TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage (Q34463859)

2 August 2017

title

TRP-ML1 is a lysosomal monovalent cation channel that undergoes proteolytic cleavage (English)

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2 August 2017

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Kirill Kiselyov

1

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2 August 2017

Jin Chen

2

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2 August 2017

Youssef Rbaibi

3

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2 August 2017

Daniel Oberdick

4

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Sandra Tjon-Kon-Sang

5

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2 August 2017

Nikolay Shcheynikov

6

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2 August 2017

Shmuel Muallem

7

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2 August 2017

Abigail Soyombo

8

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2 August 2017

language of work or name

English

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publication date

27 October 2005

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Journal of Biological Chemistry

2 August 2017

published in

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2 August 2017

volume

280

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2 August 2017

issue

52

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2 August 2017

page(s)

43218-43223

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The molecular basis of mucolipidosis type IV.

2 August 2017

cites work

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21 January 2018

Mucolipidosis type IV.

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Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel

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Cloning of the gene encoding a novel integral membrane protein, mucolipidin-and identification of the two major founder mutations causing mucolipidosis type IV

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Identification and characterization of polycystin-2, the PKD2 gene product

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Expression of the Ca2+-selective cation channel TRPV6 in human prostate cancer: a novel prognostic marker for tumor progression

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Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway

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Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel.

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Mucolipidosis type IV: novel MCOLN1 mutations in Jewish and non-Jewish patients and the frequency of the disease in the Ashkenazi Jewish population

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Golgi alpha-mannosidase II deficiency in vertebrate systems: implications for asparagine-linked oligosaccharide processing in mammals

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Signals for sorting of transmembrane proteins to endosomes and lysosomes

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Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro

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Cloning and expression of a novel mammalian homolog of Drosophila transient receptor potential (Trp) involved in calcium entry secondary to activation of receptors coupled by the Gq class of G protein

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Outer pore architecture of a Ca2+-selective TRP channel

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Functional links between mucolipin-1 and Ca2+-dependent membrane trafficking in mucolipidosis IV

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Identifiers

DOI

10.1074/JBC.M508210200

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2 August 2017

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