Results 1 to 10 of about 61,889 (286)

The effect of three urease inhibitors on H. pylori viability, urease activity and urease gene expression

open access: yesFrontiers in Microbiology
BackgroundTreatment of Helicobacter pylori (H. pylori) infections is challenged by antibiotic resistance. The urease enzyme contributes to H. pylori colonization in the gastric acidic environment by producing a neutral microenvironment.
Hanaa Shaalan   +3 more
doaj   +4 more sources

Staphylococcus aureus urease is controlled by a complex regulatory network to promote dissemination during CAUTI [PDF]

open access: yesmBio
Catheter-associated urinary tract infections (CAUTIs) are one of the most common hospital-associated infections in the United States, accounting for >1 million cases annually.
Jana Gomez   +4 more
doaj   +2 more sources

Encapsulation of urease and PEG-Urease in erythrocyte [PDF]

open access: yesArtificial Cells, Blood Substitutes, and Biotechnology, 2000
Erythrocytes can be used to entrap drugs, enzymes or other molecules with active properties, with various encapsulation procedures. The carrier is nonimmunogenic, biodegradable, and circulates freely throughout the body. Urease was covalently immobilized
Baysal, SH, Uslan, AH
core   +4 more sources

Alginate beads encapsulation matrix for urease and polyethyleneglycol-urease

open access: yesArtificial Cells, Blood Substitutes, and Biotechnology, 2007
Urease was immobilized activated PEG-5000 and encapsulated urease and PEG modified urease within alginate beads. Encapsulated urease and PEG-urease were thoroughly characterized for pH, temperature and stabilities and these properties were compared with ...
Baysal, Senay Hamarat, Baysal S.H.
core   +5 more sources

Urease-Powered Micromotors with Spatially Selective Distribution of Enzymes for Capturing and Sensing Exosomes

open access: yes, 2023
Enzyme-catalyzed micro/nanomotors (MNMs) exhibit tremendous potential for biological isolation and sensing, because of their biocompatibility, versatility, and ready access to biofuel.
Yixin Peng (8519724)   +6 more
core   +8 more sources

Urease

open access: yes, 2023
Urease is a nickel-containing enzyme encoded by several microorganisms and plants since its physiological role, involving the conversion of urea into ammonia, is crucial for their survival and/or pathogenicity.
Carradori S., D'Agostino I.
core   +3 more sources

Urease

open access: yes, 2007
Table of contents 1. Introduction 2. The structure of native urease 3. The structure of urease complexed with analogues of transition state and substrate 4. The structure-based mechanism 5.
CIURLI, STEFANO LUCIANO
core   +4 more sources

Urease

open access: yes, 2021
Urease is a nickel enzyme that catalyzes the hydrolysis of urea to ammonia and carbamate, with the latter decomposing spontaneously to yield another molecule of ammonia and bicarbonate, in the last step of organic nitrogen ...
Ciurli, Stefano   +3 more
core   +2 more sources

Urease

open access: yes, 2017
Although the discovery of urease as the first enzyme for which nickel is essential for activity dates back to 1975, the rationale for Ni selection for the active site of this hydrolase has been only recently unraveled.
L. Mazzei   +5 more
core   +3 more sources

Urease-Powered Black TiO2 Micromotors for Photothermal Therapy of Bladder Cancer

open access: yes
Urease-powered nano/micromotors can move at physiological urea concentrations, making them useful for biomedical applications, such as treating bladder cancer. However, their movement in biological environments is still challenging.
Atefeh Hasani (17784185)   +4 more
core   +7 more sources

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