Zobrazeno 1 - 10
of 106
pro vyhledávání: '"Siegmund, Reissmann"'
Autor:
Andrea-Anneliese Keller, Franziska Mussbach, Reinhard Breitling, Peter Hemmerich, Buerk Schaefer, Stefan Lorkowski, Siegmund Reissmann
Publikováno v:
Pharmaceuticals, Vol 6, Iss 2, Pp 184-203 (2013)
Modulating signaling pathways for research and therapy requires either suppression or expression of selected genes or internalization of proteins such as enzymes, antibodies, nucleotide binding proteins or substrates including nucleoside phosphates a
Externí odkaz:
https://doaj.org/article/2ae3b329f7d14aaeae08cb0c1b969b7f
Autor:
Siegmund Reissmann, M. P. Filatova
Publikováno v:
Journal of Peptide Science. 27
Cell-penetrating peptides (CPPs) can transport various cargoes through membranes of live cells. Since the first generations of CPPs suffered from insufficient cell and tissue selectivity, stability against proteases, and escape from endosomes, a new
Autor:
Ulf Teichgräber, Siegmund Reissmann, M. P. Filatova, Dmitri O. Koroev, Ingrid Hilger, Olga M. Volpina, Steffi Lange, Felista L. Tansi, Christina Schumann
Publikováno v:
Journal of Cellular Biochemistry. 120:6528-6541
In the last three decades, many new cell-penetrating peptides (CPPs) were developed that exhibited enhanced cell selectivity. Thus, we aimed to validate the tumor cell selectivity of peptides from this new generation, namely fragments mini-crotamine
Autor:
Andrea-Anneliese Keller, Stefan Lorkowski, Peter Hemmerich, Reinhard Breitling, Andreas Licht, Berith Scheiding, Siegmund Reissmann
Publikováno v:
Journal of cellular biochemistry. 120(1)
Cell-penetrating peptides (CPPs) are used to internalize different cargoes, including DNA, into live mammalian and plant cells. Despite many cells being easily transfected with this approach, other cells are rather "difficult" or "hard to transfect,"
Autor:
Siegmund Reissmann, Christoph Kaether, Eric Kallweit, Christina Schumann, Ingrid Hilger, Katarina Kappe, Felista Tansi
Publikováno v:
Journal of Cellular Biochemistry. 116:1222-1231
The internalization of near-infrared fluorescently labeled cargos into living cells and tissues allows a highly sensitive detection without interference from skin, porphins or other fluorescent cell and tissue compounds. In this study, the uptake of
Autor:
Siegmund Reissmann
Publikováno v:
Journal of Peptide Science. 20:760-784
The penetration of polar or badly soluble compounds through a cell membrane into live cells requires mechanical support or chemical helpers. Cell-penetrating peptides (CPPs) are very promising chemical helpers. Because of their low cytotoxicity and f
Autor:
Peter Hemmerich, Stefan Lorkowski, Maria Braun, Andrea-Anneliese Keller, Katarina Kappe, Buerk Schaefer, Reinhard Breitling, Berith Wittig, Siegmund Reissmann
Publikováno v:
Journal of Cellular Biochemistry. 115:243-252
Cell-penetrating peptides (CPPs) are used to transport peptides, proteins, different types of ribonucleic acids (or mimics of these molecules), and DNA into live cells, both plant and mammalian. Leishmania belongs to the class of protozoa having, in
Autor:
Stefan Lorkowski, Franziska Mussbach, Andrea-Anneliese Keller, Peter Hemmerich, Buerk Schaefer, Reinhard Breitling, Siegmund Reissmann
Publikováno v:
Pharmaceuticals, Vol 6, Iss 2, Pp 184-203 (2013)
Pharmaceuticals; Volume 6; Issue 2; Pages: 184-203
Pharmaceuticals
Pharmaceuticals; Volume 6; Issue 2; Pages: 184-203
Pharmaceuticals
Modulating signaling pathways for research and therapy requires either suppression or expression of selected genes or internalization of proteins such as enzymes, antibodies, nucleotide binding proteins or substrates including nucleoside phosphates a
Autor:
Julia Linnemann, Reinhard Breitling, Siegmund Reissmann, Stefan Lorkowski, Christian Boehme, Frank Bieber
Publikováno v:
bchm. 394:695-701
The stepwise synthesis of thymidine triphosphate (TTP) requires a kinase for phosphorylation in the last step. Because pyruvate kinase (PK) using phosphoenolpyruvate (PEP) as substrate can regenerate adenosine triphosphate and phosphorylate thymidine
Publikováno v:
Journal of Peptide Science. 16:403-413
The protein tyrosine phosphatase SHP-1 plays an important role in many physiological and pathophysiological processes. This phosphatase is activated through binding of ligands to its SH2-domains, mainly to the N-terminal one. Based on a theoretical d