 multidrug transporter.
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Transport of cyclic nucleotides and estradiol 17-beta-D-glucuronide by multidrug resistance protein 4. Resistance to 6-mercaptopurine and 6-thioguanine.

TL;DR: It is concluded that MRP4 may influence diverse cellular processes regulated by cAMP and cGMP and that its substrate range is distinct from that of any other characterized MRP family member.
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Analysis of methotrexate and folate transport by multidrug resistance protein 4 (ABCC4): MRP4 is a component of the methotrexate efflux system.

TL;DR: It is shown that MRP4 is active in the transport of MTX as well as the physiological folates folic acid (FA) and N(5)-formyltetrahydrofolic Acid (leucovorin) and that MRp4 represents a common efflux system for both MTX and certain nucleotide analogues.
Journal Article

Transport of methotrexate, methotrexate polyglutamates, and 17β-estradiol 17-(β-D-glucuronide) by ABCG2: Effects of acquired mutations at R482 on methotrexate transport

TL;DR: It is demonstrated that R482 mutations observed in drug-resistant cell lines have profound effects on the in vitro transport properties of the pump, indicating that ABCG2 is a component of the energy-dependent efflux system for certain folates and antifolates, but that its transport characteristics with respect to polyglutamates and reduced folates are not identical to those of multidrug resistance protein family members.