Isolation and characterization of aminopterin-resistant cell lines in maize

Planta ◽  
1981 ◽  
Vol 153 (5) ◽  
pp. 436-442 ◽  
Author(s):  
Ko Shimamoto ◽  
Oliver E. Nelson
1991 ◽  
Vol 11 (8) ◽  
pp. 3940-3948
Author(s):  
C T Wu ◽  
M Budding ◽  
M S Griffin ◽  
J M Croop

Mammalian multidrug-resistant cell lines, selected for resistance to a single cytotoxic agent, display cross-resistance to a broad spectrum of structurally and functionally unrelated compounds. These cell lines overproduce a membrane protein, the P-glycoprotein, which is encoded by a member(s) of a multigene family, termed mdr or pgp. The amino acid sequence of the P-glycoprotein predicts an energy-dependent transport protein with homology to a large superfamily of proteins which transport a wide variety of substances. This report describes the isolation and characterization of two Drosophila homologs of the mammalian mdr gene. These homologs, located in chromosomal sections 49EF and 65A, encode proteins that share over 40% amino acid identity to the human and murine mdr P-glycoproteins. Fly strains bearing disruptions in the homolog in section 49EF have been constructed and implicate this gene in conferring colchicine resistance to the organism. This work sets the foundation for the molecular and genetic analysis of mdr homologs in Drosophila melanogaster.


1980 ◽  
Vol 66 (2) ◽  
pp. 334-341 ◽  
Author(s):  
Arthur L. Lawyer ◽  
Mary B. Berlyn ◽  
Israel Zelitch

Cell ◽  
1978 ◽  
Vol 14 (2) ◽  
pp. 415-421 ◽  
Author(s):  
Katsuhiko Hidaka ◽  
Hideya Endo ◽  
Shin-ichi Akiyama ◽  
Michihiko Kuwano

1991 ◽  
Vol 11 (8) ◽  
pp. 3940-3948 ◽  
Author(s):  
C T Wu ◽  
M Budding ◽  
M S Griffin ◽  
J M Croop

Mammalian multidrug-resistant cell lines, selected for resistance to a single cytotoxic agent, display cross-resistance to a broad spectrum of structurally and functionally unrelated compounds. These cell lines overproduce a membrane protein, the P-glycoprotein, which is encoded by a member(s) of a multigene family, termed mdr or pgp. The amino acid sequence of the P-glycoprotein predicts an energy-dependent transport protein with homology to a large superfamily of proteins which transport a wide variety of substances. This report describes the isolation and characterization of two Drosophila homologs of the mammalian mdr gene. These homologs, located in chromosomal sections 49EF and 65A, encode proteins that share over 40% amino acid identity to the human and murine mdr P-glycoproteins. Fly strains bearing disruptions in the homolog in section 49EF have been constructed and implicate this gene in conferring colchicine resistance to the organism. This work sets the foundation for the molecular and genetic analysis of mdr homologs in Drosophila melanogaster.


Glia ◽  
1994 ◽  
Vol 10 (3) ◽  
pp. 211-226 ◽  
Author(s):  
Scott R. Whittemore ◽  
Joseph T. Neary ◽  
Naomi Kleitman ◽  
Henry R. Sanon ◽  
Adelaida Benigno ◽  
...  

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