Results 171 to 180 of about 36,400 (267)

EvolvED: Evolutionary Embeddings to Understand the Generation Process of Diffusion Models

open access: yesComputer Graphics Forum, EarlyView.
EvolvED visualises how diffusion models generate images by embedding intermediate outputs to preserve semantics and evolutionary structure. It supports analysis via (a) user‐defined goals and prompts, (b) sampling intermediate images, (c) extracting relevant features, and (d) visualising them in structured radial and rectilinear layouts for ...
Vidya Prasad   +5 more
wiley   +1 more source

RNF13 is a previously undescribed interactor of iduronate 2‐sulfatase that modifies its glycosylation and maturation

open access: yesThe FEBS Journal, EarlyView.
Iduronate 2‐sulfatase (IDS; purple) is expressed as a precursor protein that goes through multiple steps of maturation, modification, and trafficking to become an active lysosomal enzyme that degrades glycosaminoglycans. Our study shows that the transmembrane ubiquitin ligases RNF13 (orange) and RNF167 (pink) heterodimerize, affecting IDS intracellular
Valérie C. Cabana   +4 more
wiley   +1 more source

Human IDO2 exhibits unique binding affinities distinct to those of human IDO1

open access: yesThe FEBS Journal, EarlyView.
Although indoleamine 2,3‐dioxygenase 2 (IDO2) is highly homologous to IDO1, it displays markedly lower catalytic activity. We found that IDO2 binds L‐tryptophan (L‐Trp) in a flipped orientation stabilized by the IDO2‐specific residue His143. Replacement of His143 with the IDO1‐equivalent tyrosine restored an IDO1‐like binding mode and increased ...
Shunsuke Nogi   +8 more
wiley   +1 more source

Insights into the catalytic mechanism of formate dehydrogenases from different microbial sources

open access: yesThe FEBS Journal, EarlyView.
This integrated study combines experimental enzyme kinetics with QM/MM simulations to map the catalytic mechanisms of four formate dehydrogenases at the atomic level. This approach reveals the key determinants of catalytic efficiency and guides the rational design of biocatalysts for effective CO2 reduction—a crucial step towards sustainable ...
Laura Legnani   +8 more
wiley   +1 more source

Investigating transthyretin variants H88R and I107V in amyloid priming: From destabilization to complete dissociation

open access: yesThe FEBS Journal, EarlyView.
Investigated mutations in transthyretin (TTR) disrupt the F87‐centered hydrophobic core that stabilizes its tetrameric structure. The mild I107V mutation weakens inter‐chain packing, while H88R fully abolishes tetramer formation, yielding a monomeric, aggregation‐prone form. Structural, biophysical, and computational analyses reveal that both mutations
István L. Bódy   +7 more
wiley   +1 more source

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