Results 131 to 140 of about 151,216 (363)

Microsomal epoxide hydrolase polymorphisms

open access: yesMolecular Medicine Reports, 2010
Microsomal epoxide hydrolase plays a dual role in the activation and detoxification of carcinogenic compounds. Two polymorphic sites have been described in exons 3 and 4 of the microsomal epoxide hydrolase gene that change tyrosine residue 113 to histidine (Tyr113His) and histidine 139 to arginine (His139Arg), respectively.
Pinarbasi, Hatice   +2 more
openaire   +6 more sources

Nomenclature for sugar-binding subsites in glycosyl hydrolases.

open access: yesBiochemical Journal, 1997
The huge structural diversity of polysaccharides leads to their central roles in food storage and utilization, structure, cell–cell signalling, cell-wall expansion and turnover and viral invasion.
G. Davies, K. Wilson, B. Henrissat
semanticscholar   +1 more source

Overcoming Extreme Ammonia Inhibition on Methanogenesis by Artificially Constructing a Synergistically Community with Acidogenic Bacteria and Hydrogenotrophic Archaea

open access: yesAdvanced Science, EarlyView.
This study proposes a two‐step biological strategy to synergistically enhance the three stages of anaerobic digestion, ultimately eliminating the extreme ammonia inhibition and breaking through the inefficiency bottleneck of conventional biotechnology.
Heng Wu   +6 more
wiley   +1 more source

Imaging Heterogeneous Patterns of Aminopeptidase N Activity in Hierarchical Tissue Structures Through High‐Resolution Whole‐Organ 3D Mapping

open access: yesAngewandte Chemie, EarlyView.
Enzymes regulate physiological functions, and their abnormal activity is associated with diseases. Here, we present a method for high‐resolution 3D mapping of enzyme activity using tissue clearing and an activity‐based covalent probe. Focusing on aminopeptidase N, we developed ANA‐o‐BODIPY, which records enzyme activity via covalent labeling.
Bo Yi   +10 more
wiley   +2 more sources

How to find soluble proteins: a comprehensive analysis of alpha/beta hydrolases for recombinant expression in E. coli

open access: yesBMC Genomics, 2005
Background In screening of libraries derived by expression cloning, expression of active proteins in E. coli can be limited by formation of inclusion bodies.
Barth Sandra   +3 more
doaj   +1 more source

Cholesterol epoxide hydrolase and cancer

open access: yesCurrent Opinion in Pharmacology, 2012
Cholesterol epoxide hydrolase (ChEH) catalyzes the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3β,5α,6β-triol. ChEH is a hetero-oligomeric complex called the anti-estrogen binding site (AEBS) comprising 3β-hydroxysterol-Δ(8)-Δ(7)-isomerase (D8D7I) and 3β-hydroxysterol-Δ(7)-reductase (DHCR7).
Silvente-Poirot, Sandrine, Poirot, Marc
openaire   +4 more sources

Activity-based protein profiling: the serine hydrolases.

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1999
With the postgenome era rapidly approaching, new strategies for the functional analysis of proteins are needed. To date, proteomics efforts have primarily been confined to recording variations in protein level rather than activity. The ability to profile
Yongsheng Liu, M. Patricelli, B. Cravatt
semanticscholar   +1 more source

Patchouli Ethanol Extract Pogostemon cablin Benth. Against Aging Profiles in Doxorubicin‐Induced 3T3‐L1 Fibroblast Cell Lines

open access: yesAGING MEDICINE, EarlyView.
Pogostemon cablin Benth. (PCEE) is a promising antiaging agent that inhibits ROS, decreases the senescence‐associated β‐galactosidase (SA‐β‐gal) gene, and maintains telomere length in doxorubicin‐induced 3T3‐L1 fibroblast cells. The researchers extend their gratitude to www.freepik.com for providing Figure telomer.
Teguh Santoso   +6 more
wiley   +1 more source

Structural Basis of Sequential Enantioselective Epoxidation by a Flavin‐Dependent Monooxygenase in Lasalocid A Biosynthesis

open access: yesAngewandte Chemie, EarlyView.
Lsd18 is a flavin‐dependent monooxygenase from Streptomyces lasalocidi that performs two enantioselective epoxidations during lasalocid A biosynthesis. X‐ray crystal structures of Lsd18 bound to a substrate and product analogue illuminate how this enzyme performs multiple epoxidations on the same substrate molecule and how it controls stereoselectivity.
Qian Wang   +12 more
wiley   +2 more sources

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