Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Hans Peter Schnebli"'
Autor:
Hans Peter Schnebli, Uwe Heinz, Pierre Acklin, Bernard Faller, Kaspar Hegetschweiler, Rene Lattmann
Publikováno v:
Angewandte Chemie. 111:2733-2736
Einen auserordentlich stabilen 1:2-Komplex [FeL2]3− bildet der Ligand H3L (siehe Formel) mit FeIII. Seine Affinitat fur andere Biometalle ist dagegen vergleichsweise klein. Diese Eigenschaften machen ihn zu einem vielversprechenden Kandidaten fur m
Autor:
Gino Amiconi, Paolo Sarti, Svetlana Tomova, Martino Bolognesi, Hans Peter Schnebli, Enea Menegatti, Francesca Cutruzzolà, Paolo Ascenzi, Donatella Barra
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1161:201-208
Catalytic and inhibitor binding properties of bovine alpha-chymotrypsin, in which the Met-192 residue has been converted by treatment with chloramine T to the sulfoxide derivative (Met(O)192 alpha-chymotrypsin), have been examined relative to the nat
Autor:
Hans Peter Schnebli, Gino Amiconi, Alberto Guaragna, Martino Bolognesi, Patrizia Aducci, Enea Menegatti, Paolo Ascenzi, Alessandro Ballio
Publikováno v:
Journal of Molecular Recognition. 4:113-119
The binding of the recombinant proteinase inhibitor eglin c from the leech Hirudo medicinalis to serine (pro)enzymes belonging to the chymotrypsin and subtilisin families has been investigated from the thermodynamic viewpoint, between pH 4.5 and 9.5
Autor:
Hans Peter Schnebli
Publikováno v:
Annals of the New York Academy of Sciences. 624:212-218
Autor:
Uwe Heinz, Kaspar Hegetschweiler, Pierre Acklin, Hans Peter Schnebli, Bernard Faller, Rene Lattmann
Publikováno v:
Angewandte Chemie International Edition. 38:2568-2570
An exceptionally stable 1:2 complex [FeL2]3− is formed from the ligand H3L and FeIII. In contrast, the affinity of this ligand for other biometals is relatively small. These properties make H3L a highly promising candidate for medical applications
Autor:
Robert F. Hoyt, Ronald G. Crystal, E. Wilson, Hans-Peter Schnebli, C. Vogelmeier, R C Hubbard, G A Fells, Roland Buhl, R. C. Thompson
Publikováno v:
Journal of Applied Physiology. 69:1843-1848
In a variety of lung diseases the respiratory epithelial surface must contend with an increased burden of neutrophil elastase (NE). One candidate for augmenting epithelial anti-NE protection is the secretory leukoprotease inhibitor (SLPI). In vitro e
Autor:
Francesco Frigerio, Hans Peter Schnebli, Giuseppina Gatti, Luciano Antolini, Martino Bolognesi, Alessandro Coda, Gino Amiconi, Paolo Ascenzi, Enea Menegatti, Luisa Pugliese
Publikováno v:
Journal of Molecular Recognition. 3:163-168
The crystal structure of the molecular complex formed by bovine alpha-chymotrypsin and the recombinant serine proteinase inhibitor eglin c from Hirudo medicinalis has been solved using monoclinic crystals of the complex, reported previously. Four cir
Autor:
Hanspeter Nick, Hans-Peter Schnebli, Robert C. Thompson, Wayne H. Anderson, Alessandro Probst, Alain Gast, Stephen P. Eisenberg
Publikováno v:
American Review of Respiratory Disease. 141:889-894
Secretory leukocyte proteinase inhibitor (SLPI) is a potent elastase, trypsin, and chymotrypsin inhibitor occurring in all mucous secretions. Its inhibitory potency and profile suggested that it may become a therapeutic adjuvant in diseases where pro
Autor:
Hanspeter, Nick, Agnes, Wong, Pierre, Acklin, Bernard, Faller, Yi, Jin, René, Lattmann, Thomas, Sergejew, Suzanne, Hauffe, Helmut, Thomas, Hans Peter, Schnebli
Publikováno v:
Advances in experimental medicine and biology. 509
Autor:
Yi Jin, Suzanne Hauffe, Rene Lattmann, Agnes Wong, Thomas Sergejew, Bernard Faller, Hans Peter Schnebli, Helmut Thomas, Hanspeter Nick, Pierre Acklin
Publikováno v:
Iron Chelation Therapy ISBN: 9780306467851
Man is unable to actively eliminate iron from the body, once it has been acquired. Toxic and eventually lethal levels of iron accumulate as a result of repeated transfusions, e.g. in s-thalassemia major, or due to excessive dietary iron uptake in ane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39a1417431cdab73562bd67aacc82a32
https://doi.org/10.1007/978-1-4615-0593-8_10
https://doi.org/10.1007/978-1-4615-0593-8_10