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Joachim Grötzinger

Researcher at University of Kiel

Publications -  240
Citations -  11980

Joachim Grötzinger is an academic researcher from University of Kiel. The author has contributed to research in topics: Glycoprotein 130 & Receptor. The author has an hindex of 58, co-authored 240 publications receiving 10903 citations. Previous affiliations of Joachim Grötzinger include Ehime University & RWTH Aachen University.

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A bioactive designer cytokine for human hematopoietic progenitor cell expansion

TL;DR: A fusion protein of sIL-6R and IL-6, linked by a flexible peptide chain, that was expressed to high levels was used to effectively expand human hematopoietic progenitor cells ex vivo in a dose dependent fashion.
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Structural basis of calcification inhibition by α2-HS glycoprotein/fetuin-A - Formation of colloidal calciprotein particles

TL;DR: It is demonstrated that precipitation inhibition by Ahsg is caused by the transient formation of soluble, colloidal spheres, containing Ahsg, calcium, and phosphate, which turn progressively more crystalline and insoluble in a time- and temperature-dependent fashion.
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The IL-6/sIL-6R complex as a novel target for therapeutic approaches.

TL;DR: Preclinical animal disease models have provided strong evidence that specific blockade of IL-6-regulated signalling pathways represents a promising approach for the therapy of these diseases.
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Plasticity and cross-talk of interleukin 6-type cytokines.

TL;DR: Molecular mechanisms of inter-familiar cytokine cross-talk are reviewed which regulate dynamics and strength of IL-6 signal transduction and focus on IL- 6-type cytokine/cytokine receptor plasticity and cross- talk exemplified by the recently identified composite cytokines IL-30/IL-6R and IL-35, the first inter-Familiar IL-8/IL -12 family member.
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Soluble interleukin-15 receptor alpha (IL-15R alpha)-sushi as a selective and potent agonist of IL-15 action through IL-15R beta/gamma. Hyperagonist IL-15 x IL-15R alpha fusion proteins.

TL;DR: It is demonstrated that a recombinant, soluble sushi domain of IL-15R alpha, which bears most of the binding affinity forIL-15, behaves as a potent IL- 15 agonist by enhancing its binding and biological effects through the IL-14R beta/gamma heterodimer, whereas it does not affect IL-13 binding and function of the tripartite IL-16R alpha/beta/gammas membrane receptor.