Current Enzyme Inhibition最新文献

{"title":"The Inhibition of Glutathione S-Transferases and Butyrylcholinesterase by Antidepressants: A Mini-Review on Enzyme-Drug Interaction","authors":"Victor Markus, Özlem Dalmızrak, K. Teralı, N. Özer","doi":"10.2174/1573408018666220428100417","DOIUrl":"https://doi.org/10.2174/1573408018666220428100417","url":null,"abstract":"\u0000\u0000Compromises in the cellular enzymatic defense barrier can increase the duration of exposure to electrophiles and the severity of toxicity they may incur.\u0000\u0000\u0000\u0000In this mini-review, we discuss the inhibition of the enzymatic defense systems by different antidepressants commonly prescribed worldwide as well as herbal products used for various forms of depression.\u0000\u0000\u0000\u0000Our work is primarily focused on the interactions of two prominent biotransformation enzyme systems, namely glutathione S-transferases and cholinesterases, with tricyclic antidepressants (TCAs), selective serotonin reuptake inhibitors (SSRIs), and hypericin.\u0000\u0000\u0000\u0000The outcomes of available published studies and their implications in health and disease are discussed here in depth.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43689952","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"GC-MS Identification of Cholinesterase inhibitory and Antioxidant molecules from leaves of Cnidoscolus aconitifolius (Miller) I.M. Johnston (Euphorbiaceae).","authors":"Onoja O.J., Ugwueze N.J.","doi":"10.2174/1573408018666220324105559","DOIUrl":"https://doi.org/10.2174/1573408018666220324105559","url":null,"abstract":"\u0000\u0000Alzheimer’s disease (AD) is a progressive and fatal neurodegenerative disease, clinically characterized by memory and cognitive dysfunction. AD affects about 35 million people worldwide today and is estimated to nearly double every 20 years. Cnidoscolus aconitifolius (Miller) I.M. Johnston has been reported in Nigerian ethnomedicine as a memory enhancer. There is a lack of scientific evidence to justify the claims. Moreover, there are no effective neurotherapeutic agents available for the treatment of AD, hence the need arises for the search of new and more effective agents.\u0000\u0000\u0000\u0000This study aims to evaluate and identify potential molecules with anti-Alzheimer’s and antioxidant potentials from Cnidoscolus aconitifolius leaves.\u0000\u0000\u0000\u0000The air-dried leaves of Cnidoscolus aconitifolius (Miller) I.M. Johnston (PCG/UNN/0267) were extracted using the successive extraction procedure based on increasing the polarity of the eluent in the ascending order of: n-hexane, ethyl acetate and methanol. Phytochemical screening was carried out on the extracts using standard procedures. Acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitory activities were done according to Ellman’s method. Eserine was used as standard. Antioxidant potentials were evaluated using standard in vitro chemical analyses. A GC-MS (QP2010SE, SHIDMAZU JAPAN) analysis was done to identify bioactive compounds from most active fraction. Statistical analyses were performed using One-way ANOVA followed by Dunnett’s Multiple Comparison test at α0.05.\u0000\u0000\u0000\u0000Phytochemical analysis revealed the presence of tannins, resins, saponins, flavonoids, phenols, carbohydrates, alkaloids, and terpenoids. Ethyl acetate fraction demonstrated the highest acetylcholinesterase and butyrylcholinesterase inhibitory activity at 1 mg/mL with IC50 values of 0.288±0.00 mg/mL (82.9% inhibition) and 0.440±0.02 mg/mL ((75.4% inhibition), respectively compared to eserine (IC50=0.050±0.01 mg/mL) for AChE and (IC50=0.049±0.00 mg/mL) for BuChE. Metal (ferrous ion) chelating activity was also high in the ethyl acetate fraction with IC50 value of 0.160±0.00 mg/mL compared to EDTA (IC50 = 0.085±0.00 mg/mL) at 1 mg/mL. Hydroxyl radical scavenging activity was higher in the ethyl acetate fraction (IC50 = 0.352±0.01 mg/mL) when compared to BHT (IC50 = 0.074±0.00 mg/mL) at 1 mg/mL. The pro-anthocyanidin content was also higher in ethyl acetate (6.94±0.16 mg cyanidin/g of sample) compared to other fractions. GC-MS analysis of the most active fraction (ethyl acetate) revealed a total of 56 compounds.The major compounds revealed were: n-Hexadecanoic acid (Area % of 13.45%; Retention time of 14.863), Phytol (Area % of 5.13%; Retention time of 15.864), Octadecanoic acid (Area % of 4.86%; Retention time of 16.211), 9, 12, 15-Octadecatrienoic acid (Z,Z,Z) (Area % of 26.85%; Retention time of 16.09), Squalene (% Area of 2.65%; Retention time of 20.94) and alpha-Tocopheryl acetate (% Area of 1.71%; Retention time of 23.40).\u0000\u0000\u0000\u0000C. ac","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48671663","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Contribution to Pharmacological Valorisation of Algerian Arctium Minus (Hill) Bernh. Subsp. Atlanticum (Pomel) Maire; Antioxidant and Acetylcholinesterase Inhibitory Activities.","authors":"Sofiane Guettaf, Abdelmoumen Benmerzoug, Bensouici Chawki, Y. Cakmak, S. Dahamna, A. Baghiani, D. Harzallah","doi":"10.2174/1573408018666220324101521","DOIUrl":"https://doi.org/10.2174/1573408018666220324101521","url":null,"abstract":"\u0000\u0000The traditional pharmacopoeia is full of potential resources for molecules with therapeutic effects involving the inhibition of enzymes linked to some diseases.\u0000\u0000\u0000\u0000This work aimed to test invitro the neuroprotective activity against Alzheimer's disease (AD) combined with the antioxidant effect of root extracts obtained by water, water / methanol and ethyl acetate of the endemic Arctium minus. subsp. atlanticum. native of Algeria.\u0000\u0000\u0000\u0000The different extracts of the root of the studied plant were obtained by decoction or maceration. The inhibitory effect of acetyl / butyryl cholinesterase (AChE/BChE) was achieved by a colorimetric method. Similarly, the antioxidant activity was measured, based on several mechanisms: 1, 1-diphenyl-2-picryl-hydrazyl (DPPH) and galvinoxyl (GOR) radicals free scavenging assays, β-carotene bleaching inhibition activity, and cupric ion reducing antioxidant capacity (CUPRAC).\u0000\u0000\u0000\u0000In the various tests carried out, the ethyl acetate extract (EAE) possessed the most powerful antioxidant and anticholinesterase activities in comparison with the other samples. The IC50 and A0.5 values of DPPH, GOR, β-carotene, CUPRAC, anti-AChE and anti BChE assays were 69.45±5.49, 28.87±0.18, 121.58±16.76, 37.41±1.59, 265±21 and 240±6.3 µg / mL, respectively. Likewise, a correlation can be deduced between the type of extract and the potent antioxidant / anticholinesterase potential.\u0000\u0000\u0000\u0000This work evokes for the first time the anticholinesterase potential combined with the antioxidant effect of Algerian Arctium minus. subsp. atlanticum. This association between the two effects could be effective in the fight against AD and therefore, the use of this natural resource may be possible in combating this aspect of neurodegeneration.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42217301","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alpha-glucosidase and alpha-amylase inhibition activity of avocado fruit of Nepalese origin","authors":"K. Dhakal, D. Shrestha, Tamlal Pokhrel, D. P. Bhandari, A. Adhikari","doi":"10.2174/1573408018666220324110300","DOIUrl":"https://doi.org/10.2174/1573408018666220324110300","url":null,"abstract":"\u0000\u0000Diabetes has become a major health problem due to its high prevalence, morbidity, and mortality rate. Reducing postprandial hyperglycemia has become the main target in the treatment of diabetes mellitus. So, developing new drugs with fewer side effects has been a major priority.\u0000\u0000\u0000\u0000The main objective of this study is to investigate total phenolic and flavonoid content, antioxidant activity, α-glucosidase, and α-amylase inhibition activity of Persea Americana Mill (avocado) pulp and seed.\u0000\u0000\u0000\u0000The α-glucosidase and α-amylase inhibition activity were performed using substrates PNPG and CNPG3, respectively. DPPH free radical scavenging assay was used to perform the antioxidant activity. The total phenolic content was estimated using folin-ciocalu’s reagent. Likewise, aluminium trichloride method was applied to find out the total flavonoid content.\u0000\u0000\u0000\u0000The crude methanolic extract of avocado seed revealed potent α-glucosidase inhibition activity with an IC50 1.959±0.93µg/mL followed by the avocado pulp 308±2.36µg/mL. Similarly, the IC50 for the α-amylase inhibition activity of avocado seed was found to be 120.3±1.382µg/mL. In addition, the avocado pulp and seed revealed a significant antioxidant activity with IC50 value 75.01±0.72µg/mL, and 6.445±0.62µg/mL, respectively compared to the standard quercetin 1.525±0.5µg/mL. The total phenolic content of avocado pulp and the seed was reported 7.031±2.87 mg of GAE/g, and 142.96±1.589 mg of GAE/g, respectively. Similarly, the total flavonoid content of avocado pulp and the seed was found to be 6.313±1.301 mg of QE/g and 48.696±0.110 mg/GAE/g, respectively.\u0000\u0000\u0000\u0000The avocado seed of Nepali origin was found to inhibit the digestive enzyme significantly. These findings indicate that avocado fruit of Nepali origin has the potential to develop as an alternative food therapy for diabetic patients. Further research is required to find out the inhibitor compounds.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41271186","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antioxidant and tyrosinase inhibitory activities of A. sicula L. aqueous extract","authors":"K. Loucif, Fatima Benchikh, Hassiba Benabdallah, C. Bensouici, Smain Amira","doi":"10.2174/1573408018666220322163312","DOIUrl":"https://doi.org/10.2174/1573408018666220322163312","url":null,"abstract":"\u0000\u0000Overexpression of tyrosinase in humans causes an increase in melanin production in the skin, which can result in hyperpigmentation consequences such as freckles, melasma, age spots, and melanoma. Free radicals also play a significant role in the increase of the biosynthesis of melanin.\u0000\u0000\u0000\u0000Tyrosinase inhibitors capable of inhibiting the biosynthesis of melanin are used currently in various hyperpigmentation and cosmetic agents to control the formation of freckles. Several synthetic tyrosinase inhibitors have been associated with several serious side effects. Also, synthetic antioxidants had many toxicological side effects including carcinogenicity. There is an increasing interest in the search for natural tyrosinase inhibitors and antioxidant agents.\u0000\u0000\u0000\u0000The objective of this study is to evaluate total polyphenol and flavonoid contents as well as examine the antioxidative and tyrosinase inhibitory effects of A. sicula L. aqueous extract.\u0000\u0000\u0000\u0000Antioxidant activities evaluated using superoxide radical scavenging and reducing power methods. tyrosinase inhibitory assay was used to determine anti-hyperpigmentation.\u0000\u0000\u0000\u0000The results showed that this extract was rich in total polyphenols (58.01±1.18 micrograms of gallic acid equivalents per milligrams of extract) and flavonoids (17.91±1.81 micrograms quercetin equivalents per milligram of extract). A. sicula L. aqueous extract was capable of scavenging free radicals (IC50 =11.87±0.13 μg/mL) and acts as a strong reducing agent (A 0.5= 6.37±0.42µg/mL). A. sicula L. had a potent tyrosinase inhibitory potential (IC50= 12.63±1.15 μg/mL), which was higher compared to kojic acid as standard (IC50= 25,23±0,78 μg/mL, P <0.001). These results support that A. sicula L. could be a new source of antioxidant and cosmetic use. Further studies focusing on the isolation and characterization of active principles of antioxidant and tyrosinase inhibitory activities are needed.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48097819","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A review on recent PARP inhibitor advancements in cancer therapy.","authors":"Pulla Prudvi Raj, Kaviarasan L, Gowramma B, Kalirajan R, Praveen T.K, Divya jyothi Palati","doi":"10.2174/1573408018666220321115033","DOIUrl":"https://doi.org/10.2174/1573408018666220321115033","url":null,"abstract":"\u0000\u0000Poly [ADP-ribose] polymerase-1 [PARP-1] is a chromatin-bound nuclear enzyme that gets activated by DNA damage, it facilitates DNA repair by binding to DNA breaks and attracting DNA repair proteins to the site of damage. Increased PARP-1 expression is observed in melanomas, breast cancer, lung cancer, and other neoplastic diseases. PARP-1 interacts directly, indirectly with various oncogenic proteins and regulates several transcription factors thereby modulating carcinogenesis. There is a lot of pre-clinical and clinical data supporting the use of PARP-1 inhibitors [PARP-1i] in cancers that express homologous recombination deficiencies like mutations within BRCA-1/2 genes. Therapeutic inhibition of PARP-1 is therefore perceived as a promising anticancer strategy and numerous PARP-1i are currently under development and clinical evaluation. Currently, there are 4 FDA-approved PARP-1i in the market, while few are in the last stage of clinical development. All the molecules are non-selective PARP-1i. While giving promising results, PARP-1i have their own disadvantages, like safety problems, resistance, etc. Looking at the success rate of PARP-1i in various solid tumours, there is an urge for novel and selective PARP-1i. In this review, we discuss various aspects related to PARP-1i like recent developments, overcoming the resistance, and selectivity criteria of new molecules for potential PARP-1i.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"41550419","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"In Vitro Investigation of Potential Pepsin Inhibitors: New Perspectives for the Treatment of Gastroesophageal Reflux","authors":"L. Leoni, V. Damiani, R. Salvio","doi":"10.2174/1573408018666220307121130","DOIUrl":"https://doi.org/10.2174/1573408018666220307121130","url":null,"abstract":"\u0000\u0000In patients with Gastroesophageal Reflux (GER), the digestive enzyme pepsin can reach the esophagus and extraesophageal sites and cause damages with the appearance of inflammation and other tedious symptoms.\u0000\u0000\u0000\u0000In this work, a number of biocompatible, non-toxic and hypoallergenic compounds were tested in vitro as inhibitors of pepsin. The residual enzyme activity in the presence of the investigated compounds was measured through a convenient and reliable UV-vis method based on the cleavage of hemoglobin. This method is applicable even if the investigated additives are scarcely soluble in water and the test mixtures are dispersions rather than solutions.\u0000\u0000\u0000\u0000A few negatively charged saccharides showed the highest effect among the investigated compounds. The inhibitory activity of pepstatin and lovastatin was also tested with the same method in a wide range of concentrations. These compounds turned out to be effective even if present in extremely low amount. A docking and molecular dynamic investigation provides useful insights about the binding site and the mechanism of action of pepstatin as inactivating agent towards pepsin.\u0000\u0000\u0000\u0000In particular, the computational study indicates that the binding with this compound significantly increases the mobility of the active site residues and prevent them from cooperate in the reactive event.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42214836","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Meet the Regional Editor","authors":"G. Costa","doi":"10.2174/157340801801220425094500","DOIUrl":"https://doi.org/10.2174/157340801801220425094500","url":null,"abstract":"<jats:sec>\u0000<jats:title />\u0000<jats:p />\u0000</jats:sec>","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"47413600","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, Synthesis, Molecular Docking and in vitro Biological Evaluation of some Benzamide Derivatives as novel Glucokinase Activators","authors":"A. A. Kazi, V. Chatpalliwar","doi":"10.2174/1573408018666220218093451","DOIUrl":"https://doi.org/10.2174/1573408018666220218093451","url":null,"abstract":"\u0000\u0000Glucokinase (GK) is a cytoplasmic enzyme that metabolises glucose to glucose-6-phosphate and supports adjusting blood glucose levels within the normal range in humans. In pancreatic β-cells, it plays a leading role in governing the glucose-stimulated secretion of insulin, and in liver hepatocyte cells, it controls the metabolism of carbohydrates. GK acts as a promising drug target for treating patients with type 2 diabetes mellitus (T2DM).\u0000\u0000\u0000\u0000The present work has been designed to discover some novel substituted benzamide derivatives\u0000\u0000\u0000\u0000This work involved designing novel benzamide derivatives and their screening by docking studies to determine the binding interactions for the best-fit conformations in the binding site of the GK enzyme. Based on the results of docking studies, the selected molecules were synthesized and tested for in vitro GK enzyme assay. The structures of newly synthesized products were confirmed by IR, NMR, and mass spectroscopy.\u0000\u0000\u0000\u0000Amongst the designed derivatives, compounds 4c, 4d, 4e, 5h, 5j, 5l, 5m, 5n, 5p, and 5r have shown better binding energy than the native ligand present in the enzyme structure. The synthesized compounds were subjected to in vitro GK enzyme assay. Out of all, compounds 4c, 4d, 5h, 5l, and 5n showed more GK activation than control.\u0000\u0000\u0000\u0000From the present results, we have concluded that the synthesized derivatives can activate the human GK enzyme effectively, which can be helpful in the treatment of T2DM.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46449189","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification and validation of Hydroxychavicol from Betel leaf as a promising Breast cancer inhibitor - An in vitro and in silico analysis","authors":"Sangavi P, Langeswaran K, Sangeetha R","doi":"10.2174/1573408018666220210141311","DOIUrl":"https://doi.org/10.2174/1573408018666220210141311","url":null,"abstract":"\u0000\u0000Identification of promising Breast cancer inhibitors through in vitro and in silico studies.\u0000\u0000\u0000\u0000Piper betel. L. is a traditional herbal, used for varied ailments.\u0000\u0000\u0000\u0000The present investigationis designed to evaluate the anti-carcinogenic potency of HC against MCF-7 cell line using in vitroanalysis. Furtherin silicoexamination to detect and formulate protein-ligand complex of HC using Molecular Docking technique.\u0000\u0000\u0000\u0000In vitro study was conducted, using MTT assay and microscopic examinations to determine the cell viability and morphological demolitions on MCF-7 cells. In silico,scrutinizes were performed, using virtual screening, docking, ADME, DFT analysis, MMGBSA, and Molecular dynamic simulation to appraise hydroxychavicol stability.\u0000\u0000\u0000\u0000HC showed an outstanding anticancer potential, with dose and time dependant patterns in MTT assay and through the fluctuating organization of MCF-7 cells. Insilico analysis, results showed that the selected lead compound-complex exhibited good stability and a highly potent inhibitor to the target breast cancer protein.\u0000\u0000\u0000\u0000This study is evident to consider HC as an alternate potential inhibitor.\u0000","PeriodicalId":35405,"journal":{"name":"Current Enzyme Inhibition","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-02-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45058239","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}