Results 171 to 180 of about 22,376,002 (349)

The planar cell polarity protein Vangl2 interacts with the PDZ‐domains of Scribble but not with a unique PDZ‐like domain in Inturned

open access: yesFEBS Letters, EarlyView.
Structural and biochemical characterisations show that the planar cell polarity (PCP) protein Inturned harbours a unique PDZ‐like domain that does not bind canonical PDZ‐binding motifs (PBMs) like that of another PCP protein Vangl2. In contrast, the apical‐basal polarity protein Scribble contains four PDZ domains that bind Vangl2, but one PDZ domain ...
Stephan Wilmes   +4 more
wiley   +1 more source

Comparison of binocular vision indices in Parkinson's disease patients <i>vs</i> age-sex-matched healthy controls. [PDF]

open access: yesInt J Ophthalmol
Shariati-Moghaddam R   +8 more
europepmc   +1 more source

Tau acetylation at K331 has limited impact on tau pathology in vivo

open access: yesFEBS Letters, EarlyView.
We mapped tau post‐translational modifications in humanized MAPT knock‐in mice and in amyloid‐bearing double knock‐in mice. Acetylation within the repeat domain, particularly around K331, showed modest increases under amyloid pathology. To test functional relevance, we generated MAPTK331Q knock‐in mice.
Shoko Hashimoto   +3 more
wiley   +1 more source

Improving Anchor-based Explanations

open access: green, 2020
Julien Delaunay   +2 more
openalex   +2 more sources

Machine learning for accelerating process-based computation of land biogeochemical cycles

open access: gold, 2023
Yan Sun   +6 more
openalex   +1 more source

Calpain small subunit homodimerization is robust and calcium‐independent

open access: yesFEBS Letters, EarlyView.
Calpains dimerize via penta‐EF‐hand (PEF) domains. Using single‐molecule force spectroscopy, we measured the strength and kinetics of PEF–PEF homodimer binding. The interaction is robust, shows a transient conformational step before dissociation, and remains largely insensitive to Ca2+.
Nesha May O. Andoy   +4 more
wiley   +1 more source

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

open access: yesFEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa   +5 more
wiley   +1 more source

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