Cell Stress & Chaperones最新文献

{"title":"HSPA9/mortalin inhibition disrupts erythroid maturation through a TP53-dependent mechanism in human CD34+ hematopoietic progenitor cells","authors":"Christopher Butler ,&nbsp;Morgan Dunmire ,&nbsp;Jaebok Choi ,&nbsp;Gabor Szalai ,&nbsp;Anissa Johnson ,&nbsp;Wei Lei ,&nbsp;Xin Chen ,&nbsp;Liang Liu ,&nbsp;Wei Li ,&nbsp;Matthew J. Walter ,&nbsp;Tuoen Liu","doi":"10.1016/j.cstres.2024.03.006","DOIUrl":"10.1016/j.cstres.2024.03.006","url":null,"abstract":"<div><p>Myelodysplastic syndromes (MDS) are a heterogeneous group of clonal hematopoietic stem cell malignancies characterized by abnormal hematopoietic cell maturation, increased apoptosis of bone marrow cells, and anemia. They are the most common myeloid blood cancers in American adults. The full complement of gene mutations that contribute to the phenotypes or clinical symptoms in MDS is not fully understood. Around 10%–25% of MDS patients harbor an interstitial heterozygous deletion on the long arm of chromosome 5 [del(5q)], creating haploinsufficiency for a large set of genes, including <em>HSPA9</em>. The <em>HSPA9</em> gene encodes for the protein mortalin, a highly conserved heat shock protein predominantly localized in mitochondria. Our prior study showed that knockdown of <em>HSPA9</em> induces <em>TP53</em>-dependent apoptosis in human CD34+ hematopoietic progenitor cells. In this study, we explored the role of <em>HSPA9</em> in regulating erythroid maturation using human CD34+ cells. We inhibited the expression of <em>HSPA9</em> using gene knockdown and pharmacological inhibition and found that inhibition of <em>HSPA9</em> disrupted erythroid maturation as well as increased expression of p53 in CD34+ cells. To test whether the molecular mechanism of <em>HSPA9</em> regulating erythroid maturation is <em>TP53</em>-dependent, we knocked down <em>HSPA9</em> and <em>TP53</em> individually or in combination in human CD34+ cells. We found that the knockdown of <em>TP53</em> partially rescued the erythroid maturation defect induced by <em>HSPA9</em> knockdown, suggesting that the defect in cells with reduced <em>HSPA9</em> expression is <em>TP53</em>-dependent. Collectively, these findings indicate that reduced levels of <em>HSPA9</em> may contribute to the anemia observed in del(5q)-associated MDS patients due to the activation of <em>TP53</em>.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 2","pages":"Pages 300-311"},"PeriodicalIF":3.8,"publicationDate":"2024-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000580/pdfft?md5=1f5b558a892fe77e5b5e578ae5063080&pid=1-s2.0-S1355814524000580-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140173782","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Roles of heat shock protein A12A in the development of diabetic cardiomyopathy","authors":"Yunxiao Jia ,&nbsp;Yunhao Yu ,&nbsp;Chenxi Gao ,&nbsp;Yuehua Li ,&nbsp;Chuanfu Li ,&nbsp;Zhengnian Ding ,&nbsp;Qiuyue Kong ,&nbsp;Li Liu","doi":"10.1016/j.cstres.2024.03.004","DOIUrl":"10.1016/j.cstres.2024.03.004","url":null,"abstract":"<div><p>Long-term hyperglycemia can lead to diabetic cardiomyopathy (DCM), a main lethal complication of diabetes. However, the mechanisms underlying DCM development have not been fully elucidated. Heat shock protein A12A (HSPA12A) is the atypic member of the Heat shock 70kDa protein family. In the present study, we found that the expression of HSPA12A was upregulated in the hearts of mice with streptozotocin-induced diabetes, while ablation of HSPA12A improved cardiac systolic and diastolic dysfunction and increased cumulative survival of diabetic mice. An increased expression of HSPA12A was also found in H9c2 cardiac cells following treatment with high glucose (HG), while overexpression of HSPA12A-enhanced the HG-induced cardiac cell death, as reflected by higher levels of propidium iodide cells, lactate dehydrogenase leakage, and caspase 3 cleavage. Moreover, the HG-induced increase of oxidative stress, as indicated by dihydroethidium staining, was exaggerated by HSPA12A overexpression. Further studies demonstrated that the HG-induced increases of protein kinase B and forkhead box transcription factors 1 phosphorylation were diminished by HSPA12A overexpression, while pharmacologically inhibition of protein kinase B further enhanced the HG-induced lactate dehydrogenase leakage in HSPA12A overexpressed cardiac cells. Together, the results suggest that hyperglycemia upregulated HSPA12A expression in cardiac cells, by which induced cell death to promote DCM development. Targeting HSPA12A may serve as a potential approach for DCM management.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 2","pages":"Pages 272-284"},"PeriodicalIF":3.8,"publicationDate":"2024-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000555/pdfft?md5=0db4791c23c9ea66630d02b39b5ca58b&pid=1-s2.0-S1355814524000555-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140130827","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comprehensive analysis of human tissues reveals unique expression and localization patterns of HSF1 and HSF2","authors":"Jenny Joutsen ,&nbsp;Jenny C. Pessa ,&nbsp;Otto Jokelainen ,&nbsp;Reijo Sironen ,&nbsp;Jaana M. Hartikainen ,&nbsp;Lea Sistonen","doi":"10.1016/j.cstres.2024.03.001","DOIUrl":"10.1016/j.cstres.2024.03.001","url":null,"abstract":"<div><p>Heat shock factors (HSFs) are the main transcriptional regulators of the evolutionarily conserved heat shock response. Beyond cell stress, several studies have demonstrated that HSFs also contribute to a vast variety of human pathologies, ranging from metabolic diseases to cancer and neurodegeneration. Despite their evident role in mitigating cellular perturbations, the functions of HSF1 and HSF2 in physiological proteostasis have remained inconclusive. Here, we analyzed a comprehensive selection of paraffin-embedded human tissue samples with immunohistochemistry. We demonstrate that both HSF1 and HSF2 display distinct expression and subcellular localization patterns in benign tissues. HSF1 localizes to the nucleus in all epithelial cell types, whereas nuclear expression of HSF2 was limited to only a few cell types, especially the spermatogonia and the urothelial umbrella cells. We observed a consistent and robust cytoplasmic expression of HSF2 across all studied smooth muscle and endothelial cells, including the smooth muscle cells surrounding the vasculature and the high endothelial venules in lymph nodes. Outstandingly, HSF2 localized specifically at cell–cell adhesion sites in a broad selection of tissue types, such as the cardiac muscle, liver, and epididymis. To the best of our knowledge, this is the first study to systematically describe the expression and localization patterns of HSF1 and HSF2 in benign human tissues. Thus, our work expands the biological landscape of these factors and creates the foundation for the identification of specific roles of HSF1 and HSF2 in normal physiological processes.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 2","pages":"Pages 235-271"},"PeriodicalIF":3.8,"publicationDate":"2024-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000531/pdfft?md5=276acc69f3c21955b980746e1289f179&pid=1-s2.0-S1355814524000531-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140064943","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The S1 spike protein of SARS-CoV-2 upregulates the ERK/MAPK signaling pathway in DC-SIGN-expressing THP-1 cells","authors":"Emma Lee Johnson ,&nbsp;Yuki Ohkawa ,&nbsp;Noriko Kanto ,&nbsp;Reiko Fujinawa ,&nbsp;Taiki Kuribara ,&nbsp;Eiji Miyoshi ,&nbsp;Naoyuki Taniguchi","doi":"10.1016/j.cstres.2024.03.002","DOIUrl":"10.1016/j.cstres.2024.03.002","url":null,"abstract":"<div><p>Dendritic cells, macrophages, neutrophils, and other antigen-presenting cells express various C-type lectin receptors that function to recognize the glycans associated with pathogens. The dendritic cell-specific intercellular adhesion molecule-3-grabbing non-integrin (DC-SIGN) binds various pathogens such as HIV glycoprotein 120, the Ebola glycoprotein, hemagglutinin, and the dengue virus glycoprotein in addition to the SARS-CoV-2 spike protein, and also triggers antigen-presenting cell endocytosis and immune escape from systemic infections. Many studies on the binding of SARS-CoV-2 spike protein with glycans have been published, but the underlying mechanism by which intracellular signaling occurs remains unclear. In this study, we report that the S1 spike protein of SARS-CoV-2 induces the phosphorylation of extracellular signal-regulated kinases (ERKs) in THP-1 cells, a DC-SIGN-expressing human monocytic leukemic cell line. On the other hand, the phosphorylation level of NF-κB remained unchanged under the same conditions. These data suggest that the major cell signaling pathway regulated by the S1 spike protein is the ERK pathway, which is superior to the NF-κB pathway in these DC-SIGN-expressing THP-1 cells and may contribute to immune hyperactivation in SARS-CoV-2 infections. Additionally, several glycans such as mannans, mannosylated bovine serum albumin, the serum amyloid beta protein, and intracellular adhesion molecule 3 suppressed ERK phosphorylation, suggesting that these molecules are target molecules for SARS-CoV-2 infection by suppressing immune hyperactivation that occurs in the ERK signaling pathway.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 2","pages":"Pages 227-234"},"PeriodicalIF":3.8,"publicationDate":"2024-03-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000543/pdfft?md5=253303c3a8faf8c9efd6ef0f3318bbd5&pid=1-s2.0-S1355814524000543-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140058690","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"ArHsp90 is important in stress tolerance and embryo development of the brine shrimp, Artemia franciscana","authors":"Afnan Fatani ,&nbsp;Xiangyang Wu ,&nbsp;Yayra Gbotsyo ,&nbsp;Thomas H. MacRae ,&nbsp;Xiaojun Song ,&nbsp;Jiabo Tan","doi":"10.1016/j.cstres.2024.02.004","DOIUrl":"10.1016/j.cstres.2024.02.004","url":null,"abstract":"<div><p>Females of the extremophile crustacean, <em>Artemia franciscana</em>, either release motile nauplii <em>via</em> the ovoviviparous pathway or encysted embryos (cysts) <em>via</em> the oviparous pathway. Cysts contain an abundant amount of the ATP-independent small heat shock protein that contributes to stress tolerance and embryo development, however, little is known of the role of ATP-dependent molecular chaperone, heat shock protein 90 (Hsp90) in the two processes. In this study, a <em>hsp90</em> was cloned from <em>A. franciscana</em>. Characteristic domains of ArHsp90 were simulated from the deduced amino acid sequence, and 3D structures of ArHsp90 and Hsp90s of organisms from different groups were aligned. RNA interference was then employed to characterize ArHsp90 in <em>A. franciscana</em> nauplii and cysts. The partial knockdown of ArHsp90 slowed the development of nauplius-destined, but not cyst-destined embryos. ArHsp90 knockdown also reduced the survival and stress tolerance of nauplii newly released from <em>A. franciscana</em> females. Although the reduction of ArHsp90 had no effect on the development of diapause-destined embryos, the resulting cysts displayed reduced tolerance to desiccation and low temperature, two stresses normally encountered by <em>A. franciscana</em> in its natural environment. The results reveal that Hsp90 contributes to the development, growth, and stress tolerance of <em>A. franciscana</em>, an organism of practical importance as a feed source in aquaculture.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 2","pages":"Pages 285-299"},"PeriodicalIF":3.8,"publicationDate":"2024-02-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S135581452400052X/pdfft?md5=ec529d9b7effe9ea14a0b89cb3048fe4&pid=1-s2.0-S135581452400052X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140012252","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Intestinal heat shock proteins in metabolic syndrome: Novel mediators of obesity and its comorbidities resolution after metabolic surgery","authors":"Giulia Angelini ,&nbsp;Sara Russo ,&nbsp;Geltrude Mingrone","doi":"10.1016/j.cstres.2024.02.003","DOIUrl":"10.1016/j.cstres.2024.02.003","url":null,"abstract":"<div><p>Over the past 40 years, the prevalence of obesity has risen dramatically, reaching epidemic proportions. Metabolic surgery has proven to be highly effective in treating obesity, leading to significant improvements or complete resolution of obesity-related comorbidities.</p><p>Research conducted in both animals and humans suggests that the metabolic benefits achieved through metabolic surgery cannot be solely attributed to weight loss. Indeed, there has been an increasing recognition of intestinal inflammation as a novel factor influencing obesity. The gastrointestinal tract is continuously exposed to dietary components, particularly diets rich in saturated fats, which are known to contribute to obesity. It is now widely accepted that heat shock proteins can be released from various cells including intestinal epithelial cells and act as proinflammatory signals. Several studies have shown that circulating levels of glucose-regulated protein 78 (GRP78) are increased in subjects with obesity and correlate with the severity of the disease. Moreover, mice with a partial knockout of GRP78 are protected from diet-induced obesity.</p><p>In this review, we discuss the role of GRP78 in the development of obesity. Several evidence suggests that GRP78 can influence adipogenesis, lipid droplets stabilization, insulin resistance, and liver steatosis. We also provide an update on GRP78 regulation following metabolic surgery, focusing on the bypass of the small intestine as a key factor for GRP78 secretion. Finally, we discuss the potential role of monoclonal antibodies against GRP78 as a treatment for obesity.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 2","pages":"Pages 217-226"},"PeriodicalIF":3.8,"publicationDate":"2024-02-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000518/pdfft?md5=1715cd6a94ef99a5f146323a31decaec&pid=1-s2.0-S1355814524000518-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139982485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Second international symposium on the chaperone code, 2023","authors":"Johannes Buchner ,&nbsp;Milad J. Alasady ,&nbsp;Sarah J. Backe ,&nbsp;Brian S.J. Blagg ,&nbsp;Richard L. Carpenter ,&nbsp;Giorgio Colombo ,&nbsp;Ioannis Gelis ,&nbsp;Daniel T. Gewirth ,&nbsp;Lila M. Gierasch ,&nbsp;Walid A. Houry ,&nbsp;Jill L. Johnson ,&nbsp;Byoung Heon Kang ,&nbsp;Aimee W. Kao ,&nbsp;Paul LaPointe ,&nbsp;Seema Mattoo ,&nbsp;Amie J. McClellan ,&nbsp;Leonard M. Neckers ,&nbsp;Chrisostomos Prodromou ,&nbsp;Andrea Rasola ,&nbsp;Rebecca A. Sager ,&nbsp;Mark R. Woodford","doi":"10.1016/j.cstres.2024.01.003","DOIUrl":"10.1016/j.cstres.2024.01.003","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 88-96"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000439/pdfft?md5=50743cea79ad1daf680c078231bdfc5d&pid=1-s2.0-S1355814524000439-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139691320","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Expansion of the HSP70 gene family in Tegillarca granosa and expression profiles in response to zinc toxicity","authors":"Jinmu Kim ,&nbsp;Hyeon Jin Kim ,&nbsp;Eunkyung Choi ,&nbsp;Minjoo Cho ,&nbsp;Soyun Choi ,&nbsp;Mi Ae Jeon ,&nbsp;Jung Sick Lee ,&nbsp;Hyun Park","doi":"10.1016/j.cstres.2024.01.004","DOIUrl":"10.1016/j.cstres.2024.01.004","url":null,"abstract":"<div><p>Zinc (Zn) is an essential micronutrient in organisms and an abundant element in the Earth's crust. Trace amounts of Zn released from natural sources can enter aquatic ecosystems through weathering and erosion. Zn accumulates in organisms, and when its intracellular concentration exceeds a certain level, it can induce oxidative stress and trigger oxidative stress-mediated heat shock protein (HSP) modulation. HSP70 is the most evolutionarily conserved among the HSP families. Despite extensive research on HSP70 genes in bivalves, the HSP70 gene family of <em>Tegillarca granosa</em> is still poorly characterized. We identified 65 HSP70 genes belonging to 6 families in the <em>T. granosa</em> genome, with 50 HSPa12 and 11 HSPa B2 genes highly expanded. On chromosome 11, 39 HSP70 (60%) genes were identified, and the HSPa12A genes were highly duplicated. A total of 527 and 538 differentially expressed genes were identified in the gills and mantle based on Zn exposure, respectively. The Gene Ontology of cellular anatomical entities was significantly enriched with upregulated differentially expressed genes in the gills and mantle. Eight of the 11 HSPa B2 genes were upregulated in both tissues. Most of the genes identified in both tissues were involved in “protein homeostasis” and “inhibition of apoptosis,” which are associated with the HSP70 family's resistance to extrinsic and intrinsic stress. Hence, this study identified that the HSP70 gene family plays a vital role in the adaptation of aquatic organisms to heavy metal (e.g., Zn) stress in contaminated environments by compiling the different physiological responses to preserve homeostasis.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 97-112"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000440/pdfft?md5=ad09ad2baebf79c8de4bfba29f41d9e3&pid=1-s2.0-S1355814524000440-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139563624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Resolution of inflammation in chronic disease via restoration of the heat shock response (HSR)","authors":"Helena Trevisan Schroeder ,&nbsp;Carlos Henrique De Lemos Muller ,&nbsp;Thiago Gomes Heck ,&nbsp;Mauricio Krause ,&nbsp;Paulo Ivo Homem de Bittencourt Jr","doi":"10.1016/j.cstres.2024.01.005","DOIUrl":"10.1016/j.cstres.2024.01.005","url":null,"abstract":"<div><p>Effective resolution of inflammation <em>via</em> the heat shock response (HSR) is pivotal in averting the transition to chronic inflammatory states. This transition characterizes a spectrum of debilitating conditions, including insulin resistance, obesity, type 2 diabetes, nonalcoholic fatty liver disease, and cardiovascular ailments. This manuscript explores a range of physiological, pharmacological, and nutraceutical interventions aimed at reinstating the HSR in the context of chronic low-grade inflammation, as well as protocols to assess the HSR. Monitoring the progression or suppression of the HSR in patients and laboratory animals offers predictive insights into the organism’s capacity to combat chronic inflammation, as well as the impact of exercise and hyperthermic treatments (e.g., sauna or hot tub baths) on the HSR. Interestingly, a reciprocal correlation exists between the expression of HSR components in peripheral blood leukocytes (PBL) and the extent of local tissue proinflammatory activity in individuals afflicted by chronic inflammatory disorders. Therefore, the Heck index, contrasting extracellular 70 kDa family of heat shock proteins (HSP70) (proinflammatory) and intracellular HSP70 (anti-inflammatory) in PBL, serves as a valuable metric for HSR assessment. Our laboratory has also developed straightforward protocols for evaluating HSR by subjecting whole blood samples from both rodents and human volunteers to <em>ex vivo</em> heat challenges. Collectively, this discussion underscores the critical role of HSR disruption in the pathogenesis of chronic inflammatory states and emphasizes the significance of simple, cost-effective tools for clinical HSR assessment. This understanding is instrumental in the development of innovative strategies for preventing and managing chronic inflammatory diseases, which continue to exert a substantial global burden on morbidity and mortality.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 66-87"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000452/pdfft?md5=266ad508fb105aed45b464d6d281c245&pid=1-s2.0-S1355814524000452-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139680720","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Introduction of Dimitra Bourboulia as the new Editor-in-Chief of Cell Stress & Chaperones","authors":"Lawrence E. Hightower","doi":"10.1016/j.cstres.2024.01.008","DOIUrl":"10.1016/j.cstres.2024.01.008","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 1","pages":"Pages 49-50"},"PeriodicalIF":3.8,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000488/pdfft?md5=14a07f4491cf809076bffbdc5ab6e7d3&pid=1-s2.0-S1355814524000488-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139680719","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}