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Eine Ebene höher- EU-Projekte (714)
- Horizon 2020 (624)
- Marie Skłodowska Curie Actions (82)
- Marie Skłodowska-Curie Innovative Training Networks (42)
- 675074: PIPPI - Protein-excipient Interactions and Protein-Protein Interactions in formulation (9)
- Marie Skłodowska-Curie Innovative Training Networks (42)
- Marie Skłodowska Curie Actions (82)
- Horizon 2020 (624)
Anzahl der Publikationen auf dieser Ebene: 9
2022
Roche, Aisling; Gentiluomo, Lorenzo; Sibanda, Nicole; Roessner, Dierk; Friess, Wolfgang; Trainoff, Steven P. und Curtis, Robin
(2022):
Towards an improved prediction of concentrated antibody solution viscosity using the Huggins coefficient.
In: Journal of Colloid and Interface Science, Bd. 607, Nr. 2: S. 1813-1824
2020
Svilenov, Hristo 
ORCID: https://orcid.org/0000-0001-5863-9569; Kulakova, Alina; Zalar, Matja; Golovanov, Alexander P.; Harris, Pernille und Winter, Gerhard
(Januar 2020):
Orthogonal Techniques to Study the Effect of pH, Sucrose, and Arginine Salts on Monoclonal Antibody Physical Stability and Aggregation During Long-Term Storage.
In: Journal of Pharmaceutical Sciences, Bd. 109, Nr. 1: S. 584-594
[PDF, 2MB]
ORCID: https://orcid.org/0000-0001-5863-9569; Kulakova, Alina; Zalar, Matja; Golovanov, Alexander P.; Harris, Pernille und Winter, Gerhard
(Januar 2020):
Orthogonal Techniques to Study the Effect of pH, Sucrose, and Arginine Salts on Monoclonal Antibody Physical Stability and Aggregation During Long-Term Storage.
In: Journal of Pharmaceutical Sciences, Bd. 109, Nr. 1: S. 584-594
[PDF, 2MB]
Tosstorff, Andreas ORCID: https://orcid.org/0000-0002-4969-3667; Menzen, Tim und Winter, Gerhard ORCID: https://orcid.org/0000-0002-7413-6627
(Januar 2020):
Exploring Chemical Space for new Substances to stabilize a therapeutic Monoclonal Antibody.
In: Journal of Pharmaceutical Sciences
[PDF, 1MB]
ORCID: https://orcid.org/0000-0002-4969-3667; Menzen, Tim und Winter, Gerhard ORCID: https://orcid.org/0000-0002-7413-6627
(Januar 2020):
Exploring Chemical Space for new Substances to stabilize a therapeutic Monoclonal Antibody.
In: Journal of Pharmaceutical Sciences
[PDF, 1MB]
2019
Gentiluomo, Lorenzo; Roessner, Dierk; Augustijn, Dillen; Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569; Kulakova, Alina; Mahapatra, Sujata; Winter, Gerhard; Streicher, Werner; Rinnan, Asmund; Peters, Günther; Harris, Pernille und Friess, Wolfgang
(August 2019):
Application of interpretable artificial neural networks to early monoclonal antibodies development.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 141: S. 81-89
[PDF, 1MB]
ORCID: https://orcid.org/0000-0001-5863-9569; Kulakova, Alina; Mahapatra, Sujata; Winter, Gerhard; Streicher, Werner; Rinnan, Asmund; Peters, Günther; Harris, Pernille und Friess, Wolfgang
(August 2019):
Application of interpretable artificial neural networks to early monoclonal antibodies development.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 141: S. 81-89
[PDF, 1MB]
Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569 und Winter, Gerhard
(1. Mai 2019):
Rapid sample-saving biophysical characterisation and long-term storage stability of liquid interferon alpha2a formulations Is there a correlation?
In: International Journal of Pharmaceutics, Bd. 562: S. 42-50
[PDF, 1MB]
ORCID: https://orcid.org/0000-0001-5863-9569 und Winter, Gerhard
(1. Mai 2019):
Rapid sample-saving biophysical characterisation and long-term storage stability of liquid interferon alpha2a formulations Is there a correlation?
In: International Journal of Pharmaceutics, Bd. 562: S. 42-50
[PDF, 1MB]
Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569 und Winter, Gerhard
(April 2019):
The ReFOLD assay for protein formulation studies and prediction of protein aggregation during long-term storage.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 137: S. 131-139
[PDF, 2MB]
ORCID: https://orcid.org/0000-0001-5863-9569 und Winter, Gerhard
(April 2019):
The ReFOLD assay for protein formulation studies and prediction of protein aggregation during long-term storage.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 137: S. 131-139
[PDF, 2MB]
Tosstorff, Andreas ORCID: https://orcid.org/0000-0002-4969-3667; Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569; Peters, Günther H. J.; Harris, Pernille und Winter, Gerhard ORCID: https://orcid.org/0000-0002-7413-6627
(12. September 2019):
Structure-based Discovery of a new Protein-Aggregation Breaking Excipient.
In: European Journal of Pharmaceutics and Biopharmaceutics
[HTML, 1MB]
ORCID: https://orcid.org/0000-0002-4969-3667; Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569; Peters, Günther H. J.; Harris, Pernille und Winter, Gerhard ORCID: https://orcid.org/0000-0002-7413-6627
(12. September 2019):
Structure-based Discovery of a new Protein-Aggregation Breaking Excipient.
In: European Journal of Pharmaceutics and Biopharmaceutics
[HTML, 1MB]
2018
Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569; Gentiluomo, Lorenzo; Friess, Wolfgang; Roessner, Dierk und Winter, Gerhard
(Dezember 2018):
A New Approach to Study the Physical Stability of Monoclonal Antibody Formulations Dilution From a Denaturant.
In: Journal of Pharmaceutical Sciences, Bd. 107, Nr. 12: S. 3007-3013
[PDF, 1MB]
ORCID: https://orcid.org/0000-0001-5863-9569; Gentiluomo, Lorenzo; Friess, Wolfgang; Roessner, Dierk und Winter, Gerhard
(Dezember 2018):
A New Approach to Study the Physical Stability of Monoclonal Antibody Formulations Dilution From a Denaturant.
In: Journal of Pharmaceutical Sciences, Bd. 107, Nr. 12: S. 3007-3013
[PDF, 1MB]
Svilenov, Hristo ORCID: https://orcid.org/0000-0001-5863-9569; Markoja, Uros und Winter, Gerhard
(April 2018):
Isothermal chemical denaturation as a complementary tool to overcome limitations of thermal differential scanning fluorimetry in predicting physical stability of protein formulations.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 125: S. 106-113
[PDF, 1MB]
ORCID: https://orcid.org/0000-0001-5863-9569; Markoja, Uros und Winter, Gerhard
(April 2018):
Isothermal chemical denaturation as a complementary tool to overcome limitations of thermal differential scanning fluorimetry in predicting physical stability of protein formulations.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 125: S. 106-113
[PDF, 1MB]