Daniel Gau

Daniel Gau

Frankfurt/Rhein-Main
3042 Follower:innen 500+ Kontakte

Info

Passionate intrapreneur with versatile experience in R&D and CMC, focusing on ATMPs…

Aktivitäten

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Berufserfahrung

  • Eisbach Bio GmbH Grafik

    Eisbach Bio GmbH

    Munich, Bavaria, Germany

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    Zoersel, Flemish Region, Belgium

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    Seeheim

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    Oberdorf Nidwalden, Nidwalden, Switzerland

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    Bad Homburg vor der Höhe, Hessen, Deutschland

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    Oberdorf NW Switzerland

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    Frankfurt Area, Germany

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    Darmstadt Area, Germany

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    Darmstadt Area, Germany

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    Darmstadt Area, Germany

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    New Jersey, USA

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    Heidelberg Area, Germany

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    Ludwigsburg, Germany

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    Heidelberg Area, Germany

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    Heidelberg Area, Germany

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    Munich Area, Germany

Ausbildung

  • Université Louis Pasteur (Strasbourg I)

Bescheinigungen und Zertifikate

Veröffentlichungen

  • Evaluation of ultrasound velocity measurements for estimating protease activities using casein as substrate.

    Biotechnol Lett.

    Ultrasonic resonator technology (URT) was compared with the well established UV-Vis/ninhydrin assay to estimate protease activities in defined buffer systems. Hydrolysis of casein was measured using subtilisin, trypsin, halophilic protease from Haloferax mediterranei and Bacillus lentus alkaline protease. Sensitivity, reproducibility, working range as well as the limit of detection and the limit of quantification were comparable for both methods. Salt concentrations (0.5 M NaCl) interfered with…

    Ultrasonic resonator technology (URT) was compared with the well established UV-Vis/ninhydrin assay to estimate protease activities in defined buffer systems. Hydrolysis of casein was measured using subtilisin, trypsin, halophilic protease from Haloferax mediterranei and Bacillus lentus alkaline protease. Sensitivity, reproducibility, working range as well as the limit of detection and the limit of quantification were comparable for both methods. Salt concentrations (0.5 M NaCl) interfered with the URT method. The quantification of protease activity by URT was possible when the product concentration measured by the UV-Vis/ninhydrin assay was correlated to the corresponding ultrasonic velocity signals.

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  • Glucocorticoid receptor function in hepatocytes is essential to promote postnatal body growth.

    Genes Dev.

    Mice carrying a hepatocyte-specific inactivation of the glucorticoid receptor (GR) gene show a dramatic reduction in body size. Growth hormone signaling mediated by the Stat5 transcription factors is impaired. We show that Stat5 proteins physically interact with GR and GR is present in vivo on Stat5-dependent IGF-I and ALS regulatory regions. Interestingly, mice with a DNA-binding-deficient GR but an unaltered ability to interact with STAT5 (GR(dim/dim)) have a normal body size and normal…

    Mice carrying a hepatocyte-specific inactivation of the glucorticoid receptor (GR) gene show a dramatic reduction in body size. Growth hormone signaling mediated by the Stat5 transcription factors is impaired. We show that Stat5 proteins physically interact with GR and GR is present in vivo on Stat5-dependent IGF-I and ALS regulatory regions. Interestingly, mice with a DNA-binding-deficient GR but an unaltered ability to interact with STAT5 (GR(dim/dim)) have a normal body size and normal levels of Stat5-dependent mRNAs. These findings strongly support the model in which GR acts as a coactivator for Stat5-dependent transcription upon GH stimulation and reveal an essential role of hepatic GR in the control of body growth.

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  • Phosphorylation of CREB Ser142 regulates light-induced phase shifts of the circadian clock.

    Neuron. 2002 Apr 11;34(2):245-53.

    Biological rhythms are driven in mammals by a central circadian clock located in the suprachiasmatic nucleus (SCN). Light-induced phase shifting of this clock is correlated with phosphorylation of CREB at Ser133 in the SCN. Here, we characterize phosphorylation of CREB at Ser142 and describe its contribution to the entrainment of the clock. In the SCN, light and glutamate strongly induce CREB Ser142 phosphorylation. To determine the physiological relevance of phosphorylation at Ser142, we…

    Biological rhythms are driven in mammals by a central circadian clock located in the suprachiasmatic nucleus (SCN). Light-induced phase shifting of this clock is correlated with phosphorylation of CREB at Ser133 in the SCN. Here, we characterize phosphorylation of CREB at Ser142 and describe its contribution to the entrainment of the clock. In the SCN, light and glutamate strongly induce CREB Ser142 phosphorylation. To determine the physiological relevance of phosphorylation at Ser142, we generated a mouse mutant, CREB(S142A), lacking this phosphorylation site. Light-induced phase shifts of locomotion and expression of c-Fos and mPer1 in the SCN are significantly attenuated in CREB(S142A) mutants. Our findings provide genetic evidence that CREB Ser142 phosphorylation is involved in the entrainment of the mammalian clock and reveal a novel phosphorylation-dependent regulation of CREB activity.

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Sprachen

  • English

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  • German

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  • French

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  • Spanish

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