Results 41 to 50 of about 144,132 (182)

Expansion of the diversity of dispersin scaffolds

Acta Crystallographica Section D, Volume 81, Issue 3, Page 130-146, March 2025.
Five GH20‐family dispersins were characterized for activity on aryl glycosides and poly‐β‐1,6‐linked N‐acetyl‐d‐glucosamine oligomers and three crystal structures were solved, including two complexes with bound inhibitors.Microorganisms are known to secrete copious amounts of extracellular polymeric substances (EPS) that form complex matrices around ...
Alexandra Males, Olga V. Moroz, Elena Blagova, Astrid Munch, Gustav H. Hansen, Annette H. Johansen, Lars H. Østergaard, Dorotea R. Segura, Alexander Eddenden, Anne V. Due, Martin Gudmand, Jesper Salomon, Sebastian R. Sørensen, João Paulo L. Franco Cairo, Mark Nitz, Roland A. Pache, Rebecca M. Vejborg, Sandeep Bhosale, David J. Vocadlo, Gideon J. Davies, Keith S. Wilson   +20 more
wiley   +1 more source

Discovery of Lacto‐N‐Biosidases and a Novel N‐Acetyllactosaminidase Activity in the CAZy Family GH20: Functional Diversity and Structural Insights

ChemBioChem, Volume 26, Issue 2, January 14, 2025.
We report several new lacto‐N‐biosidases (LNBases) and the first report of N‐acetyllactosaminidase (LacNAcase) activity in CAZy family GH20, i. e. enzymes that catalyze the release heterodisaccharides from human milk oligosaccharides and related glycans. New crystal structures comparing a specific LNBase to an enzyme with dual LacNAcase/LNBase activity
Marlene Vuillemin, Jan Muschiol, Yan Zhang, Jesper Holck, Kristian Barrett, Jens Preben Morth, Anne S. Meyer, Birgitte Zeuner   +7 more
wiley   +1 more source

Arginine/Lysine Residues in the Cytoplasmic Tail Promote ER Export of Plant Glycosylation Enzymes [PDF]

Plant N-glycan processing enzymes are arranged along the early secretory pathway, forming an assembly line to facilitate the step-by-step modification of oligosaccharides on glycoproteins.
Andreeva, Bakker, Bakker, Barlowe, Batoko, Boevink, Bonifacino, Brandizzi, Brandizzi, Burke, Colley, Contreras, DaSilva, Dirnberger, Dominguez, Driouich, Essl, Fenteany, Giraudo, Guo, Hanton, Hartmann, Hawes, Hawes, Kornfeld, Kumar, Lee, Léonard, Maruyama, Mast, Matheson, Moreau, Nebenführ, Opat, Phillipson, Robinson, Saint-Jore, Saint-Jore-Dupas, Schähs, Sieben, Sparkes, Strasser, Strasser, Strasser, Strasser, Strasser, Strasser, Strasser, Strasser, Strasser, Takeuchi, Von Schaewen, Wilson, Yuasa   +53 more
core   +2 more sources

Transcriptomic and Metabolomic Insights Into the Prebiotic Potential of Camellia Seed Oil for Enhancing Akkermansia muciniphila Proliferation In Vitro

Food Science &Nutrition, Volume 13, Issue 1, January 2025.
Camellia seed oil is rich in bioactive compounds, which could promote the in vitro proliferation of Akkermansia muciniphila by reducing the oxidation–reduction potential of the media and activating the metabolism pathways involving energy and nucleic acid metabolism, protein synthesis, and environmental adaptation, thereby facilitating the nutrient ...
Xi Chen, Yong Zhu, Muhammad Mazhar, Likang Qin   +3 more
wiley   +1 more source

Upscaling and consistent sialylation of plant produced antibodies [PDF]

, 2015
Mestrado em Engenharia Agronómica - Instituto Superior de AgronomiaGlycoproteins are a major part of biopharmaceutical products. For their production, a high level of homogeny is required, not only for the protein but also for attached glycans, since ...
Sádio, Flávio da Silva Amaro
core  

Partial Replacement of Fish Meal With Shrimp Waste Meal: Effects on Growth, Digestibility, and Immunity in Juvenile Beluga Sturgeon (Huso huso)

Aquaculture Research, Volume 2025, Issue 1, 2025.
This study aimed to investigate the effects of replacing different levels of dietary shrimp waste meal (SWM) with fish meal (FM) on growth performance (GP), carcass composition (CC), apparent digestibility (AD), and innate immunity of juvenile beluga sturgeon (Huso huso).
Amirsoheil Taheri, Abdolmohammad Abedian Kenari, Maryam Aftabgard   +2 more
wiley   +1 more source

Purification and characterization of .ALPHA.-mannosidase and .BETA.-N-acetylhexosaminidase from watermelon fruit.

Agricultural and Biological Chemistry, 1988
Watermelon fruit was found to be rich in α-mannosidase (EC 3.2.1.24) and β-N-acetylhexosaminidase (EC 3.2.1.52). A simple procedure has been devised for the simultaneous isolation of α-mannosidase and β-N-acetylhexosaminidase from watermelon fruit. The purified enzymes were electrophoretically homogeneous and sufficiently free from other glycosidases ...
Hiroki NAKAGAWA, Noriyuki ENOMOTO, Makio ASAKAWA, Yutaka UDA   +3 more
openaire   +2 more sources

Design and synthesis of naphthalimide group-bearing thioglycosides as novel β-N-acetylhexosaminidases inhibitors

Journal of Enzyme Inhibition and Medicinal Chemistry, 2018
GH20 human β-N-acetylhexosaminidases (hsHex) and GH84 human O-GlcNAcase (hOGA) are involved in numerous pathological processes and emerged as promising targets for drug discovery. Based on the catalytic mechanism and structure of the catalytic domains of
Shengqiang Shen, Wei Chen, Lili Dong, Qing Yang, Huizhe Lu, Jianjun Zhang   +5 more
semanticscholar   +1 more source

Proteomic dynamics revealed sex‐biased responses to combined heat‐drought stress in Marchantia

Journal of Integrative Plant Biology, Volume 66, Issue 10, Page 2226-2241, October 2024.
Sex‐biased plasticity is crucial for dioecious liverworts to manage terrestrial pressures and adapt to various environments. Examining the effects of combined heat and drought stress in Marchantia polymorpha using a systems biology approach demonstrates how natural variation may have constrained this significant evolutionary step in the plant kingdom ...
Sara Guerrero, Víctor Roces, Lara García‐Campa, Luis Valledor, Mónica Meijón   +4 more
wiley   +1 more source

Enhancement of the sensitivity of a fluorometric lysozyme assay system by adding .BETA.-N-acetylhexosaminidase.

Chemical and Pharmaceutical Bulletin, 1985
The lysozyme assay using 4-methylumbelliferyl tetra-N-acetyl-β-chitotetraoside as a substrate was found to show increased sensitivity for lysozyme in the presence of jack bean β-N-acetylhexosaminidase (NAHase). The assay system containing NAHase gave a linear dose-response curve in the range of 10-70μg of lysozyme under conditions of 20-60 min ...
H, Fukuda, T, Tanimoto, T, Yamaha
openaire   +3 more sources