Results 111 to 120 of about 492,788 (273)
Editorial: Why Do Species’ Names Change?
The reason why scientific names change is because research is constantly correcting errors and scholarship is constantly untangling the related misconceptions. Until the advent of the Internet new names and name changes were approved by the International
Patricia A. Folley
doaj
In this study, we found that human cervical‐derived adipocytes maintain intracellular iron level by regulating the expression of iron transport‐related proteins during adrenergic stimulation. Melanotransferrin is predicted to interact with transferrin receptor 1 based on in silico analysis.
Rahaf Alrifai +9 more
wiley +1 more source
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
Tau acetylation at K331 has limited impact on tau pathology in vivo
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
Ski-Trail Names: A New Toponymic Category
Celia Millward, Richard Millward
doaj +1 more source
Calpain small subunit homodimerization is robust and calcium‐independent
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
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

