Preparation and solution properties of a novel cationic hydrophobically modified polyacrylamide for enhanced oil recovery

Financial support from National Natural Science Foundation of China (51504050, 51774062), Scientific and Technological Research Program of Chongqing Municipal Education Commission (KJ1601305) and Research Foundation of Chongqing University of Science & Technology (CK2016B07, CK2016Z20).Peer reviewedPostprin

Seeing What You Miss: Vision-Language Pre-training with Semantic Completion Learning

Cross-modal alignment is essential for vision-language pre-training (VLP) models to learn the correct corresponding information across different modalities. For this purpose, inspired by the success of masked language modeling (MLM) tasks in the NLP pre-training area, numerous masked modeling tasks have been proposed for VLP to further promote cross-modal interactions. The core idea of previous masked modeling tasks is to focus on reconstructing the masked tokens based on visible context for learning local-to-local alignment. However, most of them pay little attention to the global semantic features generated for the masked data, resulting in the limited cross-modal alignment ability of global representations. Therefore, in this paper, we propose a novel Semantic Completion Learning (SCL) task, complementary to existing masked modeling tasks, to facilitate global-to-local alignment. Specifically, the SCL task complements the missing semantics of masked data by capturing the corresponding information from the other modality, promoting learning more representative global features which have a great impact on the performance of downstream tasks. Moreover, we present a flexible vision encoder, which enables our model to perform image-text and video-text multimodal tasks simultaneously. Experimental results show that our proposed method obtains state-of-the-art performance on various vision-language benchmarks, such as visual question answering, image-text retrieval, and video-text retrieval

Experimental Study on Solar Cooling Tube Using Thermal/Vacuum Emptying Method

A solar cooling tube using thermal/vacuum emptying method was experimentally studied in this paper. The coefficient of performance (COP) of the solar cooling tube was mostly affected by the vacuum degree of the system. In past research, the thermal vacuum method, using an electric oven and iodine-tungsten lamp to heat up the adsorbent bed and H2O vapor to expel the air from the solar cooling tube, was used to manufacture solar cooling tubes. This paper presents a novel thermal vacuum combined with vacuum pump method allowing an increased vacuum state for producing solar cooling tubes. The following conclusions are reached: the adsorbent bed temperature of solar cooling tube could reaches up to 233°C, and this temperature is sufficient to meet desorption demand; the refrigerator power of a single solar cooling tube varies from 1 W to 12 W; the total supply refrigerating capacity is about 287 kJ; and the COP of this solar cooling tube is about 0.215

RNF8 is responsible for ATRA resistance in variant acute promyelocytic leukemia with GTF2I/RARA fusion, and inhibition of the ubiquitin–proteasome pathway contributes to the reversion of ATRA resistance

Abstract Background GTF2I-RARA is a newly identified RARA fusion gene in variant acute promyelocytic leukemia (APL) patients with t(7;17)(q11;q21). Clinical manifestation in the patient showed that it is a sort of ATRA-insensitive oncogene and is different from the classic PML-RARA in terms of therapeutic reaction. Methods To reveal the functional characteristics and regulating mechanism of the GTF2I-RARA fusion gene, we established a GTF2I-RARA-transfected HL60 cell model and examined its sensitivity to ATRA by western blot, MTT assay, flow cytometry, and Wright-Giemsa staining. Coimmunoprecipitation and confocal microscopy were used to examine the binding of GTF2I-RARA and transcriptional corepressors. We also performed ChIP-seq to search for potential target genes. Immunoprecipitation, ubiquitination assay, western blot, luciferase assay, and real-time PCR were used to analyze the effects of RNF8 on RARA. Flow cytometry and Wright-Giemsa staining were used to study the effect of MG132 and ATRA on the GTF2I-RARA-transfected HL60 cell model. Result We confirmed resistance of GTF2I-RARA to ATRA. Compared with PML-RARA, GTF2I-RARA has a higher affinity to HDAC3 under ATRA treatment. Using the ChIP-sequencing approach, we identified 221 GTF2I-RARA binding sites in model cells and found that the RING finger protein 8 (RNF8) is a target gene of GTF2I-RARA. RNF8 participates in disease progression and therapy resistance in APL with the GTF2I-RARA transcript. Elevated RNF8 expression promotes the interaction between RARA and RNF8 and induces RARA Lys-48 linkage ubiquitylation and degradation, resulting in attenuated transcriptional activation of RARA. Conclusion Our results suggest that RNF8 is a key GTF2I-RARA downstream event. Using the combination of MG132 and ATRA to treat GTF2I-RARA-HL60 cells, a synergistic effect leading to GTF2I-RARA-HL60 cell differentiation was confirmed. Taken together, the targeting of RNF8 may be an alternative choice for treatment in variant APL with GTF2I-RARA fusion

Targeting KRAS-mutant stomach/colorectal tumors by disrupting the ERK2-p53 complex

Summary: KRAS is widely mutated in human cancers, resulting in unchecked tumor proliferation and metastasis, which makes identifying KRAS-targeting therapies a priority. Herein, we observe that mutant KRAS specifically promotes the formation of the ERK2-p53 complex in stomach/colorectal tumor cells. Disruption of this complex by applying MEK1/2 and ERK2 inhibitors elicits strong apoptotic responses in a p53-dependent manner, validated by genome-wide knockout screening. Mechanistically, p53 physically associates with phosphorylated ERK2 through a hydrophobic interaction in the presence of mutant KRAS, which suppresses p53 activation by preventing the recruitment of p300/CBP; trametinib disrupts the ERK2-p53 complex by reducing ERK2 phosphorylation, allowing the acetylation of p53 protein by recruiting p300/CBP; acetylated p53 activates PUMA transcription and thereby kills KRAS-mutant tumors. Our study shows an important role for the ERK2-p53 complex and provides a potential therapeutic strategy for treating KRAS-mutant cancer