Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Jochen Hecky"'
Publikováno v:
Knorpeltherapie: Praxisleitfaden der AG Klinische Geweberegeneration der DGOU
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e3affc86bd320b34bb642fd4dc1f6695
https://doi.org/10.1515/9783110419887-026
https://doi.org/10.1515/9783110419887-026
Autor:
Jochen Hecky, Tim Kükenshöner, Padmarupa Dondapati, Christina Räuber, Katja M. Arndt, Janina Speck, Kristian M. Müller, Christoph Niemöller, Paula Schleberger, Katelyn J Mueller
Publikováno v:
Protein Engineering Design and Selection. 26:225-242
The twin-arginine translocation (TAT) pathway of the bacterial cytoplasmic membrane mediates translocation only of proteins that accomplished a native-like conformation. We deploy this feature in modular selection systems for directed evolution, in w
Autor:
Hagen Schmal, Norbert P. Südkamp, Gian M. Salzmann, Philipp Niemeyer, Jochen Hecky, Jan M. Pestka
Publikováno v:
Archives of Orthopaedic and Trauma Surgery. 131:779-789
Autologous chondrocyte implantation (ACI) is a well-established therapeutic option for the treatment of cartilage defects of the knee joint. Since information concerning the cellular aspects of ACI is still limited, the aim of the present study was t
Publikováno v:
Biochemistry. 51(24)
The stability of proteins is paramount for their therapeutic and industrial use and, thus, is a major task for protein engineering. Several types of chemical and physical stabilities are desired, and discussion revolves around whether each stability
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 352
Improving enzyme stability is a highly desirable design step in generating enzymes able to function under extreme conditions, such as elevated temperatures, while having the additional benefit of being less susceptible to cleavage by proteases. For t
Improving enzyme stability is a highly desirable design step in generating enzymes able to function under extreme conditions, such as elevated temperatures, while having the additional benefit of being less susceptible to cleavage by proteases. For t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::be6429bfe12413599a2fdd59e8fd1b5d
https://doi.org/10.1385/1-59745-187-8:275
https://doi.org/10.1385/1-59745-187-8:275
Autor:
Jochen Hecky, Kristian M. Müller
Publikováno v:
Biochemistry. 44(38)
The choice of protein for use in technical and medical applications is limited by stability issues, making understanding and engineering of stability key. Here, enzyme destabilization by truncation was combined with directed evolution to create stabl