Výsledky vyhledávání - "Frank J. P. Kühn"

Akademický článek

Modulation of activation and inactivation by Ca2+ and 2-APB in the pore of an archetypal TRPM channel from Nematostella vectensis

Autor: Frank J. P. Kühn, Winking Mathis, Kühn Cornelia, Daniel C. Hoffmann, Andreas Lückhoff

Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)

Abstract The archetypal TRPM2-like channel of the sea anemone Nematostella vectensis is gated by ADPR like its human orthologue but additionally exhibits properties of other vertebrate TRPM channels. Thus it can help towards an understanding of gatin

Externí odkaz: https://doaj.org/article/0a0f9940f18d43808c48d95e6093661a

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Species-Specific Regulation of TRPM2 by PI(4,5)P$_{2}$ via the Membrane Interfacial Cavity

Autor: Andreas Lückhoff, Daniel Barth, Frank J. P. Kühn

Publikováno v: International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 4637, p 4637 (2021)
International journal of molecular sciences 22(9), 4637 (2021). doi:10.3390/ijms22094637
Volume 22
Issue 9

International journal of molecular sciences 22(9), 4637 (2021). doi:10.3390/ijms22094637
Published by Molecular Diversity Preservation International, Basel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4b964b27bd00186ac6fb41443bc336a

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Structure-Function Relationship of TRPM2: Recent Advances, Contradictions, and Open Questions

Autor: Frank J. P. Kühn

Publikováno v: International Journal of Molecular Sciences
International journal of molecular sciences 21(18), 6481 (2020). doi:10.3390/ijms21186481
International Journal of Molecular Sciences, Vol 21, Iss 6481, p 6481 (2020)

International journal of molecular sciences 21(18), [1]-16 (2020). doi:10.3390/ijms21186481
Published by Molecular Diversity Preservation International, Basel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a47b10804ca7a1b9d6ec370850b6a9bf

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Akademický článek

Importance of a conserved sequence motif in transmembrane segment S3 for the gating of human TRPM8 and TRPM2.

Autor: Mathis Winking, Daniel C Hoffmann, Cornelia Kühn, Ralf-Dieter Hilgers, Andreas Lückhoff, Frank J P Kühn

Publikováno v: PLoS ONE, Vol 7, Iss 11, p e49877 (2012)

For mammalian TRPM8, the amino acid residues asparagine-799 and aspartate-802 are essential for the stimulation of the channel by the synthetic agonist icilin. Both residues belong to the short sequence motif N-x-x-D within the transmembrane segment

Externí odkaz: https://doaj.org/article/7b4793962f50496aba32786ec1199e52

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Functional importance of NUDT9H domain and N-terminal ADPR-binding pocket in two species variants of vertebrate TRPM2 channels

Autor: Cornelia Kühn, Wiebke Ehrlich, Frank J. P. Kühn, Andreas Lückhoff, Daniel Barth

Publikováno v: Scientific reports 9, 19224 (2019). doi:10.1038/s41598-019-55232-5
Scientific Reports, Vol 9, Iss 1, Pp 1-13 (2019)
Scientific Reports

Scientific reports 9(1), 19224 (2019). doi:10.1038/s41598-019-55232-5
Published by Macmillan Publishers Limited, part of Springer Nature, [London]

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6080d36224d59f8ac1525945ba993c5b

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ADP-Ribose Activates the TRPM2 Channel from the Sea Anemone Nematostella vectensis Independently of the NUDT9H Domain

Autor: Frank J. P. Kühn, Andreas Lückhoff, Mathis Winking, Daniel C. Hoffmann, Cornelia Kühn

Publikováno v: PLoS ONE, Vol 11, Iss 6, p e0158060 (2016)
PLOS ONE 11(6), e0158060 (2016). doi:10.1371/journal.pone.0158060
PLoS ONE

PLoS one 11(6), e0158060 (2016). doi:10.1371/journal.pone.0158060
Published by PLoS, Lawrence, Kan.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17136c5a8a54f95d5e4293ff0018f1c4

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H2O2-induced Ca2+ influx and its inhibition by N-(p-amylcinnamoyl) anthranilic acid in the β-cells: involvement of TRPM2 channels

Autor: Andreas Lückhoff, Amanda Jabin Gustafsson, Mohamed Eweida, Muhammad R. Bari, Frank J. P. Kühn, Sanian Akbar, Md. Shahidul Islam

Publikováno v: Journal of Cellular and Molecular Medicine

Type 2 melastatin-related transient receptor potential channel (TRPM2), a member of the melastatin-related TRP (transient receptor potential) subfamily is a Ca(2+)-permeable channel activated by hydrogen peroxide (H(2)O(2)). We have investigated the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0def5df592536f0e7942f6fc56942d20
http://europepmc.org/articles/PMC4516483

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Role of an N-Terminal Splice Segment in the Activation of the Cation Channel TRPM2 by ADP-Ribose and Hydrogen Peroxide

Autor: Frank J. P. Kühn, Mustafa Nazıroğlu, Cornelia Kühn, Andreas Lückhoff

Publikováno v: Neurochemical Research. 34:227-233

In the dysfunctional splice variant TRPM2-DeltaN, a stretch of 20 amino acids (aa 537-556) is missing within the N-terminal cytosolic tail of the cation channel TRPM2. The DeltaN-stretch overlaps with two IQ-like calmodulin-binding domains. Moreover,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca93433bf88a5ca9c089acc1789fab4f
https://doi.org/10.1007/s11064-008-9755-0

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The Transmembrane Segment S6 Determines Cation versus Anion Selectivity of TRPM2 and TRPM8

Autor: Andreas Lückhoff, Frank J. P. Kühn, Gabriel Knop

Publikováno v: Journal of Biological Chemistry. 282:27598-27609

TRPM2 and TRPM8, closely related members of the transient receptor potential (TRP) family, are cation channels activated by quite different mechanisms. Their transmembrane segments S5 and S6 are highly conserved. To identify common structures in S5 a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d98d4a37154cbe4f3bfa2d87cd3fd4ec
https://doi.org/10.1074/jbc.m702247200

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