检索结果-南通市图书馆

A redox-responsive self-assembling COA-4-arm PEG prodrug nanosystem for dual drug delivery suppresses cancer metastasis and drug resistance by downregulating Hsp90 expression

引用

药学学报:英文版 2023年第7期13卷 3153-3167页

作者： Yi Zhou Yingling Miao Qiudi Huang Wenwen Shi Jiacui Xie Jiachang Lin Pei Huang Chengfeng Yue Yuan Qin Xiyong Yu He Wang Linghao Qin Jianhai Chen Nanfang Hospital Southern Medical UniversityGuangzhou 510515China Key Laboratory of Molecular Target and Clinical Pharmacology and the State Key Laboratory of Respiratory Disease and the Fifth Affiliated Hospital School of Pharmaceutical SciencesGuangzhou Medical UniversityGuangzhou 511436China Center of Cancer Research The Second Affiliated HospitalGuangzhou Medical UniversityGuangzhou 510260China School of Pharmacy Guangdong Pharmaceutical UniversityGuangzhou 510006China

Metastasis and resistance are main causes to affect the outcome of the current anticancer therapies.Heat shock protein 90(Hsp90)as an ATP-dependent molecular chaperone takes important role in the tumor metastasis and resistance.Targeting Hsp90 and downregulating its expression show promising in inhibiting tumor metastasis and resistance.In this study,a redox-responsive dual-drug nanocarrier was constructed for the effective delivery of a commonly used chemotherapeutic drug PTX,and a COAmodified 4-arm PEG polymer(4PSC)was synthesized.COA,an active component in oleanolic acid that exerts strong antitumor activity by downregulating Hsp90 expression,was used as a structural and functional element to endow 4PSC with redox responsiveness and Hsp90 inhibitory activity.Our results showed that 4PSC/PTX nanomicelles efficiently delivered PTX and COA to tumor locations without inducing systemic toxicity.By blocking the Hsp90 signaling pathway,4PSC significantly enhanced the antitumor effect of PTX,inhibiting tumor proliferation and invasiveness as well as chemotherapy-induced resistance in vitro.Remarkable results were further confirmed in vivo with two preclinical tumor models.These findings demonstrate that the COA-modified 4PSC drug delivery nanosystem provides a potential platform for enhancing the efficacy of chemotherapies.

关键词： 3-O-(Z)-Coumaroyloleanolic acid Cancer metastasis Drug resistance Hsp90 Codelivery Prodrug nanosystem Chemotherapies Redox responsiveness

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

Ginsenoside Rg5 enhances the radiosensitivity of lung adenocarcinoma via reducing Hsp90-CDC37 interaction and promoting client protein degradation

引用

Journal of Pharmaceutical Analysis 2023年第11期13卷 1296-1308页

作者： Hansong Bai Jiahua Lyu Xinyu Nie Hao Kuang Long Liang Hongyuan Jia Shijie Zhou Churong Li Tao Li Sichuan Cancer Hospital Institute Sichuan Cancer CenterSchool of MedicineUniversity of Electronic Science and Technology of ChinaChengdu610041China School of Medicine University of Electronic Science and Technology of ChinaChengdu610054China School of Clinical Medicine Southwest Medical UniversityLuzhouSichuan646000China State Key Laboratory of Biotherapy and Cancer Center/Collaborative Innovation Center for Biotherapy West China HospitalSichuan UniversityChengdu610041China

Ginsenoside Rg5 is a rare ginsenoside showing promising tumor-suppressive effects.This study aimed to explore its radio-sensitizing effects and the underlying mechanisms.Human lung adenocarcinoma cell lines A549 and Calu-3 were used for in vitro and in vivo analysis.Bioinformatic molecular docking prediction and following validation by surface plasmon resonance(SPR)technology,cellular thermal shift assay(CETSA),and isothermal titration calorimetry(ITC)were conducted to explore the binding between ginsenoside Rg5 and 90 kD heat shock protein alpha(Hsp90a).The effects of ginsenoside Rg5 on Hsp90-cell division cycle 37(CDC37)interaction,the client protein stability,and the downstream regulations were further explored.Results showed that ginsenoside Rg5 could induce cell-cycle arrest at the G1 phase and enhance irradiationinduced cell apoptosis.It could bind to Hsp90a with a high affinity,but the affinity was drastically decreased by Hsp90a Y61A mutation.Co-immunoprecipitation(Co-IP)and ITC assays confirmed that ginsenoside Rg5 disrupts the Hsp90-CDC37 interaction in a dose-dependent manner.It reduced irradiation-induced upregulation of the Hsp90-CDC37 client proteins,including SRC,CDK4,RAF1,and ULK1 in A549 cell-derived xenograft(CDX)tumors.Ginsenoside Rg5 or MRT67307(an IKKε/TBK1 inhibitor)pretreatment suppressed irradiation-induced elevation of the LC3-II/b ratio and restored irradiation-induced downregulation of p62 expression.In A549 CDX tumors,ginsenoside Rg5 treatment suppressed LC3 expression and enhanced irradiation-induced DNA damage.In conclusion,ginsenoside Rg5 may be a potential radiosensitizer for lung adenocarcinoma.It interacts with Hsp90a and reduces the binding between Hsp90 and CDC37,thereby increasing the ubiquitin-mediated proteasomal degradation of the Hsp90-CDC37 client proteins.

关键词： Ginsenoside Rg5 Lung adenocarcinoma Radiotherapy Hsp90 CDC37

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

1,8-cineole ameliorates colon injury by downregulating macrophage M1 polarization via inhibiting the Hsp90-NLRP3-SGT1 complex

引用

Journal of Pharmaceutical Analysis 2023年第9期13卷 984-998页

作者： Shengsuo Ma Bing Yang Yang Du Yiwen Lv Jiarong Liu Yucong Shi Ting Huang Huachong Xu Li Deng Xiaoyin Chen School of Traditional Chinese Medicine Jinan UniversityGuangzhou510632China Guangzhou Key Laboratory of Formula-Pattern of Traditional Chinese Medicine Jinan UniversityGuangzhou510632China

Ulcerative colitis(UC)is characterized by chronic relapsing intestinal inflammation.Currently,there is no effective treatment for the disease.According to our preliminary data,1,8-cineole,which is the main active compound of Amomum compactum Sol.ex Maton volatile oil and an effective drug for the treatment of pneumonia,showed remarkable anti-inflammatory effects on colitis pathogenesis.However,its mechanism of action and direct targets remain unclear.This study investigated the direct targets and mechanism through which 1,8-cineole exerts its anti-inflammatory effects using a dextran sulfate sodium salt-induced colitis mouse model.The effects of 1,8-cineole on macrophage polarization were investigated using activated bone marrow-derived macrophages and RAW264.7 cells.In addition,1,8-cineole targets were revealed by drug affinity responsive target stability,thermal shift assay,cellular thermal shift assay,and heat shock protein 90(Hsp90)adenosine triphosphatases(ATPase)activity assays.The results showed that 1,8-cineole exhibited powerful anti-inflammatory properties in vitro and in vivo by inhibiting the macrophage M1 polarization and protecting intestinal barrier function.Mechanistically,1,8-cineole directly interacted with Hsp90 and decreased its ATPase activity,also inhibited nucleotide-binding and oligomerization domain-,leucine rich repeat-,and pyrin domain-containing 3(NLRP3)binding to Hsp90 and suppressor of G-two allele of SKP1(SGT1)and suppressed NLRP3 inflammasome activation in macrophages.These results demonstrated that 1,8-cineole is a potential drug candidate for UC treatment.

关键词： 1,8-cineole Amomum compactum Sol.ex Maton NLRP3 Hsp90 Ulcerative colitis Intestinal barrier function

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Thymoquinone affects hypoxia-inducible factor-1αexpression in pancreatic cancer cells via Hsp90 and PI3K/AKT/mTOR pathways

引用

World Journal of Gastroenterology 2024年第21期30卷 2793-2816页

作者： Zhan-Xue Zhao Shuai Li Lin-Xun Liu Department of General Surgery Qinghai Provincial People's HospitalXining 810007Qinghai ProvinceChina Department of Clinical Pharmacy The Affiliated Hospital of Qinghai UniversityXining 810001Qinghai ProvinceChina

BACKGROUND Pancreatic cancer(PC)is associated with some of the worst prognoses of all major cancers.Thymoquinone(TQ)has a long history in traditional medical practice and is known for its anti-cancer,anti-inflammatory,anti-fibrosis and antioxidant pharmacological activities.Recent studies on hypoxia-inducible factor-1α(HIF-1α)and PC have shown that HIF-1αaffects the occurrence and development of PC in many aspects.In addition,TQ could inhibit the development of renal cancer by decreasing the expression of HIF-1α.Therefore,we speculate whether TQ affects HIF-1αexpression in PC cells and explore the mechanism.AIM To elucidate the effect of TQ in PC cells and the regulatory mechanism of HIF-1αexpression.METHODS Cell counting kit-8 assay,Transwell assay and flow cytometry were performed to detect the effects of TQ on the proliferative activity,migration and invasion ability and apoptosis of PANC-1 cells and normal pancreatic duct epithelial(hTERTHPNE)cells.Quantitative real-time polymerase chain reaction and western blot assay were performed to detect the expression of HIF-1αmRNA and protein in PC cells.The effects of TQ on the HIF-1αprotein initial expression pathway and ubiquitination degradation in PANC-1 cells were examined by western blot assay and co-immunoprecipitation.RESULTS TQ significantly inhibited proliferative activity,migration,and invasion ability and promoted apoptosis of PANC-1 cells;however,no significant effects on hTERT-HPNE cells were observed.TQ significantly reduced the mRNA and protein expression levels of HIF-1αin PANC-1,AsPC-1,and BxPC-3 cells.TQ significantly inhibited the expression of the HIF-1αinitial expression pathway(PI3K/AKT/mTOR)related proteins,and promoted the ubiquitination degradation of the HIF-1αprotein in PANC-1 cells.TQ had no effect on the hydroxylation and von Hippel Lindau protein mediated ubiquitination degradation of the HIF-1αprotein but affected the stability of the HIF-1αprotein by inhibiting the interaction between HIF-1αand Hsp90,thus promoting its ubiquitination

关键词： Thymoquinone Pancreatic cancer Hypoxia-inducible factor-1α PI3K/AKT/mTOR Hsp90

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

芒柄花素通过Hsp90/AKT调控扩张型心肌病心力衰竭大鼠心肌细胞凋亡及其机制

引用

西安交通大学学报（医学版） 2023年第5期44卷 794-801页

作者：祁玉营薛松妍陈伟佳贾婷邢志政刘欢马静西北大学生命科学学院陕西西安710069 空军军医大学第一附属医院中医科陕西西安710032

目的探讨芒柄花素(formononetin,FMN)对扩张型心肌病心力衰竭大鼠心肌细胞凋亡及Hsp90/AKT的影响。方法通过超声心动图、ELISA法、组织学染色、TUNEL染色,观察不同剂量FMN对扩张型心肌病心力衰竭大鼠的保护作用及心肌细胞凋亡情况。从TC... 详细信息

目的探讨芒柄花素(formononetin,FMN)对扩张型心肌病心力衰竭大鼠心肌细胞凋亡及Hsp90/AKT的影响。方法通过超声心动图、ELISA法、组织学染色、TUNEL染色,观察不同剂量FMN对扩张型心肌病心力衰竭大鼠的保护作用及心肌细胞凋亡情况。从TCMSP、DisGeNet、GeneCards等数据库获取FMN作用于扩张型心肌病心力衰竭的潜在靶点及其交集,再根据蛋白质互作网络(PPI)获得两者交集的关键靶点,并通过分子对接和Western blotting对关键靶点进行验证。结果FMN可降低扩张型心肌病心力衰竭大鼠左心室收缩末期内径(LVIDS)、左心室舒张末期内径(LVIDD)水平及NT-pro BNP、cTn-T、CK、CK-MB和LDH含量,提高射血分数(EF)和短轴缩短率(FS)水平,减少心肌细胞凋亡;FMN与网络药理学筛出的10个关键靶点(AKT1、Hsp90AA1、CASP3、MAPK1、MMP9、SRC、ALB、HRAS、IGF1、EGFR)均具有较强的结合作用,以Hsp90AA1、AKT1结合作用最强,同时FMN可降低心肌组织Hsp90、AKT及下游CASP3蛋白表达,提高p-AKT的表达。结论FMN可能通过抑制Hsp90的表达,促进AKT磷酸化,降低CASP3的表达,减少心肌细胞凋亡,改善心肌组织损伤,达到治疗扩张型心肌病心力衰竭的目的。

关键词：芒柄花素扩张型心肌病心力衰竭 Hsp90 AKT 心肌细胞凋亡

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

家蚕热休克蛋白Hsp90相互作用蛋白的筛选与鉴定

引用

中国农业科学 2022年第6期55卷 1253-1262页

作者：龙艳碧吴云飞张倩陈鹏潘敏慧西南大学家蚕基因组生物学国家重点实验室西南大学农业农村部蚕桑生物学与遗传育种重点实验室

【目的】Hsp90 是热休克蛋白家族的成员之一，在昆虫的抗逆性和变态发育中发挥重要作用，已有研究表明 Hsp90能够促进家蚕核型多角体病毒(Bombyx mori nucleopolyhedrovirus,BmNPV)的增殖，但作用机制尚不清楚。本研究通过鉴定 BmHsp90... 详细信息

【目的】Hsp90 是热休克蛋白家族的成员之一，在昆虫的抗逆性和变态发育中发挥重要作用，已有研究表明 Hsp90能够促进家蚕核型多角体病毒(Bombyx mori nucleopolyhedrovirus,BmNPV)的增殖，但作用机制尚不清楚。本研究通过鉴定 BmHsp90 的相互作用蛋白，为其促进 BmNPV 增殖的作用机制解析提供参考。【方法】构建连接在 pIZ/V5-His 的BmHsp90HA真核过表达载体，在家蚕 BmN-SWU1 细胞中转染 48 h 后，感染 BmNPV 继续培养 48 h 后收集蛋白，保留总蛋白后将这些蛋白均分两管，进行免疫共沉淀，分别用抗 HA 抗体和 IgG 抗体钓取相互作用蛋白，对蛋白胶进行硝酸银染色后，获取差异条带并做质谱分析，将质谱结果与信息分析结合进行候选互作蛋白筛选，并克隆鉴定互作蛋白。通过免疫荧光验证 Hsp90 与互作蛋白的共定位情况，并进一步采用免疫共沉淀试验确定其是否存在相互作用关系。【结果】硝酸银染色结果显示，试验组与对照组在 90、70 和 60 kD 附近处存在差异条带，并验证了 90 kD 处的差异条带为诱饵蛋白；将另外两条差异带进行质谱分析，共鉴定到 7 个候选相互作用蛋白，通过分析选择其中两个候选蛋白作后续研究，分别为Tubulin-specific chaperone E(Tbce)和 Golgin subfamily A member 5(Golga5)。BmTbce 的最大开放阅读框长度为 1 728bp，编码 576 个氨基酸，BmGolga5 的最大开放阅读框长度为 1 854 bp，编码 618 个氨基酸；同源比对和系统进化树显示 BmTbce的微管结合结构域(cytoskeleton-associated protein-glycine-rich,CAP-Gly)位于 N 端且在不同物种之间保守性较高，BmGolga5 的跨膜区(transmembrane domain,TMD)位于 C 端，也较为保守；荧光共定位显示 BmHsp90 与 BmTbce 和 BmGolga5在细胞质中发生共定位，并进一步通过免疫共沉淀证明 BmHsp90HA和 BmTbceFlag、BmHsp90HA和 BmGolga5Flag具有相互作用关系。【结论】经过筛选与鉴定，在 BmNPV 感染家蚕细胞的过程中，与家蚕热休克蛋白 Hsp90 发生相互作用的蛋白为 BmTbce 和BmGolga5。

关键词：家蚕家蚕核型多角体病毒 Hsp90 Tbce Golga5

来源：

同方期刊数据库评论

在线全文

同方期刊数据库

学校读者我要写书评

暂无评论

The disruption of protein-protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition

引用

Acta Pharmaceutica Sinica B 2021年第6期11卷 1446-1468页

作者： Michael A.Serwetnyk Brian S.J.Blagg Department of Chemistry and Biochemistry Warren Family Research Center for Drug Discovery and DevelopmentUniversity of Notre DameIN 46556USA

The 90-kilo Dalton(kD) heat shock protein(Hsp90) is a ubiquitous,ATP-dependent molecular chaperone whose primary function is to ensure the proper folding of several hundred client protein substrates.Because many of these clients are overexpressed or become mutated during cancer progression,Hsp90 inhibition has been pursued as a potential strategy for cancer as one can target multiple oncoproteins and signaling pathways simultaneously.The first discovered Hsp90 inhibitors,geldanamycin and radicicol,function by competitively binding to Hsp90’s N-terminal binding site and inhibiting its ATPase activity.However,most of these N-terminal inhibitors exhibited detrimental activities during clinical evaluation due to induction of the pro-survival heat shock response as well as poor selectivity amongst the four isoforms.Consequently,alternative approaches to Hsp90 inhibition have been pursued and include C-terminal inhibition,isoform-selective inhibition,and the disruption of Hsp90 protein-protein interactions.Since the Hsp90 protein folding cycle requires the assembly of Hsp90 into a large heteroprotein complex,along with various co-chaperones and immunophilins,the development of small molecules that prevent assembly of the complex offers an alternative method of Hsp90 inhibition.

关键词： Hsp90 Protein-protein interactions Disruptors Natural products Small molecules Peptidomimetics

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

Hsp90/C terminal Hsc70-interacting protein regulates the stability of Ikaros in acute myeloid leukemia cells

引用

Science China(Life Sciences) 2021年第9期64卷 1481-1490页

作者： Meng Liu Jin Jin Yanjie Ji Huizhuang Shan Zhihui Zou Yang Cao Li Yang Ligen Liu Li Zhou Hu Lei Yunzhao Wu Hanzhang Xu Yingli Wu Hongqiao International Institute of Medicine Shanghai Tongren Hospital/Faculty of Basic MedicineChemical Biology Division of Shanghai Universities E-InstitutesKey Laboratory of Cell Differentiation and Apoptosis of the Chinese Ministry of EducationShanghai Jiao Tong University School of MedicineShanghai 200025China Department of Ultrasound Second Affiliated Hospital of Zhejiang UniversityHangzhou 310009China Department of Hematology The Third Affiliated Hospital of Soochow UniversityChangzhou 213003China Shanghai Institute of Hematology State Key Laboratory of Medical GenomicsNational Research Center for Translational Medicine at ShanghaiRuijin Hospital affiliated to Shanghai Jiao Tong University School of MedicineShanghai 200025China

The stability of Ikaros family zinc finger protein 1(Ikaros),a critical hematopoietic transcription factor,can be regulated by cereblon(CRBN)ubiquitin ligase stimulated by immunomodulatory drugs in multiple myeloma.However,other stabilization mechanisms of Ikaros have yet to be elucidated.In this study,we show that the pharmacologic inhibition or knockdown of Hsp90 downregulates Ikaros in acute myeloid leukemia(AML)cells.Proteasome inhibitor MG132 but not autophagy inhibitor chloroquine could suppress the Hsp90 inhibitor STA-9090-induced reduction of Ikaros,which is accompanied with the increased ubiquitination of Ikaros.Moreover,Ikaros interacts with E3 ubiquitin-ligase C terminal Hsc70 binding protein(CHIP),which mediates the STA-9090-induced ubiquitination of Ikaros.In addition,the knockdown of Ikaros effectively inhibits the proliferation of leukemia cells,but this phenomenon could be rescued by Ikaros overexpression.Collectively,our findings indicate that the interplay between Hsp90 and CHIP regulates the stability of Ikaros in AML cells,which provides a novel strategy for AML treatment through targeting the Hsp90/Ikaros/CHIP axis.

关键词： Ikaros CHIP Hsp90 AML STA-9090

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

YODA-Hsp90 Module Regulates Phosphorylation-Dependent Inactivation of SPEECHLESS to Control Stomatal Development under Acute Heat Stress in Arabidopsis

引用

Molecular Plant 2020年第4期13卷 612-633页

作者： Despina Samakovli Tereza Ticha Tereza Vavrdova Miroslav Ovecka Ivan Luptovciak Veronika Zapletalova Anna Kucharova Pavel Krenek Yuliya Krasylenko Theoni Margaritopoulou Loukia Roka Dimitra Milioni George Komis Polydefkis Hatzopoulos Jozef Samaj Centre of the Region Hana for Biotechnological and Agricultural Research Faculty of SciencePalacky University OlomoucSlechtitelu 27Olomouc 78371Czech Republic Molecular Biology Laboratory Agricultural University of Athenslera Odos 75Athens 11855Greece Present address:Laboratory of Mycology Department of PhytopathologyBenaki Phytopathological Institute8st.Delta str.GR-14561 KifissiaAtticaGreece

Stomatal ontogenesis,patterning,and function are hallmarks of environmental plant adaptation,especially to conditions limiting plant growth,such as elevated temperatures and reduced water availability.The specification and distribution of a stomatal cell lineage and its terminal differentiation into guard cells require a master regulatory protein phosphorylation cascade involving the YODA mitogen-activated protein kinase kinase kinase.YODA signaling results in the activation of MITOGEN-ACTIVATED PROTEIN KINASEs(MPK3 and MPK6),which regulate transcription factors,including SPEECHLESS(SPCH).Here,we report that acute heat stress affects the phosphorylation and deactivation of SPCH and modulates stomatal density.By using complem entary molecular,genetic,biochemical,and cell biology approaches,we provide solid evidence that HEAT SHOCK PROTEINS 90(Hsp90s)play a crucial role in transducing heat-stress response through the YODA cascade.Genetic studies revealed that YODA and Hsp90.1 are epistatic,and they likely function linearly in the same developmental pathway regulating stomata formation.Hsp90s interact with YODA,affectits cellular polarization,and modulate the phosphorylation of downstream targets,such as MPK6 and SPCH,under both normal and heat-stress conditions.Thus,Hsp90-mediated specification and differentiation of the stomatal cell lineage couples stomatal development to environmental cues,providing an adaptive heat stress response mechanism in plants.

关键词： stomata Hsp90 MAPK heat stress Arabidopsis

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability

引用

Journal of Molecular Cell Biology 2020年第6期12卷 448-461页

作者： Yuan Wu Yubo Ding Xiudan Zheng Kan Liao Key Laboratory of Systems Biology CAS Center for Excellence in Molecular Cell ScienceShanghai Institute of Biochemistry and Cell BiologyChinese Academy of SciencesUniversity of Chinese Academy of SciencesShanghai 200031China

Hsp90 is an abundant and special molecular chaperone considered to be the regulator of many transcription factors and signaling kinases. Its high abundance is indicative of its involvement in some more fundamental processes. In this study, we provide evidence that Hsp90 is required for microtubule stabilization, Golgi organization, and vesicular trafficking. We showed that Hsp90 is bound to microtubule-associated protein 4 (MAP4), which is essential for maintaining microtubule acetylation and stabilization. Hsp90 depletion led to the decrease in MAP4, causing microtubule deacetylation and destabilization. Furthermore, in Hsp90-depleted cells, the Golgi apparatus was fragmented and anterograde vesicle trafficking was impaired, with phenotypes similar to those induced by silencing MAP4. These disruptive effects of Hsp90 depletion could be rescued by the expression of exogenous MAP4 or the treatment of trichostatin A that increases microtubule acetylation as well as stability. Thus, microtubule stability is an essential cellular event regulated by Hsp90.

关键词： Hsp90 microtubule Golgi fragmentation vesicular trafficking MAP4

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：