Results 31 to 40 of about 191,408 (290)

Glycosylation site alteration in the evolution of influenza A (H1N1) viruses. [PDF]

PLoS ONE, 2011
Influenza virus typically alters protein glycosylation in order to escape immune pressure from hosts and hence to facilitate survival in different host environments.
Shisheng Sun, Qinzhe Wang, Fei Zhao, Wentian Chen, Zheng Li   +4 more
doaj   +1 more source

Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation

Cells, 2021
The Golgi is the central organelle of the secretory pathway and it houses the majority of the glycosylation machinery, which includes glycosylation enzymes and sugar transporters. Correct compartmentalization of the glycosylation machinery is achieved by
Zinia D’Souza, Farhana Taher Sumya, Amrita Khakurel, Vladimir Lupashin   +3 more
doaj   +1 more source

Disordered but rhythmic—the role of intrinsic protein disorder in eukaryotic circadian timing

FEBS Letters, EarlyView.
Unstructured domains known as intrinsically disordered regions (IDRs) are present in nearly every part of the eukaryotic core circadian oscillator. IDRs enable many diverse inter‐ and intramolecular interactions that support clock function. IDR conformations are highly tunable by post‐translational modifications and environmental conditions, which ...
Emery T. Usher, Jacqueline F. Pelham
wiley   +1 more source

Glycosylated LGALS3BP is highly secreted by bladder cancer cells and represents a novel urinary disease biomarker

Molecular Oncology, EarlyView.
Urinary LGALS3BP is elevated in bladder cancer patients compared to healthy controls as detected by the 1959 antibody–based ELISA. The antibody shows enhanced reactivity to the high‐mannose glycosylated variant secreted by cancer cells treated with kifunensine (KIF).
Asia Pece, Giulio Lovato, Ilaria Cela, Arianna Mercatelli, Benedetta Ferro, Jussi Nikkola, Sara Pagotto, Tommaso Grottola, Vincenzo De Laurenzi, Rossella Cicchetti, Antonio Marchetti, Luigi Schips, Rossano Lattanzio, Stefano Iacobelli, Emily Capone, Peter Black, Mads Daugaard, Michele Marchioni, Gianluca Sala   +18 more
wiley   +1 more source

DC-SIGN Binding Contributed by an Extra N-Linked Glycosylation on Japanese Encephalitis Virus Envelope Protein Reduces the Ability of Viral Brain Invasion

Frontiers in Cellular and Infection Microbiology, 2018
The major structural envelope (E) protein of Japanese encephalitis virus (JEV) facilitates cellular binding/entry and is the primary target of neutralizing antibodies.
Jian-Jong Liang, Min-Wei Chou, Yi-Ling Lin, Yi-Ling Lin   +3 more
doaj   +1 more source

Protein O‐glycosylation in the Bacteroidota phylum

FEBS Open Bio, EarlyView.
Species of the Bacteroidota phylum exhibit a unique O‐glycosylation system. It modifies noncytoplasmic proteins on a specific amino acid motif with a shared glycan core but a species‐specific outer glycan. A locus of multiple glycosyltransferases responsible for the synthesis of the outer glycan has been identified.
Lonneke Hoffmanns, Dennis Svedberg, André Mateus   +2 more
wiley   +1 more source

Rethinking plastic waste: innovations in enzymatic breakdown of oil‐based polyesters and bioplastics

FEBS Open Bio, EarlyView.
Plastic pollution remains a critical environmental challenge, and current mechanical and chemical recycling methods are insufficient to achieve a fully circular economy. This review highlights recent breakthroughs in the enzymatic depolymerization of both oil‐derived polyesters and bioplastics, including high‐throughput protein engineering, de novo ...
Elena Rosini, Nicolò Antonelli, Gianluca Molla   +2 more
wiley   +1 more source

Similarities and Differences in the Glycosylation Mechanisms in Prokaryotes and Eukaryotes

International Journal of Microbiology, 2010
Recent years have witnessed a rapid growth in the number and diversity of prokaryotic proteins shown to carry N- and/or O-glycans, with protein glycosylation now considered as fundamental to the biology of these organisms as it is in eukaryotic systems ...
Anne Dell, Alaa Galadari, Federico Sastre, Paul Hitchen   +3 more
doaj   +1 more source

Advances in Bacterial Oligosaccharyltransferase Structure Elucidation and Potential Application to Glycoconjugate Vaccine Design

Frontiers in Bioscience-Landmark, 2023
Glycosylation is one of the most common post-translational modifications of proteins across all kingdoms of life. Diverse monosaccharides and polysaccharides can be attached to a range of amino acid residues generating N-glycosylation, O-glycosylation, C-
Riye Lu, Pengwei Li, Li Zhu, Ming Xian Chang, Songying Ouyang   +4 more
doaj   +1 more source

Homologous expression and purification of human HAX‐1 for structural studies

FEBS Open Bio, EarlyView.
This research protocol provides detailed instructions for cloning, expressing, and purifying large quantities of the intrinsically disordered human HAX‐1 protein, N‐terminally fused to a cleavable superfolder GFP, from mammalian cells. HAX‐1 is predicted to undergo posttranslational modifications and to interact with membranes, various cellular ...
Mariana Grieben
wiley   +1 more source