Crystal structure of a bacterial homologue of Na+/Cl--dependent neurotransmitter transporters
By A. Yamashita, Satinder K. Singh, T. Kawate, Yan Jin, Eric Gouaux. Nature, 2005
1,240 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5d288529d7845103dff632d19344ab489c254a11
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In Cellular and Molecular Neuroscience
In Molecular Biology
- Jens Meiler
- Eric Gouaux
- Yigong Shi
- Jose M. Duarte
- Laura M. Geffert
- C. K. Surratt
- Stephen K. Burley
- Christine Zardecki
Citations in the corpus
- Alternating access mechanisms of LeuT-Fold transporters: trailblazing towards the promised energy landscapes (2016, background): “The leucine transporter (LeuT), a Na+-coupled symporter from Aquifex aeolicus belonging to the neurotransmitter:Na+ symporter superfamily (NSS) became the founding member of the LeuT-fold structural class following the publication of its first crystal structure in 2005 [5].”
- Practically Useful: What the Rosetta Protein Modeling Suite Can Do for You (2010, background): “(66) which has an overall sequence similarity of 17%and a binding site similarity of 50% with SERT.”
- Identification of an allosteric modulator of the serotonin transporter with novel mechanism of action. (2013, methodology): “Further modeling efforts of SERT involved use of the leucine transporter (LeuT) from a thermophilic bacteria, Aquifex aeolicus (Yamashita et al., 2005), which has provided a suitable template to understand the ion binding sites (Forrest et al., 2007) and orthosteric and allosteric binding sites in…”
- A glimpse of structural biology through X-ray crystallography. (2014, background): “Crystal structure of the sodium:leucine symporter LeuT revealed a conserved fold of ten TMs grouped into two inverted repeats, each containing five consecutive TMs (Figure 5C) (Yamashita et al., 2005).”
- Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. (2006, background): “In fact, the target protein from the C-6 construct crystallized readily, yielding crystals that diffracted beyond 1.7 Å resolution (Figures 5C–5E) (Yamashita et al., 2005).”
- RCSB Protein Data Bank: Enabling biomedical research and drug discovery (2019, background): “Recent structure-guided development of SSRIs built on MX studies of a bacterial homolog LeuT,(93) first determined in 2005 (PDB 2a65).(94) Other structures of human serotonin transporters (PDB 5i6x and others)(95) will almost certainly improve the impact of this approach for discovery and developmen”
- New design strategies for antidepressant drugs (2013, methodology): “This SERT template was provided by the crystallization of the LeuT leucine transporter [34], a bacterial homolog of SERT.”