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David H. Presky

Researcher at Hoffmann-La Roche

Publications -  50
Citations -  6328

David H. Presky is an academic researcher from Hoffmann-La Roche. The author has contributed to research in topics: Interleukin 12 & Receptor. The author has an hindex of 28, co-authored 50 publications receiving 6199 citations. Previous affiliations of David H. Presky include University of Texas Health Science Center at Houston.

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THE INTERLEUKIN-12/INTERLEUKIN-12-RECEPTOR SYSTEM: Role in Normal and Pathologic Immune Responses

TL;DR: Inhibition of IL-12 synthesis or activity may be beneficial in diseases associated with pathologic Th1 responses, such as multiple sclerosis or Crohn's disease, and administration of recombinant IL- 12 may have utility in the treatment of diseasesassociated with pathological Th2 responses such as allergic disorders and asthma.
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Selective Expression of an Interleukin-12 Receptor Component by Human T Helper 1 Cells

TL;DR: The selective expression and regulation of the IL-12R β2 subunit may help to understand the basis of Th1/Th2 differentiation and may provide therapeutic options for altering the Th1-Th2 balance in several immuno-pathological conditions such as autoimmune diseases and allergies.
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A functional interleukin 12 receptor complex is composed of two β-type cytokine receptor subunits

TL;DR: It is demonstrated that the functional high-affinity IL-12R is composed of at least two beta-type cytokine receptor subunits, each independently exhibiting a low affinity for IL- 12.
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Mouse interleukin‐12 (IL‐12) p40 homodimer: a potent IL‐12 antagonist

TL;DR: The results suggest that the majority of the structural determinants required for binding of IL‐12 to its receptor are contained within the p40 subunit, but p35 is required for signaling, and (p40)2 may be a suitable IL‐ 12 antagonist for studying the role ofIL‐12 in various immune responses in vivo as well as in vitro.
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Insight into E-selectin/ligand interaction from the crystal structure and mutagenesis of the lec/EGF domains

TL;DR: The three-dimensional structure of the ligand-binding region of human E-selectin has been determined and reveals limited contact between the two domains and a coordination of Ca2+ not predicted from other C-type lectins.