Results 91 to 100 of about 13,659,719 (307)

Table_2_Heritability Enrichment of Immunoglobulin G N-Glycosylation in Specific Tissues.xlsx

open access: yes, 2021
Genome-wide association studies (GWAS) have identified over 60 genetic loci associated with immunoglobulin G (IgG) N-glycosylation; however, the causal genes and their abundance in relevant tissues are uncertain.
Yahong Zhu (10931715)   +11 more
core   +1 more source

Remote Activation of Wnt Signaling and Cell Proliferation by E‐Cadherin Magnetomechanical Stimulation

open access: yesAdvanced Functional Materials, EarlyView.
A pioneering magnetogenetic toolkit enables non‐invasive, precise spatiotemporal modulation of intracellular Wnt/β‐catenin signaling. Functionalized magnetic nanoparticles (MNPs@E/EC15) target cellular E‐cadherins to generate localized magnetomechanical forces under low‐intensity magnetic fields.
Christian Castro‐Hinojosa   +7 more
wiley   +1 more source

Programmable Carrier‐Free All‐Enzyme Beads for Modular Continuous‐Flow Biocatalysis

open access: yesAdvanced Materials, EarlyView.
Genetically encoded enzyme building blocks self‐assemble into monodisperse, carrier‐free protein beads via a droplet‐based formulation strategy. These programmable catalytic particles enable modular continuous‐flow biocatalysis, from single‐enzyme reactions to multi‐enzyme cascades and bead–bead coupled reactor systems.
Jennifer Kühne   +12 more
wiley   +1 more source

The N-glycosylation of Equine Tetherin Affects Antiviral Activity by Regulating Its Subcellular Localization

open access: yesViruses, 2020
Tetherin is an interferon-inducible type II transmembrane glycoprotein which inhibits the release of viruses, including retroviruses, through a “physical tethering” model.
Bowen Bai   +7 more
doaj   +1 more source

Beyond the Sequon: Sites of N-Glycosylation [PDF]

open access: yes, 2012
Asparagine (N-) linked protein glycosylation is a common and essential post-translational modification of proteins in eukaryotes, archaea and some bacteria. It plays crucial roles in protein folding and in regulation of protein function. Although the general principles of Nglycosylation have been long known, the precise details governing whether a ...
openaire   +3 more sources

Table_5_Heritability Enrichment of Immunoglobulin G N-Glycosylation in Specific Tissues.xlsx

open access: yes, 2021
Genome-wide association studies (GWAS) have identified over 60 genetic loci associated with immunoglobulin G (IgG) N-glycosylation; however, the causal genes and their abundance in relevant tissues are uncertain.
Yahong Zhu (10931715)   +11 more
core   +1 more source

Culinary Chemistry as a Platform for Interfacial Materials Design

open access: yesAdvanced Materials Interfaces, EarlyView.
Culinary processes control interfaces through heating, shear, gelation, and molecular transport. This Review connects selected gastronomic examples with food‐derived nanomaterials, plasmonic sensing, anthocyanin photovoltaics, and intelligent packaging. Original agar‐based plasmonic films illustrate the proposed translation.
Josep Moreno   +12 more
wiley   +1 more source

MALDI-MS profiling of serum O-glycosylation and N-glycosylation in COG5-CDG

open access: yes, 2017
Congenital disorders of glycosylation (CDG) are due to defective glycosylation of glycoconjugates. Conserved oligomeric Golgi (COG)-CDG are genetic diseases due to defects of the COG complex subunits 1–8 causing N-glycan and O-glycan processing ...
Régal, Luc   +53 more
core   +1 more source

Engineering Microbial Particles for Next‐Generation Biomedical Platforms

open access: yesAdvanced Science, EarlyView.
Microbe‐derived particles (MDPs), which include extracellular vesicles, outer membrane vesicles, inclusion bodies, polysaccharide particles, and virus‐like particles, represent a rapidly expanding category of bioinspired nanomaterials. With their natural origin, intrinsic biocompatibility, and highly programmable functionality, MDPs serve as a ...
Yuting Li   +7 more
wiley   +1 more source

Chapter 10 - Antibody glycosylation

open access: yes, 2013
The antibody Fc region is posttranslationally modified by N-linked glycosylation. In immunoglobulin G (IgG), the processing of the glycans is restricted by the presence of extensive interaction with the protein surface.
Yu, Xiaojie   +7 more
core   +1 more source

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