Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Anne Sophie Schillinger"'
Autor:
Shailesh Narawane, Adnan Budnjo, Torgils Fossen, Bengt Erik Haug, Nathalie Reuter, Cédric Grauffel, Anne-Sophie Schillinger
Publikováno v:
Journal of Medicinal Chemistry. 57:9396-9408
Neutrophil serine proteases, proteinase 3 (PR3) and human neutrophil elastase (HNE), are considered as targets for chronic inflammatory diseases. Despite sharing high sequence similarity, the two enzymes have different substrate specificities and fun
Publikováno v:
Biochimica et biophysica acta. Biomembranes. 1859(7)
The human phospholipid scramblase 1 (SCR) distributes lipids non-selectively between the cellular membrane leaflets. SCR has long been thought to be mostly localized in the cytoplasm (amino acids 1–287) and anchored to the membrane via the insertio
Publikováno v:
Biophysical Journal. 110(3)
In contrast to lipid-specific flippases and floppases, scramblase proteins distribute lipids non-selectively between the lipid bilayer leaflets by a passive and much slower process, thereby destroying the intrinsic bilayer asymmetry. Unfortunately, t
Autor:
Anne Sophie Schillinger, Roger L. Miesfeld, James E. Pennington, Jun Isoe, Jorge Zamora, Michelle C. Brandon
Publikováno v:
Insect Biochemistry and Molecular Biology. 38:916-922
Blood meal digestion in mosquitoes occurs in two phases, an early phase that is translationally-regulated, and a late phase that is transcriptionally-regulated. Early trypsin is a well-characterized serine endoprotease that is representative of other
Autor:
Hanif Muhammad Khan, Anne-Sophie Schillinger, Nathalie Reuter, Øyvind Halskau, Cédric Grauffel
Publikováno v:
Biochimica et Biophysica Acta-Biomembranes
Neutrophil serine proteases Proteinase 3 (PR3) and human neutrophil elastase (HNE) are homologous antibiotic serine proteases of the polymorphonuclear neutrophils. Despite sharing a 56% sequence identity they have been shown to have different functio
Publikováno v:
Biophysical Journal. 102:497a
Proteinase 3 (PR3) is a serine protease of the neutrophils involved in inflammation processes. Its membrane expression is a risk factor for chronic inflammatory diseases. Experimental data led to divergent hypotheses on the binding mode of PR3 to the