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John Ziebuhr

Mikrobiologe

Name	John Ziebuhr
Time	ca. 20./21. Jahrhundert (Date of birth and death)
Place	Gießen (Wirkungsort) Deutschland
Gender	männlich
Academic degree	Prof. Dr. med.
Profession	Mikrobiologe (characteristic profession)
Variant	J. Ziebuhr
Related	Justus-Liebig-Universität Gießen
Further information	Dissertation, Universität Würzburg, 1996
Source	Promotionsakte
Record type	Person
GND-Identifier	1263818862
Record ID	1263818862
Involved in show all Peptidyl nitroalkene inhibitors of main protease rationalized by computational and crystallographic investigations as antivirals against SARS-CoV-2 Reply to: The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein Multi-level inhibition of coronavirus replication by chemical ER stress 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) Structure-activity relationships of benzamides and isoindolines designed as SARS-CoV protease inhibitors effective against SARS-CoV-2 Screening of Electrophilic Compounds Yields an Aziridinyl Peptide as New Active‐Site Directed SARS‐CoV Main Protease Inhibitor. Expression der 3C-like-Proteinase des humanen Coronavirus HCV 229E

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John Ziebuhr

Peptidyl nitroalkene inhibitors of main protease rationalized by computational and crystallographic investigations as antivirals against SARS-CoV-2

Reply to: The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein

Multi-level inhibition of coronavirus replication by chemical ER stress

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)

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

Screening of Electrophilic Compounds Yields an Aziridinyl Peptide as New Active‐Site Directed SARS‐CoV Main Protease Inhibitor.

Expression der 3C-like-Proteinase des humanen Coronavirus HCV 229E