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Christian Kersten

Apotheker

Name	Christian Kersten
Zeit	2017- (Wirkungsdaten)
Ort	Deutschland
Akademischer Grad bzw. Titel	Dr. rer. nat. (Diss. Fachbereich Chemie, Pharmazie und Geowissenschaften, Univ. Mainz) (2017)
Beruf	Apotheker (charakteristischer Beruf)
Variante	Frank Christian Kersten C. Kersten
Datensatztyp	Person
GND-Nummer	1138135593
Datensatz-ID	1138135593
Beteiligt an alle anzeigen Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes Investigation of the compatibility between warheads and peptidomimetic sequences of protease inhibitors — a comprehensive reactivity and selectivity study Thermodynamic characterization of a macrocyclic Zika virus NS2B/NS3 protease inhibitor and its acyclic analogs Peptidomimetic inhibitors of TMPRSS2 block SARS-CoV-2 infection in cell culture BANΔIT: B’‐Factor Analysis for Drug Design and Structural Biology Structure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2 Front Cover: Structure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2 (2/2021) BANΔIT: B’-factor analysis for drug design and structural biology Structure-activity relationships of benzamides and isoindolines designed as SARS-CoV protease inhibitors effective against SARS-CoV-2 Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes Selectivity determining features in N-myristoyltransferases – a model system for drug targets with conserved binding sites

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Katalog der Deutschen Nationalbibliothek

Christian Kersten

Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

Investigation of the compatibility between warheads and peptidomimetic sequences of protease inhibitors — a comprehensive reactivity and selectivity study

Thermodynamic characterization of a macrocyclic Zika virus NS2B/NS3 protease inhibitor and its acyclic analogs

Peptidomimetic inhibitors of TMPRSS2 block SARS-CoV-2 infection in cell culture

BANΔIT: B’‐Factor Analysis for Drug Design and Structural Biology

Structure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2

Front Cover: Structure‐Activity Relationships of Benzamides and Isoindolines Designed as SARS‐CoV Protease Inhibitors Effective against SARS‐CoV‐2 (2/2021)

BANΔIT: B’-factor analysis for drug design and structural biology

Structure-activity relationships of benzamides and isoindolines designed as SARS-CoV protease inhibitors effective against SARS-CoV-2

Structure, interdomain dynamics, and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

Structure, interdomain dynamics and pH-dependent autoactivation of pro-rhodesain, the main lysosomal cysteine protease from African trypanosomes

Selectivity determining features in N-myristoyltransferases – a model system for drug targets with conserved binding sites