Crystal structure of bacterial multidrug efflux transporter AcrB

By S. Murakami, R. Nakashima, E. Yamashita, A. Yamaguchi. Nature, 2002

986 citations recorded by the source corpus.

Subfields: Genetics, Molecular Biology, Molecular Medicine

View Paper: https://www.semanticscholar.org/paper/b8a2cc1f6e53ab37976ff93cf1eb3eb940f061ac

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. Xian-Zhi Li
2. R. Nusse
3. H. Nikaido
4. Hans Clevers

In Molecular Biology

1. Xian-Zhi Li
2. H. Nikaido
3. R. Nusse
4. Hans Clevers
5. G. Schulte
6. J. Petersen
7. J. Dijksterhuis

In Molecular Medicine

1. Xian-Zhi Li
2. H. Nikaido
3. E. Dassa
4. C. Orelle
5. A. Davidson
6. Jue Chen
7. P. Plésiat

Citations in the corpus

• Clinically Relevant Chromosomally Encoded Multidrug Resistance Efflux Pumps in Bacteria (2006, neutral): “OprM has 35% similarity with TolC.”
• Structure, Function, and Evolution of Bacterial ATP-Binding Cassette Systems (2008, background): “The IM-RND-type transporter AcrB, which has 12 TM domains and a large periplasmic domain, is a trimer in crystallographic form (323, 376, 544) (Fig.”
• Cryo-EM analysis of a membrane protein embedded in the liposome (2020, result): “We further compared our reconstruction with published ones for apo AcrB with C3 (PDB: 1IWG) (41) or C1 AcrB (PDB: 6BAJ) (42) symmetry.”