Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1078324 | PMC |
| http://dx.doi.org/10.1073/pnas.27.6.291 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Mechanical and functional characterisation of a 3D porous biomimetic extracellular matrix to study insulin secretion from pancreatic β-cell lines.
In Vitro Model
December 2024
Univ. Lille, Inserm, CHU Lille, Institut Pasteur Lille, U1167 - RID-AGE - Facteurs de Risque Et Déterminants Moléculaires Des Maladies Liées Au Vieillissement, F-59000 Lille, France.
Background: Extracellular matrix (ECM) is a three-dimensional (3D) structure found around cells in the tissues of many organisms. It is composed mainly of fibrous proteins, such as collagen and elastin, and adhesive glycoproteins, such as fibronectin and laminin-as well as proteoglycans, such as hyaluronic acid. The ECM performs several essential functions, including structural support of tissues, regulation of cell communication, adhesion, migration, and differentiation by providing biochemical and biomechanical cues to the cells.
View Article and Find Full Text PDFAcetylation of alginate enables the production of inks that mimic the chemical properties of biofilm.
J Mater Chem B
January 2025
Institute of Materials Science and Technology, Technische Universität Wien, Vienna, Austria.
The reason why certain bacteria, , (PA), produce acetylated alginate (Alg) in their biofilms remains one of the most intriguing facts in microbiology. Being the main structural component of the secreted biofilm, like the one formed in the lungs of cystic fibrosis (CF) patients, Alg plays a crucial role in protecting the bacteria from environmental stress and potential threats. Nonetheless, to investigate the PA biofilm environment and its lack of susceptibility to antibiotic treatment, the currently developed biofilm models use native seaweed Alg, which is a non-acetylated Alg.
View Article and Find Full Text PDFNanosized MCM-41 silica from rice husk and its application for the removal of organic dyes from water.
RSC Adv
January 2025
Dipartimento di Scienze e Innovazione Tecnologica, Università Del Piemonte Orientale A. Avogadro Viale T. Michel 11 15121 Alessandria Italy
A novel synthesis of a nanometric MCM-41 from biogenic silica obtained from rice husk is here presented. CTABr and Pluronic F127 surfactants were employed as templating agents to promote the formation of a long-range ordered 2D-hexagonal structure with cylindrical pores and to limit the particle growth at the nanoscale level thus resulting in a material with uniform particle size of 20-30 nm. The physico-chemical properties of this sample (RH-nanoMCM) were investigated through a multi-technique approach, including PXRD, Si MAS NMR, TEM, -potential and N physisorption analysis at 77 K.
View Article and Find Full Text PDFRole of Non-Canonical Stacking Interactions of Heterocyclic RNA Bases in Ribosome Function.
Biochemistry (Mosc)
December 2024
Faculty of Chemistry, Lomonosov Moscow State University, Moscow, 119991, Russia.
Identification and analysis of repetitive elements (motifs) in DNA, RNA, and protein macromolecules is an important step in studying structure and functions of these biopolymers. Functional role of NA-BSE (non-adjacent base-stacking element, a widespread tertiary structure motif in various RNAs) in RNA-RNA interactions at various stages of the ribosome function during translation has been investigated in this work. Motifs of this type have been described to date that are reversibly formed during mRNA decoding, moving of the ribosome subunits relative to each other, and moving mRNA and tRNA along the ribosome during translocation.
View Article and Find Full Text PDFEffect of C- and N-Terminal Polyhistidine Tags on Aggregation of Influenza A Virus Nuclear Export Protein.
Biochemistry (Mosc)
December 2024
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119991, Russia.
Nuclear export protein (NEP) of the influenza A virus, being one of the key components of the virus life cycle, is a promising model for studying characteristics of formation of amyloids by viral proteins. Using atomic force microscopy, comparative study of aggregation properties of the recombinant NEP variants, including the protein of natural structure, as well as modified variants with N- and C-terminal affinity His-tags, was carried out. All protein variants under physiological conditions are capable of forming aggregates of various morphologies: micelle-like nanoparticles, flexible protofibrils, rigid amyloid fibrils, etc.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!