Genipin (BioDeep_00000000465)

 

Secondary id: BioDeep_00000398651

human metabolite PANOMIX_OTCML-2023 Endogenous natural product


代谢物信息卡片


methyl (1R,4aS,7aS)-1-hydroxy-7-(hydroxymethyl)-1,4a,5,7a-tetrahydrocyclopenta[c]pyran-4-carboxylate

化学式: C11H14O5 (226.0841)
中文名称: 京尼平
谱图信息: 最多检出来源 Viridiplantae(plant) 34.14%

Reviewed

Last reviewed on 2024-11-20.

Cite this Page

Genipin. BioDeep Database v3. PANOMIX ltd, a top metabolomics service provider from China. https://query.biodeep.cn/s/genipin (retrieved 2024-12-22) (BioDeep RN: BioDeep_00000000465). Licensed under the Attribution-Noncommercial 4.0 International License (CC BY-NC 4.0).

分子结构信息

SMILES: COC(=O)C1=COC(C2C1CC=C2CO)O
InChI: InChI=1S/C11H14O5/c1-15-10(13)8-5-16-11(14)9-6(4-12)2-3-7(8)9/h2,5,7,9,11-12,14H,3-4H2,1H3

描述信息

Genipin is found in beverages. Genipin is a constituent of Genipa americana (genipap) Genipin is an aglycone derived from an iridoid glycoside called geniposide present in fruit of Gardenia jasminoides. Genipin is an excellent natural cross-linker for proteins, collagen, gelatin, and chitosan cross-linking. It has a low acute toxicity, with LD50 i.v. 382 mg/kg in mice, therefore, much less toxic than glutaraldehyde and many other commonly used synthetic cross-linking regents. It is also used for pharmaceutical purposes, such as choleretic action for liver diseases control
Genipin is an iridoid monoterpenoid. It has a role as an uncoupling protein inhibitor, a hepatotoxic agent, an apoptosis inhibitor, an antioxidant, an anti-inflammatory agent and a cross-linking reagent.
Genipin is a natural product found in Gardenia jasminoides, Rothmannia globosa, and other organisms with data available.
D005765 - Gastrointestinal Agents > D002756 - Cholagogues and Choleretics
Constituent of Genipa americana (genipap)
Genipin ((+)-Genipin) is a natural crosslinking reagent derived from Gardenia jasminoides Ellis fruits. Genipin inhibits UCP2 (uncoupling protein 2) in cells. Genipin has a variety of bioactivities, including modulation on proteins, antitumor, anti-inflammation, immunosuppression, antithrombosis, and protection of hippocampal neurons. Genipin also can be used for type 2 diabetes research[1][2].
Genipin ((+)-Genipin) is a natural crosslinking reagent derived from Gardenia jasminoides Ellis fruits. Genipin inhibits UCP2 (uncoupling protein 2) in cells. Genipin has a variety of bioactivities, including modulation on proteins, antitumor, anti-inflammation, immunosuppression, antithrombosis, and protection of hippocampal neurons. Genipin also can be used for type 2 diabetes research[1][2].
Genipin ((+)-Genipin) is a natural crosslinking reagent derived from Gardenia jasminoides Ellis fruits. Genipin inhibits UCP2 (uncoupling protein 2) in cells. Genipin has a variety of bioactivities, including modulation on proteins, antitumor, anti-inflammation, immunosuppression, antithrombosis, and protection of hippocampal neurons. Genipin also can be used for type 2 diabetes research[1][2].

同义名列表

26 个代谢物同义名

CYCLOPENTA(C)PYRAN-4-CARBOXYLIC ACID, 1,4A,5,7A-TETRAHYDRO-1-HYDROXY-7-(HYDROXYMETHYL)-, METHYL ESTER, (1R-(1.ALPHA.,4A.ALPHA.,7A.ALPHA.))-; CYCLOPENTA(C)PYRAN-4-CARBOXYLIC ACID, 1,4A,5,7A-TETRAHYDRO-1-HYDROXY-7-(HYDROXYMETHYL)-, METHYL ESTER, (1R,4AS,7AS)-; Cyclopenta[c]pyran-4-carboxylic acid, 1,4a,5,7a-tetrahydro-1-hydroxy-7-(hydroxymethyl)-, methyl ester, (1R,4aS,7aS)-; CYCLOPENTA(C)PYRAN-4-CARBOXYLIC ACID, 1,4A.ALPHA.,5,7A.ALPHA.-TETRAHYDRO-1-HYDROXY-7-(HYDROXYMETHYL)-, METHYL ESTER; Cyclopenta[c]pyran-4-carboxylic acid, 1,4a,5,7a-tetrahydro-1-hydroxy-7-(hydroxymethyl)-, methylester, (1R,4aS,7aS)-; Cyclopenta(c)pyran-4-carboxylic acid, 1,4a-alpha,5,7a-alpha-tetrahydro-1-hydroxy-7-(hydroxymethyl)-, methyl ester; (1R,4aS,7aS)-1-hydroxy-7-(hydroxymethyl)-1,4a,5,7a-tetrahydrocyclopenta[c]pyran-4-carboxylic acid methyl ester; (1R,4aS,7aS)-1-Hydroxy-7-hydroxymethyl-1,4a,5,7a-tetrahydro-cyclopenta[c]pyran-4-carboxylic acid methyl ester; 1R,4aS,5,7aS-tetrahydro-1-hydroxy-7-(hydroxymethyl)-cyclopenta[c]pyran-4-carboxylic acid, methyl ester; methyl (1R,4aS,7aS)-1-hydroxy-7-(hydroxymethyl)-1,4a,5,7a-tetrahydrocyclopenta[c]pyran-4-carboxylate; (1R,4aS,7aS)-methyl 1-hydroxy-7-(hydroxymethyl)-1,4a,5,7a-tetrahydrocyclopenta[c]pyran-4-carboxylate; 1,4a,5,7a-Tetrahydro-1-hydroxy-7-(hydroxymethyl)-cyclopenta(c)pyran-4-carboxylic acid methyl ester; methyl (1R,4aS,7aS)-1-hydroxy-7-(hydroxymethyl)-1H,4aH,5H,7aH-cyclopenta[c]pyran-4-carboxylate; Methyl (1S,2R,6S)-2-Hydroxy-9-(hydroxymethyl)-3-oxabicyclo[4.3.0]nona-4,8-diene-5-carboxylate; Methyl 1-hydroxy-7-(hydroxymethyl)-1H,4ah,5H,7ah-cyclopenta[c]pyran-4-carboxylic acid; methyl 1-hydroxy-7-(hydroxymethyl)-1H,4aH,5H,7aH-cyclopenta[c]pyran-4-carboxylate; Genipin is known as an aglycone dervied from Geniposide.; Genipin, >=98\\% (HPLC), powder; AZKVWQKMDGGDSV-BCMRRPTOSA-N; UNII-A3V2NE52YG; Tox21_500516; (+)-Genipin; A3V2NE52YG; AC1L9CSN; Genipin; Genipin



数据库引用编号

24 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

0 个相关的代谢反应过程信息。

Reactome(0)

BioCyc(0)

WikiPathways(0)

Plant Reactome(0)

INOH(0)

PlantCyc(0)

COVID-19 Disease Map(0)

PathBank(0)

PharmGKB(0)

45 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 12 AKT1, ALB, ANG, BCL2, BDNF, CASP3, MAPK8, MTOR, NFE2L2, NLRP3, PTGS2, VEGFA
Peripheral membrane protein 2 MTOR, PTGS2
Endoplasmic reticulum membrane 4 BCL2, HMOX1, MTOR, PTGS2
Nucleus 11 AKT1, ALB, ANG, BCL2, CASP3, HMOX1, MAPK8, MTOR, NFE2L2, NLRP3, VEGFA
cytosol 10 AKT1, ALB, ANG, BCL2, CASP3, HMOX1, MAPK8, MTOR, NFE2L2, NLRP3
dendrite 2 BDNF, MTOR
phagocytic vesicle 1 MTOR
centrosome 2 ALB, NFE2L2
nucleoplasm 6 AKT1, CASP3, HMOX1, MAPK8, MTOR, NFE2L2
RNA polymerase II transcription regulator complex 1 NFE2L2
Cell membrane 2 AKT1, TNF
Cytoplasmic side 2 HMOX1, MTOR
lamellipodium 1 AKT1
Multi-pass membrane protein 2 UCP1, UCP2
Golgi apparatus membrane 2 MTOR, NLRP3
Synapse 1 MAPK8
cell cortex 1 AKT1
cell surface 2 TNF, VEGFA
glutamatergic synapse 2 AKT1, CASP3
Golgi apparatus 3 ALB, NFE2L2, VEGFA
Golgi membrane 3 INS, MTOR, NLRP3
growth cone 1 ANG
lysosomal membrane 1 MTOR
mitochondrial inner membrane 2 UCP1, UCP2
neuronal cell body 3 ANG, CASP3, TNF
postsynapse 1 AKT1
synaptic vesicle 1 BDNF
Cytoplasm, cytosol 2 NFE2L2, NLRP3
Lysosome 1 MTOR
plasma membrane 3 AKT1, NFE2L2, TNF
Membrane 7 AKT1, BCL2, BDNF, HMOX1, MTOR, NLRP3, VEGFA
axon 2 BDNF, MAPK8
caveola 1 PTGS2
extracellular exosome 2 ALB, BMP3
Lysosome membrane 1 MTOR
endoplasmic reticulum 6 ALB, BCL2, HMOX1, NLRP3, PTGS2, VEGFA
extracellular space 9 ALB, ANG, BDNF, BMP3, HMOX1, IL6, INS, TNF, VEGFA
perinuclear region of cytoplasm 2 BDNF, HMOX1
adherens junction 1 VEGFA
mitochondrion 4 BCL2, NLRP3, UCP1, UCP2
protein-containing complex 4 AKT1, ALB, BCL2, PTGS2
Microsome membrane 2 MTOR, PTGS2
postsynaptic density 1 CASP3
TORC1 complex 1 MTOR
TORC2 complex 1 MTOR
Secreted 8 ALB, ANG, BDNF, BMP3, IL6, INS, NLRP3, VEGFA
extracellular region 10 ALB, ANG, BDNF, BMP3, ELN, IL6, INS, NLRP3, TNF, VEGFA
Mitochondrion outer membrane 2 BCL2, MTOR
Single-pass membrane protein 1 BCL2
mitochondrial outer membrane 3 BCL2, HMOX1, MTOR
anchoring junction 1 ALB
Nucleus membrane 1 BCL2
Bcl-2 family protein complex 1 BCL2
nuclear membrane 1 BCL2
external side of plasma membrane 1 TNF
Secreted, extracellular space, extracellular matrix 2 ELN, VEGFA
actin cytoskeleton 1 ANG
microtubule cytoskeleton 1 AKT1
nucleolus 1 ANG
cell-cell junction 1 AKT1
recycling endosome 1 TNF
Single-pass type II membrane protein 1 TNF
vesicle 1 AKT1
Mitochondrion inner membrane 2 UCP1, UCP2
Membrane raft 1 TNF
pore complex 1 BCL2
spindle 1 AKT1
extracellular matrix 2 ELN, VEGFA
basement membrane 1 ANG
Nucleus, PML body 1 MTOR
PML body 1 MTOR
Mitochondrion intermembrane space 1 AKT1
mitochondrial intermembrane space 1 AKT1
collagen-containing extracellular matrix 1 ELN
secretory granule 1 VEGFA
Cytoplasm, cytoskeleton, microtubule organizing center 1 NLRP3
Inflammasome 1 NLRP3
interphase microtubule organizing center 1 NLRP3
NLRP3 inflammasome complex 1 NLRP3
Nucleus inner membrane 1 PTGS2
Nucleus outer membrane 1 PTGS2
nuclear inner membrane 1 PTGS2
nuclear outer membrane 1 PTGS2
neuron projection 1 PTGS2
ciliary basal body 2 AKT1, ALB
chromatin 1 NFE2L2
mediator complex 1 NFE2L2
phagocytic cup 1 TNF
Chromosome 1 ANG
centriole 1 ALB
Nucleus, nucleolus 1 ANG
spindle pole 1 ALB
blood microparticle 1 ALB
nuclear envelope 1 MTOR
Endomembrane system 2 MTOR, NLRP3
endosome lumen 1 INS
microtubule organizing center 1 NLRP3
Cytoplasm, Stress granule 1 ANG
cytoplasmic stress granule 1 ANG
myelin sheath 1 BCL2
secretory granule lumen 1 INS
Golgi lumen 1 INS
endoplasmic reticulum lumen 5 ALB, BDNF, IL6, INS, PTGS2
platelet alpha granule lumen 2 ALB, VEGFA
endocytic vesicle 1 ANG
transport vesicle 1 INS
Endoplasmic reticulum-Golgi intermediate compartment membrane 1 INS
Single-pass type IV membrane protein 1 HMOX1
protein-DNA complex 1 NFE2L2
basal dendrite 1 MAPK8
death-inducing signaling complex 1 CASP3
Cytoplasmic vesicle, phagosome 1 MTOR
elastic fiber 1 ELN
[Tumor necrosis factor, soluble form]: Secreted 1 TNF
angiogenin-PRI complex 1 ANG
interleukin-6 receptor complex 1 IL6
BAD-BCL-2 complex 1 BCL2
[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
[Neurotrophic factor BDNF precursor form]: Secreted 1 BDNF
ciliary transition fiber 1 ALB
[C-domain 2]: Secreted 1 TNF
[Tumor necrosis factor, membrane form]: Membrane 1 TNF
[C-domain 1]: Secreted 1 TNF


文献列表

  • Kexin Sun, Yanyi Chen, Shijie Zheng, Wenjuan Wan, Ke Hu. Genipin ameliorates diabetic retinopathy via the HIF-1α and AGEs-RAGE pathways. Phytomedicine : international journal of phytotherapy and phytopharmacology. 2024 Jul; 129(?):155596. doi: 10.1016/j.phymed.2024.155596. [PMID: 38626646]
  • Yalu Mi, Hui Shan, Bo Wang, Huidi Tang, Jihui Jia, Xijian Liu, Qing Yang. Genipin inhibits proliferation of gastric cancer cells by inducing ferroptosis: an integrated study of network pharmacology and bioinformatics study. Medical oncology (Northwood, London, England). 2024 Jan; 41(2):46. doi: 10.1007/s12032-023-02283-4. [PMID: 38175425]
  • Zhifeng Cui, Zhe Li, Weichao Dong, Lili Qiu, Jiayu Zhang, Shaoping Wang. Comprehensive Metabolite Identification of Genipin in Rats Using Ultra-High-Performance Liquid Chromatography Coupled with High Resolution Mass Spectrometry. Molecules (Basel, Switzerland). 2023 Aug; 28(17):. doi: 10.3390/molecules28176307. [PMID: 37687136]
  • Haoyan Huang, Yulin Zhao, Chunyan Huang, Ning Lv, Jie Zhao, Shanliang Sun, Chaorui Guo, Di Zhao, Xijing Chen, Yongjie Zhang. Unraveling a Combined Inactivation Mechanism of Cytochrome P450s by Genipin, the Major Reactive Aglycone Derived from Gardeniae Fructus. Chemical research in toxicology. 2023 Aug; ?(?):. doi: 10.1021/acs.chemrestox.3c00102. [PMID: 37622730]
  • Jingjing Wang, Yongwei Qiu, Yaohui Chen, Feng Zhou, Shuaikang Wang, Liping Chen, Yinfang Chen, Riyue Yu, Liping Huang. Synthesis of Methylgenipin and Evaluation of Its Anti-Hepatic Injury Activity. Molecules (Basel, Switzerland). 2023 Jun; 28(12):. doi: 10.3390/molecules28124793. [PMID: 37375346]
  • Lixuan Xiao, Yaning Hou, Zhiyan Xue, Liangjiu Bai, Wenxiang Wang, Hou Chen, Huawei Yang, Lixia Yang, Donglei Wei. Soy Protein Isolate/Genipin-Based Nanoparticles for the Stabilization of Pickering Emulsion to Design Self-Healing Guar Gum-Based Hydrogels. Biomacromolecules. 2023 05; 24(5):2087-2099. doi: 10.1021/acs.biomac.2c01507. [PMID: 37079862]
  • Nittaya Boonmuen, Kanoknetr Suksen, Mintra Kaewkittikhun, Laongthip Ruknarong, Patamawadee Silalai, Rungnapha Saeeng, Arthit Chairoungdua, Sunhapas Soodvilai, Duangrat Tantikanlayaporn. Genipin Analogue (G300) Inhibits Adipogenic Differentiation of Human Bone Marrow-Derived Mesenchymal Stem Cells through the Suppression of Adipogenic Promoting Factors. Journal of natural products. 2023 May; ?(?):. doi: 10.1021/acs.jnatprod.3c00143. [PMID: 37137165]
  • Rita Rosado-Ramos, Gonçalo M Poças, Daniela Marques, Alexandre Foito, David M Sevillano, Mafalda Lopes-da-Silva, Luís G Gonçalves, Regina Menezes, Marcel Ottens, Derek Stewart, Alain Ibáñez de Opakua, Markus Zweckstetter, Miguel C Seabra, César S Mendes, Tiago Fleming Outeiro, Pedro M Domingos, Cláudia N Santos. Genipin prevents alpha-synuclein aggregation and toxicity by affecting endocytosis, metabolism and lipid storage. Nature communications. 2023 Apr; 14(1):1918. doi: 10.1038/s41467-023-37561-2. [PMID: 37024503]
  • Kepeng Hu, Erna Jia, Qimeng Zhang, Wei Zheng, Rongjiao Sun, Mengao Qian, Ying Tan, Wanle Hu. Injectable carboxymethyl chitosan-genipin hydrogels encapsulating tea tree oil for wound healing. Carbohydrate polymers. 2023 Feb; 301(Pt B):120348. doi: 10.1016/j.carbpol.2022.120348. [PMID: 36446509]
  • Yajun Wu, Yao Wang, Dongmin Liu. Identification of Genipin as a Potential Treatment for Type 2 Diabetes. International journal of molecular sciences. 2023 Jan; 24(3):. doi: 10.3390/ijms24032131. [PMID: 36768454]
  • Ning Luo, Gui-Bing Chen, Teng Zhang, Jie Zhao, Jing-Nan Fu, Ning Lu, Tao Ma. Genipin Attenuates Sepsis-Induced Splenocyte Apoptosis via the Inhibition of Endoplasmic Reticulum Stress. Biological & pharmaceutical bulletin. 2023; 46(2):187-193. doi: 10.1248/bpb.b22-00563. [PMID: 36724947]
  • Wentao Deng, Yu Yan, Peipei Zhuang, Xiaoxu Liu, Ke Tian, Wenfang Huang, Cai Li. Synthesis of nanocapsules blended polymeric hydrogel loaded with bupivacaine drug delivery system for local anesthetics and pain management. Drug delivery. 2022 Dec; 29(1):399-412. doi: 10.1080/10717544.2021.2023702. [PMID: 35098821]
  • Li Wang, Ge Chen, Shuyao Wu, Yihua Xu, Chenxi Guo, Manman Wang, Tingming Liang, Zhigang Guo, Hong-Jie Di, Zhigang Hu. Genipin improves lipid metabolism and sperm parametersin obese mice via regulation of miR-132 expression. Acta biochimica et biophysica Sinica. 2022 Sep; 54(9):1278-1288. doi: 10.3724/abbs.2022120. [PMID: 36082932]
  • Magdalena Bryś, Karina Urbańska, Beata Olas. Novel Findings regarding the Bioactivity of the Natural Blue Pigment Genipin in Human Diseases. International journal of molecular sciences. 2022 Jan; 23(2):. doi: 10.3390/ijms23020902. [PMID: 35055094]
  • Hiromasa Yamashita, Mitsue Nishiyama, Katsuya Ohbuchi, Hitomi Kanno, Kazuaki Tsuchiya, Junpei Yamaguchi, Takashi Mizuno, Tomoki Ebata, Masato Nagino, Yukihiro Yokoyama. Predicting Inchinkoto efficacy, in patients with obstructive jaundice associated with malignant tumors, through pharmacomicrobiomics. Pharmacological research. 2022 01; 175(?):105981. doi: 10.1016/j.phrs.2021.105981. [PMID: 34798264]
  • Man Zhang, Lili Ye, Chuanjing Cheng, Fukui Shen, Lin Niu, Yuanyuan Hou, Gang Bai. Dietary Flavone Baicalein Combinate with Genipin Attenuates Inflammation Stimulated by Lipopolysaccharide in RAW264.7 Cells or Pseudomonas aeruginosa in Mice via Regulating the Expression and Phosphorylation of AKT. Nutrients. 2021 Dec; 13(12):. doi: 10.3390/nu13124462. [PMID: 34960014]
  • Qijun Li, Shiqiang Gong, Weifan Yao, Yibin Yu, Chao Liu, Renjun Wang, Hao Pan, Minjie Wei. PEG-interpenetrated genipin-crosslinked dual-sensitive hydrogel/nanostructured lipid carrier compound formulation for topical drug administration. Artificial cells, nanomedicine, and biotechnology. 2021 Dec; 49(1):345-353. doi: 10.1080/21691401.2021.1879104. [PMID: 33784224]
  • Yaqiong Wang, Jingjing Guo, Bingjie Li, Dong Li, Zhaowei Meng, Shao-Kai Sun. Biocompatible therapeutic albumin/genipin bioglue for postoperative wound adhesion and residual tumor ablation. Biomaterials. 2021 12; 279(?):121179. doi: 10.1016/j.biomaterials.2021.121179. [PMID: 34700226]
  • Fengtao Li, Lijun Song, Jing Chen, Yu Chen, Yongjun Li, Meizi Huang, Wenchang Zhao. Effect of genipin-1-β-d-gentiobioside on diabetic nephropathy in mice by activating AMP-activated protein kinase/silencing information regulator-related enzyme 1/ nuclear factor-κB pathway. The Journal of pharmacy and pharmacology. 2021 Aug; 73(9):1201-1211. doi: 10.1093/jpp/rgab041. [PMID: 33792721]
  • Meiting Li, Nan Cai, Liang Gu, Lijun Yao, Decheng Bi, Weishan Fang, Zhijian Lin, Yan Wu, Hong Xu, Hui Li, Zhangli Hu, Xu Xu. Genipin Attenuates Tau Phosphorylation and Aβ Levels in Cellular Models of Alzheimer's Disease. Molecular neurobiology. 2021 Aug; 58(8):4134-4144. doi: 10.1007/s12035-021-02389-8. [PMID: 33948899]
  • Yusha Luo, Fangyuan Gao, Ruirui Chang, Xingjie Zhang, Jie Zhong, Jun Wen, Jianlin Wu, Tingting Zhou. Metabolomics based comprehensive investigation of Gardeniae Fructus induced hepatotoxicity. Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association. 2021 Jul; 153(?):112250. doi: 10.1016/j.fct.2021.112250. [PMID: 33964367]
  • Abhishek Indurkar, Ashish Pandit, Ratnesh Jain, Prajakta Dandekar. Plant based cross-linkers for tissue engineering applications. Journal of biomaterials applications. 2021 07; 36(1):76-94. doi: 10.1177/0885328220979273. [PMID: 33342347]
  • Chi Wang, Pei-Xu Chen, Qiong Xiao, Qiu-Ming Yang, Hui-Fen Weng, Yong-Hui Zhang, An-Feng Xiao. Chitosan Activated with Genipin: A Nontoxic Natural Carrier for Tannase Immobilization and Its Application in Enhancing Biological Activities of Tea Extract. Marine drugs. 2021 Mar; 19(3):. doi: 10.3390/md19030166. [PMID: 33808933]
  • Zhong-Shang Xia, Er-Wei Hao, Yan-Ting Wei, Xiao-Tao Hou, Zhang-Mei Chen, Man Wei, Zheng-Cai Du, Jia-Gang Deng. Genipin induces developmental toxicity through oxidative stress and apoptosis in zebrafish. Comparative biochemistry and physiology. Toxicology & pharmacology : CBP. 2021 Mar; 241(?):108951. doi: 10.1016/j.cbpc.2020.108951. [PMID: 33316388]
  • Idalina Gonçalves, Diana Hernández, Cátia Cruz, Joana Lopes, Ana Barra, Cláudia Nunes, José A Lopes da Silva, Paula Ferreira, Manuel A Coimbra. Relevance of genipin networking on rheological, physical, and mechanical properties of starch-based formulations. Carbohydrate polymers. 2021 Feb; 254(?):117236. doi: 10.1016/j.carbpol.2020.117236. [PMID: 33357844]
  • Rongtian Lin, Shuwen Rao, Yanbing Li, Lei Zhang, Liyu Xu, Yepu He, Zhijun Liu, Heru Chen. Conjugation of tacrine with genipin derivative not only enhances effects on AChE but also leads to autophagy against Alzheimer's disease. European journal of medicinal chemistry. 2021 Feb; 211(?):113067. doi: 10.1016/j.ejmech.2020.113067. [PMID: 33338868]
  • Edgardo Rivera-Delgado, Greg D Learn, Dominic J Kizek, Tejas Kashyap, Emerson J Lai, Horst A von Recum. A Polymeric Delivery System Enables Controlled Release of Genipin for Spatially-Confined In Situ Crosslinking of Injured Connective Tissues. Journal of pharmaceutical sciences. 2021 02; 110(2):815-823. doi: 10.1016/j.xphs.2020.09.044. [PMID: 33190799]
  • Jiyeon Hong, Dahun Jung, Saerom Park, Yujin Oh, Kyeong Keun Oh, Sang Hyun Lee. Immobilization of laccase via cross-linked enzyme aggregates prepared using genipin as a natural cross-linker. International journal of biological macromolecules. 2021 Feb; 169(?):541-550. doi: 10.1016/j.ijbiomac.2020.12.136. [PMID: 33358952]
  • Yihua Xu, Li Wang, Siyuan Cao, Ruihua Hu, Rui Liu, Ke Hua, Zhigang Guo, Hong-Jie Di, Zhigang Hu. Genipin improves reproductive health problems caused by circadian disruption in male mice. Reproductive biology and endocrinology : RB&E. 2020 Dec; 18(1):122. doi: 10.1186/s12958-020-00679-9. [PMID: 33308222]
  • Ruifeng Luo, Meisi Lin, Chen Zhang, Jinfeng Shi, Siyuan Zhang, Qiyan Chen, Yichen Hu, Minyue Zhang, Jinming Zhang, Fei Gao. Genipin-crosslinked human serum albumin coating using a tannic acid layer for enhanced oral administration of curcumin in the treatment of ulcerative colitis. Food chemistry. 2020 Nov; 330(?):127241. doi: 10.1016/j.foodchem.2020.127241. [PMID: 32540526]
  • Xiaofei Fan, Lin Lin, Binxin Cui, Tianming Zhao, Lihong Mao, Yan Song, Xiaoyu Wang, Hongjuan Feng, Yu Qingxiang, Jie Zhang, Kui Jiang, Xiaocang Cao, Bangmao Wang, Chao Sun. Therapeutic potential of genipin in various acute liver injury, fulminant hepatitis, NAFLD and other non-cancer liver diseases: More friend than foe. Pharmacological research. 2020 09; 159(?):104945. doi: 10.1016/j.phrs.2020.104945. [PMID: 32454225]
  • Nihui Zhang, Tao Gao, Yao Wang, Juan Liu, Junwei Zhang, Ruijuan Yao, Fang Wu. Modulating cationicity of chitosan hydrogel to prevent hypertrophic scar formation during wound healing. International journal of biological macromolecules. 2020 Jul; 154(?):835-843. doi: 10.1016/j.ijbiomac.2020.03.161. [PMID: 32194120]
  • Shahla Teimouri, Stefan Kasapis. Morphology of genipin-crosslinked BSA networks yields a measurable effect on the controlled release of vitamin B6. Food chemistry. 2020 Jun; 314(?):126204. doi: 10.1016/j.foodchem.2020.126204. [PMID: 31978719]
  • Min Wang, Zhi-Kuan Yang, Hong Liu, Rui-Qin Li, Yu Liu, Wen-Jun Zhong. Genipin inhibits the scleral expression of miR-29 and MMP2 and promotes COL1A1 expression in myopic eyes of guinea pigs. Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie. 2020 May; 258(5):1031-1038. doi: 10.1007/s00417-020-04634-7. [PMID: 32125507]
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