ReviewPflugers Archiv : European journal of physiology2005
Polycystins: polymodal receptor/ion-channel cellular sensors.
Review in Pflugers Archiv : European journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 121 citations in OpenAlex.
- Adhesion GPCRs as a paradigm for understanding polycystin-1 G protein regulation.Cellular signalling · 2020Review
- Polycystic Kidney Disease Ryanodine Receptor Domain (PKDRR) Proteins in Oomycetes.Pathogens (Basel, Switzerland) · 2020Article
- The ion channel function of polycystin-1 in the polycystin-1/polycystin-2 complex.EMBO reports · 2019Article
- PLC and IPThe Journal of general physiology · 2018Article
- Inhibition of cyst growth in PCK and Wpk rat models of polycystic kidney disease with low doses of peroxisome proliferator-activated receptorJournal of translational internal medicine · 2016Article
- The functions of TRPP2 in the vascular system.Acta pharmacologica Sinica · 2016Review
- Sexual selection and the adaptive evolution of PKDREJ protein in primates and rodents.Molecular human reproduction · 2015Article
- The Concise Guide to PHARMACOLOGY 2013/14: ion channels.British journal of pharmacology · 2013Article
- Polycystins and cellular Ca2+ signaling.Cellular and molecular life sciences : CMLS · 2013Review
- Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex.Nature communications · 2012Article
- Effect of lithium on the electrical properties of polycystin-2 (TRPP2).European biophysics journal : EBJ · 2011Article
- Polycystin-1 is required for stereocilia structure but not for mechanotransduction in inner ear hair cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Structural model of the TRPP2/PKD1 C-terminal coiled-coil complex produced by a combined computational and experimental approach.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Fenamates as TRP channel blockers: mefenamic acid selectively blocks TRPM3.British journal of pharmacology · 2011Article
- TRP channels in neurogastroenterology: opportunities for therapeutic intervention.British journal of pharmacology · 2011Review
- Physiological carbon dioxide, bicarbonate, and pH sensing.Pflugers Archiv : European journal of physiology · 2010Review
- Heteromerization of TRP channel subunits: extending functional diversity.Protein & cell · 2010Review
- Polycystins and renovascular mechanosensory transduction.Nature reviews. Nephrology · 2010Review
- Composition and sensory function of the trypanosome flagellar membrane.Current opinion in microbiology · 2010Review
- Transient receptor potential channelopathies.Pflugers Archiv : European journal of physiology · 2010Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transient receptor potential (TRP) channel proteins are divided into seven subgroups that are currently designated as TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPN (NOMP-C, from no mechanoreceptor potential-C), TRPA (ankyrin-like with transmembrane domains 1) and TRPP (polycystin). TRPC, TRPV and TRPM are related to canonical TRP proteins whereas TRPN, TRPA and TRPP (polycystin) are more divergent. Most TRP channels are linked to sensory stimuli, including phototransduction, thermosensation and mechanosensation. The TRPP subfamily was named after its founding member, polycystin kidney disease-2 (PKD2), a gene product mutated in many cases of autosomal dominant polycystic kidney disease (ADPKD). ADPKD is a major inherited nephropathy, affecting over 1:1,000 of the worldwide population, characterized by the progressive development of fluid-filled cysts from the tubules and collecting ducts of affected kidneys. Loss-of-function mutations in either polycystin-2, a non-selective cation channel, or polycystin-1 (PKD1), a large plasma membrane integral protein, give rise to ADPKD. PKD1 and PKD2 are thought to function together as part of a multiprotein receptor/ion-channel complex or independently and may be involved in transducing Ca(2+)-dependent mechanosensitive signals in response to cilia bending in renal epithelial cells and endodermally derived cells. Further information on the growing number and physiological properties of these TRP-polycystins is the basis of this review.
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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.