The ion channel function of polycystin‐1 in the polycystin‐1/polycystin‐2 complex
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Title
The ion channel function of polycystin‐1 in the polycystin‐1/polycystin‐2 complex
Authors
Keywords
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Journal
EMBO REPORTS
Volume -, Issue -, Pages -
Publisher
EMBO
Online
2019-08-23
DOI
10.15252/embr.201948336
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Note: Only part of the references are listed.- Adhesion G Protein–Coupled Receptors as Drug Targets
- (2018) Ryan H. Purcell et al. Annual Review of Pharmacology and Toxicology
- Polycystin 1 loss of function is directly linked to an imbalance in G-protein signaling in the kidney
- (2018) Bo Zhang et al. DEVELOPMENT
- A Mutation Affecting Polycystin-1 Mediated Heterotrimeric G-Protein Signaling Causes PKD
- (2018) Stephen C Parnell et al. HUMAN MOLECULAR GENETICS
- The TMEM16A channel mediates the fast polyspermy block inXenopus laevis
- (2018) Katherine L. Wozniak et al. JOURNAL OF GENERAL PHYSIOLOGY
- Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1
- (2018) Qiang Su et al. Nature Communications
- Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels
- (2018) Wang Zheng et al. Nature Communications
- Polycystin-2 is an essential ion channel subunit in the primary cilium of the renal collecting duct epithelium
- (2018) Xiaowen Liu et al. eLife
- Structure of the human PKD1-PKD2 complex
- (2018) Qiang Su et al. SCIENCE
- Genetic Complexity of Autosomal Dominant Polycystic Kidney and Liver Diseases
- (2017) Emilie Cornec-Le Gall et al. JOURNAL OF THE AMERICAN SOCIETY OF NEPHROLOGY
- Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2
- (2017) Martin Wilkes et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Molecular insights into lipid-assisted Ca2+ regulation of the TRP channel Polycystin-2
- (2017) Martin Wilkes et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The Structure of the Polycystic Kidney Disease Channel PKD2 in Lipid Nanodiscs
- (2016) Peter S. Shen et al. CELL
- Primary cilia are not calcium-responsive mechanosensors
- (2016) M. Delling et al. NATURE
- The polycystin complex mediates Wnt/Ca2+ signalling
- (2016) Seokho Kim et al. NATURE CELL BIOLOGY
- Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2)
- (2016) Mariana Grieben et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Heterotrimeric G protein signaling in polycystic kidney disease
- (2016) Taketsugu Hama et al. PHYSIOLOGICAL GENOMICS
- Function and regulation of TRPP2 ion channel revealed by a gain-of-function mutant
- (2016) Mahmud Arif Pavel et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2)
- (2016) Mariana Grieben et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The Role of G-Protein-Coupled Receptor Proteolysis Site Cleavage of Polycystin-1 in Renal Physiology and Polycystic Kidney Disease
- (2016) Marie Trudel et al. Cells
- Intraciliary Calcium Oscillations Initiate Vertebrate Left-Right Asymmetry
- (2015) Shiaulou Yuan et al. CURRENT BIOLOGY
- Altered trafficking and stability of polycystins underlie polycystic kidney disease
- (2014) Yiqiang Cai et al. JOURNAL OF CLINICAL INVESTIGATION
- Novel Functional Complexity of Polycystin-1 by GPS Cleavage In Vivo: Role in Polycystic Kidney Disease
- (2014) A. Kurbegovic et al. MOLECULAR AND CELLULAR BIOLOGY
- Ciliary membrane proteins traffic through the Golgi via a Rabep1/GGA1/Arl3-dependent mechanism
- (2014) Hyunho Kim et al. Nature Communications
- Primary cilia are specialized calcium signalling organelles
- (2013) Markus Delling et al. NATURE
- Sticky Signaling--Adhesion Class G Protein-Coupled Receptors Take the Stage
- (2013) T. Langenhan et al. Science Signaling
- Polycystin-1 binds Par3/aPKC and controls convergent extension during renal tubular morphogenesis
- (2013) Maddalena Castelli et al. Nature Communications
- Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex
- (2012) Yong Yu et al. Nature Communications
- Receptor for Activated C Kinase 1 (RACK1) Inhibits Function of Transient Receptor Potential (TRP)-type Channel Pkd2L1 through Physical Interaction
- (2011) Jungwoo Yang et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural model of the TRPP2/PKD1 C-terminal coiled-coil complex produced by a combined computational and experimental approach
- (2011) J. Zhu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- The cell biology of polycystic kidney disease
- (2010) Hannah C. Chapin et al. JOURNAL OF CELL BIOLOGY
- Identification of a Polycystin-1 Cleavage Product, P100, That Regulates Store Operated Ca2+ Entry through Interactions with STIM1
- (2010) Owen M. Woodward et al. PLoS One
- Polycystins and Primary Cilia: Primers for Cell Cycle Progression
- (2009) Jing Zhou Annual Review of Physiology
- Essential role for the putative S6 inner pore region in the activation gating of the human TRPA1 channel
- (2009) Jan Benedikt et al. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
- Structural and molecular basis of the assembly of the TRPP2/PKD1 complex
- (2009) Yong Yu et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Polycystic Kidney Disease
- (2008) Peter C. Harris et al. Annual Review of Medicine
- Expression Cloning of TMEM16A as a Calcium-Activated Chloride Channel Subunit
- (2008) Björn Christian Schroeder et al. CELL
- TMEM16A confers receptor-activated calcium-dependent chloride conductance
- (2008) Young Duk Yang et al. NATURE
- TMEM16A, A Membrane Protein Associated with Calcium-Dependent Chloride Channel Activity
- (2008) A. Caputo et al. SCIENCE
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