Type |
Details |
Score |
Publication |
First Author: |
Shanghai Model Organisms Center |
Year: |
2017 |
Journal: |
MGI Direct Data Submission |
Title: |
Information obtained from the Shanghai Model Organisms Center (SMOC), Shanghai, China |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
European Mouse Mutant Archive |
Year: |
2003 |
Journal: |
Unpublished |
Title: |
Information obtained from the European Mouse Mutant Archive (EMMA) |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mammalian Functional Genomics Centre |
Year: |
2010 |
Journal: |
MGI Direct Data Submission |
Title: |
Alleles produced for the NorCOMM project by the Mammalian Functional Genomics Centre (Mfgc), University of Manitoba |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Dickinson ME |
Year: |
2016 |
Journal: |
Nature |
Title: |
High-throughput discovery of novel developmental phenotypes. |
Volume: |
537 |
Issue: |
7621 |
Pages: |
508-514 |
|
•
•
•
•
•
|
Publication |
First Author: |
Thompson CL |
Year: |
2014 |
Journal: |
Neuron |
Title: |
A high-resolution spatiotemporal atlas of gene expression of the developing mouse brain. |
Volume: |
83 |
Issue: |
2 |
Pages: |
309-323 |
|
•
•
•
•
•
|
Publication |
First Author: |
Koscielny G |
Year: |
2014 |
Journal: |
Nucleic Acids Res |
Title: |
The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data. |
Volume: |
42 |
Issue: |
Database issue |
Pages: |
D802-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
The Gene Ontology Consortium |
Year: |
2014 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Magdaleno S |
Year: |
2006 |
Journal: |
PLoS Biol |
Title: |
BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system. |
Volume: |
4 |
Issue: |
4 |
Pages: |
e86 |
|
•
•
•
•
•
|
Publication |
First Author: |
Carninci P |
Year: |
2005 |
Journal: |
Science |
Title: |
The transcriptional landscape of the mammalian genome. |
Volume: |
309 |
Issue: |
5740 |
Pages: |
1559-63 |
|
•
•
•
•
•
|
Publication |
First Author: |
Adams DJ |
Year: |
2024 |
Journal: |
Nature |
Title: |
Genetic determinants of micronucleus formation in vivo. |
Volume: |
627 |
Issue: |
8002 |
Pages: |
130-136 |
|
•
•
•
•
•
|
Publication |
First Author: |
MGD Nomenclature Committee |
Year: |
1995 |
|
Title: |
Nomenclature Committee Use |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
GemPharmatech |
Year: |
2020 |
|
Title: |
GemPharmatech Website. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Cyagen Biosciences Inc. |
Year: |
2022 |
|
Title: |
Cyagen Biosciences Website. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators |
Year: |
2011 |
|
Title: |
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
UniProt-GOA |
Year: |
2012 |
|
Title: |
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
GOA curators |
Year: |
2016 |
|
Title: |
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
The Jackson Laboratory Mouse Radiation Hybrid Database |
Year: |
2004 |
Journal: |
Database Release |
Title: |
Mouse T31 Radiation Hybrid Data Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Okazaki Y |
Year: |
2002 |
Journal: |
Nature |
Title: |
Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs. |
Volume: |
420 |
Issue: |
6915 |
Pages: |
563-73 |
|
•
•
•
•
•
|
Publication |
First Author: |
The Gene Ontology Consortium |
Year: |
2010 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Diez-Roux G |
Year: |
2011 |
Journal: |
PLoS Biol |
Title: |
A high-resolution anatomical atlas of the transcriptome in the mouse embryo. |
Volume: |
9 |
Issue: |
1 |
Pages: |
e1000582 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2). |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
MGI Genome Annotation Group and UniGene Staff |
Year: |
2015 |
Journal: |
Database Download |
Title: |
MGI-UniGene Interconnection Effort |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas |
Year: |
2010 |
|
Title: |
Annotation inferences using phylogenetic trees |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
Year: |
2000 |
Journal: |
Database Release |
Title: |
Entrez Gene Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Allen Institute for Brain Science |
Year: |
2004 |
Journal: |
Allen Institute |
Title: |
Allen Brain Atlas: mouse riboprobes |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Consensus CDS project |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Sonneveld R |
Year: |
2017 |
Journal: |
J Am Soc Nephrol |
Title: |
Sildenafil Prevents Podocyte Injury via PPAR-γ-Mediated TRPC6 Inhibition. |
Volume: |
28 |
Issue: |
5 |
Pages: |
1491-1505 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kuwahara K |
Year: |
2006 |
Journal: |
J Clin Invest |
Title: |
TRPC6 fulfills a calcineurin signaling circuit during pathologic cardiac remodeling. |
Volume: |
116 |
Issue: |
12 |
Pages: |
3114-26 |
|
•
•
•
•
•
|
Strain |
Attribute String: |
mutant stock, targeted mutation |
|
•
•
•
•
•
|
Publication |
First Author: |
Hagmann H |
Year: |
2023 |
Journal: |
Cells |
Title: |
Capsazepine (CPZ) Inhibits TRPC6 Conductance and Is Protective in Adriamycin-Induced Nephropathy and Diabetic Glomerulopathy. |
Volume: |
12 |
Issue: |
2 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Norton N |
Year: |
2021 |
Journal: |
Front Cardiovasc Med |
Title: |
Trpc6 Promotes Doxorubicin-Induced Cardiomyopathy in Male Mice With Pleiotropic Differences Between Males and Females. |
Volume: |
8 |
|
Pages: |
757784 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chauvet S |
Year: |
2015 |
Journal: |
Biochim Biophys Acta |
Title: |
The Na+/K+-ATPase and the amyloid-beta peptide aβ1-40 control the cellular distribution, abundance and activity of TRPC6 channels. |
Volume: |
1853 |
Issue: |
11 Pt A |
Pages: |
2957-65 |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion F419, Katherina Walz |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion F615, Katherina Walz |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion F75a, Katherina Walz |
Allele Type: |
Transgenic |
Attribute String: |
Inserted expressed sequence |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(NPHS2-Trpc6)F419Walz/? |
Background: |
involves: C57BL/6J * CBA/J |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(NPHS2-Trpc6*E896K)F75aWalz/? |
Background: |
involves: C57BL/6J * CBA/J |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Tg(NPHS2-Trpc6*P111Q)F615Walz/? |
Background: |
involves: C57BL/6J * CBA/J |
Zygosity: |
ot |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Zernov N |
Year: |
2024 |
Journal: |
Sci Rep |
Title: |
Discovery of a novel piperazine derivative, cmp2: a selective TRPC6 activator suitable for treatment of synaptic deficiency in Alzheimer's disease hippocampal neurons. |
Volume: |
14 |
Issue: |
1 |
Pages: |
23512 |
|
•
•
•
•
•
|
Allele |
Name: |
transient receptor potential cation channel, subfamily C, member 6; endonuclease-mediated mutation 2, Shanghai Model Organisms Center |
Allele Type: |
Endonuclease-mediated |
Attribute String: |
Null/knockout |
|
•
•
•
•
•
|
Publication |
First Author: |
Hofmann T |
Year: |
1999 |
Journal: |
Nature |
Title: |
Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol. |
Volume: |
397 |
Issue: |
6716 |
Pages: |
259-63 |
|
•
•
•
•
•
|
Interaction Experiment |
Description: |
Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
930
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Transgene |
Type: |
transgene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
DO Term |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, endonuclease-mediated mutation, mutant strain |
|
•
•
•
•
•
|
Allele |
Name: |
transient receptor potential cation channel, subfamily C, member 6; targeted mutation 1, Shanghai Model Organisms Center |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, No functional change |
|
•
•
•
•
•
|
Publication |
First Author: |
Hofmann T |
Year: |
2002 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Subunit composition of mammalian transient receptor potential channels in living cells. |
Volume: |
99 |
Issue: |
11 |
Pages: |
7461-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Anderson M |
Year: |
2013 |
Journal: |
Am J Physiol Cell Physiol |
Title: |
Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol. |
Volume: |
305 |
Issue: |
3 |
Pages: |
C276-89 |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 1, Jeffery D Molkentin |
Allele Type: |
Transgenic |
Attribute String: |
Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
Strain |
Attribute String: |
coisogenic, mutant strain, transgenic |
|
•
•
•
•
•
|
Allele |
Name: |
transgene insertion 1, Jeffery Molkentin |
Allele Type: |
Transgenic |
Attribute String: |
Dominant negative, Humanized sequence, Inserted expressed sequence |
|
•
•
•
•
•
|
Strain |
Attribute String: |
congenic, mutant strain, targeted mutation |
|
•
•
•
•
•
|
Strain |
Attribute String: |
transgenic, mutant stock |
|
•
•
•
•
•
|
Strain |
Attribute String: |
congenic, mutant strain, transgenic |
|
•
•
•
•
•
|
Publication |
First Author: |
Millay DP |
Year: |
2009 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Calcium influx is sufficient to induce muscular dystrophy through a TRPC-dependent mechanism. |
Volume: |
106 |
Issue: |
45 |
Pages: |
19023-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li W |
Year: |
2012 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Activity-dependent BDNF release and TRPC signaling is impaired in hippocampal neurons of Mecp2 mutant mice. |
Volume: |
109 |
Issue: |
42 |
Pages: |
17087-92 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hashimotodani Y |
Year: |
2005 |
Journal: |
Neuron |
Title: |
Phospholipase Cbeta serves as a coincidence detector through its Ca2+ dependency for triggering retrograde endocannabinoid signal. |
Volume: |
45 |
Issue: |
2 |
Pages: |
257-68 |
|
•
•
•
•
•
|
Publication |
First Author: |
Catanuto P |
Year: |
2009 |
Journal: |
Kidney Int |
Title: |
17 beta-estradiol and tamoxifen upregulate estrogen receptor beta expression and control podocyte signaling pathways in a model of type 2 diabetes. |
Volume: |
75 |
Issue: |
11 |
Pages: |
1194-201 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kang JS |
Year: |
2019 |
Journal: |
Sci Rep |
Title: |
Angiotensin II-mediated MYH9 downregulation causes structural and functional podocyte injury in diabetic kidney disease. |
Volume: |
9 |
Issue: |
1 |
Pages: |
7679 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tabeling C |
Year: |
2015 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
CFTR and sphingolipids mediate hypoxic pulmonary vasoconstriction. |
Volume: |
112 |
Issue: |
13 |
Pages: |
E1614-23 |
|
•
•
•
•
•
|
Publication |
First Author: |
Krauszman A |
Year: |
2017 |
Journal: |
Cardiovasc Res |
Title: |
Role of phosphatase and tensin homolog in hypoxic pulmonary vasoconstriction. |
Volume: |
113 |
Issue: |
8 |
Pages: |
869-878 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kidokoro K |
Year: |
2023 |
Journal: |
Kidney360 |
Title: |
Insights into the Regulation of GFR by the Keap1-Nrf2 Pathway. |
Volume: |
4 |
Issue: |
10 |
Pages: |
1454-1466 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tiruppathi C |
Year: |
2002 |
Journal: |
Circ Res |
Title: |
Impairment of store-operated Ca2+ entry in TRPC4(-/-) mice interferes with increase in lung microvascular permeability. |
Volume: |
91 |
Issue: |
1 |
Pages: |
70-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang Y |
Year: |
2010 |
Journal: |
J Am Soc Nephrol |
Title: |
Activation of NFAT signaling in podocytes causes glomerulosclerosis. |
Volume: |
21 |
Issue: |
10 |
Pages: |
1657-66 |
|
•
•
•
•
•
|
Publication |
First Author: |
Boucher I |
Year: |
2012 |
Journal: |
Lab Invest |
Title: |
Gα12 activation in podocytes leads to cumulative changes in glomerular collagen expression, proteinuria and glomerulosclerosis. |
Volume: |
92 |
Issue: |
5 |
Pages: |
662-75 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kusudo T |
Year: |
2012 |
Journal: |
J Appl Physiol (1985) |
Title: |
TRPV4 deficiency increases skeletal muscle metabolic capacity and resistance against diet-induced obesity. |
Volume: |
112 |
Issue: |
7 |
Pages: |
1223-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Carnevale D |
Year: |
2018 |
Journal: |
Arterioscler Thromb Vasc Biol |
Title: |
Loss of EMILIN-1 Enhances Arteriolar Myogenic Tone Through TGF-β (Transforming Growth Factor-β)-Dependent Transactivation of EGFR (Epidermal Growth Factor Receptor) and Is Relevant for Hypertension in Mice and Humans. |
Volume: |
38 |
Issue: |
10 |
Pages: |
2484-2497 |
|
•
•
•
•
•
|
Publication |
First Author: |
Feng Y |
Year: |
2022 |
Journal: |
Int J Mol Sci |
Title: |
DOT1L Methyltransferase Regulates Calcium Influx in Erythroid Progenitor Cells in Response to Erythropoietin. |
Volume: |
23 |
Issue: |
9 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
López E |
Year: |
2018 |
Journal: |
Front Physiol |
Title: |
Stanniocalcin 2 Regulates Non-capacitative Ca2+ Entry and Aggregation in Mouse Platelets. |
Volume: |
9 |
|
Pages: |
266 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kawasaki BT |
Year: |
2006 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Role of Src in C3 transient receptor potential channel function and evidence for a heterogeneous makeup of receptor- and store-operated Ca2+ entry channels. |
Volume: |
103 |
Issue: |
2 |
Pages: |
335-40 |
|
•
•
•
•
•
|
Publication |
First Author: |
Semtner M |
Year: |
2007 |
Journal: |
J Biol Chem |
Title: |
Potentiation of TRPC5 by protons. |
Volume: |
282 |
Issue: |
46 |
Pages: |
33868-78 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wright JD |
Year: |
2017 |
Journal: |
FASEB J |
Title: |
Modeled structural basis for the recognition of α2-3-sialyllactose by soluble Klotho. |
Volume: |
31 |
Issue: |
8 |
Pages: |
3574-3586 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wang J |
Year: |
2015 |
Journal: |
Cardiovasc Res |
Title: |
Hypoxia inducible factor-1-dependent up-regulation of BMP4 mediates hypoxia-induced increase of TRPC expression in PASMCs. |
Volume: |
107 |
Issue: |
1 |
Pages: |
108-18 |
|
•
•
•
•
•
|
Publication |
First Author: |
Shimizu N |
Year: |
2018 |
Journal: |
Neurosci Lett |
Title: |
Effects of nerve growth factor neutralization on TRP channel expression in laser-captured bladder afferent neurons in mice with spinal cord injury. |
Volume: |
683 |
|
Pages: |
100-103 |
|
•
•
•
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Publication |
First Author: |
Lopez JR |
Year: |
2020 |
Journal: |
Front Physiol |
Title: |
Contribution of TRPC Channels to Intracellular Ca2 + Dyshomeostasis in Smooth Muscle From mdx Mice. |
Volume: |
11 |
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Pages: |
126 |
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Publication |
First Author: |
Sah R |
Year: |
2013 |
Journal: |
Circulation |
Title: |
Timing of myocardial trpm7 deletion during cardiogenesis variably disrupts adult ventricular function, conduction, and repolarization. |
Volume: |
128 |
Issue: |
2 |
Pages: |
101-14 |
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Publication |
First Author: |
Matsushita N |
Year: |
2014 |
Journal: |
PLoS One |
Title: |
Cardiac overexpression of constitutively active Galpha q causes angiotensin II type1 receptor activation, leading to progressive heart failure and ventricular arrhythmias in transgenic mice. |
Volume: |
9 |
Issue: |
8 |
Pages: |
e106354 |
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Publication |
First Author: |
Gammons J |
Year: |
2021 |
Journal: |
J Am Heart Assoc |
Title: |
Cardiac-Specific Deletion of Orai3 Leads to Severe Dilated Cardiomyopathy and Heart Failure in Mice. |
Volume: |
10 |
Issue: |
8 |
Pages: |
e019486 |
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Publication |
First Author: |
Hu Y |
Year: |
2020 |
Journal: |
Hypertens Res |
Title: |
High-salt intake increases TRPC3 expression and enhances TRPC3-mediated calcium influx and systolic blood pressure in hypertensive patients. |
Volume: |
43 |
Issue: |
7 |
Pages: |
679-687 |
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Publication |
First Author: |
Woo JS |
Year: |
2010 |
Journal: |
Biochem J |
Title: |
S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal muscle. |
Volume: |
427 |
Issue: |
1 |
Pages: |
125-34 |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG). |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG). |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC3, 6, and 7 interact physically and, upon coexpression, coassemble to form functional tetrameric channels [].TRPC3 is likely to be operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. It is activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C, and by inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3 [, ]. High levels of TRPC3 mRNA have been related to elevated salt intake and increased blood pressure []. |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC4 and TRPC5 are thought to be receptor-operated, Ca2+-permeable, nonselective cation channels. It is likely that heteromultimers of TRPC1 and TRPC4 or TRPC5 form receptor-operated nonselective cation channels in central neurones, and that TRPC4 contributes to nonselective cation channels in intestinal smooth muscle []. |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC4 and TRPC5 are thought to be receptor-operated, Ca2+-permeable, nonselective cation channels. It is likely that heteromultimers of TRPC1 and TRPC4 or TRPC5 form receptor-operated nonselective cation channels in central neurones, and that TRPC4 contributes to nonselective cation channels in intestinal smooth muscle []. |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC3, 6, and 7 interact physically and, upon coexpression, coassemble to form functional tetrameric channels []. |
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Protein Domain |
Type: |
Family |
Description: |
Transient receptor potential (TRP) channels can be described as tetramers formed by subunits with six transmembrane domains and containing cation-selective pores, which in several cases show high calcium permeability. The molecular architecture of TRP channels is reminiscent of voltage-gated channels and comprises six putative transmembrane segments (S1-S6), intracellular N- and C-termini, and a pore-forming reentrant loop between S5 and S6 [].TRP channels represent a superfamily conserved from worms to humans that comprise seven subfamilies []: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin or long TRPs), TRPA (ankyrin, whose only member is Transient receptor potential cation channel subfamily A member 1, TrpA1), TRPP (polycystin), TRPML (mucolipin) and TRPN (Nomp-C homologues), which has a single member that can be found in worms, flies, and zebrafish. TRPs are classified essentially according to their primary amino acid sequence rather than selectivity or ligand affinity, due to their heterogeneous properties and complex regulation.TRP channels are involved in many physiological functions, ranging from pure sensory functions, such as pheromone signalling, taste transduction, nociception, and temperature sensation, over homeostatic functions, such as Ca2+ and Mg2+ reabsorption and osmoregulation, to many other motile functions, such as muscle contraction and vaso-motor control [].The classical or canonical TRPC family (formerly short-TRPs, STRPs) encompasses channels presenting a large number of different activation modes. Some are store-operated, whereas others are receptor-operated channels activated by the production of diacylglicerol or redox processes. TRPC proteins also control growth cone guidance in both mammalian and amphibian model systems. All seven channels of this family share the common property of activation through phospholipase C (PLC)-coupled receptors []. It is believed that functional TRPC channels are generated in situ by association of four TRPC proteins to form either homotetramers or heterotetramers [].On the basis of sequence similarity, TRPC channels can be subdivided into four subgroups group 1 (TRPC1), group 2 (TRPC2), group 3 (TRPC3, TRPC6 and TRPC7) and group 4 (TRPC4 and TRPC5) []. While TRPC1 and TRPC2 are almost unique, TRPC4 and TRPC5 share approx. 65% identity. TRPC3, 6 and 7 form a structural and functional subfamily sharing 70-80% identity at the amino acid level and their common sensitivity towards diacylglycerol (DAG).TRPC3, 6, and 7 interact physically and, upon coexpression, coassemble to form functional tetrameric channels []. |
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Publication |
First Author: |
Plant TD |
Year: |
2003 |
Journal: |
Cell Calcium |
Title: |
TRPC4 and TRPC5: receptor-operated Ca2+-permeable nonselective cation channels. |
Volume: |
33 |
Issue: |
5-6 |
Pages: |
441-50 |
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Publication |
First Author: |
Dietrich A |
Year: |
2005 |
Journal: |
Naunyn Schmiedebergs Arch Pharmacol |
Title: |
Functional characterization and physiological relevance of the TRPC3/6/7 subfamily of cation channels. |
Volume: |
371 |
Issue: |
4 |
Pages: |
257-65 |
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