Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Maya Hammami"'
Autor:
Folker Schwalm, Daniela Meyer, Wolfgang Garten, Eva Schilling, Joanna Baron, Hans-Dieter Klenk, Yi Guan, Eva Böttcher-Friebertshäuser, Deborah Mayoli-Nüssle, Maya Hammami, Carolin Tarnow, Torsten Steinmetzer
Publikováno v:
Journal of Virology. 87:1811-1820
Influenza A viruses of the subtype H9N2 circulate worldwide and have become highly prevalent in poultry in many countries. Moreover, they are occasionally transmitted to humans, raising concern about their pandemic potential. Influenza virus infectiv
Autor:
Gerhard Klebe, Andreas Heine, Sebastian Wagner, Alexander Maiwald, Maya Hammami, Torsten Steinmetzer
Publikováno v:
Journal of enzyme inhibition and medicinal chemistry. 31(sup1)
The type II transmembrane serine protease matriptase is a potential target for anticancer therapy and might be involved in cartilage degradation in osteoarthritis or inflammatory skin disorders. Starting from previously described nonspecific thrombin
Autor:
Jürgen Bajorath, Michael Gütschow, Torsten Steinmetzer, Mihiret T. Sisay, Eva Maurer, Marit Stirnberg, Maya Hammami
Publikováno v:
Journal of Medicinal Chemistry. 53:5523-5535
As recently discovered, matriptase-2, a type II transmembrane serine protease, plays a crucial role in body iron homeostasis by down-regulating hepcidin expression, which results in increased iron levels. Thus, matriptase-2 represents a novel target
Autor:
Wolfgang Garten, Frank Sielaff, Eva Böttcher-Friebertshäuser, Torsten Steinmetzer, Daniela Meyer, Maya Hammami
Publikováno v:
The Biochemical journal. 452(2)
TMPRSS2 (transmembrane serine proteinase 2) is a multidomain type II transmembrane serine protease that cleaves the surface glycoprotein HA (haemagglutinin) of influenza viruses with a monobasic cleavage site, which is a prerequisite for virus fusion
Publikováno v:
ChemMedChem. 8:173-173
Autor:
Gerhard Klebe, Michael Gütschow, Torsten Steinmetzer, Andreas Heine, Eva Maurer, Eggert Rühmann, Maya Hammami
Publikováno v:
MedChemComm. 3:807
New 3-amidinophenylalanine-derived matriptase inhibitors were developed and tested against the related trypsin-like serine proteases matriptase-2, thrombin and factor Xa. The strongest matriptase inhibition was found for compounds containing an N-ter