Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems

By A. Davidson, E. Dassa, C. Orelle, Jue Chen. Microbiology and Molecular Biology Reviews, 2008

1,319 citations recorded by the source corpus.

Subfields: Genetics, Molecular Medicine, Oncology

View Paper: https://www.semanticscholar.org/paper/4325523d19a4119e80d9d8bc4dee9c8ac5df9614

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. Yuri I. Wolf
2. Eugene V. Koonin
3. Zhesheng Chen
4. K. Locher

In Molecular Medicine

1. Eugene V. Koonin
2. K. Locher

In Oncology

1. Zhesheng Chen
2. K. Locher

Citations in the corpus

• Bifidobacteria and Their Role as Members of the Human Gut Microbiota (2016, background): “ABC transporters couple ATP hydrolysis to efficient internalization of sugars and appear to represent the primary carbohydrate transport systems for bifidobacteria (Ventura et al., 2007; Davidson et al., 2008; Jojima et al., 2010).”
• Genomics of bacteria and archaea: the emerging dynamic view of the prokaryotic world (2008, background): “A case in point is numerous metabolite transport operons that consist of similarly arranged genes encoding the transmebrane permease, ATPase and periplasmic subunits of the so-called ABC transporters (94).”
• Overcoming ABC transporter-mediated multidrug resistance: Molecular mechanisms and novel therapeutic drug strategies. (2016, background): “The two NBDs contain conserved motifs such as Walker A, Walker B, ABC signature, a glutamine loop (Q-loop), and a switch motif (Davidson et al., 2008; Sharom, 2011).”
• Mechanistic diversity in ATP-binding cassette (ABC) transporters (2016, background): “The domain arrangement and conserved sequence motifs are summarized in box 1 , and representative structures of the different sub-families of ABC transporters are shown in Fig.”
• Structural basis for a bacterial Pip system plant effector recognition protein (2021, background): “Although a closed-unliganded form of an SBP is somewhat unusual (10, 11, 17), there are reports of ligand-free closed forms for other SBPs, including glucose/galactose-binding protein (GGBP) (18), glutaminebinding protein (GlnBP) (17), and choline-binding protein (ChoX) (19), none of which, however,”