Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Sven Amrhein"'
Publikováno v:
Biotechnology and Bioengineering. 114:1170-1183
The aggregation of proteins became one of the major challenges in the development of biopharmaceu-ticals since the formation of aggregates can affect drug quality and immunogenicity. However, aggregation mechanisms are highly complex and the investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd15bdba666323fd5aad07d36b1b0c5e
https://doi.org/10.1002/bit.25949
https://doi.org/10.1002/bit.25949
Publikováno v:
Engineering in Life Sciences. 16:532-537
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49c3ed8ff9f2b097044323ce03f9b7a3
https://doi.org/10.1002/elsc.201500179
https://doi.org/10.1002/elsc.201500179
Publikováno v:
Biotechnology Progress. 32:346-354
Hydrophobic interaction chromatography (HIC) is one of the most frequently used purification methods in downstream processing of biopharmaceuticals. During HIC, salts are the governing additives contributing to binding strength, binding capacity, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e98c1d2ce750c80acde252ceb944110
https://doi.org/10.1002/btpr.2166
https://doi.org/10.1002/btpr.2166
Publikováno v:
Biotechnology and Bioengineering. 112:2485-2494
The surface hydrophobicity of a protein is an important factor for its interactions in solution and thus the outcome of its production process. Yet most of the methods are not able to evaluate the influence of these hydrophobic interactions under nat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ba9ed887fa491b9748d25338efb3ec20
https://doi.org/10.1002/bit.25677
https://doi.org/10.1002/bit.25677
Publikováno v:
Journal of Chromatography A. 1367:68-77
Over the last decade, the use of design of experiment approaches in combination with fully automated high throughput (HTP) compatible screenings supported by robotic liquid handling stations (LHS), adequate fast analytics and data processing has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::720ec8c78b39e9045048231e751c5686
https://doi.org/10.1016/j.chroma.2014.09.042
https://doi.org/10.1016/j.chroma.2014.09.042
Publikováno v:
The Journal of Physical Chemistry B. 118:1707-1714
It has been shown that molecular dynamics (MD) simulations are a powerful tool to generate knowledge about complex interactions in the field of bioprocess technologies at the atomic level. In this field, one of the most important nonspecific interact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4e1991ead385dd8ed8a2f1c904d6958
https://doi.org/10.1021/jp407390f
https://doi.org/10.1021/jp407390f
Publikováno v:
Chemical Engineering Science. 104:945-956
The egg white protein avidin is known for its strong binding to biotin. Because of various applications in bioanalytics and biopharmaceutical industries, there is a great interest in the manufacturing of highly purified avidin. For the first time, th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::417ea8e20927bd5f0d4faa19d6b7a4f3
https://doi.org/10.1016/j.ces.2013.10.008
https://doi.org/10.1016/j.ces.2013.10.008
Publikováno v:
Biotechnology and bioengineering. 114(6)
The aggregation of proteins became one of the major challenges in the development of biopharmaceu-ticals since the formation of aggregates can affect drug quality and immunogenicity. However, aggregation mechanisms are highly complex and the investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d8ed3b2ee40ef4eea1c278dacfa11159
https://pubmed.ncbi.nlm.nih.gov/26853436
https://pubmed.ncbi.nlm.nih.gov/26853436
Publikováno v:
Biotechnology and bioengineering. 112(12)
The surface hydrophobicity of a protein is an important factor for its interactions in solution and thus the outcome of its production process. Yet most of the methods are not able to evaluate the influence of these hydrophobic interactions under nat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::04e2ae820a286889c49162585f4b9e01
https://pubmed.ncbi.nlm.nih.gov/26074500
https://pubmed.ncbi.nlm.nih.gov/26074500