Corrigendum to "The expression of thioredoxin-1 in acute epinephrine stressed mice" [Cell Stress and Chaperones 21 (2016) 935-941] [0.03%]
关于“急性肾上腺素刺激小鼠中硫氧还蛋白-1的表达”的更正论文(细胞压力与分子伴侣《21》(2016)935-941)
Jin-Jing Jia,Xian-Si Zeng,Kun Li et al.
Jin-Jing Jia et al.
Published Erratum
Cell stress & chaperones. 2026 Jul 30;31(5):100199. DOI:10.1016/j.cstres.2026.100199 2026
HSF1 acts as an endogenous protective mechanism in mechanically stretched alveolar epithelial cells [0.03%]
HSF1作为机械牵张的肺泡上皮细胞的内源性保护机制发挥作用
Jinqiu Ding,Xinyi Tang,Haoyue Xue et al.
Jinqiu Ding et al.
Mechanical ventilation is a key respiratory support measure for critically ill patients. During improper ventilation, continuous exposure of alveolar epithelial cells (AECs) to abnormal mechanical environment can lead to ventilator-induced ...
Size-dependent internalization of micro- and nanoplastics induces pro-inflammatory and oxidative stress responses in marine and freshwater fish cell lines [0.03%]
尺寸依赖性的微塑料和纳米塑料的内吞作用会诱导海水及淡水鱼类细胞系的促炎症反应以及氧化应激响应
Kiyun Park,Trang Thi Nguyen,Ihn-Sil Kwak
Kiyun Park
Microplastics (MPs) are ubiquitously detected in aquatic ecosystems and represent a growing environmental concern due to their persistence, accumulative toxicity, and ability to cross biological barriers, posing substantial risks to fish sp...
Hspa1b Attenuates Hypoxia/reoxygenation-induced Cardiomyocyte Injury Through Dual Suppression of P53-driven Apoptotic and Ferroptotic Pathways [0.03%]
Hspa1b通过双重抑制P53介导的凋亡和铁死亡途径减轻缺氧/复氧诱导的心肌细胞损伤
Chang Liu,Wensheng Qi,Yue Li et al.
Chang Liu et al.
While the cardioprotective role of heat shock proteins (HSPs) in cardiovascular diseases is well established, the isoform-specific functions of HSP70 members in ischemia-reperfusion (I/R) injury remain unclear. This study investigates the r...
Evolution of Hsp90 Targeting: From Stress Biology to Clinical Translation [0.03%]
Hsp90靶点的演变：从压力生物学到临床转化
Ilham Zarguan,Lamiae Belayachi,Abdelaziz Benjouad et al.
Ilham Zarguan et al.
Hsp90 inhibitors represent a decades-long experimental framework that has progressively uncovered how molecular chaperone systems are organized, regulated, and rewired in disease. Early natural products established that pharmacologic engage...
Insights into the function and structure of the R2TP chaperone complex [0.03%]
R2TP 携带蛋白复合体的结构与功能关系研究
Maryama Mohamed,Ruikai Wu,Walid A Houry
Maryama Mohamed
The R2TP chaperone complex comprises two AAA+ proteins, RUVBL1 and RUVBL2, along with RPAP3 and PIH1D1. R2TP functions in concert with other chaperones, such as HSP90 and HSP70, to facilitate the assembly of macromolecular complexes integra...
Matthias P Mayer
Matthias P Mayer
Originally J-domain proteins (JDPs) were viewed as accessory co-chaperones of 70kDa heat shock proteins (Hsp70s), the actual chaperones, stimulating ATPase activity of Hsp70s when a protein substrate is bound. This view apparently underesti...
Katie M Whalen,Brian C Freeman
Katie M Whalen
The Hsp90 molecular chaperone is a key component of the protein homeostasis (proteostasis) system. Hsp90 likely serves as a gatekeeper in a cell's protein quality control decision tree since this chaperone is linked to nascent polypeptide f...
Ninth BHD International Symposium: Advancing Research Through Global Collaboration [0.03%]
BHD国际研讨会第九届：全球协作推动研究进展
Neil Rajan,Masaya Baba,Andrea Ballabio et al.
Neil Rajan et al.
The 9th Birt-Hogg-Dubé (BHD) International Symposium convened virtually in March 2026. The meeting attracted more than 100 participants internationally and highlighted recent findings in a variety of areas, including genetic insight and mo...
Extracellular 70kDa heat shock protein in blood plasma binds insulin and modulates glycaemic control in vivo [0.03%]
血液等离子体中的细胞外70kDa热休克蛋白可结合胰岛素并调节体内血糖控制
Mirna Stela Ludwig,Thiago Gomes Heck,Vânia Cibele Minguetti-Câmara et al.
Mirna Stela Ludwig et al.
Background & hypothesis: The 70kDa heat shock protein family (HSP70) preserves the three-dimensional integrity of intracellular proteins, preventing the formation of cytotoxic aggregates that activate inflammatory pathway...