Transporters containing an ATP-binding cassette encoded by the MHC class II region seem to be responsible for this transport 1-8.

The structure of MsbA from Escherichia coli [ 22], an ATP-binding cassette (ABC) transporter homolog, was recently solved.

They are capable of picking up cholesterol, carried internally, from cells by interaction with the ATP-binding cassette transporter A1 (ABCA1).

This protein is a product of multidrug resistance gene MDR1 and a member of family of ATP-dependent transporters (ATP-binding cassette).

Specific ATP-binding cassette (ABC) transporters direct the export and processing of small antibacterial peptides called bacteriocins.

We have noticed interesting associations among membrane proteins, ion channels, electron transporters, ATP-binding cassettes, and genes involving metabolism on chromosomes 2, 5 and 7.

To overcome this difficulty, the ATP-binding cassette (ABC) transporter C1 (ABCC1) serves as the "exit door" for S1P.

ATP-binding cassette, sub-family B member 11 also known as ABCB11 is a protein which in humans is encoded by the ABCB11 gene.

Proteins are classified as ABC transporters based on the sequence and organization of their ATP-binding cassette (ABC) domain(s).

ABC transporters are built with up to four domains consisting of two unrelated modules, ATP-binding cassette and an integral membrane module, arranged in various combinations.