Extreme vetting of dopamine receptor oligomerization

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Extreme vetting of dopamine receptor oligomerization. / Asher, Wesley B.; Mathiasen, Signe; Holsey, Michael D.; Grinnell, Steven G.; Lambert, Nevin A.; Javitch, Jonathan A.

Receptors. Humana Press, 2017. p. 99-127 (Receptors, Vol. 33).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Asher, WB, Mathiasen, S, Holsey, MD, Grinnell, SG, Lambert, NA & Javitch, JA 2017, Extreme vetting of dopamine receptor oligomerization. in Receptors. Humana Press, Receptors, vol. 33, pp. 99-127. https://doi.org/10.1007/978-3-319-60174-8_5

APA

Asher, W. B., Mathiasen, S., Holsey, M. D., Grinnell, S. G., Lambert, N. A., & Javitch, J. A. (2017). Extreme vetting of dopamine receptor oligomerization. In Receptors (pp. 99-127). Humana Press. Receptors Vol. 33 https://doi.org/10.1007/978-3-319-60174-8_5

Vancouver

Asher WB, Mathiasen S, Holsey MD, Grinnell SG, Lambert NA, Javitch JA. Extreme vetting of dopamine receptor oligomerization. In Receptors. Humana Press. 2017. p. 99-127. (Receptors, Vol. 33). https://doi.org/10.1007/978-3-319-60174-8_5

Author

Asher, Wesley B. ; Mathiasen, Signe ; Holsey, Michael D. ; Grinnell, Steven G. ; Lambert, Nevin A. ; Javitch, Jonathan A. / Extreme vetting of dopamine receptor oligomerization. Receptors. Humana Press, 2017. pp. 99-127 (Receptors, Vol. 33).

Bibtex

@inbook{b0af8e5e3637458c990a9d445f359590,
title = "Extreme vetting of dopamine receptor oligomerization",
abstract = "Numerous reports have emerged over the past two decades suggesting that dopamine receptors form dimeric and/or higher-order oligomeric complexes. The existence of these complexes and their functional properties are of significant interest, as they may provide strategies for developing novel therapeutics that selectively target dopamine receptor complexes with the potential for more refined cellular therapeutics and reduced side-effects. However, there is still great debate and controversy surrounding the structural and functional aspects of dopamine receptor oligomers as well as their physiological relevance. Much of the uncertainty stems from the methodologies employed to understand these complexes, which have clear limitations and/or are not yet fully understood. Herein, we provide an overview of the literature focusing mainly on dopamine receptor homomeric complexes and selected dopamine receptor heteromeric complexes with the goal of providing a critical discussion of the methodology and the logic of the scientific inferences in this body of work.",
keywords = "BRET, Co-immunoprecipitation, Dimerization, Dopamine receptors, FRET, Methodology, Oligomerization, Signaling crosstalk, Structure",
author = "Asher, {Wesley B.} and Signe Mathiasen and Holsey, {Michael D.} and Grinnell, {Steven G.} and Lambert, {Nevin A.} and Javitch, {Jonathan A.}",
note = "Publisher Copyright: {\textcopyright} Springer International Publishing AG 2017.",
year = "2017",
doi = "10.1007/978-3-319-60174-8_5",
language = "English",
series = "Receptors",
publisher = "Humana Press",
pages = "99--127",
booktitle = "Receptors",
address = "United States",

}

RIS

TY - CHAP

T1 - Extreme vetting of dopamine receptor oligomerization

AU - Asher, Wesley B.

AU - Mathiasen, Signe

AU - Holsey, Michael D.

AU - Grinnell, Steven G.

AU - Lambert, Nevin A.

AU - Javitch, Jonathan A.

N1 - Publisher Copyright: © Springer International Publishing AG 2017.

PY - 2017

Y1 - 2017

N2 - Numerous reports have emerged over the past two decades suggesting that dopamine receptors form dimeric and/or higher-order oligomeric complexes. The existence of these complexes and their functional properties are of significant interest, as they may provide strategies for developing novel therapeutics that selectively target dopamine receptor complexes with the potential for more refined cellular therapeutics and reduced side-effects. However, there is still great debate and controversy surrounding the structural and functional aspects of dopamine receptor oligomers as well as their physiological relevance. Much of the uncertainty stems from the methodologies employed to understand these complexes, which have clear limitations and/or are not yet fully understood. Herein, we provide an overview of the literature focusing mainly on dopamine receptor homomeric complexes and selected dopamine receptor heteromeric complexes with the goal of providing a critical discussion of the methodology and the logic of the scientific inferences in this body of work.

AB - Numerous reports have emerged over the past two decades suggesting that dopamine receptors form dimeric and/or higher-order oligomeric complexes. The existence of these complexes and their functional properties are of significant interest, as they may provide strategies for developing novel therapeutics that selectively target dopamine receptor complexes with the potential for more refined cellular therapeutics and reduced side-effects. However, there is still great debate and controversy surrounding the structural and functional aspects of dopamine receptor oligomers as well as their physiological relevance. Much of the uncertainty stems from the methodologies employed to understand these complexes, which have clear limitations and/or are not yet fully understood. Herein, we provide an overview of the literature focusing mainly on dopamine receptor homomeric complexes and selected dopamine receptor heteromeric complexes with the goal of providing a critical discussion of the methodology and the logic of the scientific inferences in this body of work.

KW - BRET

KW - Co-immunoprecipitation

KW - Dimerization

KW - Dopamine receptors

KW - FRET

KW - Methodology

KW - Oligomerization

KW - Signaling crosstalk

KW - Structure

UR - http://www.scopus.com/inward/record.url?scp=85051712989&partnerID=8YFLogxK

U2 - 10.1007/978-3-319-60174-8_5

DO - 10.1007/978-3-319-60174-8_5

M3 - Book chapter

AN - SCOPUS:85051712989

T3 - Receptors

SP - 99

EP - 127

BT - Receptors

PB - Humana Press

ER -

ID: 311722496