Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Petra Engele"'
Autor:
Monika Cserjan-Puschmann, Nico Lingg, Petra Engele, Christina Kröß, Julian Loibl, Andreas Fischer, Florian Bacher, Anna-Carina Frank, Christoph Öhlknecht, Cécile Brocard, Chris Oostenbrink, Matthias Berkemeyer, Rainer Schneider, Gerald Striedner, Alois Jungbauer
Publikováno v:
Biomolecules, Vol 10, Iss 12, p 1592 (2020)
Caspase-2 is the most specific protease of all caspases and therefore highly suitable as tag removal enzyme creating an authentic N-terminus of overexpressed tagged proteins of interest. The wild type human caspase-2 is a dimer of heterodimers genera
Externí odkaz:
https://doaj.org/article/2d01827ae641474f8a84268f9ca5864a
Autor:
Bernhard Sprenger, Christina Kröß, Sonja Katz, Rainer Schneider, Chris Oostenbrink, Petra Engele, Christoph Öhlknecht
Publikováno v:
Journal of Chemical Information and Modeling. 61:1193-1203
Rational-design methods have proven to be a valuable toolkit in the field of protein design. Numerical approaches such as free-energy calculations or QM/MM methods are fit to widen the understanding of a protein-sequence space but require large amoun
Autor:
Nico Lingg, Petra Engele, Monika Cserjan-Puschmann, Cécile Brocard, Gerald Striedner, Matthias Berkemeyer, Alois Jungbauer, Rainer Schneider, Andreas Fischer, Christina Kröß
Publikováno v:
Journal of Chemical Technology & Biotechnology. 96:1515-1522
BACKGROUND: Recombinant proteins produced for use as biopharmaceuticals need to harbor their native N‐terminus. A drawback in expression of recombinant proteins as fusion proteins with an affinity fusion‐tag is that enzymatic or chemical processi
Autor:
Nico Lingg, Christina Kröß, Petra Engele, Christoph Öhlknecht, Christoph Köppl, Andreas Fischer, Bettina Lier, Julian Loibl, Bernhard Sprenger, Jakob Liu, Patrick Scheidl, Matthias Berkemeyer, Wolfgang Buchinger, Cécile Brocard, Gerald Striedner, Chris Oostenbrink, Rainer Schneider, Alois Jungbauer, Monika Cserjan-Puschmann
Publikováno v:
New biotechnology. 71
Fusion protein technologies improve the expression and purification of recombinant proteins, but the removal of the tags involved requires specific proteases. The circularly permuted caspase-2 (cpCasp2) with its specific cleavage site, efficiently ge
Autor:
Nico Lingg, Christina Kröß, Bernhard Sprenger, Drazen Petrov, Rainer Schneider, Andreas Fischer, Christoph Öhlknecht, Petra Engele, Chris Oostenbrink
Publikováno v:
Proteins
The N‐terminal cleavage of fusion tags to restore the native N‐terminus of recombinant proteins is a challenging task and up to today, protocols need to be optimized for different proteins individually. Within this work, we present a novel protea
Autor:
Magdalena Baier, Bettina Lier, Bernhard Sprenger, Alois Jungbauer, Rainer Schneider, Petra Engele, Andreas Fischer, Christoph Öhlknecht, Christina Kröß, Nico Lingg, Chris Oostenbrink, Gerald Striedner, Monika Cserjan-Puschmann
Publikováno v:
The Journal of Biological Chemistry
Proteases serve as important tools in biotechnology and as valuable drugs or drug targets. Efficient protein engineering methods to study and modulate protease properties are thus of great interest for a plethora of applications. We established PROFI
Autor:
Christoph, Öhlknecht, Sonja, Katz, Christina, Kröß, Bernhard, Sprenger, Petra, Engele, Rainer, Schneider, Chris, Oostenbrink
Publikováno v:
Journal of Chemical Information and Modeling
Rational-design methods have proven to be a valuable toolkit in the field of protein design. Numerical approaches such as free-energy calculations or QM/MM methods are fit to widen the understanding of a protein-sequence space but require large amoun
Autor:
Rainer Schneider, Cécile Brocard, Florian Bacher, Alois Jungbauer, Anna-Carina Frank, Nico Lingg, Petra Engele, Christoph Öhlknecht, Chris Oostenbrink, Julian Loibl, Gerald Striedner, Andreas Fischer, Matthias Berkemeyer, Monika Cserjan-Puschmann, Christina Kröß
Publikováno v:
Biomolecules
Volume 10
Issue 12
Biomolecules, Vol 10, Iss 1592, p 1592 (2020)
Volume 10
Issue 12
Biomolecules, Vol 10, Iss 1592, p 1592 (2020)
Caspase-2 is the most specific protease of all caspases and therefore highly suitable as tag removal enzyme creating an authentic N-terminus of overexpressed tagged proteins of interest. The wild type human caspase-2 is a dimer of heterodimers genera
Autor:
Drazen Petrov, Rainer Schneider, Nico Lingg, Chris Oostenbrink, Christoph Öhlknecht, Christina Kröß, Petra Engele, Bernhard Sprenger, Andreas Fischer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fed4eedafe655bdd808c6d53d1d06b35
https://doi.org/10.1002/prot.25950/v2/response1
https://doi.org/10.1002/prot.25950/v2/response1