Rainfall-induced reactivation mechanism of a landslide with multiple-soft layers

The aim of this chapter is to show how omnichannel tools must be applied through the process of creating experiences for the consumers. During the literature review, some authors make approaches to the key concepts connecting omnichannels and consumer experiences; therefore, they explain through the analysis of data the reality of the Ecuadorian environment and global trends. With this context, this chapter will present how, by using macro environment and accessibility, a unique experience may be created in the customer journey in omnichannel.

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Electrical Activation, Deactivation, and Reactivation Mechanism Study of Plasma Doping Processes

IEEE Transactions on Electron Devices ◽

10.1109/ted.2015.2406534 ◽

2015 ◽

Vol 62 (6) ◽

pp. 1991-1997 ◽

Cited By ~ 3

Author(s):

Shu Qin

Keyword(s):

Electrical Activation ◽

Mechanism Study ◽

Plasma Doping ◽

Reactivation Mechanism

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The reversible inactivation of pig kidney alkaline phosphatase at low pH

Biochemical Journal ◽

10.1042/bj1080243 ◽

1968 ◽

Vol 108 (2) ◽

pp. 243-246 ◽

Cited By ~ 10

Author(s):

P. J. Butterworth

Keyword(s):

Alkaline Phosphatase ◽

Acid Treatment ◽

Gel Filtration ◽

Reversible Inactivation ◽

Pig Kidney ◽

Reactivation Mechanism ◽

Increasing Temperature ◽

Filtration Properties ◽

Kinetics Of ◽

Kidney Alkaline Phosphatase

1. Pig kidney alkaline phosphatase is inactivated by treatment with acid at 0°. 2. Inactivated enzyme can be partially reactivated by incubation at 30° in neutral or alkaline buffer. The amount of reactivation that occurs depends on the degree of acid treatment; enzyme that has been inactivated below pH3·3 shows very little reactivation. 3. Studies of the kinetics of reactivation indicate that the process is greatly accelerated by increasing temperature and proceeds by a unimolecular mechanism. The reactivated enzyme has electrophoretic and gel-filtration properties identical with those of non-treated enzyme. 4. The results can be best explained by assuming that a lowering of the pH causes a reversible conformational change of the alkaline phosphatase molecule to a form that is no longer enzymically active but is very susceptible to permanent denaturation by prolonged acid treatment. A reactivation mechanism involving sub-unit recombination seems unlikely.

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Structure of a prereaction complex between the nerve agent sarin, its biological target acetylcholinesterase, and the antidote HI-6

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.1523362113 ◽

2016 ◽

Vol 113 (20) ◽

pp. 5514-5519 ◽

Cited By ~ 22

Author(s):

Anders Allgardsson ◽

Lotta Berg ◽

Christine Akfur ◽

Andreas Hörnberg ◽

Franz Worek ◽

...

Keyword(s):

Dft Calculations ◽

Density Functional ◽

Deuterium Oxide ◽

Conformational Dynamics ◽

Reactive Systems ◽

Nerve Agent ◽

Hi 6 ◽

Starting Point ◽

Biological Target ◽

Reactivation Mechanism

Organophosphorus nerve agents interfere with cholinergic signaling by covalently binding to the active site of the enzyme acetylcholinesterase (AChE). This inhibition causes an accumulation of the neurotransmitter acetylcholine, potentially leading to overstimulation of the nervous system and death. Current treatments include the use of antidotes that promote the release of functional AChE by an unknown reactivation mechanism. We have used diffusion trap cryocrystallography and density functional theory (DFT) calculations to determine and analyze prereaction conformers of the nerve agent antidote HI-6 in complex with Mus musculus AChE covalently inhibited by the nerve agent sarin. These analyses reveal previously unknown conformations of the system and suggest that the cleavage of the covalent enzyme–sarin bond is preceded by a conformational change in the sarin adduct itself. Together with data from the reactivation kinetics, this alternate conformation suggests a key interaction between Glu202 and the O-isopropyl moiety of sarin. Moreover, solvent kinetic isotope effect experiments using deuterium oxide reveal that the reactivation mechanism features an isotope-sensitive step. These findings provide insights into the reactivation mechanism and provide a starting point for the development of improved antidotes. The work also illustrates how DFT calculations can guide the interpretation, analysis, and validation of crystallographic data for challenging reactive systems with complex conformational dynamics.

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QM/MM study on the spontaneous reactivation mechanism of (±)methamidophos-inhibited-acetylcholinesterase

Computational and Theoretical Chemistry ◽

10.1016/j.comptc.2011.11.035 ◽

2012 ◽

Vol 980 ◽

pp. 108-114 ◽

Cited By ~ 8

Author(s):

Yanwei Li ◽

Xiaomin Sun ◽

Likai Du ◽

Qingzhu Zhang ◽

Wenxing Wang

Keyword(s):

Reactivation Mechanism ◽

Spontaneous Reactivation

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Histone Acetylation and Reactivation of Epstein-Barr Virus from Latency

Journal of Virology ◽

10.1128/jvi.74.2.710-720.2000 ◽

2000 ◽

Vol 74 (2) ◽

pp. 710-720 ◽

Cited By ~ 87

Author(s):

Peter J. Jenkins ◽

Ulrich K. Binné ◽

Paul J. Farrell

Keyword(s):

Histone Acetylation ◽

Epstein Barr Virus ◽

Lytic Cycle ◽

Vector System ◽

Promoter Elements ◽

Barr Virus ◽

Episomal Vector ◽

Bzlf1 Gene ◽

Epstein Barr ◽

Reactivation Mechanism

ABSTRACT Induction of the viral BZLF1 gene has previously been shown to be one of the first steps in the reactivation of Epstein-Barr virus (EBV). Using an EBV oriP episomal vector system, we have reconstituted the regulation of the promoter for BZLF1 on stably transfected episomes, mapped promoter elements required for that regulation, and investigated mechanisms that may control the switch between latency and the lytic cycle. Changes in histone acetylation at the promoter for the BZLF1 gene appear to be a key part of the reactivation mechanism of this herpesvirus.

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