Apo-calmodulin binds with its C-terminal domain to the N-methyl-D-aspartate receptor NR1 C0 region. (Q44608916)

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19 December 2019

title

Apo-calmodulin binds with its C-terminal domain to the N-methyl-D-aspartate receptor NR1 C0 region (English)

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19 December 2019

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19 December 2019

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19 December 2019

Zeynep Akyol

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19 December 2019

Michelle A Merrill

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19 December 2019

Laurel A Faga

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19 December 2019

Olav R Jaren

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19 December 2019

Johannes W Hell

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19 December 2019

language of work or name

English

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publication date

15 October 2003

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Journal of Biological Chemistry

19 December 2019

published in

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19 December 2019

volume

279

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19 December 2019

issue

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19 December 2019

page(s)

2166-2175

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The TiPS/TINS lecture: the molecular biology of mammalian glutamate receptor channels

19 December 2019

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Inactivation of NMDA receptors by direct interaction of calmodulin with the NR1 subunit

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Calmodulin mediates calcium-dependent inactivation of N-methyl-D-aspartate receptors

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Competitive binding of alpha-actinin and calmodulin to the NMDA receptor

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Novel aspects of calmodulin target recognition and activation

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Mutations in paramecium calmodulin indicate functional differences between the C-terminal and N-terminal lobes in vivo

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In vivo Paramecium mutants show that calmodulin orchestrates membrane responses to stimuli

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Phenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorder

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Paramecium calmodulin mutants defective in ion channel regulation can bind calcium and undergo calcium-induced conformational switching.

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Paramecium calmodulin mutants defective in ion channel regulation associate with melittin in the absence of calcium but require it for tertiary collapse

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Calmodulin bifurcates the local Ca2+ signal that modulates P/Q-type Ca2+ channels.

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Ca2+/calmodulin binds to and modulates P/Q-type calcium channels

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Calmodulin supports both inactivation and facilitation of L-type calcium channels.

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Lobe-dependent regulation of ryanodine receptor type 1 by calmodulin.

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Interactions between domains of apo calmodulin alter calcium binding and stability.

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Cyclic AMP-dependent protein kinase and protein kinase C phosphorylate N-methyl-D-aspartate receptors at different sites

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Assembly of Cell Regulatory Systems Through Protein Interaction Domains

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8 Spectroscopic analyses of calmodulin and its interactions

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21 January 2018

Identifiers

DOI

10.1074/JBC.M302542200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:14530275%20AND%20SRC:MED&resulttype=core&format=json

19 December 2019

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