Glutamate receptors: variation in structure-function coupling

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Glutamate receptors : variation in structure-function coupling. / Kristensen, Anders S; Geballe, Matthew T; Snyder, James P; Traynelis, Stephen F.

In: Trends in Pharmacological Sciences, Vol. 27, No. 2, 02.2006, p. 65-9.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kristensen, AS, Geballe, MT, Snyder, JP & Traynelis, SF 2006, 'Glutamate receptors: variation in structure-function coupling', Trends in Pharmacological Sciences, vol. 27, no. 2, pp. 65-9. https://doi.org/10.1016/j.tips.2005.12.005

APA

Kristensen, A. S., Geballe, M. T., Snyder, J. P., & Traynelis, S. F. (2006). Glutamate receptors: variation in structure-function coupling. Trends in Pharmacological Sciences, 27(2), 65-9. https://doi.org/10.1016/j.tips.2005.12.005

Vancouver

Kristensen AS, Geballe MT, Snyder JP, Traynelis SF. Glutamate receptors: variation in structure-function coupling. Trends in Pharmacological Sciences. 2006 Feb;27(2):65-9. https://doi.org/10.1016/j.tips.2005.12.005

Author

Kristensen, Anders S ; Geballe, Matthew T ; Snyder, James P ; Traynelis, Stephen F. / Glutamate receptors : variation in structure-function coupling. In: Trends in Pharmacological Sciences. 2006 ; Vol. 27, No. 2. pp. 65-9.

Bibtex

@article{6531585824d74789ac93110303a36ea6,
title = "Glutamate receptors: variation in structure-function coupling",
abstract = "Fast excitatory synaptic transmission in the CNS relies almost entirely on the neurotransmitter glutamate and its family of ion channel receptors. An appreciation of the coupling between agonist binding and channel opening has advanced rapidly during the past five years, largely as a result of new structural information about the agonist-binding site. Recent studies suggest that despite many structural similarities different family members use different mechanisms to translate agonist binding into channel opening.",
keywords = "Animals, Humans, Models, Molecular, Receptors, Glutamate, Structure-Activity Relationship, Synaptic Transmission",
author = "Kristensen, {Anders S} and Geballe, {Matthew T} and Snyder, {James P} and Traynelis, {Stephen F}",
year = "2006",
month = feb,
doi = "10.1016/j.tips.2005.12.005",
language = "English",
volume = "27",
pages = "65--9",
journal = "Trends in Pharmacological Sciences",
issn = "0165-6147",
publisher = "Elsevier Ltd. * Trends Journals",
number = "2",

}

RIS

TY - JOUR

T1 - Glutamate receptors

T2 - variation in structure-function coupling

AU - Kristensen, Anders S

AU - Geballe, Matthew T

AU - Snyder, James P

AU - Traynelis, Stephen F

PY - 2006/2

Y1 - 2006/2

N2 - Fast excitatory synaptic transmission in the CNS relies almost entirely on the neurotransmitter glutamate and its family of ion channel receptors. An appreciation of the coupling between agonist binding and channel opening has advanced rapidly during the past five years, largely as a result of new structural information about the agonist-binding site. Recent studies suggest that despite many structural similarities different family members use different mechanisms to translate agonist binding into channel opening.

AB - Fast excitatory synaptic transmission in the CNS relies almost entirely on the neurotransmitter glutamate and its family of ion channel receptors. An appreciation of the coupling between agonist binding and channel opening has advanced rapidly during the past five years, largely as a result of new structural information about the agonist-binding site. Recent studies suggest that despite many structural similarities different family members use different mechanisms to translate agonist binding into channel opening.

KW - Animals

KW - Humans

KW - Models, Molecular

KW - Receptors, Glutamate

KW - Structure-Activity Relationship

KW - Synaptic Transmission

U2 - 10.1016/j.tips.2005.12.005

DO - 10.1016/j.tips.2005.12.005

M3 - Journal article

C2 - 16406088

VL - 27

SP - 65

EP - 69

JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

SN - 0165-6147

IS - 2

ER -

ID: 156344707