Cell Stress & Chaperones最新文献

{"title":"Isopimaric acid derived from Torreya nucifera blocks autophagy and mitophagy to sensitize colon cancer cells to nutrient starvation","authors":"Rambukkana Maggonage Thiruni Dananjana Perera ,&nbsp;Su-Lim Kim ,&nbsp;Ji-Hyang Kim ,&nbsp;Kyeoung Cheol Kim ,&nbsp;Dong-Sun Lee","doi":"10.1016/j.cstres.2026.100151","DOIUrl":"10.1016/j.cstres.2026.100151","url":null,"abstract":"<div><div>Autophagy and mitophagy are essential survival mechanisms that enable cancer cells to adapt to metabolic stress, particularly during nutrient deprivation. Therefore, targeting these pathways presents a promising therapeutic strategy. Thus, this study aimed to investigate the potential of isopimaric acid (IPA), a diterpenoid compound derived from <em>Torreya nucifera</em>, to disrupt autophagy-related processes in colon cancer cells. Notably, IPA treatment promoted the accumulation of autophagosomes, as indicated by increased LC3-II and p62 protein levels, suggesting an inhibition of autophagic flux rather than an enhancement of initiation. Further analysis revealed that IPA impaired lysosomal function and blocked autophagosome degradation. IPA also suppressed mitophagy by downregulating key regulators, including PINK1 and Parkin, resulting in mitochondrial dysfunction and the accumulation of reactive oxygen species (ROS). Particularly, IPA was non-toxic under nutrient-rich conditions but induced significant cell death under serum starvation conditions. To our knowledge, these findings are the first to show that IPA selectively induces apoptotic cell death in nutrient-deprived colon cancer cells by disrupting both late-stage autophagy and PINK1/Parkin-mediated mitophagy. Furthermore, this research establishes the development of innovative therapeutic strategies that specifically target metabolic stress and combination therapy.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 2","pages":"Article 100151"},"PeriodicalIF":3.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146177936","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"New allosteric modulators of molecular chaperone TRAP1 from the integration of computational biology, medicinal chemistry, and biophysics","authors":"Federica Guarra ,&nbsp;Denis Komarov ,&nbsp;Andrea Ciamarone ,&nbsp;Luca Torielli ,&nbsp;Viola Previtali ,&nbsp;Natasha Margaroli ,&nbsp;Elisa Romeo ,&nbsp;Martina La Spina ,&nbsp;Francesca Sbuelz ,&nbsp;Claudio Laquatra ,&nbsp;Marina Veronesi ,&nbsp;Marco Lolicato ,&nbsp;Cristina Arrigoni ,&nbsp;Elisabetta Moroni ,&nbsp;Stefano A. Serapian ,&nbsp;Stefania Girotto ,&nbsp;Andrea Rasola ,&nbsp;Giorgio Colombo","doi":"10.1016/j.cstres.2026.100162","DOIUrl":"10.1016/j.cstres.2026.100162","url":null,"abstract":"<div><div>Protein homeostasis is one of the key mechanisms that determine cellular life, and the Hsp90 family of molecular chaperones plays a key role in it. While Hsp90 dysregulation is a hallmark of numerous diseases, ranging from cancer to neurodegeneration, traditional inhibitors targeting its highly conserved ATPase site have largely failed in the clinic due to off-target toxicity and compensatory stress responses. One of the challenges in drug discovery, as well as in the development of chemical tools to investigate the specific roles of single family members, lies in achieving isoform specificity across the cytoplasm, endoplasmic reticulum, and mitochondria.Here, we exploit the intrinsic asymmetry of mitochondrial isoform TRAP1 and combine it with a fragment-design inspired approach to develop new possible TRAP1 targeting leads. We start from the consideration that the TRAP1 catalytic cycle relies on a strained, asymmetric dimer conformation that enforces sequential ATP hydrolysis. By integrating advanced computational dynamics with biochemical profiling, we demonstrate that small molecules can be rationally designed to target these transient asymmetric states. Our findings reveal that targeting allosteric, symmetry-breaking interfaces allows for the modulation of TRAP1, offering a novel platform and starting point for next-generation, isoform-specific anticancer therapeutics.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 2","pages":"Article 100162"},"PeriodicalIF":3.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147316628","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Embracing diversity: Post-translational modifications, the chaperone code, and the emergence of new chaperone entities","authors":"Chander S. Digwal ,&nbsp;Shujuan Wang ,&nbsp;Gabriela Chiosis","doi":"10.1016/j.cstres.2026.100148","DOIUrl":"10.1016/j.cstres.2026.100148","url":null,"abstract":"<div><div>Dr Len Neckers played a pioneering role in establishing that HSP90 is regulated by post-translational modifications (PTMs), fundamentally reshaping how molecular chaperones are understood. This insight laid the foundation for what has become known as the “chaperone code,” the concept that coordinated PTM patterns act as regulatory signals governing chaperone function, interactions, and stress responsiveness. In this short perspective, I reflect on how Len’s early work seeded this conceptual shift and how subsequent advances have revealed that PTMs not only fine-tune canonical chaperone activities but can also enable chaperones to adopt non-canonical functional states under specific stress conditions. These developments have expanded the landscape of chaperone biology, illustrating how chemical encoding can diversify chaperone behavior and reconfigure protein networks. Together, they highlight the enduring impact of Len’s contributions and the importance of embracing complexity in understanding chaperone function.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 2","pages":"Article 100148"},"PeriodicalIF":3.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146123899","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The 13th International Symposium on Heat Shock Proteins in Biology, Medicine, and the Environment: Honoring legacy, celebrating scientific advances, and fostering collaboration","authors":"Laura J. Blair ,&nbsp;Richard L. Carpenter","doi":"10.1016/j.cstres.2026.100147","DOIUrl":"10.1016/j.cstres.2026.100147","url":null,"abstract":"<div><div>The 13th International Symposium on Heat Shock Proteins in Biology, Medicine and the Environment, organized by the Cell Stress Society International (CSSI), was held in October 2025 in Syracuse, NY, and brought together investigators spanning basic, translational, and clinical stress biology. The meeting highlighted the continued evolution of the heat shock response from a canonical transcriptional program to a complex, multi-layered network integrating transcriptional condensates, posttranslational regulation of chaperones, spatial organization, and system-level stress adaptation. Scientific sessions showcased advances in stress-induced transcription and genome control, the expanding Hsp90/Hsp70 “chaperone code,” proteostasis and protein quality control, mitochondrial chaperones and metabolic regulation, cancer–immune interfaces, host–pathogen interactions, and the roles of chaperones in aging and neurodegenerative disease. Particular emphasis was placed on emerging therapeutic and diagnostic strategies, including isoform-specific chaperone inhibitors, co-chaperone targeting, theranostic approaches, and clinical-stage candidates. Systems-level analyses of stress resilience, extracellular chaperone signaling, and organismal adaptation further underscored the breadth of stress biology across scales. The symposium also honored the legacy of Dr Len Neckers, whose pioneering contributions to Hsp90 biology shaped the field, and recognized outstanding scientific achievements through CSSI awards and fellowships. Collectively, the work presented reflects a field that continues to deepen mechanistic understanding while advancing toward precision-based therapeutic and diagnostic applications. This meeting report summarizes these developments and highlights future directions for stress biology research.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 2","pages":"Article 100147"},"PeriodicalIF":3.2,"publicationDate":"2026-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146103739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protein quality control: From molecular mechanisms to aging and disease—EMBO workshop, May 18-23, 2025, Hersonissos, Greece","authors":"Claes Andréasson ,&nbsp;Anat Ben-Zvi","doi":"10.1016/j.cstres.2025.100139","DOIUrl":"10.1016/j.cstres.2025.100139","url":null,"abstract":"<div><div>Cells safeguard the functionality of the proteome using complex pathways of protein quality control. The centerpiece of this proteostasis network is a large set of molecular chaperones and proteases that impact the entire lifespan of proteins by controlling protein folding and degradation. Dysfunction of the proteostasis network is associated with many diseases and age-associated functional decline of neurons, including Alzheimer’s and Parkinson’s diseases, as well as several motor neuron diseases. The 2025 EMBO workshop “Protein quality control: from molecular mechanisms to aging and disease” gathered the large and interdisciplinary community of researchers that study protein quality control, from its fundamental molecular mechanisms via higher-order organization in organisms to its impact on and use in the medical field. Here we summarize the workshop and report research findings.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 1","pages":"Article 100139"},"PeriodicalIF":3.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145780388","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"J-domain proteins: from molecular mechanisms to diseases","authors":"Janine Kirstein ,&nbsp;Rina Rosenzweig ,&nbsp;Paolo De Los Rios ,&nbsp;Pierre Genevaux ,&nbsp;Charlotte Adang ,&nbsp;Claes Andreasson ,&nbsp;David Balchin ,&nbsp;Alessandro Barducci ,&nbsp;Gregory L. Blatch ,&nbsp;Janice E.A. Braun ,&nbsp;Jeffrey L. Brodsky ,&nbsp;Bernd Bukau ,&nbsp;J. Paul Chapple ,&nbsp;Michael E. Cheetham ,&nbsp;Elizabeth A. Craig ,&nbsp;Douglas M. Cyr ,&nbsp;Sébastien Dementin ,&nbsp;Ofrah Faust ,&nbsp;Olivier Genest ,&nbsp;Jason E. Gestwicki ,&nbsp;Harm H. Kampinga","doi":"10.1016/j.cstres.2025.100142","DOIUrl":"10.1016/j.cstres.2025.100142","url":null,"abstract":"<div><div>J-domain proteins (JDPs) are known to drive the functional specificity of Hsp70 chaperone machines. Here we report on the latest findings presented at the third international JDP workshop held in 2025 in Gdansk, Poland. Investigators from many different disciplines, including structural biology, genetics, chemical biology, translational research, computational sciences, and biophysics, took part in the meeting. This article includes short summaries of the seminars presented by many of the speakers, which provided exciting new insights into the chaperone-dependent and chaperone-independent functions of JDPs, some of which go beyond Hsp70-dependent functions. We also provide a revised classification of members of the (human) JDP family that emerged from open discussion at the meeting. This workshop continues to serve as the premier venue for discussions of JDP evolution, structure, function, and roles in health, aging, and disease.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 1","pages":"Article 100142"},"PeriodicalIF":3.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145803082","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heat shock-induced PI(4)P increase drives HSPA1A translocation to the plasma membrane in cancer and stressed cells through PI4KIII alpha activation","authors":"Alberto Arce ,&nbsp;Rachel Altman ,&nbsp;Allen Badolian ,&nbsp;Jensen Low ,&nbsp;Azalea Blythe Cuaresma ,&nbsp;Georgia Halkia ,&nbsp;Uri Keshet ,&nbsp;Oliver Fiehn ,&nbsp;Robert V. Stahelin ,&nbsp;Nikolas Nikolaidis","doi":"10.1016/j.cstres.2025.100130","DOIUrl":"10.1016/j.cstres.2025.100130","url":null,"abstract":"<div><div>Heat shock protein A1A (HSPA1A), a major heat shock (HS) protein, is known to translocate to the plasma membrane (PM) in response to cellular stress and cancer, where it plays protective roles in membrane integrity and stress resistance. Although phosphatidylinositol 4-phosphate [PI(4)P] is essential in this translocation, the signals that trigger and facilitate HSPA1A's movement remain undefined. Given that membrane lipid composition dynamically shifts during stress, we hypothesized that HS-induced PI(4)P changes are crucial for HSPA1A's PM localization. To test this hypothesis, we investigated the mechanisms driving PI(4)P changes and HSPA1A PM localization under HS. Lipidomic analysis, enzyme-linked immunosorbent assay (ELISA), and confocal imaging revealed a rapid PI(4)P increase at the PM post-HS, with levels peaking immediately after HS (0 h recovery) and declining by 8 h of recovery. RNA sequencing and protein quantification indicated no transcriptional increase in PI4KIII alpha, the kinase responsible for PI(4)P synthesis, suggesting an alternative regulatory mechanism. Hypothesizing that HS enhances PI4KIII alpha activity, we performed ELISA coupled with immunoprecipitation, confirming a significant rise in PI4KIII alpha activity following HS. Functional analyses further demonstrated that RNAi-mediated PI4KIII alpha depletion or pharmacological PI(4)P reduction, using GSK-A1, impairs HSPA1A's localization to the PM, confirming that HSPA1A translocation is PI(4)P-dependent. Our findings identify PI4KIII alpha activity as a key regulator of PI(4)P accumulation and subsequent HSPA1A recruitment to the PM in stressed and cancer cells. This lipid-mediated response offers new insights into stress adaptation and potentially modifiable pathways for therapeutic interventions to control HSPA1A function in cancer.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 1","pages":"Article 100130"},"PeriodicalIF":3.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145630392","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Distribution and evolutionary significance of the DnaK-DnaJ-GrpE (KJE) chaperone system in archaea","authors":"Mathieu E. Rebeaud","doi":"10.1016/j.cstres.2026.100145","DOIUrl":"10.1016/j.cstres.2026.100145","url":null,"abstract":"<div><div>A prevailing hypothesis for the emergence of life on Earth holds that it might have originated in hydrothermal vents, where the environmental conditions, although physically and chemically extreme (acidity, lack of oxygen, high pressure, very high temperature), vary very little. According to this view, single-celled organisms that appeared under these conditions subsequently began to colonize first all aquatic environments, then terrestrial ones. Here, I study the proteomes of more than 250 reference proteomes of archaea as well as those of a few non-reference Promethearchaeati (ASGARD), which have an optimal growth temperature of between 10 °C and 100 °C. I found a correlation between the chaperome present in these organisms, and in particular the presence/absence of the Hsp70 family (DnaK-DnaJ-GrpE, KJE for brevity), the proteome size, and the optimal growth temperature. These findings suggest that the presence of Hsp70s in mesophilic archaea is associated with larger proteomes and may have facilitated adaptation to more diverse environments.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 1","pages":"Article 100145"},"PeriodicalIF":3.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146028485","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heat stress-induced heat shock protein 90 alpha family class A member 1 upregulation stabilizes yes-associated protein through ubiquitination inhibition to boost hepatic cancer radiofrequency hyperthermia resistance","authors":"Zhehan Bao,&nbsp;Yi Jiang,&nbsp;WeiRen Liang,&nbsp;Dinghu Zhang,&nbsp;Liwen Guo","doi":"10.1016/j.cstres.2025.100140","DOIUrl":"10.1016/j.cstres.2025.100140","url":null,"abstract":"<div><h3>Background</h3><div>Hepatocellular carcinoma (HCC) is a prevalent and aggressive form of liver cancer. Understanding how HCC responds to environmental stresses, such as heat stress, is crucial for developing effective treatments. This study explored the relationship between heat shock protein 90 alpha family class A member 1 (HSP90AA1), a key heat shock protein, and the Hippo signaling pathway, particularly yes-associated protein (YAP), in liver cancer cells under heat stress.</div></div><div><h3>Methods</h3><div>Liver cancer cells (HepG2 and Huh7) were subjected to heat stress (43 °C for 30 min) and analyzed for protein expression using Western blotting. Gene knockout and overexpression models were developed in nude mice and liver cancer cells to elucidate the influence of HSP90AA1-YAP interactions on tumorigenesis. Furthermore, functional analysis and advanced molecular biology techniques were employed to uncover the intricate regulatory network governed by HSP90AA1-YAP interactions in HCC.</div></div><div><h3>Results</h3><div>Heat stress upregulated heat shock protein expression, notably HSP90AA1, in liver cancer cells. Bioinformatics analyses linked HSP90AA1 to the Hippo-YAP pathway. Moreover, heat stress activated YAP, reducing large tumor suppressor 1 (LATS1)/YAP phosphorylation and increasing YAP levels. Inhibition of YAP weakened this effect, suggesting YAP's role in protecting liver cancer cells from heat stress-induced cytotoxicity. Additionally, silencing HSP90AA1 mitigated YAP pathway activation and enhanced heat stress-induced cytotoxicity in liver cancer cells by inhibiting YAP ubiquitination and stabilizing YAP. In liver cancer xenografts, HSP90AA1 silencing increased sensitivity to radiofrequency hyperthermia (RFH), reducing tumor growth and proliferation.</div></div><div><h3>Conclusions</h3><div>This study revealed that heat stress upregulates HSP90AA1, which stabilizes YAP by inhibiting ubiquitination, activates the YAP pathway, and protects liver cancer cells from cytotoxicity. These findings suggest that HSP90AA1 may be a potential therapeutic target for HCC.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 1","pages":"Article 100140"},"PeriodicalIF":3.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145803117","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Defective mitochondrial unfolded protein response in cancer acts as a lifeline for tumor growth and survival","authors":"Uttam Sharma ,&nbsp;Vaishnavi Vishwas ,&nbsp;Rajiv Ranjan Kumar ,&nbsp;Nikita Agarwal ,&nbsp;Akshi Shree ,&nbsp;Jaya Kanta Gorain ,&nbsp;Archana Sasi ,&nbsp;Surender K. Sharawat ,&nbsp;Archna Singh ,&nbsp;Jayanth Kumar Palanichamy ,&nbsp;Sameer Bakhshi","doi":"10.1016/j.cstres.2025.100143","DOIUrl":"10.1016/j.cstres.2025.100143","url":null,"abstract":"<div><div>Defective mitochondrial unfolded protein response (UPRmt) plays an important role in driving tumor growth and treatment resistance. Under physiological conditions, UPRmt preserves mitochondrial protein homeostasis and structure by inducing chaperones such as heat shock proteins (HSP60, HSP70, HSP10) and proteases like caseinolytic peptidase ATP-dependent, proteolytic subunit (ClpP), and Lon peptidase 1 (LONP1). However, dysfunctional UPRmt in cancer cells may allow them to tolerate mitochondrial damage and metabolic dysregulation and avoid cell death, thus promoting therapy resistance. Our current understanding of how transcriptional regulators such as activating transcription factor 5 (ATF5), C/EBP homologous protein (CHOP), and forkhead box protein O3a (FOXO3a), along with signaling circuits including ATF5-ATF4-CHOP, sirtuin 3 (SIRT3)–FOXO3a, and protein kinase B (AKT)-estrogen receptor alpha (ERα), coordinate detrimental forms of UPRmt activation in cancer cells remains limited. This review describes known interactions among mediators of the UPRmt pathway and how they may be dysregulated in cancer cells. We also explore how this altered stress response may provide avenues for therapeutic targeting.</div></div>","PeriodicalId":9684,"journal":{"name":"Cell Stress & Chaperones","volume":"31 1","pages":"Article 100143"},"PeriodicalIF":3.2,"publicationDate":"2026-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145803059","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}