Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Soren Tullin"'
Autor:
Christian T. Madsen, Jan C. Refsgaard, Felix G. Teufel, Sonny K. Kjærulff, Zhe Wang, Guangjun Meng, Carsten Jessen, Petteri Heljo, Qunfeng Jiang, Xin Zhao, Bo Wu, Xueping Zhou, Yang Tang, Jacob F. Jeppesen, Christian D. Kelstrup, Stephen T. Buckley, Søren Tullin, Jan Nygaard-Jensen, Xiaoli Chen, Fang Zhang, Jesper V. Olsen, Dan Han, Mads Grønborg, Ulrik de Lichtenberg
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
Bioactive peptides regulate many physiological functions but progress in discovering them has been slow. Here, the authors use a machine learning framework to predict mammalian peptide candidates from the global and local structure of large-scale tis
Externí odkaz:
https://doaj.org/article/a22e4dc1d677467ea63d53214d5a93bc
Autor:
Anette Sams, Christoph Kalthoff, Akiko Higuchi, Noriyuki Ouchi, Kenneth Walsh, Koji Ohashi, Noyan Gokce, Soren Tullin, Ross Summer, Joseph A. Vita, Jennifer L. Parker, Anette A. Pedersen
Publikováno v:
Journal of Biological Chemistry. 285:6153-6160
It is established that the adipocyte-derived cytokine adiponectin protects against cardiovascular and metabolic diseases, but the effect of this adipokine on macrophage polarization, an important mediator of disease progression, has never been assess
Autor:
Preben H. Olsen, Birgit Sehested Hansen, Phing-How Lou, Soren Tullin, Michael P. Murphy, Martin D. Brand
Publikováno v:
Biochemical Journal. 407:129-140
We have discovered that some weak uncouplers (typified by butylated hydroxytoluene) have a dynamic range of more than 106in vitro: the concentration giving measurable uncoupling is less than one millionth of the concentration causing full uncoupling.
Publikováno v:
Endocrinology. 141:3397-3402
Growth hormone secretagogues (GHSs) are synthetic compounds that induce GH release in several species, including man. The aim of the current study was to identify hypothalamic GHS receptor (GHS-R) agonists. This led to the discovery of adenosine as a
Publikováno v:
Biochemical Journal. 337:211-218
The alpha isoform of protein kinase C (PKCalpha) is a ubiquitous protein kinase, which, upon activation, translocates rapidly from the cytoplasm to the plasma membrane. To follow this translocation, PKCalpha was tagged with a highly fluorescent deriv
Autor:
Wei Gong, Anette A. Pedersen, Yun Liu, Jakob Brandt, Claus Bekker Jeppesen, Soren Tullin, Kirsten Dahl, Jørn Meidahl Petersen, Christoph Kalthoff, Per-Olof Wahlund, Grith Skytte Olsen, Bidda Rolin, Thomas N. Krogh, Anette Sams
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e44270 (2012)
PLoS ONE
PLoS ONE
AIMS/HYPOTHESIS: Several studies have shown that adiponectin can lower blood glucose in diabetic mice. The aim of this study was to establish an effective adiponectin production process and to evaluate the anti-diabetic potential of the different adi
Publikováno v:
Cellular signalling. 16(8)
We report on a novel method to monitor changes in intracellular cAMP concentration ([cAMP] i ) within intact living cells using a chimeric fusion of the catalytic subunit of cAMP-dependent protein kinase to green fluorescent protein (PKAcat-GFP). In
Publikováno v:
Molecular pharmacology. 59(1)
The highly potent vanilloid receptor (VR) agonist resiniferatoxin has been radiolabeled with 125I, and the pharmacology to the cloned rodent VR, VR1, and the endogenous VR in rat spinal cord membranes has been characterized. [125I]RTX binding to huma
Autor:
Søren Tullin, Anette Sams, Jakob Brandt, Kirsten Dahl, Wei Gong, Claus Bekker Jeppesen, Thomas Nylandsted Krogh, Grith Skytte Olsen, Yun Liu, Anette Amstrup Pedersen, Jørn Meidahl Petersen, Bidda Rolin, Per-Olof Wahlund, Christoph Kalthoff
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e44270 (2012)
AIMS/HYPOTHESIS: Several studies have shown that adiponectin can lower blood glucose in diabetic mice. The aim of this study was to establish an effective adiponectin production process and to evaluate the anti-diabetic potential of the different adi
Externí odkaz:
https://doaj.org/article/e93a27552f644947bcfb9fc8a38f3cd6