New molecular mechanisms on the activation of TRPM2 channels by oxidative stress and ADP-ribose (Q36846822)

16 August 2017

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title

New molecular mechanisms on the activation of TRPM2 channels by oxidative stress and ADP-ribose (English)

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16 August 2017

Mustafa Naziroğlu

1

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16 August 2017

12 June 2007

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16 August 2017

Neurochemical Research

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16 August 2017

32

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16 August 2017

11

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16 August 2017

1990-2001

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https://scigraph.springernature.com/pub.10.1007/s11064-007-9386-x

16 August 2017

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Accumulation of free ADP-ribose from mitochondria mediates oxidative stress-induced gating of TRPM2 cation channels

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Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels

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Hydrogen peroxide and ADP-ribose induce TRPM2-mediated calcium influx and cation currents in microglia.

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Amyloid beta-peptide(1-42) and hydrogen peroxide-induced toxicity are mediated by TRPM2 in rat primary striatal cultures

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Critical intracellular Ca2+ dependence of transient receptor potential melastatin 2 (TRPM2) cation channel activation

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Extracellular-added ADP-ribose increases intracellular free Ca2+ concentration through Ca2+ release from stores, but not through TRPM2-mediated Ca2+ entry, in rat beta-cell line RIN-5F.

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Sites of the NUDT9-H domain critical for ADP-ribose activation of the cation channel TRPM2.

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Response to ADP-ribose by activation of TRPM2 in the CRI-G1 insulinoma cell line

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TRPM2 is an ion channel that modulates hematopoietic cell death through activation of caspases and PARP cleavage.

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12 December 2020

10.1007/S11064-007-9386-X

Identifiers

DOI

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16 August 2017

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PubMed ID

17562166