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Our structure provides a structural basis for the study of the pathogenesis of VHL disease and rationale for the design of novel compounds that may modulate cullin-substrate receptor interactions.
Our structure provides evidence for substrate channeling.
Our structure provides mechanistic insights into RNA encapsidation in the genus Hantavirus and constitutes a template for drug discovery efforts aimed at combating hantavirus infections.
Our structure provides the first atomic-resolution data on any part of a claudin molecule and reveals that claudin's CPE-binding fingerprint (NPLVP) is in a tight turn conformation and binds, as expected, in CPE's C-terminal claudin-binding groove.
Our structure provides vital clues that may have remarkable implications on the possible function(s) of BfrA that have not yet been deliberated for this family of proteins.
Our structure provides a clear mechanism for how transphosphorylation occurs on the activation segment and has many precedents in other dimeric protein kinases.
Similar(53)
Our structures provide evidence for structural plasticity within the active site involving E96, which directly coordinates Mg2+ and is captured in three different conformations.
Our structures provide important insights into the structural basis of the B″/PR72 PP2A family.
When compared with the previously reported structures of various E1 enzymes, our structures provide the basis of the preferences of these inhibitors for different Ub/Ubl-activating enzymes.
Our structures provide insight into the nature of the interaction with the P-product fragment.
Hence, our structures provide crucial insights into the regulation of the replicative DNA polymerase PolIIIα by its associated proteins clamp, exonuclease and τc.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com