A5033509166- Glycosylation and Glycoproteins Research
- Transgenic Plants and Applications
- Cellular transport and secretion
- Monoclonal and Polyclonal Antibodies Research
- Viral Infectious Diseases and Gene Expression in Insects
- Microtubule and mitosis dynamics
- Complement system in diseases
- Infant Nutrition and Health
- Proteoglycans and glycosaminoglycans research
- Blood Coagulation and Thrombosis Mechanisms
- Platelet Disorders and Treatments
- Adenosine and Purinergic Signaling
- Neonatal Health and Biochemistry
- Carbohydrate Chemistry and Synthesis
- Endoplasmic Reticulum Stress and Disease
- Escherichia coli research studies
- Fungal and yeast genetics research
- Fluorine in Organic Chemistry
Weizmann Institute of Science
2022-2025
Ben-Gurion University of the Negev
2019
Mucus is made of enormous mucin glycoproteins that polymerize by disulfide crosslinking in the Golgi apparatus. QSOX1 a catalyst bond formation localized to Golgi. Both and mucins are highly expressed goblet cells mucosal tissues, leading hypothesis catalyzes disulfide-mediated polymerization. We found knockout mice lacking had impaired mucus barrier function due production defective mucus. However, an investigation on molecular level revealed normal polymerization related glycoproteins....
Domains known as von Willebrand factor type D (VWD) are found in extracellular and cell-surface proteins including factor, mucins, various signaling molecules receptors. Many VWD domains have a glycine-aspartate-proline-histidine (GDPH) amino-acid sequence motif, which is hydrolytically cleaved post-translationally between the aspartate (Asp) proline (Pro). The Fc IgG binding protein (FCGBP), intestinal mucus secretions other environments, contains 13 domains, 11 of GDPH cleavage site. In...
Secreted mucins are multimegadalton glycoprotein polymers that share the function of protecting mucosal tissues but diversified for activities in different organs body. Structural studies secreted complicated by enormous sizes, flexibility, and complex supramolecular assembly modes these glycoproteins. The two major respiratory MUC5AC MUC5B. Here, we present structures a large amino-terminal segment form helical filaments. These filaments differ from filamentous tubular observed previously...
The von Willebrand factor (VWF) glycoprotein is stored in tubular form Weibel-Palade bodies (WPBs) before secretion from endothelial cells into the bloodstream. organization of VWF tubules promotes formation covalently linked polymers and enables orderly without polymer tangling. Recent studies have described high-resolution structure helical cores formed vitro by D1D2 D'D3 amino-terminal protein segments VWF. Here we show that with geometry observed for intracellular WPBs requires also VWA1...
Abstract Humanization is an essential step in developing animal-derived antibodies into therapeutics, and approximately one third of approved have been humanized. Conventional humanization approaches graft the complementarity-determining regions (CDRs) animal antibody onto several homologous human frameworks. This process, however, often drastically lowers stability antigen binding, demanding iterative mutational fine-tuning to recover original properties. Here, we present Computational...
Abstract Mucus shields the intestinal epithelium from pathogens and provides a supportive environment for commensal bacteria. is composed of enormous, heavily glycosylated proteins called mucins, which become disulfide crosslinked in multi-step biosynthetic pathway culminating Golgi apparatus secretory granules goblet cells. We observed that knockout mice lacking Golgi-localized catalyst QSOX1 produced poorly protective colon mucus, were hypersensitive to induced colitis, had an altered...