Results 171 to 180 of about 16,214,189 (289)

Identifying and characterising a plant GH1 β‐glucosidase that exhibits hydrolytic activity on N‐linked glucopyranoside

open access: yesFEBS Open Bio, EarlyView.
We report the first β‐glucosidase with demonstrated hydrolytic activity on an N‐linked glycopyranoside. The enzyme, native to maize, was biochemically characterised for this novel reaction, and structural modelling of the enzyme–substrate complex revealed several clues to the underlying reduced catalytic rate relative to its native O‐glycopyranoside ...
Hani Gharabli   +3 more
wiley   +1 more source

Bioinformatics Across the Cutaneous Scar Spectrum: Molecular States, Digital Phenotypes and Clinical Translation. [PDF]

open access: yesClin Cosmet Investig Dermatol
Zhang Y   +8 more
europepmc   +1 more source

Structural studies and functional engineering of NanX: an anhydro‐sialic acid transporter from Escherichia coli

open access: yesFEBS Open Bio, EarlyView.
Biophysical characterisation shows that NanX, a membrane transport protein from the major facilitator superfamily (MFS), forms both monomers and dimers after purification. AlphaFold modelling and substrate docking provide information on residues likely involved in substrate recognition for NanX and another MFS member, NanT.
Michael C. Newton‐Vesty   +13 more
wiley   +1 more source

Naturalistic spatial education engages distinct neural processes for mental rotation, cognitive load, and linguistic demands. [PDF]

open access: yesProc Natl Acad Sci U S A
Gacetta EB   +6 more
europepmc   +1 more source

Potential and Conditions for the Development of the Creative Sector in Warsaw

open access: yesMiscellanea Geographica: Regional Studies on Development, 2011
Dudek-Mańkowska Sylwia   +3 more
doaj   +1 more source

In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols

open access: yesFEBS Open Bio, EarlyView.
Tyrosinase from Ralstonia pseudosolanacearum is a promising biocatalyst for producing valuable catechols from monophenol substrates. This tyrosinase is uniquely suited to this due to its high monophenolase : diphenolase ratio. We combined in silico docking and in vivo kinetic characterisation of this tyrosinase with 11 industrially relevant monophenols,
James Britton   +6 more
wiley   +1 more source

Home - About - Disclaimer - Privacy