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The Zalpha domain from human ADAR1 binds to the Z-DNA conformer of many different sequencesThe solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNAThe solution structure of the N-terminal domain of E3L shows a tyrosine conformation that may explain its reduced affinity to Z-DNA in vitroDesign and structure of stapled peptides binding to estrogen receptorsNMR fragment screening: Advantages and applications.Structure-function analysis of the Z-DNA-binding domain Zalpha of dsRNA adenosine deaminase type I reveals similarity to the (alpha + beta) family of helix-turn-helix proteinsDiscovery of low-molecular-weight ligands for the AF6 PDZ domain.Small-molecule inhibitors of AF6 PDZ-mediated protein-protein interactions.Antigen 85C inhibition restricts Mycobacterium tuberculosis growth through disruption of cord factor biosynthesisA 6 bp Z-DNA hairpin binds two Zα domains from the human RNA editing enzyme ADAR1
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description
researcher ORCID ID = 0000-0002-5538-5767
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wetenschapper
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name
Markus Schade
@ast
Markus Schade
@en
Markus Schade
@es
Markus Schade
@nl
type
label
Markus Schade
@ast
Markus Schade
@en
Markus Schade
@es
Markus Schade
@nl
prefLabel
Markus Schade
@ast
Markus Schade
@en
Markus Schade
@es
Markus Schade
@nl
P214
P106
P214
P31
P496
0000-0002-5538-5767