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Bedaquiline inhibits the yeast and human mitochondrial ATP synthases.
- Published in:
- Communications Biology, 2020, v. 3, n. 1, p. N.PAG, doi. 10.1038/s42003-020-01173-z
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- Article
Structure and mechanism of a redesigned multidrug transporter from the Major Facilitator Superfamily.
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- Scientific Reports, 2020, v. 10, n. 1, p. 1, doi. 10.1038/s41598-020-60332-8
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- Article
Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition.
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- Communications Biology, 2019, v. 2, n. 1, p. N.PAG, doi. 10.1038/s42003-019-0446-y
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- Article
Structure and function of the divalent anion/Na<sup>+</sup> symporter from Vibrio cholerae and a humanized variant.
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- Nature Communications, 2017, v. 8, n. 4, p. 15009, doi. 10.1038/ncomms15009
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- Article
Structural basis for the blockade of MATE multidrug efflux pumps.
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- Nature Communications, 2015, v. 6, n. 8, p. 7995, doi. 10.1038/ncomms8995
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- Article
Structural insights into H<sup>+</sup>-coupled multidrug extrusion by a MATE transporter.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 11, p. 1310, doi. 10.1038/nsmb.2687
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- Article
Structure of the c<sub>10</sub> ring of the yeast mitochondrial ATP synthase in the open conformation.
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- Nature Structural & Molecular Biology, 2012, v. 19, n. 5, p. 485, doi. 10.1038/nsmb.2284
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- Article
Characterization of the mitochondrial ATP synthase from yeast Saccharomyces cerevisae.
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- Journal of Bioenergetics & Biomembranes, 2011, v. 43, n. 4, p. 333, doi. 10.1007/s10863-011-9364-5
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- Article
Structural genomics of Caenorhabditis elegans: Crystal structure of the tropomodulin C-terminal domain.
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- Proteins, 2004, v. 56, n. 2, p. 384, doi. 10.1002/prot.10597
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- Article
Structural genomics of Caenorhabditis elegans: Triosephosphate isomerase.
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- Proteins, 2003, v. 51, n. 3, p. 484, doi. 10.1002/prot.10364
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- Article
Unexpected formation of a 11 H-pyrido[2,1- b]quinazolin-11-one derivative from 5,11-dihydro-6 H-pyrido[2,3- b]-1,4-benzodiazepin-6-one.
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- Journal of Heterocyclic Chemistry, 1989, v. 26, n. 5, p. 1229, doi. 10.1002/jhet.5570260505
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- Article