Structure‐Based Design of Ultrapotent Tricyclic Ligands for FK506‐Binding Proteins
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Structure‐Based Design of Ultrapotent Tricyclic Ligands for FK506‐Binding Proteins ; day:25 ; month:07 ; year:2024 ; extent:8
Chemistry - a European journal ; (25.07.2024) (gesamt 8)
- Creator
- DOI
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10.1002/chem.202401405
- URN
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urn:nbn:de:101:1-2407261406560.551785864612
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:59 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
- Krajczy, Patryk
- Meyners, Christian
- Repity, Maximilian L.
- Hausch, Felix
Other Objects (12)
Structure‐Based Design of Ultrapotent Tricyclic Ligands for FK506‐Binding Proteins
Design and synthesis of selective ligands for the FK506-binding protein 51
Design and synthesis of ligands for the FK506-binding proteins and the serotonin transporter
Design and synthesis of ligands for the FK506-binding proteins and the serotonin transporter
Design and synthesis of bicyclic ligands for the FK506-binding proteins 51 and 52
Targeted protein degradation of FK506-binding proteins
Structure‐Based Evolution of Subtype‐Selective Neurotensin Receptor Ligands
Development of Novel Small-Molecule Degraders of FK506-Binding Protein 51
Structure-based pose prediction: Non-cognate docking extended to macrocyclic ligands
FK506-binding protein 11, a novel antibody folding catalyst in plasma cells
Structure-based development of nonpeptidic fluorescent probes, PET tracers and homobivalent neuropeptide Y Y1 receptor ligands with picomolar binding affinities
Synergistische immunsuppressive Effekte bei Kombination von FK506 und seiner Metabolite 13-Demethyl-FK506 und 13,15-Demethyl-FK506 in vitro
Structure‐Based Design of Ultrapotent Tricyclic Ligands for FK506‐Binding Proteins
Design and synthesis of selective ligands for the FK506-binding protein 51
Design and synthesis of ligands for the FK506-binding proteins and the serotonin transporter
Design and synthesis of ligands for the FK506-binding proteins and the serotonin transporter
Design and synthesis of bicyclic ligands for the FK506-binding proteins 51 and 52
Targeted protein degradation of FK506-binding proteins
Structure‐Based Evolution of Subtype‐Selective Neurotensin Receptor Ligands
Development of Novel Small-Molecule Degraders of FK506-Binding Protein 51
Structure-based pose prediction: Non-cognate docking extended to macrocyclic ligands
FK506-binding protein 11, a novel antibody folding catalyst in plasma cells
Structure-based development of nonpeptidic fluorescent probes, PET tracers and homobivalent neuropeptide Y Y1 receptor ligands with picomolar binding affinities
Synergistische immunsuppressive Effekte bei Kombination von FK506 und seiner Metabolite 13-Demethyl-FK506 und 13,15-Demethyl-FK506 in vitro
Structure‐Based Design of Ultrapotent Tricyclic Ligands for FK506‐Binding Proteins
Design and synthesis of selective ligands for the FK506-binding protein 51
Design and synthesis of ligands for the FK506-binding proteins and the serotonin transporter
Design and synthesis of ligands for the FK506-binding proteins and the serotonin transporter
Design and synthesis of bicyclic ligands for the FK506-binding proteins 51 and 52
Targeted protein degradation of FK506-binding proteins
Structure‐Based Evolution of Subtype‐Selective Neurotensin Receptor Ligands
Development of Novel Small-Molecule Degraders of FK506-Binding Protein 51
Structure-based pose prediction: Non-cognate docking extended to macrocyclic ligands
FK506-binding protein 11, a novel antibody folding catalyst in plasma cells
Structure-based development of nonpeptidic fluorescent probes, PET tracers and homobivalent neuropeptide Y Y1 receptor ligands with picomolar binding affinities