Results 61 to 70 of about 4,321,073 (342)

Spatiotemporal and quantitative analyses of phosphoinositides – fluorescent probe—and mass spectrometry‐based approaches

open access: yesFEBS Letters, EarlyView.
Fluorescent probes allow dynamic visualization of phosphoinositides in living cells (left), whereas mass spectrometry provides high‐sensitivity, isomer‐resolved quantitation (right). Their synergistic use captures complementary aspects of lipid signaling. This review illustrates how these approaches reveal the spatiotemporal regulation and quantitative
Hiroaki Kajiho   +3 more
wiley   +1 more source

Active Site

open access: yes, 2008
Citation: 'active site' in the IUPAC Compendium of Chemical Terminology, 3rd ed.; International Union of Pure and Applied Chemistry; 2006. Online version 3.0.1, 2019. 10.1351/goldbook.A00108 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms.
  +4 more sources

Determination of the Bridging Ligand in the Active Site of Tyrosinase

open access: yesMolecules, 2017
Tyrosinase is a type-3 copper enzyme that is widely distributed in plants, fungi, insects, and mammals. Developing high potent inhibitors against tyrosinase is of great interest in diverse fields including tobacco curing, food processing, bio ...
Congming Zou   +7 more
doaj   +1 more source

The Metallo-β-lactamase GOB Is a Mono-Zn(II) Enzyme with a Novel Active Site [PDF]

open access: yes, 2007
Metallo-β-lactamases (MβLs) are zinc-dependent enzymes able to hydrolyze and inactivate most β-lactam antibiotics. The large diversity of active site structures and metal content among MβLs from different sources has limited the design of a pan-MβL ...
Bennett, Brian   +10 more
core   +1 more source

The anti‐CRISPR protein AcrIE8.1 inhibits the type I‐E CRISPR‐Cas system by directly binding to the Cascade subunit Cas11

open access: yesFEBS Letters, EarlyView.
In this study, we present the structure of AcrIE8.1, a previously uncharacterized anti‐CRISPR protein that inhibits the type I‐E CRISPR‐Cas system. Through a combination of structural and biochemical analyses, we demonstrate that AcrIE8.1 directly binds to the Cas11 subunit of the Cascade complex to inhibit the CRISPR‐Cas system.
Young Woo Kang, Hyun Ho Park
wiley   +1 more source

Design and Characterisation of Inhibitory Peptides against Bleg1_2478, an Evolutionary Divergent B3 Metallo-β-lactamase

open access: yesMolecules, 2020
Previously, a hypothetical protein (HP) termed Bleg1_2437 (currently named Bleg1_2478) from Bacillus lehensis G1 was discovered to be an evolutionary divergent B3 subclass metallo-β-lactamase (MBL).
Gayathri Selvaraju   +3 more
doaj   +1 more source

A Cre‐dependent lentiviral vector for neuron subtype‐specific expression of large proteins

open access: yesFEBS Letters, EarlyView.
We designed a versatile and modular lentivector comprising a Cre‐dependent switch and self‐cleaving 2A peptide and tested it for co‐expression of GFP and a 2.8 kb gene of interest (GOI) in mouse cortical parvalbumin (PV+) interneurons and midbrain dopamine (TH+) neurons.
Weixuan Xue   +6 more
wiley   +1 more source

Operando Study of the Active Phase in Liquid GaPt Alloy Catalysts

open access: yesSmall Science
The operando study investigates propane dehydrogenation (PDH) using a liquid gallium‐platinum catalyst based on the supported catalytically active liquid metal solutions (SCALMS) concept.
Michael S. Moritz   +4 more
doaj   +1 more source

By dawn or dusk—how circadian timing rewrites bacterial infection outcomes

open access: yesFEBS Letters, EarlyView.
The circadian clock shapes immune function, yet its influence on infection outcomes is only beginning to be understood. This review highlights how circadian timing alters host responses to the bacterial pathogens Salmonella enterica, Listeria monocytogenes, and Streptococcus pneumoniae revealing that the effectiveness of immune defense depends not only
Devons Mo   +2 more
wiley   +1 more source

Active Site of Cytochrome cbb3 [PDF]

open access: yesJournal of Biological Chemistry, 2009
Cytochrome cbb(3) is the most distant member of the heme-copper oxidase family still retaining the following major feature typical of these enzymes: reduction of molecular oxygen to water coupled to proton translocation across the membrane. The thermodynamic properties of the six redox centers, five hemes and a copper ion, in cytochrome cbb(3) from ...
Virve, Rauhamäki   +3 more
openaire   +2 more sources

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