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Crosslinking mass spectrometry (MS) has emerged as an important technique for elucidating the in-solution structures of protein complexes and the topology of protein-protein interaction networks. However, the expanding user community lacked an integrated visualisation tool that helped them make use of the crosslinking data for investigating biological mechanisms. We addressed this need by developing xiVIEW, a web-based application designed to streamline crosslinking MS data analysis, which we present here. xiVIEW provides a user-friendly interface for accessing coordinated views of mass spectrometric data, network visualisation, annotations extracted from trusted repositories like UniProtKB, and available 3D structures. In accordance with recent recommendations from the crosslinking MS community, xiVIEW (i) provides a standards compliant parser to improve data integration and (ii) offers accessible visualisation tools. By promoting the adoption of standard file formats and providing a comprehensive visualisation platform, xiVIEW empowers both experimentalists and modellers alike to pursue their respective research interests. We anticipate that xiVIEW will advance crosslinking MS-inspired research, and facilitate broader and more effective investigations into complex biological systems.
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http://dx.doi.org/10.1016/j.jmb.2024.168656 | DOI Listing |
Eur J Pharm Sci
September 2025
Department of Medicinal Chemistry, Uppsala University, SE-75123 Uppsala, Sweden. Electronic address:
Subcutaneous (SC) injection is the primary alternative to oral administration for therapeutic proteins and peptides. However, bioavailability and absorption rate are often variable and difficult to predict. Therefore, there is a need for new biorelevant and predictive SC in vitro methods.
View Article and Find Full Text PDFJ Invest Dermatol
September 2025
LEO Foundation Skin Immunology Research Center, Department of Immunology and Microbiology, University of Copenhagen, Copenhagen, DK. Electronic address:
Liquid chromatography-mass spectrometry (LC-MS) is an evolving tool for comprehensive proteomic analyses across tissues. Despite the widespread use of LC-MS in dermatology, full-thickness human skin remains challenging to analyse. The skin extracellular matrix (ECM) presents two major obstacles: the extensive crosslinking complicates protein extraction and the high abundance of ECM proteins can mask lower-abundance proteins, reducing identification numbers.
View Article and Find Full Text PDFCarbohydr Polym
November 2025
Department of Polymers for Health and Biomaterials, IBMM, Univ Montpellier, CNRS, ENSCM, Montpellier, France; Department of Pharmacy, Nîmes University Hospital, 30900 Nimes, France. Electronic address:
Polysaccharide-based hydrogels often lack mechanical strength and, when used for protein delivery, are generally limited to diffusion-based release. In this work, we developed robust polysaccharide- and polyester-based near-infrared (NIR)-responsive hydrogels. Hydrogels are made from photo-crosslinked methacrylated dextran (DEX-MA), methacrylated polylactide containing oxygen reactive species (ROS) sensitive thioketal groups (PLA-TK-MA), and covalently bound protoporphyrin IX (PPIX) that generates ROS under NIR irradiation.
View Article and Find Full Text PDFCarbohydr Polym
November 2025
Jiangsu Key Laboratory for pathogens and ecosystems, Jiangsu Engineering and Technology Research Center for Industrialization of Microbial Resources, College of Life Science, Nanjing Normal University, 1 Wenyuan Road, Nanjing 210023, China. Electronic address:
The fungal cell wall provides the cell with enough strength to withstand turgor pressure and keeps adequate plasticity to extend the cell wall size under turgor pressure for cell growth. The cell walls of apical growing hyphae and budding growth yeast have been studied in detailed which share common components of chitin and β-1,3-glucan in their scaffold structures while other polysaccharide components vary on species. In contrast, the cell walls of elongating growth mushroom stipe remains poorly studied.
View Article and Find Full Text PDFMol Cell Proteomics
September 2025
Institute of Biotechnology, HiLIFE, Faculty of Medicine, University of Helsinki, Helsinki, Finland. Electronic address:
Structural proteomics has undergone a profound transformation, driven by the convergence of advanced experimental methodologies and computational innovations. Cutting-edge mass spectrometry (MS)-based approaches, including cross-linking MS (XL-MS), hydrogen-deuterium exchange MS (HDX-MS), and limited proteolysis MS (LiP-MS), now enable unprecedented insights into protein topology, conformational dynamics, and protein-protein interactions. These methods, complemented by affinity purification (AP), co-immunoprecipitation (co-IP), proximity labeling (PL), and spatial proteomics techniques, have expanded our ability to characterize the structural proteome at a systems-wide scale.
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