Computationally Empowered Workflow Identifies Novel Covalent Allosteric Binders for KRAS G12C
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
Computationally Empowered Workflow Identifies Novel Covalent Allosteric Binders for KRAS G12C ; volume:15 ; number:10 ; year:2020 ; pages:827-832 ; extent:6
ChemMedChem ; 15, Heft 10 (2020), 827-832 (gesamt 6)
- Urheber
-
Mortier, Jérémie
Friberg, Anders
Badock, Volker
Moosmayer, Dieter
Schroeder, Jens
Steigemann, Patrick
Siegel, Franziska
Gradl, Stefan
Bauser, Marcus
Hillig, Roman C.
Briem, Hans
Eis, Knut
Bader, Benjamin
Nguyen, Duy
Christ, Clara D.
- DOI
-
10.1002/cmdc.201900727
- URN
-
urn:nbn:de:101:1-2022062512384711766473
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:36 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Mortier, Jérémie
- Friberg, Anders
- Badock, Volker
- Moosmayer, Dieter
- Schroeder, Jens
- Steigemann, Patrick
- Siegel, Franziska
- Gradl, Stefan
- Bauser, Marcus
- Hillig, Roman C.
- Briem, Hans
- Eis, Knut
- Bader, Benjamin
- Nguyen, Duy
- Christ, Clara D.
Ähnliche Objekte (12)
The energetic and allosteric landscape for KRAS inhibition
Covalent-allosteric inhibitors to achieve akt isoform-selectivity
Covalent‐Allosteric Inhibitors to Achieve Akt Isoform‐Selectivity
A β-Lactone for Covalent Inhibition of KRAS G12S
Covalent allosteric inhibitors of Akt generated using a click fragment approach
Covalent Allosteric Inhibitors of Akt Generated Using a Click Fragment Approach
Drugging the Undruggable using Irreversible Covalent K-Ras G12C Inhibitors
Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme
KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
Dimethyl fumarate is an allosteric covalent inhibitor of the p90 ribosomal S6 kinases
RAS-ON inhibition overcomes clinical resistance to KRAS G12C-OFF covalent blockade
Electrically empowered microcomb laser
The energetic and allosteric landscape for KRAS inhibition
Covalent-allosteric inhibitors to achieve akt isoform-selectivity
Covalent‐Allosteric Inhibitors to Achieve Akt Isoform‐Selectivity
A β-Lactone for Covalent Inhibition of KRAS G12S
Covalent allosteric inhibitors of Akt generated using a click fragment approach
Covalent Allosteric Inhibitors of Akt Generated Using a Click Fragment Approach
Drugging the Undruggable using Irreversible Covalent K-Ras G12C Inhibitors
Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme
KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
Dimethyl fumarate is an allosteric covalent inhibitor of the p90 ribosomal S6 kinases
RAS-ON inhibition overcomes clinical resistance to KRAS G12C-OFF covalent blockade
Electrically empowered microcomb laser
The energetic and allosteric landscape for KRAS inhibition
Covalent-allosteric inhibitors to achieve akt isoform-selectivity
Covalent‐Allosteric Inhibitors to Achieve Akt Isoform‐Selectivity
A β-Lactone for Covalent Inhibition of KRAS G12S
Covalent allosteric inhibitors of Akt generated using a click fragment approach
Covalent Allosteric Inhibitors of Akt Generated Using a Click Fragment Approach
Drugging the Undruggable using Irreversible Covalent K-Ras G12C Inhibitors
Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme
KRAS-specific inhibition using a DARPin binding to a site in the allosteric lobe
Dimethyl fumarate is an allosteric covalent inhibitor of the p90 ribosomal S6 kinases
RAS-ON inhibition overcomes clinical resistance to KRAS G12C-OFF covalent blockade