研究热点和Endoplasmic网膜压力趋势在肥胖2014年至2024年:一个CiteSpace可视化分析分析
Xiaotian Zhang1, Mengjie Kang2, Yuan Cai1
1Pathology and Pathophysiology, Baoji Central Hospital, Baoji, CHN.
Cureus
|September 29, 2025
概括
研究表明,内等质网膜 (ER) 压力越来越多地与肥胖有关. 关键趋势集中在分子机制,疾病联系和肥胖和相关疾病的新治疗点上.
科学领域:
- 生物医学研究生物医学研究
- 代谢障碍 代谢障碍 代谢障碍
- 细胞生物学 细胞生物学
背景情况:
- 肥胖是一个日益严重的全球健康问题.
- 细胞内膜网膜 (ER) 压力与代谢功能障碍有关.
- 了解ER压力与肥胖之间的联系对于开发干预措施至关重要.
研究的目的:
- 分析2014-2024年ER压力和肥胖的研究趋势和关键话题.
- 确定这个研究领域的新兴焦点和合作.
- 为未来的研究方向和治疗策略提供见解.
主要方法:
- 从科学网络核心集合 (2014-2024) 中对出版物的图书统计分析.
- 利用CiteSpace软件进行趋势,关键字和集群的视觉分析.
- 专注于"文章"和"评论"以捕捉全面的研究见解.
主要成果:
- 观察到,关于ER压力和肥胖的年度出版物显著增加.
- 中国和美国是这项研究的主要贡献者.
- 关键词包括"内质网膜应激"",胰岛素抵抗"",氧化应激"",肥胖"和"未折叠的蛋白质反应".
- 显著的集群被确定为:"卵泡功能障碍"",能量稳态"和"激活转录因子".
- 持续的主题包括"能量稳态"",代谢综合征"和"饮食引起的非酒精性脂肪肝炎".
结论:
- 关于ER压力和肥胖的研究正在迅速扩大,重点关注分子机制和疾病关联.
- 这些发现突出了开发肥胖相关疾病的新疗法点的潜力.
- 未来的研究应该继续探索这些分子途径的临床转化.
相关概念视频
01:17Role of ER in the Secretory Pathway
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Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
6.9K
01:37The Unfolded Protein Response
6.2K
The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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01:29Protein Folding Quality Check in the RER
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.0K
01:31Regulation of the Unfolded Protein Response
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.9K
01:26Protein Modifications in the RER
6.9K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.9K
01:27Post-translational Translocation of Proteins to the RER
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
7.5K