BackgroundEnteropeptidase (EP) is a type II transmembrane serine protease and a physiological activator of trypsinogen. Extensive studies related to EP have been conducted to date. However, no bibliometric analysis has systematically investigated this theme. Our study aimed to visualize the current landscape and frontier trends of scientific achievements on EP, provide an overview of the past 120 years and insights for researchers and clinicians to facilitate future collaborative research and clinical intervention.MethodsQuantitative analysis of publications relating to EP from 1900 to 2020 was interpreted and graphed through the Science Citation Index Expanded of Web of Science Core Collection (limited to SCIE). Microsoft office 2019, GraphPad Prism 8, VOSviewer, and R-bibliometrix were used to conduct the bibliometric analysis.ResultsFrom 1900 to 2020, a total of 1,034 publications were retrieved. The USA had the largest number of publications, making the greatest contribution to the topic (n = 260, 25.15%). Active collaborations between countries/regions were also enrolled. Grant and Hermontaylor were perhaps the most impactful researchers in the landscape of EP. Protein Expression and Purification and the Journal of Biological Chemistry were the most prevalent (79/1,034, 7.64%) and cited journals (n = 2,626), respectively. Using the top 15 citations and co-citations achievements clarified the theoretical basis of the EP research field. Important topics mainly include the structure of EP, the affective factors for activating substrates by EP, EP-related disorders, and inhibitors of EP.ConclusionBased on the bibliometric analysis, we have gained a comprehensive analysis of the global status and research frontiers of studies investigating EP, which provides some guidance and reference for researchers and clinicians engaged in EP research.
Background: Calcium silicate biomaterials (CSB) have witnessed rapid development in the past 30 years. This study aimed to accomplish a comprehensive bibliometric analysis of the published research literature on CSB for biomedical applications and explore the research hotspot and current status.Methods: Articles related to CSB published in the last three decades (1990–2020) were retrieved from Web of Science Core Collection. The R bibliometrix package and VOSviewer were used to construct publication outputs and collaborative networking among authors, their institutes, countries, journals’ matrices and keywords plus.Results: A total of 872 publications fulfilling the search criteria were included. CSB is mainly reported for bone tissues and dental applications. Among researchers, Chang J from Chinese Academy of Sciences and Gandolfi MG from the University of Bologna are the most productive author in these two fields, respectively. China was the leading contributor to the research on CSB in the medical field. A total of 130 keywords appeared more ten or more times were identified. The term “mineral trioxide aggregate” ranked first with 268 occurrences. The co-occurrence analysis identified three major clusters: CSB in dentistry, bone tissue and vitro bioactivity.Conclusion: Calcium silicate biomaterials have a promising scope for various biomedical applications ranging from regeneration of hard tissues (bone and teeth) to skin, tumor, cardiac muscle and other soft tissues. This study may help researchers further understand the frontiers of the field.
Cathepsin B (CTSB) is a lysosomal protease implicated in the progression of various diseases. A large number of CTSB-related studies have been conducted to date. However, there is no comprehensive bibliometric analysis on this subject. In our study, we performed quantitative analysis of CTSB-related publications retrieved from the Science Citation Index Expanded (SCIE) of the Web of Science Core Collection (reference period: 2011–2021). A total of 3,062 original articles and reviews were retrieved. The largest number of publications were from USA (n = 847, 27.66%). The research output of each country showed positive correlation with gross domestic product (GDP) (r = 0.9745, P < 0.0001). Active collaborations between countries/regions were also observed. Reinheckel T and Sloane BF were perhaps the most impactful researchers in the research landscape of CTSB. Plos ONE was the most prevalent (119/3,062, 3.89%) and cited journal (3,021 citations). Comprehensive analysis of the top citations, co-citations, and keywords was performed to acquire the theoretical basis and hotspots of CTSB-related research. The main topics included CTSB-related cancers and inflammatory diseases, CTSB-associated cell death pattern, and the applications of CTSB. These results provide comprehensive insights into the current status of global CTSB-related research especially in pancreas, which is worthy of continued follow-up by practitioners and clinicians in this field.
BackgroundTo describe the development process and structural relationships of scientific achievements in endoscopic ultrasonography (EUS) in pancreatic tumors over the past decades and to reveal the key research topics using bibliometric analysis.MethodsAll relevant publications covering the research of EUS in pancreatic tumors from 1984 to 2021 were involved through the Web of Science Core Collection. R-bibliometrix was used to conduct the bibliometric analysis, and VOSviewer software was used to explore the hot spots and networks related to this field.ResultsBetween 1984 and 2021, 4071 publications were involved. The number of annual publications increased from 1 to 310. The United States contributed the most publications to this field (n=1433, 35.20%), followed by Japan (n=827, 20.31%) and Germany (n=319, 7.84%). There was active cooperation between countries/regions. Gastrointestinal Endoscopy (GIE) was the most productive journal and the most influential journal. Professor Giovannini M, who produced the most publications, had a great influence on this research. The focus in this field was clarified by analyzing the top 10 citations and co-citations publications. Moreover, the analysis of the keywords showed Important topics: “Classification of pancreatic tumor disease” “Development of EUS in the diagnosis of pancreatic tumor diseases,” and “Development of EUS in the treatment of pancreatic tumor diseases.”ConclusionFor the first time, bibliometric analysis was used to gain a deep understanding of the global trends of studies investigating EUS in pancreatic tumor diseases. The EUS field is rapidly evolving, and our study may be a critical reference for clinical researchers related to this field.
Enteropeptidase (EP) initiates intestinal digestion by proteolytically processing trypsinogen, generating catalytically active trypsin. EP dysfunction causes a series of pancreatic diseases including acute necrotizing pancreatitis. However, the molecular mechanisms of EP activation and substrate recognition remain elusive, due to the lack of structural information on the EP heavy chain. Here, we report cryo-EM structures of human EP in inactive, active, and substrate-bound states at resolutions from 2.7 to 4.9 Å. The EP heavy chain was observed to clamp the light chain with CUB2 domain for substrate recognition. The EP light chain N-terminus induced a rearrangement of surface-loops from inactive to active conformations, resulting in activated EP. The heavy chain then served as a hinge for light-chain conformational changes to recruit and subsequently cleave substrate. Our study provides structural insights into rearrangements of EP surface-loops and heavy chain dynamics in the EP catalytic cycle, advancing our understanding of EP-associated pancreatitis.
The enteropeptidase (EP) initiates the intestinal digestion by proteolytic processing of trypsinogen, generating catalytic active trypsin. The dysfunction of EP will cause a series of pancreatic diseases, the most severe of which is acute necrotizing pancreatitis. However, the molecular mechanism of EP activation and substrate recognition remain elusive due to the lack of structural information, hampering the structure-based research of EP and even further EP-targeted drug design. Here we report cryo-EM structures of human EP in multiple states, covering the functional cycle spanning from inactive to active state and eventually to the substrate binding state, with the inactive core region reached an atomic 2.7-Å-resolution. The heavy chain of EP exhibits a clamping configuration with the CUB2 domain serving for substrate recognition. The N-terminus of light chain induces the surface loop remodeling from inactive to active conformation, resulting in a highly dynamic and active EP. Then the heavy chain performs like a hinge to ensure the flexibility of light chain for substrate recruitment and subsequent cleavage. Our study provides structural insights of EP remodeling and heavy chain dynamics while performing enzymatic function, facilitating our understanding of the pathogenies of EP-related pancreatitis and the EP-targeted treatment of pancreatitis.
The enteropeptidase (EP) initiates the intestinal digestion by proteolytic processing of trypsinogen, generating catalytic active trypsin. The dysfunction of EP will cause a series of pancreatic diseases, the most severe of which is acute necrotizing pancreatitis. However, the molecular mechanism of EP activation and substrate recognition remain elusive due to the lack of structural information, hampering the structure-based research of EP and even further EP-targeted drug design. Here we report cryo-EM structures of human EP in multiple states, covering the functional cycle spanning from inactive to active state and eventually to the substrate binding state, with the inactive core region reached an atomic resolution of 2.7 angstrom. The heavy chain of EP exhibits a clamping configuration with the CUB2 domain serving for substrate recognition. The N-terminus of light chain induces the surface loop remodeling from inactive to active conformation, resulting in a highly dynamic and active EP. Then the heavy chain performs like a hinge to ensure the flexibility of light chain for substrate recruitment and subsequent cleavage. Our study provides structural insights of EP remodeling and heavy chain dynamics while performing enzymatic function, facilitating our understanding of the pathogenies of EP-related pancreatitis and the EP-targeted treatment of pancreatitis.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.