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1.
PLoS Negl Trop Dis ; 16(1): e0010094, 2022 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-35007298

RESUMEN

Hemorrhagic fever with renal syndrome (HFRS) is a zoonosis characterized by clinical features of high fever, hemorrhage, and renal damage. China has the largest number of HFRS cases worldwide, accounting for over 90% of the total reported cases. In this paper, we used surveyed HFRS data and satellite imagery to conduct geostatistical analysis for investigating the associations of rapid urbanization, water bodies, and other factors on the spatiotemporal dynamics of HFRS from year 2005 to 2018 in Xi'an City, Northwest China. The results revealed an evident epidemic aggregation in the incidence of HFRS within Xi'an City with a phenomenal fluctuation in periodic time series. Rapid urbanization was found to greatly affect the HFRS incidence in two different time phases. HFRS caused by urbanization influences farmers to a lesser extent than it does to non-farmers. The association of water bodies with the HFRS incidence rate was found to be higher within the radii of 696.15 m and 1575.39 m, which represented significant thresholds. The results also showed that geomatics approaches can be used for spatiotemporally investigating the HFRS dynamic characteristics and supporting effective allocations of resources to formulate strategies for preventing epidemics.


Asunto(s)
Fiebre Hemorrágica con Síndrome Renal/epidemiología , Fiebre Hemorrágica con Síndrome Renal/prevención & control , Prevención Primaria/métodos , Animales , China/epidemiología , Ciudades/epidemiología , Vectores de Enfermedades , Geografía , Orthohantavirus/clasificación , Fiebre Hemorrágica con Síndrome Renal/mortalidad , Humanos , Incidencia , Murinae/virología , Ratas , Estudios Retrospectivos , Imágenes Satelitales , Estaciones del Año , Urbanización
2.
Opt Express ; 28(9): 12837-12846, 2020 Apr 27.
Artículo en Inglés | MEDLINE | ID: mdl-32403772

RESUMEN

In this work, the design, fabrication and characterization are reported for a distributed Bragg reflector (DBR) filter with a specific wavelength and angular dependency, which aims to improve the light collection from a wavelength-converter-based light source into a smaller angle than the full angle Lambertian emission. The desired design is obtained by optimizing the transmission characteristics of a multi-layer structure. Titania (TiO2) and silica (SiO2) are used as high and low refractive index materials, respectively. The deposition is made by electron beam evaporation without substrate heating, followed by a post-annealing procedure. The optical properties of the evaporated layers are analyzed by ellipsometer and spectrometer measurements. The angular and wavelength dependency of the fabricated DBR is in good agreement with simulations for the designed structure.

3.
Protein Sci ; 28(5): 889-899, 2019 05.
Artículo en Inglés | MEDLINE | ID: mdl-30825227

RESUMEN

Amyloid-ß peptides (Aßs) are generated in a membrane-embedded state by sequential processing of amyloid precursor protein (APP). Although shedding of membrane-embedded Aß is essential for its secretion and neurotoxicity, the mechanism behind shedding regulation is not fully elucidated. Thus, we devised a Langmuir film balance-based assay to uncover this mechanism. We found that Aß shedding was enhanced under acidic pH conditions and in lipid compositions resembling raft microdomains, which are directly related to the microenvironment of Aß generation. Furthermore, Aß shedding efficiency was determined by the length of the C-terminal membrane-spanning region, whereas pH responsiveness appears to depend on the N-terminal ectodomain. These findings indicate that Aß shedding may be directly coupled to its generation and represents an unrecognized control mechanism regulating the fate of membrane-embedded products of APP processing.


Asunto(s)
Péptidos beta-Amiloides/química , Micropartículas Derivadas de Células/metabolismo , Endosomas/química , Péptidos beta-Amiloides/metabolismo , Animales , Micropartículas Derivadas de Células/química , Dicroismo Circular , Endosomas/metabolismo , Humanos , Concentración de Iones de Hidrógeno , Microdominios de Membrana/metabolismo , Dominios Proteicos
4.
Sci Rep ; 8(1): 1494, 2018 01 24.
Artículo en Inglés | MEDLINE | ID: mdl-29367639

RESUMEN

The causal relationship between conformational folding and disulfide bonding in protein oxidative folding remains incompletely defined. Here we show a stage-dependent interplay between the two events in oxidative folding of C-reactive protein (CRP) in live cells. CRP is composed of five identical subunits, which first fold spontaneously to a near-native core with a correctly positioned C-terminal helix. This process drives the formation of the intra-subunit disulfide bond between Cys36 and Cys97. The second stage of subunit folding, however, is a non-spontaneous process with extensive restructuring driven instead by the intra-subunit disulfide bond and guided by calcium binding-mediated anchoring. With the folded subunits, pentamer assembly ensues. Our results argue that folding spontaneity is the major determinant that dictates which event acts as the driver. The stepwise folding pathway of CRP further suggests that one major route might be selected out of the many in theory for efficient folding in the cellular environment.


Asunto(s)
Proteína C-Reactiva/química , Disulfuros/química , Conformación Proteica , Pliegue de Proteína , Humanos , Modelos Moleculares , Oxidación-Reducción
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