To save content items to your account,
please confirm that you agree to abide by our usage policies.
If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account.
Find out more about saving content to .
To save content items to your Kindle, first ensure firstname.lastname@example.org
is added to your Approved Personal Document E-mail List under your Personal Document Settings
on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part
of your Kindle email address below.
Find out more about saving to your Kindle.
Note you can select to save to either the @free.kindle.com or @kindle.com variations.
‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi.
‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.
Genetic approaches are increasingly advantageous in characterizing treatment-resistant schizophrenia (TRS). We aimed to identify TRS-associated functional brain proteins, providing a potential pathway for improving psychiatric classification and developing better-tailored therapeutic targets.
TRS-related proteome-wide association studies (PWAS) were conducted on genome-wide association studies (GWAS) from CLOZUK and the Psychiatric Genomics Consortium (PGC), which provided TRS individuals (n = 10,501) and non-TRS individuals (n = 20,325), respectively. The reference datasets for the human brain proteome were obtained from ROS/MAP and Banner, with 8,356 and 11,518 proteins collected, respectively. We then performed colocalization analysis and functional enrichment analysis to further explore the biological functions of the proteins identified by PWAS.
In PWAS, two statistically significant proteins were identified using the ROS/MAP and then replicated using the Banner reference dataset, including CPT2 (PPWAS-ROS/MAP = 4.15 × 10−2 and PPWAS-Banner = 3.38 × 10−3) and APOL2 (PPWAS-ROS/MAP = 4.49 × 10−3 and PPWAS-Banner = 8.26 × 10−3). Colocalization analysis identified three variants that were causally related to protein expression in the human brain, including CCDC91 (PP4 = 0.981), PRDX1 (PP4 = 0.894), and WARS2 (PP4 = 0.757). We extended PWAS results from gene-based analysis to pathway-based analysis, identifying 14 gene ontology (GO) terms and the only candidate pathway for TRS, metabolic pathways (all P < 0.05).
Our results identified two protein biomarkers, and cautiously support that the pathological mechanism of TRS is linked to lipid oxidation and inflammation, where mitochondria-related functions may play a role.
Flower-like AgI/Bi5O7I hybrid photocatalysts were fabricated via a hydrothermal method and the subsequent heating process with AgI/Bi4O5I2 as the intermediate. X-ray powder diffraction, Raman, X-ray photoelectron spectroscopy, diffuse reflectance spectra, scanning electron microscopy, transmission electron microscopy, photoluminescence, and electrochemical methods were used to reveal the structure, elemental content, morphology, and charge separation capabilities of the as-prepared samples. The photocatalytic test showed that the AgI/Bi5O7I composites own much higher photoactivity than pure AgI and Bi5O7I. Based on the result of XPS analysis, the composite is believed to be the Ag/AgI/Bi5O7I system. Due to the suitable band potentials of AgI and Bi5O7I, the ternary system can form a heterojunction structure which works in a Z-scheme mechanism with Ag nanoparticles as the transfer media. The guided charge transfer in the composite prolongs the life time of charge carriers and eventually leads to the high photocatalytic activity of AgI/Bi5O7I. Additionally, the flower-like structure of the composite also contributes to the photocatalytic reaction.
Email your librarian or administrator to recommend adding this to your organisation's collection.