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Objective: In this study, we utilized bibliometric methods to assess the worldwide scientific output and identify hotspots related to the research on the volume-regulated anion channel VRAC from to To analyzed the data, we utilized VOSviewer, a tool for visualizing network, to create networks based on the collaboration between countries, institutions, and authors. Additionally, we performed an analysis of journal co-citation, document citation, and co-occurrence of keywords. Furthermore, we employed CiteSpace 6. R6 Advanced to analyzed keywords and co-cited references with the strongest burst. Results: The final analysis included a total of related articles and reviews, covering the period from to The United States emerged as the leading country contributing to this field, while the University of Copenhagen stood out as the most prominent institution. The author with most publications and most citations was Thomas J. Among the cited references, the article by Voss et al. Through the analysis of keyword co-occurrence, it was discovered that VRAC is involved in various physiological processes including cell growth, migration, apoptosis, swelling, and myogenesis, as well as anion and organic osmolyte transport including chloride, taurine, glutamate and ATP. VRAC is also associated with related ion channels such as TMEM16A, TMEM16F, pannexin, and CFTR, and associated with various diseases including epilepsy, leukodystrophy, atherosclerosis, hypertension, cerebral edema, stroke, and different types of cancer including gastric cancer, glioblastoma and hepatocellular carcinoma. Furthermore, VRAC is involved in anti-tumor drug resistance by regulating the uptake of platinum-based drugs and temozolomide. Conclusion: The aim of this bibliometric analysis is to provide an overall perspective for research on VRAC. VRAC has become a topic of increasing interest, and our analysis shows that it continues to be a prominent area.

Cell-volume regulation: P-glycoprotein-a cautionary tale. Figure 4B depicts the co-authorship network involving institutions with more than two papers to the VRAC research lee vrac.

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Inactivation and anion selectivity of volume-regulated anion channels VRACs depend on C-terminal residues of the first extracellular loop. Bioessays 34 , — Functional significance of cell volume regulatory mechanisms. Figure 4B depicts the co-authorship network involving institutions with more than two papers to the VRAC research field. Kern, D. The articles we identified in this analysis were categorized into 44 research areas. Next, we examined a network of authors who collaborated on over three publications Figure 6. The thickness of the lines indicates the relationship strength. Identification of key signaling molecules involved in the activation of the swelling-activated chloride current in human glioblastoma cells. Subunit-dependent oxidative stress sensitivity of LRRC8 volume-regulated anion channels.

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Not yet checked. Among them, the United States had the most publications with 85 articles, accounting for VRAC has been suggested to be one of these ion channels. The results revealed a consistent increase in the quantity of research papers on VRAC during the past 8 years, with an average annual publication count of Despite the growing body of research in the VRAC field, there has been a lack of systematic investigation into the topics and characteristics of most-cited articles regarding the VRAC channel. Lutter, D. In vivo studies in nude mouse models have also shown that LRRC8A downregulation suppressed the proliferation of colon carcinoma, hepatocellular carcinoma, and cervical cancer Zhang et al. LRRC8A-dependent volume-regulated anion channels contribute to ischemia-induced brain injury and glutamatergic input to hippocampal neurons. With the inclusion of a vast majority of papers published between and , the latest published studies would not significantly impact the final results. The site is secure. Top ten widely explored and extensively researched fields on VRAC. A year journey from volume-regulated anion currents to molecular structure of the LRRC8 channel.