Results 51 to 60 of about 232,627 (303)
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 +3 more
doaj +1 more source
FEBS Letters, EarlyView.Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley +1 more source
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 +3 more
doaj +1 more source
Discerning protein pools by selective staining with self‐labeling tags
FEBS Letters, EarlyView.Cell surface proteins have an intra‐ and extracellular pool. Combining genetic fusion to self‐labeling tags that can be addressed with small molecule fluorophores allows separating these pools. We highlight recent developments and techniques for state‐of‐the‐art interrogation of cell surface proteins in the complex tissue setting.
Kati Fischermanns, Johannes Broichhagen
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 +3 more
doaj +1 more source
Cold Spring Harbor Perspectives in Biology, 2011 Glycosylation is a very common modification of protein and lipid, and most glycosylation reactions occur in the Golgi. Although the transfer of initial sugar(s) to glycoproteins or glycolipids occurs in the ER or on the ER membrane, the subsequent addition of the many different sugars that make up a mature glycan is accomplished in the Golgi.
openaire +2 more sources
, 2022 Immune checkpoint therapy (ICT) with a monoclonal antibody (MAb) against programmed cell death protein 1 (PD-1) is a powerful clinical treatment for tumors.
Dan Lu (135836) +10 more
core +1 more source
Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation
FEBS Letters, EarlyView.Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang +2 more
wiley +1 more source
Intramolecular glycosylation [PDF]
Beilstein Journal of Organic Chemistry, 2017 Carbohydrate oligomers remain challenging targets for chemists due to the requirement for elaborate protecting and leaving group manipulations, functionalization, tedious purification, and sophisticated characterization. Achieving high stereocontrol in glycosylation reactions is arguably the major hurdle that chemists experience.
Xiao G. Jia, Alexei V. Demchenko
openaire +3 more sources
Analysing the Glycosylation Profile of Triple Negative Breast Cancer [PDF]
Protein glycosylation is a sequential process that involves many enzymes and aids in protein stability and cell signalling. Protein glycosylation is altered in cancer and can increase its invasive and metastatic potential.
Sutherland, Shannon Theresa
core +1 more source