Global research development of chondrosarcoma from 2003 to 2022: a bibliometric analysis

BackgroundChondrosarcomas are common primary malignant bone tumors; however, comprehensive bibliometric analysis in this field has not yet been conducted. Therefore, this study aimed to explore the research hotspots and trends in the field of chondrosarcoma through bibliometric analysis to help researchers understand the current status and direction of research in the field.MethodsArticles and reviews related to chondrosarcoma published between 2003 and 2022 were retrieved from the Web of Science. Countries, institutions, authors, journals, references, and keywords in this field were visualized and analyzed using CtieSpace and VOSviewer software.ResultsBetween 2003 and 2022, 4,149 relevant articles were found. The number of articles published on chondrosarcoma has increased significantly annually, mainly from 569 institutions in China and the United States, and 81 in other countries. In total, 904 authors participated in the publication of studies related to chondrosarcomas. Over the past 20 years, articles on chondrosarcoma have been published in 958 academic journals, with Skeletal Radiology having the highest number of publications. Furthermore, keywords such as “gene expression,” “radiotherapy,” “experience,” and “apoptosis” have been popular in recent years.ConclusionOver the past 20 years, the global trend in chondrosarcoma research has primarily been clinical research, with basic research as a supplement. In the future, communication and exchange between countries and institutions should be strengthened. Further, the future main research hotspots in the field of chondrosarcoma include mutated genes and signaling pathways, precision surgical treatment, proton therapy, radiation therapy, chemotherapy, immunotherapy, and other aspects

Optimization and development of the welding system for fiber-optic duct joints

At present, the fiber optic ducts are connected by a mechanical type of joint. In this method, two ducts cut in the right angle are pushed in from both sides of the joint, and takes approximately one second to joint ducts together. The problem with the existing joint technology is that if there is water inside of the joint, it will be damaged when the water freezes into ice, and then may cause leakage. There is a risk of explosion when compressed air to blow the fiber. Thus, a joint protection device (silicone rubber sleeve) was developed to seal the joint for protection utterly. However, this will cause the larger size of the entire joint and limit the number of single-duct joints next to each other in a multi-duct joint. Fiber optic ducts are made of High-Density Polyethylene, which is the best plastic for remelting and can be welded by using the electro-fusion welding method. Based on the thermoplasticity of this material, this thesis developed a plastic joint with a built-in conductive metal wire inside. The applied voltage will heat the wire, then remelt the duct surfaces to weld them together through the joint. The welding system uses a portable battery operating system, so there is no need to connect it to the grid. To prevent the battery from being damaged by supplying too much current, a capacitor bank is used to store high energy for the preheating joints. The system uses a microcontroller to control and monitor current and voltage to ensure uniform heating of the metal wire. Theemphasisof this thesis isplacedon the implementation of basic experiments to run the welding system. Multiple welding experiments show that the welding system can manually set parameters to control the welding current of different joints, thereby ensuring the welding quality. Using a 2.5Ω joint to weld ducts will approximately consume 120J from the battery, so a fully charged 42V, 4.4AH rechargeable battery can perform almost 5600 times of welding. The suitable range of joint resistance will decrease as the required energy consumption increases/ the welding time decreases

Design and Development of a Battery Powered Electrofusion Welding System for Optical Fiber Microducts

At present, optical fiber microducts are coupled together by mechanical types of joints. Mechanical joints are thick, require a large space, and reduce the installation distance in multi-microduct installation. They may leak or explode in the blown fiber installation process. Mechanical joints are subjected to time dependent deterioration under long service times beneath the earth's surface. It may start with a small leakage, followed by damage due to water freezing inside the optical fiber microduct. Optical fiber microducts are made up of high-density polyethylene, which is considered most suitable for thermoelectric welding. For thermoelectric welding of two optical fiber microducts, the welding time should be one second, and should not cause any damage to the inner structure of the microducts that are being coupled. To fulfill these requirements, an LTspice simulation model for the welding system was developed and validated. The developed LTspice model has two parts. The first part models the power input to joule heating wire and the second part models the heat propagation inside the different layers of the optical fiber microduct and surrounding joint by using electro-thermal analogy. In order to validate the simulation results, a battery powered prototype welding system was developed and tested. The prototype welding system consists of a custom-built electrofusion joint and a controller board. A 40 volt 4 ampere-hour Li-Ion battery was used to power the complete system. The power drawn from the battery was controlled by charging and discharging of a capacitor bank, which makes sure that the battery is not overloaded. After successful welding, a pull strength test and an air pressure leakage test were performed to ensure that the welded joints met the requirements set by the mechanical joints. The results show that this new kind of joint and welding system can effectively replace mechanical joints in future optical fiber duct installations

SVDD Challenge 2024: A Singing Voice Deepfake Detection Challenge (CtrSVDD Track, Training/Development Set)

<p>For more information about SVDD Challenge 2024, please refer to https://challenge.singfake.org/.<br><br>We have released the training and development set here and other relevant scripts on GitHub (https://github.com/SVDDChallenge/SVDD_Utils). For evaluation, we will provide a test set with undisclosed labels at a later date and ask teams to score each utterance. Using the submitted scores, we will calculate and rank participant systems on EER.<br><br>Please note that due to licensing issues, the training and development set here is <strong>not complete.</strong> Please follow the instructions detailed in the GitHub repository to complete the generation process of the dataset.</p&gt

Hepatitis B virus RNAs co-opt ELAVL1 for stabilization and CRM1-dependent nuclear export.

Hepatitis B virus (HBV) chronically infects 296 million people worldwide, posing a major global health threat. Export of HBV RNAs from the nucleus to the cytoplasm is indispensable for viral protein translation and genome replication, however the mechanisms regulating this critical process remain largely elusive. Here, we identify a key host factor embryonic lethal, abnormal vision, Drosophila-like 1 (ELAVL1) that binds HBV RNAs and controls their nuclear export. Using an unbiased quantitative proteomics screen, we demonstrate direct binding of ELAVL1 to the HBV pregenomic RNA (pgRNA). ELAVL1 knockdown inhibits HBV RNAs posttranscriptional regulation and suppresses viral replication. Further mechanistic studies reveal ELAVL1 recruits the nuclear export receptor CRM1 through ANP32A and ANP32B to transport HBV RNAs to the cytoplasm via specific AU-rich elements, which can be targeted by a compound CMLD-2. Moreover, ELAVL1 protects HBV RNAs from DIS3+RRP6+ RNA exosome mediated nuclear RNA degradation. Notably, we find HBV core protein is dispensable for HBV RNA-CRM1 interaction and nuclear export. Our results unveil ELAVL1 as a crucial host factor that regulates HBV RNAs stability and trafficking. By orchestrating viral RNA nuclear export, ELAVL1 is indispensable for the HBV life cycle. Our study highlights a virus-host interaction that may be exploited as a new therapeutic target against chronic hepatitis B

AU-rich elements in HBV RNAs are essential for ELAVL1 binding.

(A) Sequence of wild type pgRNA and mutant pgRNA used for RNA pulldown. (B) HepG2-NTCP cell lysates were incubated with biotinylated pgRNA or its mutant coated magnetic beads to pull down binding proteins. Levels of ELAVL1 in beads elutes were detected by WB. (C) Venn diagram of pgRNA and its mutant binders identified by RNA pulldown-LC-MS/MS. (D) Myc-ELAVL1 and Myc-HBc were co-transfected with pCDNA3.1-T7-pgRNA into Huh7 cells respectively. RIP assay was conducted to investigate interaction of ELAVL1-pgRNA and HBc-pgRNA. (E) Schematic diagram of pgRNA probe (227nt) and its mutant used for REMSA. (F) In vitro expressed and purified ELAVL1 were incubated with biotin labeled pgRNA probes. The samples were subjected to REMSA assay to detect the pgRNA probe and ELAVL1 binding. (G) The biotin labeled pgRNAAUUUA to AUCUC probe or wild type pgRNA probe was incubated with in vitro purified ELAVL1. REMSA assay was performed to detected pgRNA and ELAVL1 binding. Unlabeled wild type pgRNA probe and biotin labeled IRE1 probe as control. (H) Before biotin labeled pgRNA probe incubation, unlabeled pgRNA probe or the mutant was incubated with ELAVL1 (for cold compete). Before biotin labeled pgRNA probe incubation, the purified ELAVL1 was incubated with ELAVL1 targeted antibody (for super shift assay). The samples were subjected to REMSA assay for biotin labeled pgRNA probe and ELAVL1 binding detection. (I and J) Huh7 cells were transfected with pgRNA or its mutant (mutation site as indicated in A) expressing plasmid. (I) Levels of HBc expression were determined by WB. (J) Subcellular levels of HBV mRNA in cytoplasm and nucleus were determined by qPCR (% of WT). (K) The cells were treated with 10 nM Actinomycin D for times as indicated. Levels of pgRNA were determined by qPCR (normalized to Cp value of pCDNA3.1-pgRNAWT or pCDNA3.1-pgRNAMut, % of 0 hour). (L) The plasmids expressing pcRNA, pgRNA, PreS1 mRNA, PreS2/S mRNA, and HBx mRNA were transfected into Huh7 cells respectively. RIP assay was conducted to investigate their binding ability to ELAVL1. (M) Sequence analysis for AREs in HBV RNAs.</p

Homology analysis for AREs in different HBV genotypes.

Homology analysis for AREs in different HBV genotypes.</p

Critical commercial kits.

Hepatitis B virus (HBV) chronically infects 296 million people worldwide, posing a major global health threat. Export of HBV RNAs from the nucleus to the cytoplasm is indispensable for viral protein translation and genome replication, however the mechanisms regulating this critical process remain largely elusive. Here, we identify a key host factor embryonic lethal, abnormal vision, Drosophila-like 1 (ELAVL1) that binds HBV RNAs and controls their nuclear export. Using an unbiased quantitative proteomics screen, we demonstrate direct binding of ELAVL1 to the HBV pregenomic RNA (pgRNA). ELAVL1 knockdown inhibits HBV RNAs posttranscriptional regulation and suppresses viral replication. Further mechanistic studies reveal ELAVL1 recruits the nuclear export receptor CRM1 through ANP32A and ANP32B to transport HBV RNAs to the cytoplasm via specific AU-rich elements, which can be targeted by a compound CMLD-2. Moreover, ELAVL1 protects HBV RNAs from DIS3+RRP6+ RNA exosome mediated nuclear RNA degradation. Notably, we find HBV core protein is dispensable for HBV RNA-CRM1 interaction and nuclear export. Our results unveil ELAVL1 as a crucial host factor that regulates HBV RNAs stability and trafficking. By orchestrating viral RNA nuclear export, ELAVL1 is indispensable for the HBV life cycle. Our study highlights a virus-host interaction that may be exploited as a new therapeutic target against chronic hepatitis B.</div

NXF1 regulates ELAVL1 and CRM1 expression to support HBV RNAs nucleocytoplasmic transport.

(A-E) NXF1 knockdown HepG2-NTCP cells were pretreated with 2.5% DMSO for 2 days following HBV infection at an MOI of 200 and were maintained with DMEM containing 2.5% DMSO for 7 days. (A) Knockdown efficiency of was confirmed by WB. (B) Levels of HBV DNA in supernatants were determined by qPCR (% of shCtrl). Secreted HBeAg and HBsAg levels were determined by ELISA (% of shCtrl). (C) Subcellular levels of HBV RNAs in cytoplasm and nucleus were determined by qPCR (% of shCtrl). Graphs show mean ± SD. *p (TIF)</p

Chemicals.

Hepatitis B virus (HBV) chronically infects 296 million people worldwide, posing a major global health threat. Export of HBV RNAs from the nucleus to the cytoplasm is indispensable for viral protein translation and genome replication, however the mechanisms regulating this critical process remain largely elusive. Here, we identify a key host factor embryonic lethal, abnormal vision, Drosophila-like 1 (ELAVL1) that binds HBV RNAs and controls their nuclear export. Using an unbiased quantitative proteomics screen, we demonstrate direct binding of ELAVL1 to the HBV pregenomic RNA (pgRNA). ELAVL1 knockdown inhibits HBV RNAs posttranscriptional regulation and suppresses viral replication. Further mechanistic studies reveal ELAVL1 recruits the nuclear export receptor CRM1 through ANP32A and ANP32B to transport HBV RNAs to the cytoplasm via specific AU-rich elements, which can be targeted by a compound CMLD-2. Moreover, ELAVL1 protects HBV RNAs from DIS3+RRP6+ RNA exosome mediated nuclear RNA degradation. Notably, we find HBV core protein is dispensable for HBV RNA-CRM1 interaction and nuclear export. Our results unveil ELAVL1 as a crucial host factor that regulates HBV RNAs stability and trafficking. By orchestrating viral RNA nuclear export, ELAVL1 is indispensable for the HBV life cycle. Our study highlights a virus-host interaction that may be exploited as a new therapeutic target against chronic hepatitis B.</div