Cell Stress & Chaperones最新文献

{"title":"Genome-wide DNA methylation profiles regulate distinct heat stress response in zebu (Bos indicus) and crossbred (Bos indicus × Bos taurus) cattle","authors":"Basavaraj Sajjanar ,&nbsp;Mohd Tanzeel Aalam ,&nbsp;Owais Khan ,&nbsp;Sujoy K Dhara ,&nbsp;Jyotirmoy Ghosh ,&nbsp;Ravi Kumar Gandham ,&nbsp;Praveen K Gupta ,&nbsp;Pallab Chaudhuri ,&nbsp;Triveni Dutt ,&nbsp;Gyanendra Singh ,&nbsp;Bishnu Prasad Mishra","doi":"10.1016/j.cstres.2024.06.005","DOIUrl":"10.1016/j.cstres.2024.06.005","url":null,"abstract":"<div><p>Epigenetic variations result from long-term adaptation to environmental factors. The <em>Bos indicus</em> (zebu) adapted to tropical conditions, whereas <em>Bos taurus</em> adapted to temperate conditions; hence native zebu cattle and its crossbred (<em>B indicus</em> × <em>B taurus</em>) show differences in responses to heat stress. The present study evaluated genome-wide DNA methylation profiles of these two breeds of cattle that may explain distinct heat stress responses. Physiological responses to heat stress and estimated values of Iberia heat tolerance coefficient and Benezra's coefficient of adaptability revealed better relative thermotolerance of Hariana compared to the Vrindavani cattle. Genome-wide DNA methylation patterns were different for Hariana and Vrindavani cattle. The comparison between breeds indicated the presence of 4599 significant differentially methylated CpGs with 756 hypermethylated and 3845 hypomethylated in Hariana compared to the Vrindavani cattle. Further, we found 79 genes that showed both differential methylation and differential expression that are involved in cellular stress response functions. Differential methylations in the microRNA coding sequences also revealed their functions in heat stress responses. Taken together, epigenetic differences represent the potential regulation of long-term adaptation of Hariana (<em>B indicus</em>) cattle to the tropical environment and relative thermotolerance.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 4","pages":"Pages 603-614"},"PeriodicalIF":3.3,"publicationDate":"2024-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524001081/pdfft?md5=27758b5ec87f0e9fa45caa56cc3037e8&pid=1-s2.0-S1355814524001081-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141466372","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 influence of HSP inducers on salinity stress in sterlet sturgeon (Acipenser ruthenus): In vitro study on HSP expression, immune responses, and antioxidant capacity","authors":"Sevda Zarei ,&nbsp;Hossein Ghafouri ,&nbsp;Leila Vahdatiraad ,&nbsp;Behrooz Heidari","doi":"10.1016/j.cstres.2024.06.004","DOIUrl":"10.1016/j.cstres.2024.06.004","url":null,"abstract":"<div><p>Heat shock proteins (HSPs) play a crucial role in antioxidant systems, immune responses, and enzyme activation during stress conditions. Salinity changes can cause stress and energy expenditure in fish, resulting in mortality, especially in fingerlings. The purpose of this study was to examine the relationship between salinity and HSPs in stressed fish by assessing the effects of various HSP inducers (HSPis), including Pro-Tex® (800 mM), amygdalin (80 mM), and a novel synthetic compound derived from pirano piranazole (80 µM), on isolated cells from Sterlet Sturgeon (<em>Acipenser ruthenus</em>) exposed to 13 ‰ salinity (S13). After liver, kidney, and gill cells were cultured, the HSPi compounds were treated <em>in vitro</em> in the presence and absence of salinity. The expression patterns of HSP27, HSP70, and HSP90 were assessed by Western blotting. Biochemical enzymes (aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, and lactate dehydrogenase), cortisol levels, and immune parameters (component 3, immunoglobulin M, and lysozyme) were measured before and after treatment with HSPis and HSPi + S13. According to these findings, HSPis positively modulate HSP expression, immune responses, and antioxidant levels. Furthermore, they increased <em>in vitro</em> cell survival by maintaining cortisol levels and biochemical enzyme activities in <em>A. ruthenus</em> under saline conditions (<em>P</em> &lt; 0.0001). In conclusion, HSPis can increase <em>A. ruthenus</em> resistance to salinity stress. However, the results also indicated that these compounds can reverse the adverse effects of salinity. The effectiveness of this approach depends on further research into the effects of these ecological factors on the health status of the species, especially <em>in vivo</em> and in combination with other stresses.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 4","pages":"Pages 552-566"},"PeriodicalIF":3.3,"publicationDate":"2024-06-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S135581452400107X/pdfft?md5=2f833a27219496ed1b914784a7d3a04a&pid=1-s2.0-S135581452400107X-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141442105","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":"Genome-wide identification of the HSP70 genes in Pacific oyster Magallana gigas and their response to heat stress","authors":"Hongbo Lu ,&nbsp;Chang Liu ,&nbsp;Chuanyan Yang ,&nbsp;Zhaoyu He ,&nbsp;Lingling Wang ,&nbsp;Linsheng Song","doi":"10.1016/j.cstres.2024.06.002","DOIUrl":"10.1016/j.cstres.2024.06.002","url":null,"abstract":"<div><p>Heat shock protein 70 (HSP70), the most prominent and well-characterized stress protein in animals, plays an important role in assisting animals in responding to various adverse conditions. In the present study, a total of 113 HSP70 gene family members were identified in the updated genome of <em>Magallana gigas</em> (designated <em>Mg</em>HSP70) (previously known as <em>Crassostrea gigas</em>). There were 75, 12, 11, and 8 HSP70s located in the cytoplasm, nucleus, mitochondria, and endoplasmic reticulum, respectively, and 7 HSP70s were located in both the nucleus and cytoplasm. Among 113 <em>Mg</em>HSP70 genes, 107 were unevenly distributed in 8 chromosomes of <em>M. gigas</em> with the greatest number in chromosome 07 (61 genes, 57.01%). The <em>Mg</em>HSP70 gene family members were mainly assigned into five clusters, among which the HSPa12 subfamily underwent lineage-specific expansion, consisting of 89 members. A total of 68 <em>Mg</em>HSP70 genes (60.18%) were tandemly duplicated and formed 30 gene pairs, among which 14 gene pairs were under strong positive selection. In general, the expression of <em>Mg</em>HSP70s was tissue-specific, with the highest expression in labial palp and gill and the lowest expression in adductor muscle and hemocytes. There were 35, 31, and 47 significantly upregulated genes at 6, 12, and 24 h after heat shock treatment (28 °C), respectively. The expression patterns of different tandemly duplicated genes exhibited distinct characteristics after shock treatment, indicating that these genes may have different functions. Nevertheless, genes within the same tandemly duplicated group exhibit similar expression patterns. Most of the tandemly duplicated HSP70 gene pairs showed the highest expression levels at 24 h. This study provides a comprehensive description of the <em>Mg</em>HSP70 gene family in <em>M. gigas</em> and offers valuable insights into the functions of HSP70 in the mollusc adaptation of oysters to environmental stress.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 4","pages":"Pages 589-602"},"PeriodicalIF":3.3,"publicationDate":"2024-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524001056/pdfft?md5=ec23a97084c8a16561a542b74788cdac&pid=1-s2.0-S1355814524001056-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141440200","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":"Biochemical characterization of ClpB and DnaK from Anaplasma phagocytophilum","authors":"Chathurange B. Ranaweera ,&nbsp;Sunitha Shiva ,&nbsp;Swetha Madesh ,&nbsp;Deepika Chauhan ,&nbsp;Roman R. Ganta ,&nbsp;Michal Zolkiewski","doi":"10.1016/j.cstres.2024.06.003","DOIUrl":"10.1016/j.cstres.2024.06.003","url":null,"abstract":"<div><p><em>Anaplasma phagocytophilum</em> is an intracellular tick-transmitted bacterial pathogen that infects neutrophils in mammals and causes granulocytic anaplasmosis. In this study, we investigated the molecular chaperones ClpB and DnaK from <em>A. phagocytophilum</em>. In <em>Escherichia coli</em>, ClpB cooperates with DnaK and its co-chaperones DnaJ and GrpE in ATP-dependent reactivation of aggregated proteins. Since ClpB is not produced in metazoans, it is a promising target for developing antimicrobial therapies, which generates interest in studies on that chaperone’s role in pathogenic bacteria. We found that ClpB and DnaK are transcriptionally upregulated in <em>A. phagocytophilum</em> 3–5 days after infection of human HL-60 and tick ISE6 cells, which suggests an essential role of the chaperones in supporting the pathogen’s intracellular life cycle. Multiple sequence alignments show that <em>A. phagocytophilum</em> ClpB and DnaK contain all structural domains that were identified in their previously studied orthologs from other bacteria. Both <em>A. phagocytophilum</em> ClpB and DnaK display ATPase activity, which is consistent with their participation in the ATP-dependent protein disaggregation system. However, despite a significant sequence similarity between the chaperones from <em>A. phagocytophilum</em> and those from <em>E. coli</em>, the former were not as effective as their <em>E. coli</em> orthologs during reactivation of aggregated proteins <em>in vitro</em> and in supporting the survival of <em>E. coli</em> cells under heat stress. We conclude that the <em>A. phagocytophilum</em> chaperones might have evolved with distinct biochemical properties to maintain the integrity of pathogenic proteins under unique stress conditions of an intracellular environment of host cells.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 4","pages":"Pages 540-551"},"PeriodicalIF":3.3,"publicationDate":"2024-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524001068/pdfft?md5=49daff0ee5c7e6a52943d2057ee3c41f&pid=1-s2.0-S1355814524001068-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141440199","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":"Mild heat shock at 40 °C increases levels of autophagy: Role of Nrf2","authors":"Mélanie Grondin,&nbsp;Claire Chabrol,&nbsp;Diana A. Averill-Bates","doi":"10.1016/j.cstres.2024.06.001","DOIUrl":"10.1016/j.cstres.2024.06.001","url":null,"abstract":"<div><p>The exposure to low doses of stress induces an adaptive survival response that involves the upregulation of cellular defense systems such as heat shock proteins (Hsps), anti-apoptosis proteins, and antioxidants. Exposure of cells to elevated, non-lethal temperatures (39–41 °C) is an adaptive survival response known as thermotolerance, which protects cells against subsequent lethal stress such as heat shock (&gt;41.5 °C). However, the initiating factors in this adaptive survival response are not understood. This study aims to determine whether autophagy can be activated by heat shock at 40 °C and if this response is mediated by the transcription factor Nrf2. Thermotolerant cells, which were developed during 3 h at 40 °C, were resistant to caspase activation at 42 °C. Autophagy was activated when cells were heated from 5 to 60 min at 40 °C. Levels of acidic vesicular organelles (AVOs) and autophagy proteins Beclin-1, LC3-II/LC3-I, Atg7, Atg5, Atg12–Atg5, and p62 were increased. When Nrf2 was overexpressed or depleted in cells, levels of AVOs and autophagy proteins were higher in unstressed cells, compared to the wild type. Stress induced by mild heat shock at 40 °C further increased levels of most autophagy proteins in cells with overexpression or depletion of Nrf2. Colocalization of p62 and Keap1 occurred. When Nrf2 levels are low, activation of autophagy would likely compensate as a defense mechanism to protect cells against stress. An improved understanding of autophagy in the context of cellular responses to physiological heat shock could be useful for cancer treatment by hyperthermia and the protective role of adaptive responses against environmental stresses.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 4","pages":"Pages 567-588"},"PeriodicalIF":3.3,"publicationDate":"2024-06-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000786/pdfft?md5=f2b8911030277b82acebd30bccee89e5&pid=1-s2.0-S1355814524000786-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141330405","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":"An update on the status of HSP90 inhibitors in cancer clinical trials","authors":"Shraddha Rastogi ,&nbsp;Abhinav Joshi ,&nbsp;Nahoko Sato ,&nbsp;Sunmin Lee ,&nbsp;Min-Jung Lee ,&nbsp;Jane B. Trepel ,&nbsp;Len Neckers","doi":"10.1016/j.cstres.2024.05.005","DOIUrl":"10.1016/j.cstres.2024.05.005","url":null,"abstract":"<div><p>The evolutionary conserved molecular chaperone heat shock protein 90 (HSP90) plays an indispensable role in tumorigenesis by stabilizing client oncoproteins. Although the functionality of HSP90 is tightly regulated, cancer cells exhibit a unique dependence on this chaperone, leading to its overexpression, which has been associated with poor prognosis in certain malignancies. While various strategies targeting heat shock proteins (HSPs) involved in carcinogenesis have been explored, only inhibition of HSP90 has consistently and effectively resulted in proteasomal degradation of its client proteins. To date, a total of 22 HSP90 inhibitors (HSP90i) have been tested in 186 cancer clinical trials, as reported by clinicaltrials.gov. Among these trials, 60 % have been completed, 10 % are currently active, and 30 % have been suspended, terminated, or withdrawn. HSP90 inhibitors (HSP90i) have been used as single agents or in combination with other drugs for the treatment of various cancer types in clinical trials. Notably, improved clinical outcomes have been observed when HSP90i are used in combination therapies, as they exhibit a synergistic antitumor effect. However, as single agents, HSP90i have shown limited clinical activity due to drug-related toxicity or therapy resistance. Recently, active trials conducted in Japan evaluating TAS-116 (pimitespib) have demonstrated promising results with low toxicity as monotherapy and in combination with the immune checkpoint inhibitor nivolumab. Exploratory biomarker analyses performed in various trials have demonstrated target engagement that suggests the potential for identifying patient populations that may respond favorably to the therapy. In this review, we discuss the advances made in the past 5 years regarding HSP90i and their implications in anticancer therapeutics. Our focus lies in evaluating drug efficacy, prognosis forecast, pharmacodynamic biomarkers, and clinical outcomes reported in published trials. Through this comprehensive review, we aim to shed light on the progress and potential of HSP90i as promising therapeutic agents in cancer treatment.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 4","pages":"Pages 519-539"},"PeriodicalIF":3.3,"publicationDate":"2024-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000774/pdfft?md5=db192ffc0850103c8e0e50259ad55281&pid=1-s2.0-S1355814524000774-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141327280","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":"Editorial Board Members/Copyright","authors":"","doi":"10.1016/S1355-8145(24)00104-4","DOIUrl":"https://doi.org/10.1016/S1355-8145(24)00104-4","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 3","pages":"Page i"},"PeriodicalIF":3.8,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524001044/pdfft?md5=b068a17900e10325cf65c9a3c10b176e&pid=1-s2.0-S1355814524001044-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141325236","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":"Cover and caption","authors":"","doi":"10.1016/S1355-8145(24)00103-2","DOIUrl":"https://doi.org/10.1016/S1355-8145(24)00103-2","url":null,"abstract":"","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 3","pages":"Page OFC"},"PeriodicalIF":3.8,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524001032/pdfft?md5=6de4fd41fce078676ab53363f4ba2cba&pid=1-s2.0-S1355814524001032-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141325235","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":"Mechanisms involved in the regulation of mitochondrial quality control by PGAM5 in heart failure","authors":"Yanli Wang ,&nbsp;Tiantian Ren ,&nbsp;Cuizhi Li ,&nbsp;Qiaomin Wu,&nbsp;Jinfeng Liu,&nbsp;Xuanke Guan,&nbsp;Xing Chang,&nbsp;Zhiming Liu,&nbsp;Ruxiu Liu","doi":"10.1016/j.cstres.2024.05.004","DOIUrl":"10.1016/j.cstres.2024.05.004","url":null,"abstract":"<div><p>Heart failure (HF) refers to a group of clinical syndromes in which various heart diseases lead to the inability of cardiac output to meet the metabolic needs of the body’s tissues. Cardiac metabolism requires enormous amounts of energy; thus, impaired myocardial energy metabolism is considered a key factor in the occurrence and development of HF. Mitochondria serve as the primary energy source for cardiomyocytes, and their regular functionality underpins healthy cardiac function. The mitochondrial quality control system is a crucial mechanism for regulating the functionality of cardiomyocytes, and any abnormality in this system can potentially impact the morphology and structure of mitochondria, as well as the energy metabolism of cardiomyocytes. Phosphoglycerate mutase 5 (PGAM5), a multifunctional protein, plays a key role in the regulation of mitochondrial quality control through multiple pathways. Therefore, abnormal PGAM5 function is closely related to mitochondrial damage. This article reviews the mechanism of PGAM5′s involvement in the regulation of the mitochondrial quality control system in the occurrence and development of HF, thereby providing a theoretical basis for future in-depth research.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 3","pages":"Pages 510-518"},"PeriodicalIF":3.8,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000762/pdfft?md5=aadafd8230818ef5065e9efa8c5b8594&pid=1-s2.0-S1355814524000762-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141183946","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":"Mitochondrial Chaperone Code: Just warming up","authors":"R. Felipe Perez ,&nbsp;Gianna Mochi ,&nbsp;Ariba Khan ,&nbsp;Mark Woodford","doi":"10.1016/j.cstres.2024.05.002","DOIUrl":"10.1016/j.cstres.2024.05.002","url":null,"abstract":"<div><p>More than 99% of the mitochondrial proteome is encoded by the nucleus and requires refolding following import. Therefore, mitochondrial proteins require the coordinated action of molecular chaperones for their folding and activation. Several heat shock protein (Hsp) molecular chaperones, including members of the Hsp27, Hsp40/70, and Hsp90 families, as well as the chaperonin complex Hsp60/10 have an established role in mitochondrial protein import and folding. The “Chaperone Code” describes the regulation of chaperone activity by dynamic post-translational modifications; however, little is known about the post-translational regulation of mitochondrial chaperones. Dissecting the regulation of chaperone function is essential for understanding their differential regulation in pathogenic conditions and the potential development of efficacious therapeutic strategies. Here, we summarize the recent literature on post-translational regulation of mitochondrial chaperones, the consequences for mitochondrial function, and potential implications for disease.</p></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"29 3","pages":"Pages 483-496"},"PeriodicalIF":3.8,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S1355814524000749/pdfft?md5=cabf429f9e7da88a1b10fe4fb854cd6b&pid=1-s2.0-S1355814524000749-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141024712","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}