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Svilenov, Hristo 
ORCID: https://orcid.org/0000-0001-5863-9569 und Winter, Gerhard
(April 2020):
Formulations that suppress aggregation during long-term storage of a bispecific antibody are characterized by high refoldability and colloidal stability.
In: Journal of Pharmaceutical Sciences
[PDF, 4MB]
ORCID: https://orcid.org/0000-0001-5863-9569 und Winter, Gerhard
(April 2020):
Formulations that suppress aggregation during long-term storage of a bispecific antibody are characterized by high refoldability and colloidal stability.
In: Journal of Pharmaceutical Sciences
[PDF, 4MB]
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]
Krieg, Dennis; Svilenov, Hristo; Gitter, Julian H. und Winter, Gerhard
(2020):
Overcoming challenges in co-formulation of proteins with contradicting stability profiles - EPO plus G-CSF.
In: European Journal of Pharmaceutical Sciences, Bd. 141, 105073
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]
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]
Augustijn, Dillen; Mahapatra, Sujata; Streicher, Werner; Svilenov, Hristo; Kulakova, Ahna; Pohl, Christin und Rinnan, Asmund
(2019):
Novel non-linear curve fitting to resolve protein unfolding transitions in intrinsic fluorescence differential scanning fluorimetry.
In: European Journal of Pharmaceutics and Biopharmaceutics, Bd. 142: S. 506-517
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]