ArticleBiochemistry2008
Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
57 citing papers in PubMed, 105 citations in OpenAlex.
- The in vivo TRPV6 protein starts at a non-AUG triplet, decoded as methionine, upstream of canonical initiation at AUG.The Journal of biological chemistry · 2013Trial
- Transient receptor potential vanilloid channels in inflammatory bowel diseases: linking inflammation, angiogenesis, and oxidative stress.Inflammopharmacology · 2026Review
- Recent advances on the structure and the function relationships of the TRPV4 ion channel.Channels (Austin, Tex.) · 2024Review
- TRPV Channels in Osteoarthritis: A Comprehensive Review.Biomolecules · 2024Review
- Intrinsically disordered regions in TRPV2 mediate protein-protein interactions.Communications biology · 2023Article
- TRP (transient receptor potential) ion channel family: structures, biological functions and therapeutic interventions for diseases.Signal transduction and targeted therapy · 2023Review
- TRPV3: Structure, Diseases and Modulators.Molecules (Basel, Switzerland) · 2023Review
- TRPV6 channel mediates alcohol-induced gut barrier dysfunction and systemic response.Cell reports · 2022Article
- Calcium selective channel TRPV6: Structure, function, and implications in health and disease.Gene · 2022Review
- Dynamic evolution of transient receptor potential vanilloid (TRPV) ion channel family with numerous gene duplications and losses.Frontiers in endocrinology · 2022Article
- Endothelial TRPV4 channels in lung edema and injury.Current topics in membranes · 2022Review
- Transient Receptor Potential Channel Ankyrin 1: A Unique Regulator of Vascular Function.Cells · 2021Review
- TRPing to the Point of Clarity: Understanding the Function of the Complex TRPV4 Ion Channel.Cells · 2021Review
- Structural insights into the gating mechanisms of TRPV channels.Cell calcium · 2020Review
- Heat activation mechanism of TRPV1: New insights from molecular dynamics simulation.Temperature (Austin, Tex.) · 2019Review
- Store-Operated CaInternational journal of molecular sciences · 2018Review
- TRPV6 Variants Interfere with Maternal-Fetal Calcium Transport through the Placenta and Cause Transient Neonatal Hyperparathyroidism.American journal of human genetics · 2018Article
- Decrypting the Heat Activation Mechanism of TRPV1 Channel by Molecular Dynamics Simulation.Biophysical journal · 2018Article
- X-ray crystallography of TRP channels.Channels (Austin, Tex.) · 2018Review
- Structural basis of TRPV5 channel inhibition by econazole revealed by cryo-EM.Nature structural & molecular biology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Transient receptor potential (TRP) proteins are cation channels composed of a transmembrane domain flanked by large N- and C-terminal cytoplasmic domains. All members of the vanilloid family of TRP channels (TRPV) possess an N-terminal ankyrin repeat domain (ARD). The ARD of mammalian TRPV6, an important regulator of calcium uptake and homeostasis, is essential for channel assembly and regulation. The 1.7 A crystal structure of the TRPV6-ARD reveals conserved structural elements unique to the ARDs of TRPV proteins. First, a large twist between the fourth and fifth repeats is induced by residues conserved in all TRPV ARDs. Second, the third finger loop is the most variable region in sequence, length and conformation. In TRPV6, a number of putative regulatory phosphorylation sites map to the base of this third finger. Size exclusion chromatography and crystal packing indicate that the TRPV6-ARD does not assemble as a tetramer and is monomeric in solution. Adenosine triphosphate-agarose and calmodulin-agarose pull-down assays show that the TRPV6-ARD does not interact with either ligand, indicating a different functional role for the TRPV6-ARD than in the paralogous thermosensitive TRPV1 channel. Similar biochemical findings are also presented for the highly homologous mammalian TRPV5-ARD. The implications of the structural and biochemical data on the role of the ankyrin repeats in different TRPV channels are discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.