Molecular properties of the CRF receptor

Joachim Spiess; Frank M. Dautzenberg; Sabine Sydow; Richard L. Hauger; Andreas Rühmann; Thomas Blank; Jelena Radulovic

doi:10.1016/S1043-2760(98)00037-X

Molecular properties of the CRF receptor

Joachim Spiess
, Frank M. Dautzenberg
, Sabine Sydow
, Richard L. Hauger
, Andreas Rühmann
, Thomas Blank
, Jelena Radulovic

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

42 Scopus citations

Abstract

Research into the biology of corticotropin-releasing factor (CRF) has been intensified significantly by the structural characterization of the CRF receptor (CRF-R). Two receptor subtypes, CRF-R1 and CRF-R2, and three functional splice variants of CRF-R2 have been discovered. It appears that ligand binding requires interaction of the N-terminal domain with one or two other extracellular domains of the CRF-R. In contrast to the mammalian CRF- R1, the frog CRF-R1 discriminates between naturally occurring CRF-like peptides.

Original language	English (US)
Pages (from-to)	140-145
Number of pages	6
Journal	Trends in Endocrinology and Metabolism
Volume	9
Issue number	4
DOIs	https://doi.org/10.1016/S1043-2760(98)00037-X
State	Published - Dec 1 1998
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

ASJC Scopus subject areas

Endocrinology, Diabetes and Metabolism
Endocrinology

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10.1016/S1043-2760(98)00037-X

Cite this

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title = "Molecular properties of the CRF receptor",

abstract = "Research into the biology of corticotropin-releasing factor (CRF) has been intensified significantly by the structural characterization of the CRF receptor (CRF-R). Two receptor subtypes, CRF-R1 and CRF-R2, and three functional splice variants of CRF-R2 have been discovered. It appears that ligand binding requires interaction of the N-terminal domain with one or two other extracellular domains of the CRF-R. In contrast to the mammalian CRF- R1, the frog CRF-R1 discriminates between naturally occurring CRF-like peptides.",

author = "Joachim Spiess and Dautzenberg, \{Frank M.\} and Sabine Sydow and Hauger, \{Richard L.\} and Andreas R{\"u}hmann and Thomas Blank and Jelena Radulovic",

year = "1998",

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doi = "10.1016/S1043-2760(98)00037-X",

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TY - JOUR

T1 - Molecular properties of the CRF receptor

AU - Spiess, Joachim

AU - Dautzenberg, Frank M.

AU - Sydow, Sabine

AU - Hauger, Richard L.

AU - Rühmann, Andreas

AU - Blank, Thomas

AU - Radulovic, Jelena

PY - 1998/12/1

Y1 - 1998/12/1

N2 - Research into the biology of corticotropin-releasing factor (CRF) has been intensified significantly by the structural characterization of the CRF receptor (CRF-R). Two receptor subtypes, CRF-R1 and CRF-R2, and three functional splice variants of CRF-R2 have been discovered. It appears that ligand binding requires interaction of the N-terminal domain with one or two other extracellular domains of the CRF-R. In contrast to the mammalian CRF- R1, the frog CRF-R1 discriminates between naturally occurring CRF-like peptides.

AB - Research into the biology of corticotropin-releasing factor (CRF) has been intensified significantly by the structural characterization of the CRF receptor (CRF-R). Two receptor subtypes, CRF-R1 and CRF-R2, and three functional splice variants of CRF-R2 have been discovered. It appears that ligand binding requires interaction of the N-terminal domain with one or two other extracellular domains of the CRF-R. In contrast to the mammalian CRF- R1, the frog CRF-R1 discriminates between naturally occurring CRF-like peptides.

UR - https://www.scopus.com/pages/publications/0031778124

UR - https://www.scopus.com/pages/publications/0031778124#tab=citedBy

U2 - 10.1016/S1043-2760(98)00037-X

DO - 10.1016/S1043-2760(98)00037-X

M3 - Review article

C2 - 18406257

AN - SCOPUS:0031778124

SN - 1043-2760

VL - 9

SP - 140

EP - 145

JO - Trends in Endocrinology and Metabolism

JF - Trends in Endocrinology and Metabolism

IS - 4

ER -

Molecular properties of the CRF receptor

Abstract

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