Plumbagin (BioDeep_00000229786)

 

Secondary id: BioDeep_00000003768

natural product PANOMIX_OTCML-2023 Antitumor activity


代谢物信息卡片


InChI=1/C11H8O3/c1-6-5-9(13)10-7(11(6)14)3-2-4-8(10)12/h2-5,12H,1H

化学式: C11H8O3 (188.0473)
中文名称: 白花丹醌, 白花丹素, 兰雪醌, 1,4-二氨基-2,3-二氯蒽醌
谱图信息: 最多检出来源 Homo sapiens(blood) 10.73%

分子结构信息

SMILES: CC1=CC(=O)C2=C(C1=O)C=CC=C2O
InChI: InChI=1S/C11H8O3/c1-6-5-9(13)10-7(11(6)14)3-2-4-8(10)12/h2-5,12H,1H3

描述信息

Plumbagin is a hydroxy-1,4-naphthoquinone that is 1,4-naphthoquinone in which the hydrogens at positions 2 and 5 are substituted by methyl and hydroxy groups, respectively. It has a role as a metabolite, an immunological adjuvant, an anticoagulant and an antineoplastic agent. It is a member of phenols and a hydroxy-1,4-naphthoquinone.
Plumbagin is a compound investigated for its anticancer activity. It has been found that it inactivates the Akt/NF-kB, MMP-9 and VEGF pathways.
Plumbagin is a natural product found in Drosera slackii, Diospyros hebecarpa, and other organisms with data available.
Synthetic Plumbagin PCUR-101 is a synthetic form of the plant-derived medicinal agent, plumbagin, with potential antineoplastic activity. Plumbagin may act by inhibiting the expression of protein kinase C epsilon (PKCe), signal transducers and activators of transcription 3 phosphorylation (Stat3), protein kinase B (AKT), and certain epithelial-to-mesenchymal transition (EMT) markers, including vimentin and slug. This results in possible inhibition of proliferation in susceptible tumor cells. PKCe, Stat3, AKT, and the EMT markers vimentin and slug have been linked to the induction and progression of prostate cancer.
A hydroxy-1,4-naphthoquinone that is 1,4-naphthoquinone in which the hydrogens at positions 2 and 5 are substituted by methyl and hydroxy groups, respectively.
D000890 - Anti-Infective Agents > D000977 - Antiparasitic Agents > D000871 - Anthelmintics
D012102 - Reproductive Control Agents > D003270 - Contraceptive Agents
C274 - Antineoplastic Agent > C2189 - Signal Transduction Inhibitor
D020011 - Protective Agents > D002316 - Cardiotonic Agents
D006401 - Hematologic Agents > D000925 - Anticoagulants
D000970 - Antineoplastic Agents
D002317 - Cardiovascular Agents
D007155 - Immunologic Factors
relative retention time with respect to 9-anthracene Carboxylic Acid is 0.955
relative retention time with respect to 9-anthracene Carboxylic Acid is 0.957
relative retention time with respect to 9-anthracene Carboxylic Acid is 0.960
Plumbagin (2-Methyljuglone) is a naphthoquinone isolated from Plumbago zeylanica, exhibits anticancer and antiproliferative activities[1].
Plumbagin (2-Methyljuglone) is a naphthoquinone isolated from Plumbago zeylanica, exhibits anticancer and antiproliferative activities[1].

同义名列表

33 个代谢物同义名

InChI=1/C11H8O3/c1-6-5-9(13)10-7(11(6)14)3-2-4-8(10)12/h2-5,12H,1H; 5-hydroxy-2-methyl-1,4-dihydronaphthalene-1,4-dione; 4-08-00-02376 (Beilstein Handbook Reference); 1,4-Naphthalenedione, 5-hydroxy-2-methyl-; 5-Hydroxy-2-methyl-naphthalene-1,4-dione; 1,4-NAPHTHOQUINONE, 5-HYDROXY-2-METHYL-; 5-Hydroxy-2-methyl-1,4-naphthalenedione; 5-Hydroxy-2-methylnaphthalene-1,4-dione; 5-Hydroxy-2-methyl-[1,4]naphthoquinone; 2-methyl-5-hydroxy-1,4-naphthoquinone; 5-hydroxy-2-methyl-1,4-naphthoquinone; 5- HYDROXY,2-METHYL-1,4-NAPHTOQUINONE; Plumbagin from Plumbago indica; 1, 5-hydroxy-2-methyl-; WLN: L66 BV EVJ C1 GQ; Plumbagin [WHO-DD]; 2-Methyljuglone; UNII-YAS4TBQ4OQ; PLUMBAGIN [MI]; NCI60_001904; ACon1_001611; Plumbagine; Plumbagone; Ophioxylin; YAS4TBQ4OQ; Plumbaein; Plumbagin; AI3-38055; plumbapin; Pumbagin; A1-00788; RTK1; Plumbagin



数据库引用编号

33 个数据库交叉引用编号

分类词条

253 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, BRCA1, CAT, CCND1, CDKN1A, CTNNB1, EGFR, EP300, ERBB2, MAPK8, MSMP, MTOR, NOX4, PIK3CA, STAT3, TP53
Peripheral membrane protein 1 MTOR
Endosome membrane 2 EGFR, ERBB2
Endoplasmic reticulum membrane 3 EGFR, MTOR, NOX4
Nucleus 13 ANG, BRCA1, CCND1, CDKN1A, CTNNB1, EGFR, EP300, ERBB2, MAPK8, MTOR, NOX4, STAT3, TP53
cytosol 12 ANG, CAT, CCND1, CDKN1A, CTNNB1, EP300, ERBB2, MAPK8, MTOR, PIK3CA, STAT3, TP53
dendrite 1 MTOR
nuclear body 2 BRCA1, CDKN1A
phagocytic vesicle 1 MTOR
centrosome 3 CCND1, CTNNB1, TP53
nucleoplasm 10 BRCA1, CCND1, CDKN1A, CTNNB1, EP300, ERBB2, MAPK8, MTOR, STAT3, TP53
RNA polymerase II transcription regulator complex 1 STAT3
Cell membrane 5 CTNNB1, EGFR, ERBB2, NOX4, TNF
Cytoplasmic side 1 MTOR
lamellipodium 2 CTNNB1, PIK3CA
ruffle membrane 2 EGFR, ERBB2
Early endosome membrane 1 EGFR
Multi-pass membrane protein 1 NOX4
Golgi apparatus membrane 1 MTOR
Synapse 2 CTNNB1, MAPK8
cell cortex 1 CTNNB1
cell junction 2 CTNNB1, EGFR
cell surface 2 EGFR, TNF
glutamatergic synapse 2 CTNNB1, EGFR
Golgi membrane 2 EGFR, MTOR
growth cone 1 ANG
lysosomal membrane 1 MTOR
neuromuscular junction 1 ERBB2
neuronal cell body 2 ANG, TNF
presynaptic membrane 2 CTNNB1, ERBB2
Lysosome 1 MTOR
endosome 1 EGFR
plasma membrane 8 BRCA1, CTNNB1, EGFR, ERBB2, NOX4, PIK3CA, STAT3, TNF
Membrane 8 BRCA1, CAT, CTNNB1, EGFR, ERBB2, MTOR, NOX4, TP53
apical plasma membrane 2 EGFR, ERBB2
axon 2 CCK, MAPK8
basolateral plasma membrane 3 CTNNB1, EGFR, ERBB2
extracellular exosome 2 CAT, CTNNB1
Lysosome membrane 1 MTOR
endoplasmic reticulum 2 NOX4, TP53
extracellular space 7 ANG, CCK, EGFR, IL17A, IL6, MSMP, TNF
perinuclear region of cytoplasm 6 CDKN1A, CTNNB1, EGFR, ERBB2, NOX4, PIK3CA
Schaffer collateral - CA1 synapse 1 CTNNB1
adherens junction 1 CTNNB1
apicolateral plasma membrane 1 CTNNB1
bicellular tight junction 2 CCND1, CTNNB1
intercalated disc 1 PIK3CA
mitochondrion 3 CAT, NOX4, TP53
protein-containing complex 6 BRCA1, CAT, CDKN1A, CTNNB1, EGFR, TP53
intracellular membrane-bounded organelle 1 CAT
Microsome membrane 1 MTOR
TORC1 complex 1 MTOR
TORC2 complex 1 MTOR
Single-pass type I membrane protein 2 EGFR, ERBB2
Secreted 5 ANG, CCK, IL17A, IL6, MSMP
extracellular region 7 ANG, CAT, CCK, ERBB2, IL17A, IL6, TNF
Mitochondrion outer membrane 1 MTOR
mitochondrial outer membrane 1 MTOR
Mitochondrion matrix 1 TP53
mitochondrial matrix 2 CAT, TP53
transcription regulator complex 4 CTNNB1, EP300, STAT3, TP53
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome 1 TP53
Nucleus membrane 1 CCND1
nuclear membrane 2 CCND1, EGFR
external side of plasma membrane 2 IL17A, TNF
actin cytoskeleton 1 ANG
Z disc 1 CTNNB1
beta-catenin destruction complex 1 CTNNB1
cytoplasmic vesicle 1 ERBB2
nucleolus 4 ANG, CDKN1A, NOX4, TP53
Wnt signalosome 1 CTNNB1
Early endosome 1 ERBB2
apical part of cell 1 CTNNB1
cell-cell junction 1 CTNNB1
recycling endosome 1 TNF
Single-pass type II membrane protein 1 TNF
postsynaptic membrane 1 CTNNB1
Cell projection, ruffle membrane 1 ERBB2
Cytoplasm, perinuclear region 2 ERBB2, NOX4
Membrane raft 2 EGFR, TNF
Cell junction, focal adhesion 1 NOX4
Cytoplasm, cytoskeleton 2 CTNNB1, TP53
focal adhesion 4 CAT, CTNNB1, EGFR, NOX4
Cell junction, adherens junction 1 CTNNB1
flotillin complex 1 CTNNB1
Peroxisome 1 CAT
basement membrane 1 ANG
intracellular vesicle 1 EGFR
Peroxisome matrix 1 CAT
peroxisomal matrix 1 CAT
peroxisomal membrane 1 CAT
Nucleus, PML body 2 MTOR, TP53
PML body 2 MTOR, TP53
fascia adherens 1 CTNNB1
lateral plasma membrane 1 CTNNB1
receptor complex 2 EGFR, ERBB2
chromatin 3 EP300, STAT3, TP53
phagocytic cup 1 TNF
cell periphery 1 CTNNB1
Chromosome 3 ANG, BRCA1, EP300
Cytoplasm, cytoskeleton, cilium basal body 1 CTNNB1
[Isoform 5]: Cytoplasm 2 BRCA1, NOX4
Nucleus, nucleolus 2 ANG, NOX4
spindle pole 1 CTNNB1
postsynaptic density, intracellular component 1 CTNNB1
microvillus membrane 1 CTNNB1
site of double-strand break 1 TP53
nuclear envelope 1 MTOR
Endomembrane system 2 CTNNB1, MTOR
lateral element 1 BRCA1
Cytoplasm, Stress granule 1 ANG
cytoplasmic stress granule 1 ANG
euchromatin 1 CTNNB1
germ cell nucleus 1 TP53
replication fork 1 TP53
myelin sheath 1 ERBB2
ubiquitin ligase complex 1 BRCA1
basal plasma membrane 2 EGFR, ERBB2
[Isoform 3]: Cytoplasm 1 NOX4
synaptic membrane 1 EGFR
ficolin-1-rich granule lumen 1 CAT
secretory granule lumen 1 CAT
endoplasmic reticulum lumen 1 IL6
nuclear matrix 1 TP53
transcription repressor complex 2 CCND1, TP53
male germ cell nucleus 1 BRCA1
phosphatidylinositol 3-kinase complex 1 PIK3CA
phosphatidylinositol 3-kinase complex, class IA 1 PIK3CA
XY body 1 BRCA1
endocytic vesicle 1 ANG
beta-catenin-TCF complex 1 CTNNB1
perinuclear endoplasmic reticulum 1 NOX4
semaphorin receptor complex 1 ERBB2
presynaptic active zone cytoplasmic component 1 CTNNB1
clathrin-coated endocytic vesicle membrane 1 EGFR
ribonucleoprotein complex 1 BRCA1
[Isoform 1]: Nucleus 1 TP53
histone acetyltransferase complex 1 EP300
protein-DNA complex 2 CTNNB1, EP300
basal dendrite 1 MAPK8
[Isoform 1]: Cell membrane 1 ERBB2
intracellular non-membrane-bounded organelle 1 BRCA1
DNA repair complex 1 BRCA1
Cytoplasmic vesicle, phagosome 1 MTOR
catenin complex 1 CTNNB1
BRCA1-C complex 1 BRCA1
[Isoform 4]: Nucleus 1 NOX4
cyclin-dependent protein kinase holoenzyme complex 2 CCND1, CDKN1A
multivesicular body, internal vesicle lumen 1 EGFR
Shc-EGFR complex 1 EGFR
[Tumor necrosis factor, soluble form]: Secreted 1 TNF
angiogenin-PRI complex 1 ANG
catalase complex 1 CAT
ERBB3:ERBB2 complex 1 ERBB2
NADPH oxidase complex 1 NOX4
interleukin-6 receptor complex 1 IL6
[Isoform 6]: Cytoplasm 1 NOX4
cyclin D1-CDK4 complex 1 CCND1
PCNA-p21 complex 1 CDKN1A
beta-catenin-TCF7L2 complex 1 CTNNB1
cyclin D1-CDK6 complex 1 CCND1
beta-catenin-ICAT complex 1 CTNNB1
Scrib-APC-beta-catenin complex 1 CTNNB1
BRCA1-A complex 1 BRCA1
BRCA1-B complex 1 BRCA1
BRCA1-BARD1 complex 1 BRCA1
gamma-tubulin ring complex 1 BRCA1
nuclear ubiquitin ligase complex 1 BRCA1
phosphatidylinositol 3-kinase complex, class IB 1 PIK3CA
[C-domain 2]: Secreted 1 TNF
[Tumor necrosis factor, membrane form]: Membrane 1 TNF
[C-domain 1]: Secreted 1 TNF


文献列表

  • Carlos José Rocha Teixeira, Barbara Pereira Dos Santos, Carolina Julia Costa Saraiva, Heloísa de Paula Pedroza, Silvia Catarina Salgado Oloris, Benito Soto-Blanco. TLC and HPLC methods for the determination of plumbagin for the diagnosis of poisoning by Plumbago scandens L. Toxicon : official journal of the International Society on Toxinology. 2024 Feb; 239(?):107634. doi: 10.1016/j.toxicon.2024.107634. [PMID: 38307130]
  • Ranjith Palanisamy, Nimnaka Indrajith Kahingalage, David Archibald, Ilaria Casari, Marco Falasca. Synergistic Anticancer Activity of Plumbagin and Xanthohumol Combination on Pancreatic Cancer Models. International journal of molecular sciences. 2024 Feb; 25(4):. doi: 10.3390/ijms25042340. [PMID: 38397018]
  • Songtao Bie, Qiuyue Mo, Chen Shi, Hui Yuan, Chunshuang Li, Tong Wu, Wenlong Li, Heshui Yu. Interactions of plumbagin with five common antibiotics against Staphylococcus aureus in vitro. PloS one. 2024; 19(1):e0297493. doi: 10.1371/journal.pone.0297493. [PMID: 38277418]
  • Tiehan Cui, Yun Lan, Fei Yu, Suai Lin, Jiaxuan Qiu. Plumbagin alleviates temporomandibular joint osteoarthritis progression by inhibiting chondrocyte ferroptosis via the MAPK signaling pathways. Aging. 2023 11; 15(22):13452-13470. doi: 10.18632/aging.205253. [PMID: 38032278]
  • Suresh Awale, Hayato Baba, Nguyen Duy Phan, Min Jo Kim, Juthamart Maneenet, Koichi Sawaki, Mitsuro Kanda, Tomoyuki Okumura, Tsutomu Fujii, Takuya Okada, Takahiro Maruyama, Takahiro Okada, Naoki Toyooka. Targeting Pancreatic Cancer with Novel Plumbagin Derivatives: Design, Synthesis, Molecular Mechanism, In Vitro and In Vivo Evaluation. Journal of medicinal chemistry. 2023 May; ?(?):. doi: 10.1021/acs.jmedchem.3c00394. [PMID: 37257133]
  • Devendra Kumar Pandey, Kajal Katoch, Tuyelee Das, Madhumita Majumder, Kuldeep Dhama, Abhijit Bhagwan Mane, Abilash Valsala Gopalakrishnan, Abhijit Dey. Approaches for in vitro propagation and production of plumbagin in Plumbago spp. Applied microbiology and biotechnology. 2023 May; ?(?):. doi: 10.1007/s00253-023-12511-6. [PMID: 37199750]
  • Kaihua Wang, Beibei Wang, Henan Ma, Ziwen Wang, Yuxiu Liu, Qingmin Wang. Natural Products for Pesticides Discovery: Structural Diversity Derivation and Biological Activities of Naphthoquinones Plumbagin and Juglone. Molecules (Basel, Switzerland). 2023 Apr; 28(8):. doi: 10.3390/molecules28083328. [PMID: 37110562]
  • Beatrycze Nowicka, Jan Walczak, Maja Kapsiak, Karolina Barnaś, Julia Dziuba, Aleksandra Suchoń. Impact of cytotoxic plant naphthoquinones, juglone, plumbagin, lawsone and 2-methoxy-1,4-naphthoquinone, on Chlamydomonas reinhardtii reveals the biochemical mechanism of juglone toxicity by rapid depletion of plastoquinol. Plant physiology and biochemistry : PPB. 2023 Apr; 197(?):107660. doi: 10.1016/j.plaphy.2023.107660. [PMID: 36996637]
  • Huan Liu, Wenchao Zhang, Lijie Jin, Shasha Liu, Liying Liang, Yanfei Wei. Plumbagin Exhibits Genotoxicity and Induces G2/M Cell Cycle Arrest via ROS-Mediated Oxidative Stress and Activation of ATM-p53 Signaling Pathway in Hepatocellular Cells. International journal of molecular sciences. 2023 Mar; 24(7):. doi: 10.3390/ijms24076279. [PMID: 37047251]
  • Babita Shukla, Poonam Kushwaha. Development and Validation of HPLC Method for Quantification of Plumbagin in Plumbago Zeylanica L. Roots. Drug research. 2023 Feb; ?(?):. doi: 10.1055/a-2019-4985. [PMID: 36822215]
  • Arati P Vasav, Balu G Meshram, Anupama A Pable, Vitthal T Barvkar. Artificial microRNA mediated silencing of cyclase and aldo-keto reductase genes reveal their involvement in the plumbagin biosynthetic pathway. Journal of plant research. 2023 Jan; 136(1):47-62. doi: 10.1007/s10265-022-01415-7. [PMID: 36227455]
  • Zhaowei Cai, Shaojuan He, Rongju Liu, Liling Zhou, Li Zhao. Plumbagin rescues the granulosa cell's pyroptosis by reducing WTAP-mediated N6-methylation in polycystic ovary syndrome. Journal of ovarian research. 2022 Dec; 15(1):126. doi: 10.1186/s13048-022-01058-1. [PMID: 36463191]
  • Arati P Vasav, Rucha C Godbole, Ashwini M Darshetkar, Anupama A Pable, Vitthal T Barvkar. Functional genomics-enabled characterization of CYP81B140 and CYP81B141 from Plumbago zeylanica L. substantiates their involvement in plumbagin biosynthesis. Planta. 2022 Oct; 256(6):102. doi: 10.1007/s00425-022-04014-x. [PMID: 36282353]
  • Shulan Han, Shengnan Bi, Tingting Guo, Dandan Sun, Yifang Zou, Lingzhi Wang, Liu Song, Di Chu, Anqi Liao, Xiaohuan Song, Zhuo Yu, Jianfeng Guo. Nano co-delivery of Plumbagin and Dihydrotanshinone I reverses immunosuppressive TME of liver cancer. Journal of controlled release : official journal of the Controlled Release Society. 2022 08; 348(?):250-263. doi: 10.1016/j.jconrel.2022.05.057. [PMID: 35660631]
  • Mandeep Kumar Arora, Anish Ratra, Syed Mohammed Basheeruddin Asdaq, Ali A Alshamrani, Abdulkhaliq J Alsalman, Mehnaz Kamal, Ritu Tomar, Jagannath Sahoo, Jangra Ashok, Mohd Imran. Plumbagin Alleviates Intracerebroventricular-Quinolinic Acid Induced Depression-like Behavior and Memory Deficits in Wistar Rats. Molecules (Basel, Switzerland). 2022 Mar; 27(6):. doi: 10.3390/molecules27061834. [PMID: 35335195]
  • Mitayani Purwoko, Harijono Kario Sentono, Bambang Purwanto, Dono Indarto. Phytochemical evaluation of Plumbago zeylanica roots from Indonesia and assessment of its plumbagin concentration. Folia medica. 2022 Feb; 64(1):96-102. doi: 10.3897/folmed.64.e58086. [PMID: 35851881]
  • Avinash M Yadav, Manali M Bagade, Soni Ghumnani, Sujatha Raman, Bhaskar Saha, Katharina F Kubatzky, Richa Ashma. The phytochemical plumbagin reciprocally modulates osteoblasts and osteoclasts. Biological chemistry. 2022 01; 403(2):211-229. doi: 10.1515/hsz-2021-0290. [PMID: 34882360]
  • Niyatee Thakor, Bhavyata Janathia. Plumbagin: A Potential Candidate for Future Research and Development. Current pharmaceutical biotechnology. 2022; 23(15):1800-1812. doi: 10.2174/1389201023666211230113146. [PMID: 34967293]
  • Kinga Siatkowska, Milena Chraniuk, Piotr Bollin, Rafał Banasiuk. Light emitting diodes optimisation for secondary metabolites production by Droseraceae plants. Journal of photochemistry and photobiology. B, Biology. 2021 Nov; 224(?):112308. doi: 10.1016/j.jphotobiol.2021.112308. [PMID: 34543848]
  • Yang Zhang, Ri Wang, He Zhang, Liya Liu, Jianbin An, Jun Hao, Jingxue Ma. Plumbagin Inhibits Proliferation, Migration, and Invasion of Retinal Pigment Epithelial Cells Induced by FGF-2. Tissue & cell. 2021 Oct; 72(?):101547. doi: 10.1016/j.tice.2021.101547. [PMID: 33964605]
  • Madhu Manti Patra, Poulami Ghosh, Shreya Sengupta, Sujoy K Das Gupta. DNA binding and gene regulatory functions of MSMEG_2295, a repressor encoded by the dinB2 operon of Mycobacterium smegmatis. Microbiology (Reading, England). 2021 10; 167(10):. doi: 10.1099/mic.0.001097. [PMID: 34665112]
  • Isaac J Bello, Olubukola T Oyebode, John O Olanlokun, Todiimu O Omodara, Olufunso O Olorunsogo. Plumbagin induces testicular damage via mitochondrial-dependent cell death. Chemico-biological interactions. 2021 Sep; 347(?):109582. doi: 10.1016/j.cbi.2021.109582. [PMID: 34302802]
  • Liang Yue, Nan Jiang, Anguo Wu, Wenqiao Qiu, Xin Shen, Dalian Qin, Hong Li, Jing Lin, Sicheng Liang, Jianming Wu. Plumbagin can potently enhance the activity of xanthine oxidase: in vitro, in vivo and in silico studies. BMC pharmacology & toxicology. 2021 07; 22(1):45. doi: 10.1186/s40360-021-00511-z. [PMID: 34274011]
  • Nidal Jaradat, Ahmad Ibrahim Khasati, Nawaf Al-Maharik, Ahmad M Eid, Waheed Jundi, Nidal Abd Aljaber Zatar, Mohammed Saleem Ali-Shtayeh, Rana Jamous. Isolation, identification, and antimycotic activity of plumbagin from Plumbago europaea L. roots, leaves and stems. Pakistan journal of pharmaceutical sciences. 2021 Jul; 34(4):1421-1428. doi: ". [PMID: 34799317]
  • Ze-Bo Jiang, Cong Xu, Wenjun Wang, Yi-Zhong Zhang, Ju-Min Huang, Ya-Jia Xie, Qian-Qian Wang, Xing-Xing Fan, Xiao-Jun Yao, Chun Xie, Xuan-Run Wang, Pei-Yu Yan, Yu-Po Ma, Qi-Biao Wu, Elaine Lai-Han Leung. Plumbagin suppresses non-small cell lung cancer progression through downregulating ARF1 and by elevating CD8+ T cells. Pharmacological research. 2021 07; 169(?):105656. doi: 10.1016/j.phrs.2021.105656. [PMID: 33964470]
  • Hong-Hsiang Guan, Yen-Hua Huang, En-Shyh Lin, Chun-Jung Chen, Cheng-Yang Huang. Plumbagin, a Natural Product with Potent Anticancer Activities, Binds to and Inhibits Dihydroorotase, a Key Enzyme in Pyrimidine Biosynthesis. International journal of molecular sciences. 2021 Jun; 22(13):. doi: 10.3390/ijms22136861. [PMID: 34202294]
  • Yuqin Lei, Yuling Li, Yuping Tan, Zhiyong Qian, Qiao Zhou, Da Jia, Qingxiang Sun. Novel Mechanistic Observations and NES-Binding Groove Features Revealed by the CRM1 Inhibitors Plumbagin and Oridonin. Journal of natural products. 2021 05; 84(5):1478-1488. doi: 10.1021/acs.jnatprod.0c01231. [PMID: 33890470]
  • Marta Krychowiak-Maśnicka, Mirosława Krauze-Baranowska, Sylwia Godlewska, Zbigniew Kaczyński, Aleksandra Bielicka-Giełdoń, Natalia Grzegorczyk, Magdalena Narajczyk, Joanna E Frackowiak, Aleksandra Krolicka. Potential of Silver Nanoparticles in Overcoming the Intrinsic Resistance of Pseudomonas aeruginosa to Secondary Metabolites from Carnivorous Plants. International journal of molecular sciences. 2021 May; 22(9):. doi: 10.3390/ijms22094849. [PMID: 34063704]
  • Nattawut Suchaichit, Natcha P Suchaichit, Kwanjai Kanokmedhakul, Patcharaporn Boottanun, Rasana W Sermswan, Panawan Moosophon, Somdej Kanokmedhakul. A new cytotoxic plumbagin derivative from roots of Diospyros undulata. Natural product research. 2021 May; 35(10):1605-1612. doi: 10.1080/14786419.2019.1630120. [PMID: 31203668]
  • Edward Owen Norman, Hayden Tuohey, David Pizzi, Milane Saidah, Rachael Bell, Robert Brkljača, Jonathan M White, Robin B Gasser, Aya C Taki, Sylvia Urban. Phytochemical Profiling and Biological Activity of the Australian Carnivorous Plant, Drosera magna. Journal of natural products. 2021 04; 84(4):964-971. doi: 10.1021/acs.jnatprod.0c00869. [PMID: 33631073]
  • Sevinj Sultanli, Soni Ghumnani, Richa Ashma, Katharina F Kubatzky. Plumbagin, a Biomolecule with (Anti)Osteoclastic Properties. International journal of molecular sciences. 2021 Mar; 22(5):. doi: 10.3390/ijms22052779. [PMID: 33803472]
  • Danfeng Xue, Xiongming Zhou, Jiaxuan Qiu. Cytotoxicity mechanisms of plumbagin in drug-resistant tongue squamous cell carcinoma. The Journal of pharmacy and pharmacology. 2021 Mar; 73(1):98-109. doi: 10.1093/jpp/rgaa027. [PMID: 33791802]
  • Asifur Rahman-Soad, Alberto Dávila-Lara, Christian Paetz, Axel Mithöfer. Plumbagin, a Potent Naphthoquinone from Nepenthes Plants with Growth Inhibiting and Larvicidal Activities. Molecules (Basel, Switzerland). 2021 Feb; 26(4):. doi: 10.3390/molecules26040825. [PMID: 33562562]
  • Revathy Nadhan, Dipyaman Patra, Neethu Krishnan, Arathi Rajan, Srinivas Gopala, Dashnamoorthy Ravi, Priya Srinivas. Perspectives on mechanistic implications of ROS inducers for targeting viral infections. European journal of pharmacology. 2021 Jan; 890(?):173621. doi: 10.1016/j.ejphar.2020.173621. [PMID: 33068588]
  • Arpita Roy. Plumbagin: A Potential Anti-cancer Compound. Mini reviews in medicinal chemistry. 2021; 21(6):731-737. doi: 10.2174/1389557520666201116144421. [PMID: 33200707]
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