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Article ; Online: Interactions of the Anti-SARS-CoV-2 Agents Molnupiravir and Nirmatrelvir/Paxlovid with Human Drug Transporters.

Bakos, Éva / Temesszentandrási-Ambrus, Csilla / Özvegy-Laczka, Csilla / Gáborik, Zsuzsanna / Sarkadi, Balázs / Telbisz, Ágnes

International journal of molecular sciences

2023 Volume 24, Issue 14

Abstract: Orally administered small molecules may have important therapeutic potential in treating COVID-19 disease. The recently developed antiviral agents, Molnupiravir and Nirmatrelvir, have been reported to be efficient treatments, with only moderate side ... ...

Abstract	Orally administered small molecules may have important therapeutic potential in treating COVID-19 disease. The recently developed antiviral agents, Molnupiravir and Nirmatrelvir, have been reported to be efficient treatments, with only moderate side effects, especially when applied in the early phases of this disease. However, drug-drug and drug-transporter interactions have already been noted by the drug development companies and in the application notes. In the present work, we have studied some of the key human transporters interacting with these agents. The nucleoside analog Molnupiravir (EIDD-2801) and its main metabolite (EIDD-1931) were found to inhibit CNT1,2 in addition to the ENT1,2 nucleoside transporters; however, it did not significantly influence the relevant OATP transporters or the ABCC4 nucleoside efflux transporter. The active component of Paxlovid (PF-07321332, Nirmatrelvir) inhibited the function of several OATPs and of ABCB1 but did not affect ABCG2. However, significant inhibition was observed only at high concentrations of Nirmatrelvir and probably did not occur in vivo. Paxlovid, as used in the clinic, is a combination of Nirmatrelvir (viral protease inhibitor) and Ritonavir (a "booster" inhibitor of Nirmatrelvir metabolism). Ritonavir is known to inhibit several drug transporters; therefore, we have examined these compounds together, in relevant concentrations and ratios. No additional inhibitory effect of Nirmatrelvir was observed compared to the strong transporter inhibition caused by Ritonavir. Our current in vitro results should help to estimate the potential drug-drug interactions of these newly developed agents during COVID-19 treatment.
MeSH term(s)	Humans ; Ritonavir/pharmacology ; SARS-CoV-2 ; COVID-19 ; Nucleosides ; COVID-19 Drug Treatment ; Membrane Transport Proteins ; Antiviral Agents/pharmacology
Chemical Substances	nirmatrelvir and ritonavir drug combination ; Ritonavir (O3J8G9O825) ; molnupiravir (YA84KI1VEW) ; Nucleosides ; Membrane Transport Proteins ; Antiviral Agents
Language	English
Publishing date	2023-07-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms241411237
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Article ; Online: Interaction of crown ethers with the ABCG2 transporter and their implication for multidrug resistance reversal.

Mioč, Marija / Telbisz, Ágnes / Radman, Katarina / Bertoša, Branimir / Šumanovac, Tatjana / Sarkadi, Balázs / Kralj, Marijeta

Histochemistry and cell biology

2022 Volume 158, Issue 3, Page(s) 261–277

Abstract: Overexpression of ABC transporters, such as ABCB1 and ABCG2, plays an important role in mediating multidrug resistance (MDR) in cancer. This feature is also attributed to a subpopulation of cancer stem cells (CSCs), having enhanced tumourigenic potential. ...

Abstract	Overexpression of ABC transporters, such as ABCB1 and ABCG2, plays an important role in mediating multidrug resistance (MDR) in cancer. This feature is also attributed to a subpopulation of cancer stem cells (CSCs), having enhanced tumourigenic potential. ABCG2 is specifically associated with the CSC phenotype, making it a valuable target for eliminating aggressive and resistant cells. Several natural and synthetic ionophores have been discovered as CSC-selective drugs that may also have MDR-reversing ability, whereas their interaction with ABCG2 has not yet been explored. We previously reported the biological activities, including ABCB1 inhibition, of a group of adamantane-substituted diaza-18-crown-6 (DAC) compounds that possess ionophore capabilities. In this study, we investigated the mechanism of ABCG2-inhibitory activity of DAC compounds and the natural ionophores salinomycin, monensin and nigericin. We used a series of functional assays, including real-time microscopic analysis of ABCG2-mediated fluorescent substrate transport in cells, and docking studies to provide comparative aspects for the transporter-compound interactions and their role in restoring chemosensitivity. We found that natural ionophores did not inhibit ABCG2, suggesting that their CSC selectivity is likely mediated by other mechanisms. In contrast, DACs with amide linkage in the side arms demonstrated noteworthy ABCG2-inhibitory activity, with DAC-3Amide proving to be the most potent. This compound induced conformational changes of the transporter and likely binds to both Cavity 1 and the NBD-TMD interface. DAC-3Amide reversed ABCG2-mediated MDR in model cells, without affecting ABCG2 expression or localization. These results pave the way for the development of new crown ether compounds with improved ABCG2-inhibitory properties.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily G, Member 2/metabolism ; Antineoplastic Agents/pharmacology ; Cell Line, Tumor ; Crown Ethers/pharmacology ; Drug Resistance, Multiple ; Drug Resistance, Neoplasm ; Ionophores/pharmacology
Chemical Substances	ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Antineoplastic Agents ; Crown Ethers ; Ionophores
Language	English
Publishing date	2022-06-01
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1222930-1
ISSN	1432-119X ; 0301-5564 ; 0948-6143
ISSN (online)	1432-119X
ISSN	0301-5564 ; 0948-6143
DOI	10.1007/s00418-022-02106-z
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Article ; Online: Recent advances in the exploration of the bile salt export pump (BSEP/ABCB11) function.

Telbisz, Ágnes / Homolya, László

Expert opinion on therapeutic targets

2016 Volume 20, Issue 4, Page(s) 501–514

Abstract: Introduction: The bile salt export pump (BSEP/ABCB11), residing in the apical membrane of hepatocyte, mediates the secretion of bile salts into the bile. A range of human diseases is associated with the malfunction of BSEP, including fatal hereditary ... ...

Abstract	Introduction: The bile salt export pump (BSEP/ABCB11), residing in the apical membrane of hepatocyte, mediates the secretion of bile salts into the bile. A range of human diseases is associated with the malfunction of BSEP, including fatal hereditary liver disorders and mild cholestatic conditions. Manifestation of these diseases primarily depends on the mutation type; however, other factors such as hormonal changes and drug interactions can also trigger or influence the related diseases. Areas covered: Here, we summarize the recent knowledge on BSEP by covering its transport properties, cellular localization, regulation and major mutations/polymorphisms, as well as the hereditary and acquired diseases associated with BSEP dysfunction. We discuss the different model expression systems employed to understand the function of the BSEP variants, their drug interactions and the contemporary therapeutic interventions. Expert opinion: The limitations of the available model expression systems for BSEP result in controversial conclusions, and obstruct our deeper insight into BSEP deficiencies and BSEP-related drug interactions. The knowledge originating from different methodologies, such as clinical studies, molecular genetics, as well as in vitro and in silico modeling, should be integrated and harmonized. Increasing availability of robust molecular biological tools and our better understanding of the mechanism of BSEP deficiencies should make the personalized, mutation-based therapeutic interventions more attainable.
MeSH term(s)	ATP Binding Cassette Subfamily B Member 11 ; ATP-Binding Cassette Transporters/genetics ; ATP-Binding Cassette Transporters/metabolism ; Animals ; Bile Acids and Salts/metabolism ; Cholestasis/genetics ; Cholestasis/physiopathology ; Computer Simulation ; Hepatocytes/metabolism ; Humans ; Liver Diseases/genetics ; Liver Diseases/physiopathology ; Molecular Biology ; Mutation ; Polymorphism, Genetic
Chemical Substances	ABCB11 protein, human ; ATP Binding Cassette Subfamily B Member 11 ; Bile Acids and Salts
Language	English
Publishing date	2016
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2055208-7
ISSN	1744-7631 ; 1472-8222
ISSN (online)	1744-7631
ISSN	1472-8222
DOI	10.1517/14728222.2016.1102889
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Article ; Online: Interactions of anti-COVID-19 drug candidates with hepatic transporters may cause liver toxicity and affect pharmacokinetics.

Ambrus, Csilla / Bakos, Éva / Sarkadi, Balázs / Özvegy-Laczka, Csilla / Telbisz, Ágnes

Scientific reports

2021 Volume 11, Issue 1, Page(s) 17810

Abstract: Transporters in the human liver play a major role in the clearance of endo- and xenobiotics. Apical (canalicular) transporters extrude compounds to the bile, while basolateral hepatocyte transporters promote the uptake of, or expel, various compounds ... ...

Abstract	Transporters in the human liver play a major role in the clearance of endo- and xenobiotics. Apical (canalicular) transporters extrude compounds to the bile, while basolateral hepatocyte transporters promote the uptake of, or expel, various compounds from/into the venous blood stream. In the present work we have examined the in vitro interactions of some key repurposed drugs advocated to treat COVID-19 (lopinavir, ritonavir, ivermectin, remdesivir and favipiravir), with the key drug transporters of hepatocytes. These transporters included ABCB11/BSEP, ABCC2/MRP2, and SLC47A1/MATE1 in the canalicular membrane, as well as ABCC3/MRP3, ABCC4/MRP4, SLC22A1/OCT1, SLCO1B1/OATP1B1, SLCO1B3/OATP1B3, and SLC10A1/NTCP, residing in the basolateral membrane. Lopinavir and ritonavir in low micromolar concentrations inhibited BSEP and MATE1 exporters, as well as OATP1B1/1B3 uptake transporters. Ritonavir had a similar inhibitory pattern, also inhibiting OCT1. Remdesivir strongly inhibited MRP4, OATP1B1/1B3, MATE1 and OCT1. Favipiravir had no significant effect on any of these transporters. Since both general drug metabolism and drug-induced liver toxicity are strongly dependent on the functioning of these transporters, the various interactions reported here may have important clinical relevance in the drug treatment of this viral disease and the existing co-morbidities.
Language	English
Publishing date	2021-09-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-97160-3
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Article ; Online: Interactions of anti-COVID-19 drug candidates with hepatic transporters may cause liver toxicity and affect pharmacokinetics

Csilla Ambrus / Éva Bakos / Balázs Sarkadi / Csilla Özvegy-Laczka / Ágnes Telbisz

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 10

Abstract: Abstract Transporters in the human liver play a major role in the clearance of endo- and xenobiotics. Apical (canalicular) transporters extrude compounds to the bile, while basolateral hepatocyte transporters promote the uptake of, or expel, various ... ...

Abstract	Abstract Transporters in the human liver play a major role in the clearance of endo- and xenobiotics. Apical (canalicular) transporters extrude compounds to the bile, while basolateral hepatocyte transporters promote the uptake of, or expel, various compounds from/into the venous blood stream. In the present work we have examined the in vitro interactions of some key repurposed drugs advocated to treat COVID-19 (lopinavir, ritonavir, ivermectin, remdesivir and favipiravir), with the key drug transporters of hepatocytes. These transporters included ABCB11/BSEP, ABCC2/MRP2, and SLC47A1/MATE1 in the canalicular membrane, as well as ABCC3/MRP3, ABCC4/MRP4, SLC22A1/OCT1, SLCO1B1/OATP1B1, SLCO1B3/OATP1B3, and SLC10A1/NTCP, residing in the basolateral membrane. Lopinavir and ritonavir in low micromolar concentrations inhibited BSEP and MATE1 exporters, as well as OATP1B1/1B3 uptake transporters. Ritonavir had a similar inhibitory pattern, also inhibiting OCT1. Remdesivir strongly inhibited MRP4, OATP1B1/1B3, MATE1 and OCT1. Favipiravir had no significant effect on any of these transporters. Since both general drug metabolism and drug-induced liver toxicity are strongly dependent on the functioning of these transporters, the various interactions reported here may have important clinical relevance in the drug treatment of this viral disease and the existing co-morbidities.
Keywords	Medicine ; R ; Science ; Q
Subject code	500
Language	English
Publishing date	2021-09-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article: Expression, Function and Trafficking of the Human ABCG2 Multidrug Transporter Containing Mutations in an Unstructured Cytoplasmic Loop.

Mózner, Orsolya / Zámbó, Boglárka / Bartos, Zsuzsa / Gergely, Anna / Szabó, Kata Sára / Jezsó, Bálint / Telbisz, Ágnes / Várady, György / Homolya, László / Hegedűs, Tamás / Sarkadi, Balázs

Membranes

2023 Volume 13, Issue 10

Abstract: The human ABCG2 multidrug transporter plays a crucial role in the absorption and excretion of xeno- and endobiotics, contributes to cancer drug resistance and the development of gout. In this work, we have analyzed the effects of selected variants, ... ...

Abstract	The human ABCG2 multidrug transporter plays a crucial role in the absorption and excretion of xeno- and endobiotics, contributes to cancer drug resistance and the development of gout. In this work, we have analyzed the effects of selected variants, residing in a structurally unresolved cytoplasmic region (a.a. 354-367) of ABCG2 on the function and trafficking of this protein. A cluster of four lysines (K357-360) and the phosphorylation of a threonine (T362) residue in this region have been previously suggested to significantly affect the cellular fate of ABCG2. Here, we report that the naturally occurring K360del variant in human cells increased ABCG2 plasma membrane expression and accelerated cellular trafficking. The variable alanine replacements of the neighboring lysines had no significant effect on transport function, and the apical localization of ABCG2 in polarized cells has not been altered by any of these mutations. Moreover, in contrast to previous reports, we found that the phosphorylation-incompetent T362A, or the phosphorylation-mimicking T362E variants in this loop had no measurable effects on the function or expression of ABCG2. Molecular dynamics simulations indicated an increased mobility of the mutant variants with no major effects on the core structure of the protein. These results may help to decipher the potential role of this unstructured region within this transporter.
Language	English
Publishing date	2023-10-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2614641-1
ISSN	2077-0375
ISSN	2077-0375
DOI	10.3390/membranes13100822
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Article ; Online: The transport pathway in the ABCG2 protein and its regulation revealed by molecular dynamics simulations.

Nagy, Tamás / Tóth, Ágota / Telbisz, Ágnes / Sarkadi, Balázs / Tordai, Hedvig / Tordai, Attila / Hegedűs, Tamás

Cellular and molecular life sciences : CMLS

2020 Volume 78, Issue 5, Page(s) 2329–2339

Abstract: Atomic-level structural insight on the human ABCG2 membrane protein, a pharmacologically important transporter, has been recently revealed by several key papers. In spite of the wealth of structural data, the pathway of transmembrane movement for the ... ...

Abstract	Atomic-level structural insight on the human ABCG2 membrane protein, a pharmacologically important transporter, has been recently revealed by several key papers. In spite of the wealth of structural data, the pathway of transmembrane movement for the large variety of structurally different ABCG2 substrates and the physiological lipid regulation of the transporter has not been elucidated. The complex molecular dynamics simulations presented here may provide a breakthrough in understanding the steps of the substrate transport process and its regulation by cholesterol. Our analysis revealed drug binding cavities other than the central binding site and delineated a putative dynamic transport pathway for substrates with variable structures. We found that membrane cholesterol accelerated drug transport by promoting the closure of cytoplasmic protein regions. Since ABCG2 is present in all major biological barriers and drug-metabolizing organs, influences the pharmacokinetics of numerous clinically applied drugs, and plays a key role in uric acid extrusion, this information may significantly promote a reliable prediction of clinically important substrate characteristics and drug-drug interactions.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily G, Member 2/chemistry ; ATP Binding Cassette Transporter, Subfamily G, Member 2/genetics ; ATP Binding Cassette Transporter, Subfamily G, Member 2/metabolism ; Binding Sites/genetics ; Biological Transport ; Cholesterol/chemistry ; Cholesterol/metabolism ; Humans ; Irinotecan/chemistry ; Irinotecan/metabolism ; Membrane Lipids/chemistry ; Membrane Lipids/metabolism ; Molecular Dynamics Simulation ; Mutation ; Neoplasm Proteins/chemistry ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Protein Binding ; Protein Domains
Chemical Substances	ABCG2 protein, human ; ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Membrane Lipids ; Neoplasm Proteins ; Irinotecan (7673326042) ; Cholesterol (97C5T2UQ7J)
Language	English
Publishing date	2020-09-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1358415-7
ISSN	1420-9071 ; 1420-682X
ISSN (online)	1420-9071
ISSN	1420-682X
DOI	10.1007/s00018-020-03651-3
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Article: Interactions of Potential Anti-COVID-19 Compounds with Multispecific ABC and OATP Drug Transporters.

Telbisz, Ágnes / Ambrus, Csilla / Mózner, Orsolya / Szabó, Edit / Várady, György / Bakos, Éva / Sarkadi, Balázs / Özvegy-Laczka, Csilla

Pharmaceutics

2021 Volume 13, Issue 1

Abstract: During the COVID-19 pandemic, several repurposed drugs have been proposed to alleviate the major health effects of the disease. These drugs are often applied with analgesics or non-steroid anti-inflammatory compounds, and co-morbid patients may also be ... ...

Abstract	During the COVID-19 pandemic, several repurposed drugs have been proposed to alleviate the major health effects of the disease. These drugs are often applied with analgesics or non-steroid anti-inflammatory compounds, and co-morbid patients may also be treated with anticancer, cholesterol-lowering, or antidiabetic agents. Since drug ADME-tox properties may be significantly affected by multispecific transporters, in this study, we examined the interactions of the repurposed drugs with the key human multidrug transporters present in the major tissue barriers and strongly affecting the pharmacokinetics. Our in vitro studies, using a variety of model systems, explored the interactions of the antimalarial agents chloroquine and hydroxychloroquine; the antihelmintic ivermectin; and the proposed antiviral compounds ritonavir, lopinavir, favipiravir, and remdesivir with the ABCB1/Pgp, ABCG2/BCRP, and ABCC1/MRP1 exporters, as well as the organic anion-transporting polypeptide (OATP)2B1 and OATP1A2 uptake transporters. The results presented here show numerous pharmacologically relevant transporter interactions and may provide a warning on the potential toxicities of these repurposed drugs, especially in drug combinations at the clinic.
Language	English
Publishing date	2021-01-09
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527217-2
ISSN	1999-4923
ISSN	1999-4923
DOI	10.3390/pharmaceutics13010081
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Article ; Online: Fluorescent probes for the dual investigation of MRP2 and OATP1B1 function and drug interactions.

Székely, Virág / Patik, Izabel / Ungvári, Orsolya / Telbisz, Ágnes / Szakács, Gergely / Bakos, Éva / Özvegy-Laczka, Csilla

European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences

2020 Volume 151, Page(s) 105395

Abstract: Detoxification in hepatocytes is a strictly controlled process, in which the governed action of membrane transporters involved in the uptake and efflux of potentially dangerous molecules has a crucial role. Major transporters of hepatic clearance belong ... ...

Abstract	Detoxification in hepatocytes is a strictly controlled process, in which the governed action of membrane transporters involved in the uptake and efflux of potentially dangerous molecules has a crucial role. Major transporters of hepatic clearance belong to the ABC (ATP Binding Cassette) and Solute Carrier (SLC) protein families. Organic anion-transporting polypeptide OATP1B1 (encoded by the SLCO1B1 gene) is exclusively expressed in the sinusoidal membrane of hepatocytes, where it mediates the cellular uptake of bile acids, bilirubin, and also that of various drugs. The removal of toxic molecules from hepatocytes to the bile is accomplished by several ABC transporters, including P-glycoprotein (ABCB1), MRP2 (ABCC2) and BCRP (ABCG2). Owing to their pharmacological relevance, monitoring drug interaction with OATP1B1/3 and ABC proteins is recommended. Our aim was to assess the interaction of recently identified fluorescent OATP substrates (various dyes used in cell viability assays, pyranine, Cascade Blue hydrazide (CB) and sulforhodamine 101 (SR101)) (Bakos et al., 2019; Patik et al., 2018) with MRP2 and ABCG2 in order to find fluorescent probes for the simultaneous characterization of both uptake and efflux processes. Transport by MRP2 and ABCG2 was investigated in inside-out membrane vesicles (IOVs) allowing a fast screen of the transport of membrane impermeable substrates by efflux transporters. Next, transcellular transport of shared OATP and ABC transporter substrate dyes was evaluated in MDCKII cells co-expressing OATP1B1 and MRP2 or ABCG2. Our results indicate that pyranine is a general substrate of OATP1B1, OATP1B3 and OATP2B1, and we find that the dye Live/Dead Violet and CB are good tools to investigate ABCG2 function in IOVs. Besides their suitability for MRP2 functional tests in the IOV setup, pyranine, CB and SR101 are the first dual probes that can be used to simultaneously measure OATP1B1 and MRP2 function in polarized cells by a fluorescent method.
MeSH term(s)	ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Drug Interactions ; Fluorescent Dyes ; Hepatocytes ; Neoplasm Proteins ; Organic Anion Transporters ; Solute Carrier Organic Anion Transporter Family Member 1B3
Chemical Substances	ATP Binding Cassette Transporter, Subfamily G, Member 2 ; Fluorescent Dyes ; Neoplasm Proteins ; Organic Anion Transporters ; Solute Carrier Organic Anion Transporter Family Member 1B3
Language	English
Publishing date	2020-05-29
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1154366-8
ISSN	1879-0720 ; 0928-0987
ISSN (online)	1879-0720
ISSN	0928-0987
DOI	10.1016/j.ejps.2020.105395
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Article ; Online: Antibacterial and Resistance Modifying Activities of

Mouwakeh, Ahmad / Telbisz, Ágnes / Spengler, Gabriella / Mohácsi-Farkas, Csilla / Kiskó, Gabriella

In vivo (Athens, Greece)

2018 Volume 32, Issue 4, Page(s) 737–743

Abstract: Background/aim: N. sativa essential oil (EO) and its compounds (thymoquinone, carvacrol and p-cymene) have a broad antimicrobial spectrum. The aim of this study was to investigate the antimicrobial and resistance modifying activity of N. sativa EO, ... ...

Abstract	Background/aim: N. sativa essential oil (EO) and its compounds (thymoquinone, carvacrol and p-cymene) have a broad antimicrobial spectrum. The aim of this study was to investigate the antimicrobial and resistance modifying activity of N. sativa EO, thymoquinone, carvacrol and p-cymene against Listeria monocytogenes. Materials and methods: N. sativa EO, thymoquinone, carvacrol and p-cymene was assessed for its antimicrobial activity, modulation of antimicrobial resistance, inhibition of antimicrobial efflux and membrane integrity by broth microdilution, ethidium bromide accumulation and LIVE/DEAD BacLight™ assays. Results: L. monocytogenes showed substantial susceptibility toward N. sativa EO, thymoquinone, and carvacrol. A significant reduction in MIC's of EtBr and ciprofloxacin was noticed when tested in combination with N. sativa EO, thymoquinone, carvacrol and reserpine. In the presence of each compound the membrane integrity was disintegrated, and the EtBr accumulation increased which was comparable to positive control reserpine. Conclusion: N. sativa EO might have a potential for controlling the antibiotic resistance in Listeria.
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Benzoquinones/chemistry ; Drug Resistance, Bacterial/drug effects ; Listeria monocytogenes/drug effects ; Listeria monocytogenes/pathogenicity ; Nigella sativa/chemistry ; Oils, Volatile/chemistry ; Plant Oils/chemistry ; Plant Oils/pharmacology
Chemical Substances	Anti-Bacterial Agents ; Benzoquinones ; Oils, Volatile ; Plant Oils ; caraway oil (C2J9B08Q3I) ; thymoquinone (O60IE26NUF)
Language	English
Publishing date	2018-06-25
Publishing country	Greece
Document type	Journal Article
ZDB-ID	807031-3
ISSN	1791-7549 ; 0258-851X
ISSN (online)	1791-7549
ISSN	0258-851X
DOI	10.21873/invivo.11302
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