Legumelin (BioDeep_00000002571)

 

Secondary id: BioDeep_00000230126

human metabolite PANOMIX_OTCML-2023


代谢物信息卡片


(1S,14S)-17,18-dimethoxy-7,7-dimethyl-2,8,21-trioxapentacyclo[12.8.0.0³,¹².0⁴,⁹.0¹⁵,²⁰]docosa-3(12),4(9),5,10,15,17,19-heptaen-13-one

化学式: C23H22O6 (394.1416)
中文名称: (-)-鱼藤素, 魚藤素
谱图信息: 最多检出来源 Homo sapiens(plant) 21.74%

分子结构信息

SMILES: C12OC(C)(C)C=CC1=C1O[C@]3([H])COC4C=C(OC)C(OC)=CC=4[C@]3([H])C(=O)C1=CC=2
InChI: InChI=1S/C23H22O6/c1-23(2)8-7-12-15(29-23)6-5-13-21(24)20-14-9-17(25-3)18(26-4)10-16(14)27-11-19(20)28-22(12)13/h5-10,19-20H,11H2,1-4H3

描述信息

Legumelin, also known as (-)-cis-deguelin, is a member of the class of compounds known as rotenones. Rotenones are rotenoids with a structure based on a 6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one skeleton. Thus, legumelin is considered to be a flavonoid lipid molecule. Legumelin is practically insoluble (in water) and a very weakly acidic compound (based on its pKa). Legumelin can be found in soy bean, which makes legumelin a potential biomarker for the consumption of this food product.
Deguelin, a naturally occurring rotenoid, acts as a chemopreventive agent by blocking multiple pathways like PI3K-Akt, IKK-NF-κB, and MAPK-mTOR-survivin-mediated apoptosis. Deguelin binding to Hsp90 leads to a decreased expression of numerous oncogenic proteins, including MEK1/2, Akt, HIF1α, COX-2, and NF-κB.
Deguelin, a naturally occurring rotenoid, acts as a chemopreventive agent by blocking multiple pathways like PI3K-Akt, IKK-NF-κB, and MAPK-mTOR-survivin-mediated apoptosis. Deguelin binding to Hsp90 leads to a decreased expression of numerous oncogenic proteins, including MEK1/2, Akt, HIF1α, COX-2, and NF-κB.
Deguelin, a naturally occurring rotenoid, acts as a chemopreventive agent by blocking multiple pathways like PI3K-Akt, IKK-NF-κB, and MAPK-mTOR-survivin-mediated apoptosis. Deguelin binding to Hsp90 leads to a decreased expression of numerous oncogenic proteins, including MEK1/2, Akt, HIF1α, COX-2, and NF-κB.

同义名列表

9 个代谢物同义名

(1S,14S)-17,18-dimethoxy-7,7-dimethyl-2,8,21-trioxapentacyclo[12.8.0.0³,¹².0⁴,⁹.0¹⁵,²⁰]docosa-3(12),4(9),5,10,15,17,19-heptaen-13-one; 13,13a-dihydro-9,10-dimethoxy-3,3-dimethyl-3H-bis(1)benzopyrano(3,4-b:6,5-e)pyran-7(7aH)-one; (-)-Deguelin;(-)-cis-Deguelin; (-)-cis-deguelin; Legumelin; Deguelin; (-)-Deguelin; Deguelin; Deguelin



数据库引用编号

20 个数据库交叉引用编号

分类词条

相关代谢途径

Reactome(0)

BioCyc(0)

PlantCyc(0)

代谢反应

2 个相关的代谢反应过程信息。

Reactome(0)

BioCyc(1)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(1)

COVID-19 Disease Map(0)

PathBank(0)

PharmGKB(0)

19 个相关的物种来源信息

在这里通过桑基图来展示出与当前的这个代谢物在我们的BioDeep知识库中具有相关联信息的其他代谢物。在这里进行关联的信息来源主要有:

  • PubMed: 来源于PubMed文献库中的文献信息,我们通过自然语言数据挖掘得到的在同一篇文献中被同时提及的相关代谢物列表,这个列表按照代谢物同时出现的文献数量降序排序,取前10个代谢物作为相关研究中关联性很高的代谢物集合展示在桑基图中。
  • NCBI Taxonomy: 通过文献数据挖掘,得到的代谢物物种来源信息关联。这个关联信息同样按照出现的次数降序排序,取前10个代谢物作为高关联度的代谢物集合展示在桑吉图上。
  • Chemical Taxonomy: 在物质分类上处于同一个分类集合中的其他代谢物
  • Chemical Reaction: 在化学反应过程中,存在为当前代谢物相关联的生化反应过程中的反应底物或者反应产物的关联代谢物信息。

点击图上的相关代谢物的名称,可以跳转到相关代谢物的信息页面。

亚细胞结构定位 关联基因列表
Cytoplasm 16 ANG, ANXA5, BCL2, BCL2L1, BIRC5, CASP3, CCND1, EGFR, HIF1A, MAPK14, MTOR, NPM1, PIK3C3, PIK3CA, PIK3R6, VEGFA
Peripheral membrane protein 4 ANXA5, GORASP1, MTOR, PIK3R6
Endosome membrane 1 EGFR
Endoplasmic reticulum membrane 4 BCL2, EGFR, HSP90B1, MTOR
Mitochondrion membrane 1 BCL2L1
Cytoplasmic vesicle, autophagosome 1 PIK3C3
Nucleus 12 ANG, BCL2, BIRC5, CASP3, CCND1, EGFR, HIF1A, HSP90B1, MAPK14, MTOR, NPM1, VEGFA
autophagosome 1 PIK3C3
cytosol 15 ANG, ANXA5, BCL2, BCL2L1, BIRC5, CASP3, CCND1, HIF1A, HSP90B1, MAPK14, MTOR, NPM1, PIK3C3, PIK3CA, PIK3R6
dendrite 1 MTOR
nuclear body 1 HIF1A
phagocytic vesicle 1 MTOR
phosphatidylinositol 3-kinase complex, class III 1 PIK3C3
centrosome 3 BCL2L1, CCND1, NPM1
nucleoplasm 7 BIRC5, CASP3, CCND1, HIF1A, MAPK14, MTOR, NPM1
RNA polymerase II transcription regulator complex 1 HIF1A
Cell membrane 2 EGFR, PIK3R6
Cytoplasmic side 3 BCL2L1, GORASP1, MTOR
lamellipodium 1 PIK3CA
ruffle membrane 1 EGFR
Early endosome membrane 1 EGFR
Golgi apparatus membrane 2 GORASP1, MTOR
cell junction 1 EGFR
cell surface 2 EGFR, VEGFA
glutamatergic synapse 4 CASP3, EGFR, MAPK14, PIK3C3
Golgi apparatus 2 GORASP1, VEGFA
Golgi membrane 3 EGFR, GORASP1, MTOR
growth cone 1 ANG
lysosomal membrane 1 MTOR
mitochondrial inner membrane 1 BCL2L1
neuronal cell body 2 ANG, CASP3
sarcolemma 1 ANXA5
smooth endoplasmic reticulum 1 HSP90B1
Cytoplasm, cytosol 1 BCL2L1
Lysosome 1 MTOR
endosome 2 EGFR, PIK3C3
plasma membrane 3 EGFR, PIK3CA, PIK3R6
synaptic vesicle membrane 1 BCL2L1
Membrane 9 ANXA5, BCL2, EGFR, HSP90B1, MTOR, NPM1, PIK3C3, PIK3R6, VEGFA
apical plasma membrane 1 EGFR
basolateral plasma membrane 1 EGFR
extracellular exosome 2 ANXA5, HSP90B1
Lysosome membrane 1 MTOR
endoplasmic reticulum 4 BCL2, BCL2L1, HSP90B1, VEGFA
extracellular space 3 ANG, EGFR, VEGFA
perinuclear region of cytoplasm 3 EGFR, HSP90B1, PIK3CA
adherens junction 1 VEGFA
bicellular tight junction 1 CCND1
intercalated disc 1 PIK3CA
mitochondrion 3 BCL2, BCL2L1, MAPK14
protein-containing complex 6 BCL2, BIRC5, EGFR, HIF1A, HSP90B1, NPM1
Microsome membrane 1 MTOR
postsynaptic density 1 CASP3
TORC1 complex 1 MTOR
TORC2 complex 1 MTOR
Single-pass type I membrane protein 1 EGFR
Secreted 3 ANG, PRB1, VEGFA
extracellular region 6 ANG, ANXA5, HSP90B1, MAPK14, PRB1, VEGFA
Mitochondrion outer membrane 3 BCL2, BCL2L1, MTOR
Single-pass membrane protein 2 BCL2, BCL2L1
mitochondrial outer membrane 3 BCL2, BCL2L1, MTOR
Mitochondrion matrix 1 BCL2L1
mitochondrial matrix 1 BCL2L1
motile cilium 1 HIF1A
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome 2 BCL2L1, NPM1
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane 1 BCL2L1
Nucleus membrane 3 BCL2, BCL2L1, CCND1
Bcl-2 family protein complex 2 BCL2, BCL2L1
nuclear membrane 4 BCL2, BCL2L1, CCND1, EGFR
external side of plasma membrane 1 ANXA5
Secreted, extracellular space, extracellular matrix 1 VEGFA
actin cytoskeleton 1 ANG
microtubule cytoskeleton 1 BIRC5
nucleolus 2 ANG, NPM1
axon cytoplasm 1 HIF1A
midbody 3 BIRC5, HSP90B1, PIK3C3
Membrane raft 1 EGFR
pore complex 1 BCL2
Cytoplasm, cytoskeleton, spindle 1 BIRC5
focal adhesion 4 ANXA5, EGFR, HSP90B1, NPM1
microtubule 1 BIRC5
spindle 1 BIRC5
GABA-ergic synapse 1 PIK3C3
cis-Golgi network 1 GORASP1
extracellular matrix 1 VEGFA
Peroxisome 1 PIK3C3
basement membrane 1 ANG
intracellular vesicle 1 EGFR
Nucleus, PML body 1 MTOR
PML body 1 MTOR
collagen-containing extracellular matrix 2 ANXA5, HSP90B1
secretory granule 1 VEGFA
axoneme 1 PIK3C3
nuclear speck 2 HIF1A, MAPK14
interphase microtubule organizing center 1 BIRC5
Late endosome 1 PIK3C3
receptor complex 1 EGFR
Zymogen granule membrane 1 ANXA5
chromatin 1 HIF1A
phagocytic vesicle membrane 1 PIK3C3
Chromosome 2 ANG, BIRC5
centriole 1 BIRC5
Nucleus, nucleolus 2 ANG, NPM1
spindle pole 1 MAPK14
nuclear chromosome 1 BIRC5
nuclear envelope 1 MTOR
Endomembrane system 1 MTOR
Chromosome, centromere 1 BIRC5
Chromosome, centromere, kinetochore 1 BIRC5
phagophore assembly site 1 PIK3C3
phosphatidylinositol 3-kinase complex, class III, type I 1 PIK3C3
phosphatidylinositol 3-kinase complex, class III, type II 1 PIK3C3
Nucleus, nucleoplasm 1 NPM1
Melanosome 1 HSP90B1
Cytoplasm, Stress granule 1 ANG
cytoplasmic stress granule 1 ANG
Nucleus speckle 1 HIF1A
euchromatin 1 HIF1A
myelin sheath 1 BCL2
sperm plasma membrane 1 HSP90B1
basal plasma membrane 1 EGFR
synaptic membrane 1 EGFR
ficolin-1-rich granule lumen 1 MAPK14
secretory granule lumen 1 MAPK14
endoplasmic reticulum lumen 1 HSP90B1
transcription repressor complex 1 CCND1
platelet alpha granule lumen 1 VEGFA
phosphatidylinositol 3-kinase complex 2 PIK3CA, PIK3R6
phosphatidylinositol 3-kinase complex, class IA 2 PIK3CA, PIK3R6
kinetochore 1 BIRC5
endocytic vesicle 1 ANG
Endoplasmic reticulum-Golgi intermediate compartment membrane 1 GORASP1
presynaptic endosome 1 PIK3C3
Golgi apparatus, cis-Golgi network membrane 1 GORASP1
chromosome, centromeric region 1 BIRC5
vesicle membrane 1 ANXA5
clathrin-coated endocytic vesicle membrane 1 EGFR
Sarcoplasmic reticulum lumen 1 HSP90B1
chromosome passenger complex 1 BIRC5
spindle pole centrosome 1 NPM1
ribonucleoprotein complex 1 NPM1
cytoplasmic microtubule 1 BIRC5
protein-DNA complex 1 NPM1
spindle microtubule 1 BIRC5
survivin complex 1 BIRC5
death-inducing signaling complex 1 CASP3
Cytoplasmic vesicle, phagosome 1 MTOR
granular component 1 NPM1
cyclin-dependent protein kinase holoenzyme complex 1 CCND1
postsynaptic endosome 1 PIK3C3
multivesicular body, internal vesicle lumen 1 EGFR
Shc-EGFR complex 1 EGFR
endocytic vesicle lumen 1 HSP90B1
Autolysosome 1 PIK3C3
angiogenin-PRI complex 1 ANG
endoplasmic reticulum chaperone complex 1 HSP90B1
endothelial microparticle 1 ANXA5
BAD-BCL-2 complex 1 BCL2
cyclin D1-CDK4 complex 1 CCND1
[N-VEGF]: Cytoplasm 1 VEGFA
[VEGFA]: Secreted 1 VEGFA
[Isoform L-VEGF189]: Endoplasmic reticulum 1 VEGFA
[Isoform VEGF121]: Secreted 1 VEGFA
[Isoform VEGF165]: Secreted 1 VEGFA
VEGF-A complex 1 VEGFA
cyclin D1-CDK6 complex 1 CCND1
phosphatidylinositol 3-kinase complex, class IB 2 PIK3CA, PIK3R6
[Isoform Bcl-X(L)]: Mitochondrion inner membrane 1 BCL2L1


文献列表

  • Peiwen Zhang, Mengzi Zhang, Terri A Mellich, Brian J Pearson, Jianjun Chen, Zhixiang Zhang. Variation in Rotenone and Deguelin Contents among Strains across Four Tephrosia Species and Their Activities against Aphids and Whiteflies. Toxins. 2022 05; 14(5):. doi: 10.3390/toxins14050339. [PMID: 35622585]
  • Hardeep Singh Tuli, Sonam Mittal, Mariam Loka, Vaishali Aggarwal, Diwakar Aggarwal, Akshara Masurkar, Ginpreet Kaur, Mehmet Varol, Katrin Sak, Manoj Kumar, Gautam Sethi, Anupam Bishayee. Deguelin targets multiple oncogenic signaling pathways to combat human malignancies. Pharmacological research. 2021 04; 166(?):105487. doi: 10.1016/j.phrs.2021.105487. [PMID: 33581287]
  • Aziza H Said, Anita Solhaug, Morten Sandvik, Flower E Msuya, Margareth S Kyewalyanga, Aviti J Mmochi, Jan L Lyche, Selma Hurem. Isolation of the Tephrosia vogelii extract and rotenoids and their toxicity in the RTgill-W1 trout cell line and in zebrafish embryos. Toxicon : official journal of the International Society on Toxinology. 2020 Aug; 183(?):51-60. doi: 10.1016/j.toxicon.2020.05.013. [PMID: 32454059]
  • Weibo Liao, Xin Liu, Quanlue Yang, Huifang Liu, Bingyu Liang, Junjun Jiang, Jiegang Huang, Chuanyi Ning, Ning Zang, Bo Zhou, Yanyan Liao, Jingzhao Chen, Li Tian, Wenzhe Ho, Abu S Abdullah, Lingbao Kong, Hao Liang, Hui Chen, Li Ye. Deguelin inhibits HCV replication through suppressing cellular autophagy via down regulation of Beclin1 expression in human hepatoma cells. Antiviral research. 2020 02; 174(?):104704. doi: 10.1016/j.antiviral.2020.104704. [PMID: 31917237]
  • Yanbei Tu, Chuanhai Wu, Yunyao Kang, Qin Li, Chao Zhu, Yanfang Li. Bioactivity-guided identification of flavonoids with cholinesterase and β-amyloid peptide aggregation inhibitory effects from the seeds of Millettia pachycarpa. Bioorganic & medicinal chemistry letters. 2019 05; 29(10):1194-1198. doi: 10.1016/j.bmcl.2019.03.024. [PMID: 30910460]
  • Tan Zhang, Kangxian Zhao, Weiqi Han, Wanlei Yang, Xuanyuan Lu, Qian Liu, Xiucheng Li, Yu Qian. Deguelin inhibits RANKL-induced osteoclastogenesis in vitro and prevents inflammation-mediated bone loss in vivo. Journal of cellular physiology. 2019 03; 234(3):2719-2729. doi: 10.1002/jcp.27087. [PMID: 30078209]
  • Wei Zeng, Wei Qi, Jiao Mu, Yi Wei, Li-Ling Yang, Qian Zhang, Qiong Wu, Jian-Ying Tang, Bing Feng. MG132 protects against renal dysfunction by regulating Akt-mediated inflammation in diabetic nephropathy. Scientific reports. 2019 02; 9(1):2049. doi: 10.1038/s41598-018-38425-2. [PMID: 30765727]
  • Mehmet A Kocdor, Hakan Cengiz, Halil Ates, Hilal Kocdor. Inhibition of Cancer Stem-Like Phenotype by Curcumin and Deguelin in CAL-62 Anaplastic Thyroid Cancer Cells. Anti-cancer agents in medicinal chemistry. 2019; 19(15):1887-1898. doi: 10.2174/1871520619666191004144025. [PMID: 31584382]
  • Ji Chen, Wenjie Liu, Han Yi, Xiaoling Hu, Liangyu Peng, Fengrui Yang. The Natural Rotenoid Deguelin Ameliorates Diabetic Neuropathy by Decreasing Oxidative Stress and Plasma Glucose Levels in Rats via the Nrf2 Signalling Pathway. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology. 2018; 48(3):1164-1176. doi: 10.1159/000491983. [PMID: 30045011]
  • Yung-Ting Hsiao, Ming-Jen Fan, An-Cheng Huang, Jin-Cherng Lien, Jen-Jyh Lin, Jaw-Chyun Chen, Te-Chun Hsia, Rick Sai-Chuen Wu, Jing-Gung Chung. Deguelin Impairs Cell Adhesion, Migration and Invasion of Human Lung Cancer Cells through the NF-[Formula: see text]B Signaling Pathways. The American journal of Chinese medicine. 2018; 46(1):209-229. doi: 10.1142/s0192415x1850012x. [PMID: 29402127]
  • Elina Karhu, Janne Isojärvi, Pia Vuorela, Leena Hanski, Adyary Fallarero. Identification of Privileged Antichlamydial Natural Products by a Ligand-Based Strategy. Journal of natural products. 2017 10; 80(10):2602-2608. doi: 10.1021/acs.jnatprod.6b01052. [PMID: 29043803]
  • Sarah Preston, Pasi K Korhonen, Laurent Mouchiroud, Matteo Cornaglia, Sean L McGee, Neil D Young, Rohan A Davis, Simon Crawford, Cameron Nowell, Brendan R E Ansell, Gillian M Fisher, Katherine T Andrews, Bill C H Chang, Martin A M Gijs, Paul W Sternberg, Johan Auwerx, Jonathan Baell, Andreas Hofmann, Abdul Jabbar, Robin B Gasser. Deguelin exerts potent nematocidal activity via the mitochondrial respiratory chain. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2017 10; 31(10):4515-4532. doi: 10.1096/fj.201700288r. [PMID: 28687609]
  • H M P Dilrukshi Herath, Sarah Preston, Andreas Hofmann, Rohan A Davis, Anson V Koehler, Bill C H Chang, Abdul Jabbar, Robin B Gasser. Screening of a small, well-curated natural product-based library identifies two rotenoids with potent nematocidal activity against Haemonchus contortus. Veterinary parasitology. 2017 Sep; 244(?):172-175. doi: 10.1016/j.vetpar.2017.07.005. [PMID: 28917310]
  • Xia Zhang, Zichu Zhao, Sha Yi, Lu Wen, Jing He, Jingyu Hu, Jun Ruan, Jun Fang, Yan Chen. Deguelin induced differentiation of mutated NPM1 acute myeloid leukemia in vivo and in vitro. Anti-cancer drugs. 2017 08; 28(7):723-738. doi: 10.1097/cad.0000000000000494. [PMID: 28471807]
  • Rini Muharini, Adriana Díaz, Weaam Ebrahim, Attila Mándi, Tibor Kurtán, Nidja Rehberg, Rainer Kalscheuer, Rudolf Hartmann, Raha S Orfali, Wenhan Lin, Zhen Liu, Peter Proksch. Antibacterial and Cytotoxic Phenolic Metabolites from the Fruits of Amorpha fruticosa. Journal of natural products. 2017 01; 80(1):169-180. doi: 10.1021/acs.jnatprod.6b00809. [PMID: 28075580]
  • Yuh Baba, Toyonobu Maeda, Atsuko Suzuki, Satoshi Takada, Masato Fujii, Yasumasa Kato. Deguelin Potentiates Apoptotic Activity of an EGFR Tyrosine Kinase Inhibitor (AG1478) in PIK3CA-Mutated Head and Neck Squamous Cell Carcinoma. International journal of molecular sciences. 2017 Jan; 18(2):. doi: 10.3390/ijms18020262. [PMID: 28134774]
  • Zhang Bao, Pei Zhang, Yinan Yao, Guohua Lu, Zhongkai Tong, Bing Yan, Lingfang Tu, Guangdie Yang, Jianying Zhou. Deguelin Attenuates Allergic Airway Inflammation via Inhibition of NF-κb Pathway in Mice. International journal of biological sciences. 2017; 13(4):492-504. doi: 10.7150/ijbs.17238. [PMID: 28529457]
  • Kaitlin Deardorff, William Ray, Eric Winterstein, MacKenzie Brown, Jocelyn McCornack, Brianda Cardenas-Garcia, Kiah Jones, Sarah McNutt, Shannon Fulkerson, Daneel Ferreira, Charlotte Gény, Xiaoyan Chen, Gil Belofsky, Blaise Dondji. Phenolic Metabolites of Dalea ornata Affect Both Survival and Motility of the Human Pathogenic Hookworm Ancylostoma ceylanicum. Journal of natural products. 2016 09; 79(9):2296-303. doi: 10.1021/acs.jnatprod.6b00444. [PMID: 27584977]
  • Danielle da Costa, Consuelo E Silva, Aline Pinheiro, Débora Frommenwiler, Mara Arruda, Giselle Guilhon, Cláudio Alves, Alberto Arruda, Milton Da Silva. Using LC and Hierarchical Cluster Analysis as Tools to Distinguish Timbó Collections into Two Deguelia Species: A Contribution to Chemotaxonomy. Molecules (Basel, Switzerland). 2016 Apr; 21(5):. doi: 10.3390/molecules21050569. [PMID: 27144548]
  • Curtis J Henrich, Laura K Cartner, Jennifer A Wilson, Richard W Fuller, Anthony E Rizzo, Karlyne M Reilly, James B McMahon, Kirk R Gustafson. Deguelins, Natural Product Modulators of NF1-Defective Astrocytoma Cell Growth Identified by High-Throughput Screening of Partially Purified Natural Product Extracts. Journal of natural products. 2015 Nov; 78(11):2776-81. doi: 10.1021/acs.jnatprod.5b00753. [PMID: 26467198]
  • Sha Yi, Lu Wen, Jing He, Youping Wang, Fei Zhao, Jie Zhao, Zichu Zhao, Guohui Cui, Yan Chen. Deguelin, a selective silencer of the NPM1 mutant, potentiates apoptosis and induces differentiation in AML cells carrying the NPM1 mutation. Annals of hematology. 2015 Feb; 94(2):201-10. doi: 10.1007/s00277-014-2206-x. [PMID: 25242579]
  • Yuh Baba, Masato Fujii, Toyonobu Maeda, Atsuko Suzuki, Satoshi Yuzawa, Yasumasa Kato. Deguelin induces apoptosis by targeting both EGFR-Akt and IGF1R-Akt pathways in head and neck squamous cell cancer cell lines. BioMed research international. 2015; 2015(?):657179. doi: 10.1155/2015/657179. [PMID: 26075254]
  • Haoyu Ye, Caifeng Xie, Wenshuang Wu, Minli Xiang, Zhuowei Liu, Yanfang Li, Minghai Tang, Shucai Li, Jianhong Yang, Huan Tang, Kai Chen, Chaofeng Long, Aihua Peng, Lijuan Chen. Millettia pachycarpa exhibits anti-inflammatory activity through the suppression of LPS-induced NO/iNOS expression. The American journal of Chinese medicine. 2014; 42(4):949-65. doi: 10.1142/s0192415x14500608. [PMID: 25004885]
  • Julie A Vrana, Nathan Boggs, Holly N Currie, Jonathan Boyd. Amelioration of an undesired action of deguelin. Toxicon : official journal of the International Society on Toxinology. 2013 Nov; 74(?):83-91. doi: 10.1016/j.toxicon.2013.07.028. [PMID: 23933198]
  • Mei-ling Bai, Hai-jun Li, Lin-xi Zhang. [Effects of deguelin on the proliferation and apoptosis of human esophageal cancer cell Ec-109: an experimental research]. Zhongguo Zhong xi yi jie he za zhi Zhongguo Zhongxiyi jiehe zazhi = Chinese journal of integrated traditional and Western medicine. 2013 Mar; 33(3):397-400. doi: . [PMID: 23713258]
  • Rajeshwari Mehta, Harshadadevi Katta, Fatouma Alimirah, Rutulkumar Patel, Genoveva Murillo, Xinjian Peng, Miguel Muzzio, Rajendra G Mehta. Deguelin action involves c-Met and EGFR signaling pathways in triple negative breast cancer cells. PloS one. 2013; 8(6):e65113. doi: 10.1371/journal.pone.0065113. [PMID: 23762292]
  • M K Kalume, B Losson, L Angenot, M Tits, J N Wauters, M Frédérich, C Saegerman. Rotenoid content and in vitro acaricidal activity of Tephrosia vogelii leaf extract on the tick Rhipicephalus appendiculatus. Veterinary parasitology. 2012 Nov; 190(1-2):204-9. doi: 10.1016/j.vetpar.2012.06.015. [PMID: 22795670]
  • Steven R Belmain, Barbara A Amoah, Stephen P Nyirenda, John F Kamanula, Philip C Stevenson. Highly variable insect control efficacy of Tephrosia vogelii chemotypes. Journal of agricultural and food chemistry. 2012 Oct; 60(40):10055-63. doi: 10.1021/jf3032217. [PMID: 22970736]
  • John E Casida. The greening of pesticide-environment interactions: some personal observations. Environmental health perspectives. 2012 Apr; 120(4):487-93. doi: 10.1289/ehp.1104405. [PMID: 22472325]
  • Cheng Jiang, Shengzi Liu, Weihong He, Xiongming Luo, Si Zhang, Zhihui Xiao, Ximin Qiu, Hao Yin. A new prenylated flavanone from Derris trifoliata Lour. Molecules (Basel, Switzerland). 2012 Jan; 17(1):657-63. doi: 10.3390/molecules17010657. [PMID: 22237680]
  • Gabriele Multhoff, Jürgen Radons. Radiation, inflammation, and immune responses in cancer. Frontiers in oncology. 2012; 2(?):58. doi: 10.3389/fonc.2012.00058. [PMID: 22675673]
  • Hyunseung Lee, Ju-Hee Lee, Kyung Hee Jung, Soon-Sun Hong. Deguelin promotes apoptosis and inhibits angiogenesis of gastric cancer. Oncology reports. 2010 Oct; 24(4):957-63. doi: 10.3892/or.2010.957. [PMID: 20811676]
  • Wei Ji, Yulan Cui, Renjuan Chen, Xinren Lin, Qingxin Zhou, Chunji Gan. [Separation and preparation of two rotenoids from the roots of Derris by high-speed counter-current chromatography]. Se pu = Chinese journal of chromatography. 2010 Aug; 28(8):813-6. doi: 10.3724/sp.j.1123.2010.00813. [PMID: 21261054]
  • Ville Härmä, Johannes Virtanen, Rami Mäkelä, Antti Happonen, John-Patrick Mpindi, Matias Knuuttila, Pekka Kohonen, Jyrki Lötjönen, Olli Kallioniemi, Matthias Nees. A comprehensive panel of three-dimensional models for studies of prostate cancer growth, invasion and drug responses. PloS one. 2010 May; 5(5):e10431. doi: 10.1371/journal.pone.0010431. [PMID: 20454659]
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