Cation channel regulation by COOH-terminal cytoplasmic tail of polycystin-1: mutational and functional analysis (Q40747347)

23 September 2017

title

Cation channel regulation by COOH-terminal cytoplasmic tail of polycystin-1: mutational and functional analysis (English)

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23 September 2017

David H Vandorpe

1

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23 September 2017

Sabine Wilhelm

2

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23 September 2017

Lianwei Jiang

3

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23 September 2017

Oxana Ibraghimov-Beskrovnaya

4

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23 September 2017

Marina N Chernova

5

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23 September 2017

Alan K Stuart-Tilley

6

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23 September 2017

Seth L Alper

7

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23 September 2017

publication date

28 February 2002

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23 September 2017

published in

Physiological Genomics

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23 September 2017

volume

8

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23 September 2017

issue

2

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23 September 2017

page(s)

87-98

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Molecular genetics and pathogenesis of autosomal dominant polycystic kidney disease

23 September 2017

cites work

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The structure of a PKD domain from polycystin-1: implications for polycystic kidney disease

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Transport function of the naturally occurring pathogenic polycystin-2 mutant, R742X.

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Polycystin-2, the protein mutated in autosomal dominant polycystic kidney disease (ADPKD), is a Ca2+-permeable nonselective cation channel

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Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins

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Strong homophilic interactions of the Ig-like domains of polycystin-1, the protein product of an autosomal dominant polycystic kidney disease gene, PKD1

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21 January 2018

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21 January 2018

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PKD1 interacts with PKD2 through a probable coiled-coil domain

21 January 2018

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The molecular basis of focal cyst formation in human autosomal dominant polycystic kidney disease type I.

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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The cytoplasmic C-terminal fragment of polycystin-1 regulates a Ca2+-permeable cation channel

21 January 2018

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Polycystin-2 is a novel cation channel implicated in defective intracellular Ca(2+) homeostasis in polycystic kidney disease

21 January 2018

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21 January 2018

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The polycystin-1 C-type lectin domain binds carbohydrate in a calcium-dependent manner, and interacts with extracellular matrix proteins in vitro

21 January 2018

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21 January 2018

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10.1152/PHYSIOLGENOMICS.00092.2001

21 January 2018

Identifiers

DOI

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23 September 2017

1 reference