Fragmentbasiertes Design von p97-Liganden: Identifizierung von Startstrukturen zur Entwicklung von Protein-Protein-Interaktionsinhibitoren für die SHP-Bindestelle der AAA+ ATPase p97
- Alternative title
-
Fragment-based design of p97-ligands: Identification of starting points for the development of protein-protein-interaction inhibitors targeting the SHP-binding site of the AAA+ ATPase p97
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Deutsch
- Notes
-
Würzburg, Universität Würzburg, Dissertation, 2021
- Keyword
-
Proteine
Bindestelle
Inhibitor
Ligand
Arzneimitteldesign
Wirkstoffdesign
- Event
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Veröffentlichung
- (where)
-
Würzburg
- (who)
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Universität Würzburg
- (when)
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2021
- Creator
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Bothe, Sebastian
- Contributor
- DOI
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10.25972/OPUS-23911
- URN
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urn:nbn:de:bvb:20-opus-239112
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:57 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Bothe, Sebastian
- Sotriffer, Christoph
- Schindelin, Hermann
- Universität Würzburg
Time of origin
- 2021
Other Objects (12)
UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
The AAA-ATPase p97 in mitosis and fertilization
AAA+ ATPase chaperone p97/VCPFAF2 governs basal pexophagy
Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97
Characterizing ATP processing by the AAA+ protein p97 at the atomic level
Analysis of a novel allosteric inhibitor of the AAA+ ATPase p97 and its mechanism
The AAA-ATPase p97 and its cofactors in regulatory degradation of substrate proteins after DNA damage or replication stress
Analysis of the functions of the AAA-ATPase p97 in DNA double-strand break repair
Functional characterization of a novel p97:ASPL protein complex
Tab.I. p.97 - Metallschnitte
VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase
Die UBX-Domäne von UBXD1 organisiert die Ubiquitinbindung am C-Terminus der AAA-ATPase VCP/p97 zum proteasomalen Abbau
UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
The AAA-ATPase p97 in mitosis and fertilization
AAA+ ATPase chaperone p97/VCPFAF2 governs basal pexophagy
Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97
Characterizing ATP processing by the AAA+ protein p97 at the atomic level
Analysis of a novel allosteric inhibitor of the AAA+ ATPase p97 and its mechanism
The AAA-ATPase p97 and its cofactors in regulatory degradation of substrate proteins after DNA damage or replication stress
Analysis of the functions of the AAA-ATPase p97 in DNA double-strand break repair
Functional characterization of a novel p97:ASPL protein complex
Tab.I. p.97 - Metallschnitte
VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase
Die UBX-Domäne von UBXD1 organisiert die Ubiquitinbindung am C-Terminus der AAA-ATPase VCP/p97 zum proteasomalen Abbau
UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97
The AAA-ATPase p97 in mitosis and fertilization
AAA+ ATPase chaperone p97/VCPFAF2 governs basal pexophagy
Fragment screening using biolayer interferometry reveals ligands targeting the SHP-motif binding site of the AAA+ ATPase p97
Characterizing ATP processing by the AAA+ protein p97 at the atomic level
Analysis of a novel allosteric inhibitor of the AAA+ ATPase p97 and its mechanism
The AAA-ATPase p97 and its cofactors in regulatory degradation of substrate proteins after DNA damage or replication stress
Analysis of the functions of the AAA-ATPase p97 in DNA double-strand break repair
Functional characterization of a novel p97:ASPL protein complex
Tab.I. p.97 - Metallschnitte
VAPB/ALS8 interacts with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase