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A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form.

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A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form. / Hampe, Wolfgang; Urny, J; Franke, I; Hoffmeister-Ullerich, S A; Herrmann, D; Petersen, C M; Lohmann, J; Schaller, H C.

in: DEVELOPMENT, Jahrgang 126, Nr. 18, 18, 1999, S. 4077-4086.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Hampe, W, Urny, J, Franke, I, Hoffmeister-Ullerich, SA, Herrmann, D, Petersen, CM, Lohmann, J & Schaller, HC 1999, 'A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form.', DEVELOPMENT, Jg. 126, Nr. 18, 18, S. 4077-4086. <http://www.ncbi.nlm.nih.gov/pubmed/10457016?dopt=Citation>

APA

Hampe, W., Urny, J., Franke, I., Hoffmeister-Ullerich, S. A., Herrmann, D., Petersen, C. M., Lohmann, J., & Schaller, H. C. (1999). A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form. DEVELOPMENT, 126(18), 4077-4086. [18]. http://www.ncbi.nlm.nih.gov/pubmed/10457016?dopt=Citation

Vancouver

Hampe W, Urny J, Franke I, Hoffmeister-Ullerich SA, Herrmann D, Petersen CM et al. A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form. DEVELOPMENT. 1999;126(18):4077-4086. 18.

Bibtex

@article{ae91ca9d27e0490daef85f76ddfb3f42,
title = "A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form.",
abstract = "The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.",
author = "Wolfgang Hampe and J Urny and I Franke and Hoffmeister-Ullerich, {S A} and D Herrmann and Petersen, {C M} and J Lohmann and Schaller, {H C}",
year = "1999",
language = "Deutsch",
volume = "126",
pages = "4077--4086",
journal = "DEVELOPMENT",
issn = "0950-1991",
publisher = "Company of Biologists Ltd",
number = "18",

}

RIS

TY - JOUR

T1 - A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form.

AU - Hampe, Wolfgang

AU - Urny, J

AU - Franke, I

AU - Hoffmeister-Ullerich, S A

AU - Herrmann, D

AU - Petersen, C M

AU - Lohmann, J

AU - Schaller, H C

PY - 1999

Y1 - 1999

N2 - The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.

AB - The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.

M3 - SCORING: Zeitschriftenaufsatz

VL - 126

SP - 4077

EP - 4086

JO - DEVELOPMENT

JF - DEVELOPMENT

SN - 0950-1991

IS - 18

M1 - 18

ER -