ABC transporters: physiology, structure and mechanism--an overview.

By C. Higgins. Research in Microbiology, 2001

645 citations recorded by the source corpus.

Subfields: Genetics, Molecular Medicine, Oncology

View Paper: https://www.semanticscholar.org/paper/de6d4c9bd5c504c2a640a865d5e726efef8522b4

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Genetics

1. Andrés Moya
2. G. Price
3. Francisco J. Silva
4. M. Badger

In Molecular Medicine

1. G. Price
2. M. Badger

In Oncology

1. G. Price
2. S. Cole
3. M. Badger
4. R. Deeley
5. Christopher J Westlake

Citations in the corpus

• CO2 concentrating mechanisms in algae: mechanisms, environmental modulation, and evolution. (2005, background): “(132) thoroughly characterized a low CO2-induced ABC-type (68) HCO3 uniporter, named BCT1, with a high affinity for HCO3 .”
• Advances in understanding the cyanobacterial CO2-concentrating-mechanism (CCM): functional components, Ci transporters, diversity, genetic regulation and prospects for engineering into plants. (2008, background): “Early studies implicated NDH-1 in active CO2 uptake by cyanobacteria (Ogawa, 1992), and initially it was thought that this involved a supply of ATP generated by NDH-1 cyclic electron flow.”
• Recent advances in CO2 uptake and fixation mechanism of cyanobacteria and microalgae (2016, background): “They belong to the diverse subfamily of bacterial ATP-binding cassette (ABC) transporter (Higgins, 2001).”
• Determination of the Core of a Minimal Bacterial Gene Set (2004, background): “Many ATP binding subunits appear to be “orphan” proteins with unknown partners, which are apparently overrepresented compared to the other two subunits in all genomes sequenced thus far (32), including the reduced genomes under study.”
• Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. (2006, background): “These L-shaped domains are functionally separated into two arms: arm I, an F1-like ATP-binding unit comprised of the Walker A and Walker B elements, and arm II, containing the C motif (172).”