ArticleScientific reports2017
The crystal structure of the regulatory domain of the human sodium-driven chloride/bicarbonate exchanger.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- The role of NaPflugers Archiv : European journal of physiology · 2024Review
- Cryo-EM structure of the sodium-driven chloride/bicarbonate exchanger NDCBE.Nature communications · 2021Article
- IRBIT activates NBCe1-B by releasing the auto-inhibition module from the transmembrane domain.The Journal of physiology · 2021Article
- Transport and Use of Bicarbonate in Plants: Current Knowledge and Challenges Ahead.International journal of molecular sciences · 2018Review
- Protons as Messengers of Intercellular Communication in the Nervous System.Frontiers in cellular neuroscience · 2018Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sodium-driven chloride/bicarbonate exchanger (NDCBE) is essential for maintaining homeostatic pH in neurons. The crystal structure at 2.8 Å resolution of the regulatory N-terminal domain of human NDCBE represents the first crystal structure of an electroneutral sodium-bicarbonate cotransporter. The crystal structure forms an equivalent dimeric interface as observed for the cytoplasmic domain of Band 3, and thus establishes that the consensus motif VTVLP is the key minimal dimerization motif. The VTVLP motif is highly conserved and likely to be the physiologically relevant interface for all other members of the SLC4 family. A novel conserved Zn
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