Fibrocystin interacts with CAML, a protein involved in Ca2+ signaling (Q24338821)

GOA release 2020-03-11

author name string

Junko Nagano

1

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Kenichiro Kitamura

2

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Kristine M Hujer

3

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Christopher J Ward

4

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Richard J Bram

5

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Ulrich Hopfer

6

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Kimio Tomita

7

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Chunfa Huang

8

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R Tyler Miller

Biochemical and Biophysical Research Communications

9

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language of work or name

English

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publication date

16 December 2005

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published in

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volume

338

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issue

2

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page(s)

880-9

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cites work

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PKHD1 protein encoded by the gene for autosomal recessive polycystic kidney disease associates with basal bodies and primary cilia in renal epithelial cells

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A hydrophobic domain of Ca2+-modulating cyclophilin ligand modulates calcium influx signaling in T lymphocytes

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Parallel activation of phosphatidylinositol 4-kinase and phospholipase C by the extracellular calcium-sensing receptor

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Calcium restriction allows cAMP activation of the B-Raf/ERK pathway, switching cells to a cAMP-dependent growth-stimulated phenotype

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Polyductin, the PKHD1 gene product, comprises isoforms expressed in plasma membrane, primary cilium, and cytoplasm

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NF-AT activation induced by a CAML-interacting member of the tumor necrosis factor receptor superfamily

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Kaposi's sarcoma-associated herpesvirus mitochondrial K7 protein targets a cellular calcium-modulating cyclophilin ligand to modulate intracellular calcium concentration and inhibit apoptosis

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