caa a22 4500 463208390 CHVBK 20180405153132.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9122-x doi (NATIONALLICENCE)springer-10.1007/s10863-007-9122-x ABCG transporters: structure, substrate specificities and physiological roles [Elektronische Daten] A Brief Overview [Saroj Velamakanni, Shen Wei, Tavan Janvilisri, Hendrik van Veen] The ATP-binding cassette (ABC) transporter superfamily is one of the largest protein families with representatives in all kingdoms of life. Members of this superfamily are involved in a wide variety of transport processes with substrates ranging from small ions to relatively large polypeptides and polysaccharides. The G subfamily of ABC transporters consists of half-transporters, which oligomerise to form the functional transporter. While ABCG1, ABCG4 and ABCG5/8 are involved in the ATP-dependent translocation of steroids and, possibly, other lipids, ABCG2 (also termed the breast cancer resistance protein) has been identified as a multidrug transporter that confers resistance on tumor cells. Evidence will be summarized suggesting that ABCG2 can also mediate the binding/transport of non-drug substrates, including free and conjugated steroids. The characterization of the substrate specificities of ABCG proteins at a molecular level might provide further clues about their potential physiological role(s), and create new opportunities for the modulation of their activities in relation to human disease. Springer Science+Business Media, LLC, 2007 ABC transporter nationallicence ABCG family nationallicence Breast cancer resistance protein (BCRP) nationallicence Steroid transport nationallicence Multidrug resistance nationallicence Velamakanni Saroj Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut Wei Shen Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut Janvilisri Tavan Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut van Veen Hendrik Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 465-471 0145-479X 39:5-6<465 2007 39 10863 https://doi.org/10.1007/s10863-007-9122-x text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9122-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Velamakanni Saroj Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut NATIONALLICENCE 700 1- Wei Shen Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut NATIONALLICENCE 700 1- Janvilisri Tavan Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut NATIONALLICENCE 700 1- van Veen Hendrik Department of Pharmacology, University of Cambridge, Tennis Court Road, CB2 1PD, Cambridge, UK aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 465-471 0145-479X 39:5-6<465 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer