Synthesis, Molecular Docking and β-Glucuronidase Inhibitory Potential of Indole Base Oxadiazole Derivatives.
SAR
indole
molecular docking
oxadiazole
synthesis
β-glucuronidase
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
08 Mar 2019
08 Mar 2019
Historique:
received:
14
02
2019
revised:
01
03
2019
accepted:
03
03
2019
entrez:
13
3
2019
pubmed:
13
3
2019
medline:
21
6
2019
Statut:
epublish
Résumé
β-glucuronidase is a lysosomal glycosidase enzyme which catalyzes the extracellular matrix of cancer and normal cells and the glycosaminoglycans of the cell membrane, which is important for cancer cell proliferation, invasion, and metastasis. Liver cancer, colon carcinoma, and neoplasm bladder are triggered by the increase of the level of β-glucuronidase activity. The most valuable structures are indole and oxadiazole which has gain immense attention because of its pharmacological behavior and display many biological properties. Twenty-two (
Identifiants
pubmed: 30857263
pii: molecules24050963
doi: 10.3390/molecules24050963
pmc: PMC6429331
pii:
doi:
Substances chimiques
Enzyme Inhibitors
0
Indoles
0
Oxadiazoles
0
Glucuronidase
EC 3.2.1.31
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Deanship of Scientific Research at Prince Sattam Bin Abdulaziz University
ID : 2017/01/7199
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
Références
Arch Pharm Res. 2001 Dec;24(6):564-7
pubmed: 11794536
J Pharmacol Exp Ther. 2002 Apr;301(1):223-8
pubmed: 11907177
Chem Rev. 2005 Jul;105(7):2873-920
pubmed: 16011327
Dis Markers. 2008;25(4-5):233-42
pubmed: 19126967
J Comput Chem. 2009 Dec;30(16):2785-91
pubmed: 19399780
Clin Cancer Res. 2009 Jul 15;15(14):4600-11
pubmed: 19584154
J Med Chem. 1991 Jan;34(1):140-51
pubmed: 1992112
Biochem Soc Trans. 2011 Jan;39(1):406-9
pubmed: 21265813
Bioorg Med Chem. 2011 Jul 15;19(14):4286-94
pubmed: 21684753
Bioorg Med Chem Lett. 2012 Jan 15;22(2):969-72
pubmed: 22197387
J Am Chem Soc. 2012 Feb 15;134(6):3103-10
pubmed: 22239495
Bioorg Med Chem Lett. 2013 Feb 1;23(3):864-8
pubmed: 23265873
Eur J Med Chem. 2013 Feb;60:23-8
pubmed: 23279864
Eur J Med Chem. 2013 Apr;62:84-8
pubmed: 23353735
Eur J Med Chem. 2013 Jul;65:276-83
pubmed: 23727537
Rejuvenation Res. 2013 Oct;16(5):352-63
pubmed: 23777470
Eur J Med Chem. 2013 Sep;67:54-9
pubmed: 23835482
PLoS One. 2013 Nov 19;8(11):e79687
pubmed: 24260279
Molecules. 2014 Jun 25;19(7):8788-802
pubmed: 24968334
BMC Med. 2014 Sep 18;12:159
pubmed: 25286285
Bioorg Med Chem. 2015 Jul 1;23(13):3119-25
pubmed: 26001340
Bioorg Chem. 2015 Aug;61:36-44
pubmed: 26073618
Curr Med Chem. 2015;22(38):4412-33
pubmed: 26438249
Bioorg Med Chem. 2015 Dec 1;23(23):7394-404
pubmed: 26526743
Eur J Med Chem. 2016 Jan 27;108:415-422
pubmed: 26706352
Bioorg Chem. 2016 Apr;65:48-56
pubmed: 26855413
Biochemistry. 2016 May 31;55(21):3020-35
pubmed: 27110637
Bioorg Med Chem. 2016 Aug 15;24(16):3696-704
pubmed: 27312423
Bioorg Chem. 2016 Oct;68:15-22
pubmed: 27414468
Bioorg Chem. 2016 Oct;68:56-63
pubmed: 27454618
Eur J Med Chem. 2017 Aug 18;136:184-194
pubmed: 28494255
Bioorg Chem. 2017 Jun;72:323-332
pubmed: 28505547
Nat Chem Biol. 2017 Aug;13(8):867-873
pubmed: 28581485
Eur J Med Chem. 2018 Apr 25;150:9-29
pubmed: 29505935
J Enzyme Inhib Med Chem. 2018 Dec;33(1):686-700
pubmed: 29560733
Scand J Rheumatol. 1993;22(2):83-5
pubmed: 8480143
Nat Struct Biol. 1996 Apr;3(4):375-81
pubmed: 8599764