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Article ; Online: Dual-Target

Ramharack, Pritika / Salifu, Elliasu Y / Agoni, Clement

International journal of molecular sciences

2023 Volume 24, Issue 18

Abstract: The escalating prevalence of drug-resistant strains ... ...

Abstract	The escalating prevalence of drug-resistant strains of
MeSH term(s)	Mycobacterium tuberculosis ; Folic Acid Antagonists/pharmacology ; Aspartic Acid ; Catalysis ; Folic Acid
Chemical Substances	Folic Acid Antagonists ; Aspartic Acid (30KYC7MIAI) ; Folic Acid (935E97BOY8)
Language	English
Publishing date	2023-09-13
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/ijms241814021
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Article ; Online: Unravelling the Structural Mechanism of Action of 5-methyl-5-[4-(4-oxo-3H-quinazolin-2-yl)phenyl]imidazolidine-2,4-dione in Dual-Targeting Tankyrase 1 and 2: A Novel Avenue in Cancer Therapy.

Peters, Xylia Q / Agoni, Clement / Soliman, Mahmoud E S

Cell biochemistry and biophysics

2022 Volume 80, Issue 3, Page(s) 505–518

Abstract: Tankyrase (TNKS) belonging to the poly(ADPribose) polymerase family, are known for their multi-functioning capabilities, and play an essential role in the Wnt β-catenin pathway and various other cellular processes. Although showing inhibitory potential ... ...

Abstract	Tankyrase (TNKS) belonging to the poly(ADPribose) polymerase family, are known for their multi-functioning capabilities, and play an essential role in the Wnt β-catenin pathway and various other cellular processes. Although showing inhibitory potential at a nanomolar level, the structural dual-inhibitory mechanism of the novel TNKS inhibitor, 5-methyl-5-[4-(4-oxo-3H-quinazolin-2-yl)phenyl]imidazolidine-2,4-dione, remains unexplored. By employing advanced molecular modeling, this study provides these insights. Results of sequence alignments of binding site residues identified conserved residues; GLY1185 and ILE1224 in TNKS-1 and PHE1035 and PRO1034 in TNKS-2 as crucial mediators of the dual binding mechanism of 5-methyl-5-[4-(4-oxo-3H-quinazolin-2-yl)phenyl]imidazolidine-2,4-dione, corroborated by high per-residue energy contributions and consistent high-affinity interactions of these residues. Estimation of the binding free energy of 5-methyl-5-[4-(4-oxo-3H-quinazolin-2-yl)phenyl]imidazolidine-2,4-dione showed estimated total energy of -43.88 kcal/mol and -30.79 kcal/mol towards TNKS-1 and 2, respectively, indicating favorable analogous dual binding as previously reported. Assessment of the conformational dynamics of TNKS-1 and 2 upon the binding of 5-methyl-5-[4-(4-oxo-3H-quinazolin-2-yl)phenyl]imidazolidine-2,4-dione revealed similar structural changes characterized by increased flexibility and solvent assessible surface area of the residues inferring an analogous structural binding mechanism. Insights from this study show that peculiar, conserved residues are the driving force behind the dual inhibitory mechanism of 5-methyl-5-[4-(4-oxo-3H-quinazolin-2-yl)phenyl]imidazolidine-2,4-dione and could aid in the design of novel dual inhibitors of TNKS-1 and 2 with improved therapeutic properties.
MeSH term(s)	Humans ; Hydantoins ; Imidazolidines ; Neoplasms ; Tankyrases/chemistry ; Tankyrases/metabolism ; Wnt Signaling Pathway
Chemical Substances	Hydantoins ; Imidazolidines ; TNKS2 protein, human (EC 2.4.2.30) ; Tankyrases (EC 2.4.2.30) ; TNKS protein, human (EC 2.4.4.30)
Language	English
Publishing date	2022-05-30
Publishing country	United States
Document type	Journal Article
ZDB-ID	1357904-6
ISSN	1559-0283 ; 1085-9195
ISSN (online)	1559-0283
ISSN	1085-9195
DOI	10.1007/s12013-022-01076-2
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Article ; Online: Structural Insights into the Role of Pseudouridimycin Binding in Disruption of Bacterial RNA Polymerase Bridge Helix Conformational Arrangement.

H Rabbad, Ali / Agoni, Clement / E Soliman, Mahmoud

Current pharmaceutical biotechnology

2022 Volume 24, Issue 4, Page(s) 562–569

Abstract: Background: The bridge helix (BH) is a crucial region in bacterial RNA polymerase (RNAP) catalysis. It plays an essential role in the nucleotide addition cycle (NAC) by performing many modulated rearrangements and conformational changes. Any changes in ... ...

Abstract	Background: The bridge helix (BH) is a crucial region in bacterial RNA polymerase (RNAP) catalysis. It plays an essential role in the nucleotide addition cycle (NAC) by performing many modulated rearrangements and conformational changes. Any changes in the bridge helix conformational arrangements could perturb the NAC. Objective: Pseudouridimycin (PUM) was recently reported as a new RNAP inhibitor. However, the crucial role of the bridge helix in the inhibitory activity of PUM remains unclear, hence the aim of this study. Methods: The PUM interaction and the structural dynamics of bacterial Bridge Helix upon PUM binding were investigated using various dynamic analysis approaches. Results: Besides establishing the importance of the bridge helix residues in the binding of PUM, the findings of this study revealed that the adjacent binding of PUM induces a stabilized and structurally rigid bridge helix characterized by a reduction of individual residue flexibility, which could interfere with its role in the NAC. In addition, a hydrophobic structural rearrangement of the bridge helix is observed, evidenced by the burial and folding of residues into the hydrophobic core and a switch in the secondary structure of some regions of the bridge helix from the turn and bend to the alpha helix. The observed conformational disruption of the bridge helix upon binding of PUM also accounts for the reported inhibitory prowess and broad-spectrum activity as widely reported. Conclusion We believe findings from this study will further complement current drug discovery knowledge on disrupting bacterial RNAP machinery.
MeSH term(s)	DNA-Directed RNA Polymerases ; Nucleosides ; Bacteria/metabolism ; Protein Structure, Secondary
Chemical Substances	pseudouridimycin ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Nucleosides
Language	English
Publishing date	2022-05-12
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2132197-8
ISSN	1873-4316 ; 1389-2010
ISSN (online)	1873-4316
ISSN	1389-2010
DOI	10.2174/1389201023666220511211433
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Article ; Online: The Binding of Remdesivir to SARS-CoV-2 RNA-Dependent RNA Polymerase May Pave The Way Towards the Design of Potential Drugs for COVID-19 Treatment.

Agoni, Clement / Soliman, Mahmoud E S

Current pharmaceutical biotechnology

2020 Volume 22, Issue 11, Page(s) 1520–1537

Abstract: Aim: We seek to provide an understanding of the binding mechanism of Remdesivir, as well as structural and conformational implications on SARS-CoV-2 virus RNA-dependent RNA polymerase upon its binding and identify its crucial pharmacophoric moieties.: ...

Abstract	Aim: We seek to provide an understanding of the binding mechanism of Remdesivir, as well as structural and conformational implications on SARS-CoV-2 virus RNA-dependent RNA polymerase upon its binding and identify its crucial pharmacophoric moieties. Background: The coronavirus disease of 2019 (COVID-19) pandemic had infected over a million people, with 65,000 deaths as of the first quarter of 2020. The current limitation of effective treatment options with no approved vaccine or targeted therapeutics for the treatment of COVID-19 has posed serious global health threats. This has necessitated several drug and vaccine development efforts across the globe. To date, the farthest in the drug development pipeline is Remdesivir. Objectives: We performed the molecular dynamics simulation, quantified the energy contributions of binding site residues using per-residue energy decomposition calculations, and subsequently generated a pharmacophore model for the identification of potential SARS-CoV-2 virus RNA-dependent RNA polymerase inhibitors. Methods: Integrative molecular dynamics simulations and thermodynamic calculations coupled with advanced post-molecular dynamics analysis techniques were employed. Results: Our analysis showed that the modulatory activity of Remdesivir is characterized by an extensive array of high-affinity and consistent molecular interactions with specific active site residues that anchor Remdemsivir within the binding pocket for efficient binding. These residues are ASP452, THR456, ARG555, THR556, VAL557, ARG624, THR680, SER681, and SER682. Results also showed that Remdesivir binding induces minimal individual amino acid perturbations, subtly interferes with deviations of C-α atoms, and restricts the systematic transition of SARS-CoV-2 RNA-dependent RNA polymerase from the "buried" hydrophobic region to the "surface-exposed" hydrophilic region. We also mapped a pharmacophore model based on the observed high-affinity interactions with SARSCoV- 2 virus RNA-dependent RNA polymerase, which showcased the crucial functional moieties of Remdesivir and was subsequently employed for virtual screening. Conclusion: The structural insights and the provided optimized pharmacophoric model would augment the design of improved analogs of Remdesivir that could expand treatment options for COVID-19.
MeSH term(s)	Adenosine Monophosphate/analogs & derivatives ; Alanine/analogs & derivatives ; Antiviral Agents/pharmacology ; COVID-19/drug therapy ; Humans ; Pharmaceutical Preparations ; RNA, Viral ; RNA-Dependent RNA Polymerase/genetics ; SARS-CoV-2
Chemical Substances	Antiviral Agents ; Pharmaceutical Preparations ; RNA, Viral ; remdesivir (3QKI37EEHE) ; Adenosine Monophosphate (415SHH325A) ; RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; Alanine (OF5P57N2ZX)
Keywords	covid19
Language	English
Publishing date	2020-10-27
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2132197-8
ISSN	1873-4316 ; 1389-2010
ISSN (online)	1873-4316
ISSN	1389-2010
DOI	10.2174/1389201021666201027154833
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Article ; Online: Repurposing antiviral phytochemicals from the leaf extracts of Spondias mombin (Linn) towards the identification of potential SARSCOV-2 inhibitors.

Boadu, Akwasi / Agoni, Clement / Karpoormath, Rajshekhar / Soliman, Mahmoud / Nlooto, Manimbulu

Scientific reports

2022 Volume 12, Issue 1, Page(s) 10896

Abstract: Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), a pneumonia-like disease with a pattern of acute respiratory symptoms, currently remains a significant public health concern causing tremendous human suffering. Although several approved ... ...

Abstract	Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2), a pneumonia-like disease with a pattern of acute respiratory symptoms, currently remains a significant public health concern causing tremendous human suffering. Although several approved vaccines exist, vaccine hesitancy, limited vaccine availability, high rate of viral mutation, and the absence of approved drugs account for the persistence of SARS-CoV-2 infections. The investigation of possibly repurposing of phytochemical compounds as therapeutic alternatives has gained momentum due to their reported affordability and minimal toxicity. This study investigated anti-viral phytochemical compounds from ethanolic leaf extracts of Spondias mombin L as potential inhibitor candidates against SARS-CoV-2. We identified Geraniin and 2-O-Caffeoyl-(+)-allohydroxycitric acid as potential SARS-CoV-2 inhibitor candidates targeting the SARS-CoV-2 RNA-dependent polymerase receptor-binding domain (RBD) of SARS-CoV-2 viral S-protein and the 3C-like main protease (3CL
MeSH term(s)	Anacardiaceae ; Antiviral Agents/chemistry ; Antiviral Agents/pharmacology ; Coronavirus 3C Proteases ; Cysteine Endopeptidases/chemistry ; Drug Repositioning ; Humans ; Phytochemicals/pharmacology ; RNA, Viral ; SARS-CoV-2 ; Viral Proteins/chemistry ; COVID-19 Drug Treatment
Chemical Substances	Antiviral Agents ; Phytochemicals ; RNA, Viral ; Viral Proteins ; Cysteine Endopeptidases (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
Language	English
Publishing date	2022-06-28
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-14558-3
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Article ; Online: Dual-Knockout of Mutant Isocitrate Dehydrogenase 1 and 2 Subtypes Towards Glioma Therapy: Structural Mechanistic Insights on the Role of Vorasidenib.

Poonan, Preantha / Agoni, Clement / Soliman, Mahmoud E S

Chemistry & biodiversity

2021

Abstract: Recently, Vorasidenib (AG-881) has been reported as a therapeutic alternative that exerts potent dual inhibitory activity against mIDH1/2 towards the treatment of low-grade glioma. However, structural and dynamic events associated with its dual ... ...

Abstract	Recently, Vorasidenib (AG-881) has been reported as a therapeutic alternative that exerts potent dual inhibitory activity against mIDH1/2 towards the treatment of low-grade glioma. However, structural and dynamic events associated with its dual inhibition mechanism remain unclear. As such, we employ integrative computer-assisted atomistic techniques to provide thorough structural and dynamic insights. Our analysis proved that the dual-targeting ability of AG-881 is mediated by Val255/Val294 within the binding pockets of both mIDH1 and mIDH2 which are shown to elicit a strong intermolecular interaction, thus favoring binding affinity. The structural orientations of AG-881 within the respective hydrophobic pockets allowed favorable interactions with binding site residues which accounted for its high binding free energy of -28.69 kcal/mol and -19.89 kcal/mol towards mIDH1 and mIDH2, respectively. Interestingly, upon binding, AG-881 was found to trigger systemic alterations of mIDH1 and mIDH2 characterized by restricted residue flexibility and a reduction in exposure of residues to the solvent surface area. As a result of these structural alterations, crucial interactions of the mutant enzymes were inhibited, a phenomenon that results in a suppression of the production of oncogenic stimulator 2-HG. Findings therefore provide thorough structural and dynamic insights associated with the dual inhibitory activity of AG-881 towards glioma therapy.
Language	English
Publishing date	2021-05-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2139001-0
ISSN	1612-1880 ; 1612-1872
ISSN (online)	1612-1880
ISSN	1612-1872
DOI	10.1002/cbdv.202100110
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Article ; Online: Glioma-Targeted Therapeutics: Computer-Aided Drug Design Prospective.

Poonan, Preantha / Agoni, Clement / Ibrahim, Mahmoud A A / Soliman, Mahmoud E S

The protein journal

2021 Volume 40, Issue 5, Page(s) 601–655

Abstract: Amongst the several types of brain cancers known to humankind, glioma is one of the most severe and life-threatening types of cancer, comprising 40% of all primary brain tumors. Recent reports have shown the incident rate of gliomas to be 6 per 100,000 ... ...

Abstract	Amongst the several types of brain cancers known to humankind, glioma is one of the most severe and life-threatening types of cancer, comprising 40% of all primary brain tumors. Recent reports have shown the incident rate of gliomas to be 6 per 100,000 individuals per year globally. Despite the various therapeutics used in the treatment of glioma, patient survival rate remains at a median of 15 months after undergoing first-line treatment including surgery, radiation, and chemotherapy with Temozolomide. As such, the discovery of newer and more effective therapeutic agents is imperative for patient survival rate. The advent of computer-aided drug design in the development of drug discovery has emerged as a powerful means to ascertain potential hit compounds with distinctively high therapeutic effectiveness against glioma. This review encompasses the recent advances of bio-computational in-silico modeling that have elicited the discovery of small molecule inhibitors and/or drugs against various therapeutic targets in glioma. The relevant information provided in this report will assist researchers, especially in the drug design domains, to develop more effective therapeutics against this global disease.
MeSH term(s)	Antineoplastic Agents/chemistry ; Antineoplastic Agents/therapeutic use ; Brain Neoplasms/drug therapy ; Brain Neoplasms/genetics ; Brain Neoplasms/metabolism ; Drug Design ; Drug Discovery ; Glioma/drug therapy ; Glioma/genetics ; Glioma/metabolism ; Humans
Chemical Substances	Antineoplastic Agents
Language	English
Publishing date	2021-09-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2143071-8
ISSN	1875-8355 ; 1572-3887
ISSN (online)	1875-8355
ISSN	1572-3887
DOI	10.1007/s10930-021-10021-w
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Article: The Binding of Remdesivir to SARS-CoV-2 RNA-Dependent RNA polymerase May Pave The Way Towards the Design of Potential Drugs for COVID-19 Treatment

Agoni, Clement / Soliman, Mahmoud E S

Curr pharm. biotechnol

Abstract: AIM: We seek to provide an understanding of the binding mechanism of Remdesivir, provide structural and conformational implications on SARS-CoV-2 virus RNA-dependent RNA polymerase upon its binding and identify its crucial pharmacophoric moieties. ... ...

Abstract	AIM: We seek to provide an understanding of the binding mechanism of Remdesivir, provide structural and conformational implications on SARS-CoV-2 virus RNA-dependent RNA polymerase upon its binding and identify its crucial pharmacophoric moieties. BACKGROUND: The coronavirus disease of 2019 (COVID-19) pandemic has infected over a million people, with over 65,000 deaths as of the first quarter of 2020. The current limitation of effective treatment options with no approved vaccine or targeted therapeutics for the treatment of COVID-19 has posed serious global health threats. This has necessitated several drug and vaccine development efforts across the globe. To date, the farthest in the drug development pipeline so far is Remdesivir. OBJECTIVES: We perform molecular dynamics simulation, quantify the energy contributions of binding site residues using per-residue energy decomposition calculations, and subsequently generate a pharmacophore model for the identification of potential SARS-CoV-2 virus RNA-dependent RNA polymerase inhibitors. METHODS: Integrative molecular dynamics simulations and thermodynamic calculations coupled with advanced postmolecular dynamics analysis techniques were employed. RESULTS: Our analysis showed that the modulatory activity of Remdesivir is characterized by an extensive array of highaffinity and consistent molecular interactions with specific active site residues that anchor Remdemsivir within the binding pocket for efficient binding. These residues are ASP452, THR456, ARG555, THR556, VAL557, ARG624, THR680, SER681, and SER682. Results also showed that Remdesivir binding, induces minimal individual amino acid perturbations, subtly interferes with deviations of C-α atoms and restricts the systematic transition of SARS-CoV-2 RNA-dependent RNA polymerase from the "buried" hydrophobic region to the "surface-exposed" hydrophilic region. We also mapped a pharmacophore model based on observed high-affinity interactions with SARS-CoV-2 virus RNA-dependent RNA polymerase, which showcased the crucial functional moieties of Remdesivir and was subsequently employed for virtual screening. CONCLUSION: The structural insights and the optimized pharmacophoric model provided would augment the design of improved analogs of Remdesivir that could expand treatment options for COVID-19.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #895210
Database	COVID19

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Article ; Online: Dual-Inhibition of Human N-Myristoyltransferase Subtypes Halts Common Cold Pathogenesis: Atomistic Perspectives from the Case of IMP-1088.

Agoni, Clement / Salifu, Elliasu Y / Enslin, Gill / Kwofie, Samuel K / Soliman, Mahmoud E

Chemistry & biodiversity

2022 Volume 19, Issue 2, Page(s) e202100748

Abstract: The pharmacological inhibition of human N-myristoyltransferase (HsNMT) has emerged as an efficient strategy to completely prevent the replication process of rhinoviruses, a potential treatment for the common cold. This was corroborated by the recent ... ...

Abstract	The pharmacological inhibition of human N-myristoyltransferase (HsNMT) has emerged as an efficient strategy to completely prevent the replication process of rhinoviruses, a potential treatment for the common cold. This was corroborated by the recent discovery of compound IMP-1088, a novel inhibitor that demonstrated a dual-inhibitory activity against the two HsNMT subtypes 1 and 2 without inducing cytotoxicity. However, the molecular and structural basis for the dual-inhibitory potential of IMP-1088 has not been investigated. As such, we employ molecular modelling techniques to resolve the structural mechanisms that account for the dual-inhibitory prowess of IMP-1088. Sequence and nanosecond-based analyses identified Tyr296, Phe190, Tyr420, Leu453, Gln496, Val181, Leu474, Glu182, and Asn246 as residues common within the binding pockets of both HsNMT1 and HsNMT2 subtypes whose consistent interactions with IMP-1088 underpin the basis for its dual inhibitory potency. Nano-second-based assessment of interaction dynamics revealed that Tyr296 consistently elicited high-affinity π-π stacked interaction with IMP-1088, thus further highlighting its cruciality corroborating previous report. An exploration of resulting structural changes upon IMP-1088 binding further revealed a characteristic impeding of residue fluctuations, structural compactness, and a consequential burial of crucial hydrophobic residues, features required for HsNMT1/2 functionality. Findings present essential structural perspectives that augment previous experimental efforts and could also advance drug development for treating respiratory tract infections, especially those mediated by rhinoviruses.
MeSH term(s)	Acyltransferases/antagonists & inhibitors ; Common Cold/drug therapy ; Humans ; Inosine Monophosphate/metabolism ; Models, Molecular
Chemical Substances	Inosine Monophosphate (131-99-7) ; Acyltransferases (EC 2.3.-) ; glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97)
Language	English
Publishing date	2022-01-11
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2139001-0
ISSN	1612-1880 ; 1612-1872
ISSN (online)	1612-1880
ISSN	1612-1872
DOI	10.1002/cbdv.202100748
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Article ; Online: Extended Double Bond Conjugation in the Chalcone Framework Favours MAO-B Inhibition: A Structural Perspective on Molecular Dynamics.

Agoni, Clement / Issahaku, Abdul Rashid / Abdelgawad, Mohamed A / Khames, Ahmed / Soliman, Mahmoud E S / Mathew, Bijo

Combinatorial chemistry & high throughput screening

2022 Volume 25, Issue 12, Page(s) 2059–2069

Abstract: Background: The monotropic membrane protein monoamine oxidase B (MAO-B) has been shown to be a crucial drug target for the treatment of neurodegenerative diseases. The design of recent inhibitor therapeutic agents of MAO-B involves conjugation and ... ...

Abstract	Background: The monotropic membrane protein monoamine oxidase B (MAO-B) has been shown to be a crucial drug target for the treatment of neurodegenerative diseases. The design of recent inhibitor therapeutic agents of MAO-B involves conjugation and modification of a chalcone scaffold comprising two aryl or heteroaryl rings connected via a short spacer unit with rotatable bonds. Supported by experimental data, these modifications often result in high potent inhibitor compounds. Methods: In this study, we employ molecular dynamics simulations to unravel the impact of extended double bond conjugation in two novel compounds, F1 and MO10, toward the inhibition of the MAO-B protein. It was revealed that extended double bond conjugation induced a unidirectional orientation and motion of F1 and MO10, suggesting a stable binding pocket anchorage favouring high-affinity pocket interactions. Results: Conformational analyses also revealed that the incorporated double bond extension impeded the motion of individual binding pocket residues, which subsequently disrupted the functionality of MAO-B. Discussion: Real-time structural dynamics also revealed that the extended double bond conjugation mediated peculiar interactions with MAO-B binding pocket residues characterized by π-alkyl, π-π stacking, and π-sulphur interactions which buried both compounds into the hydrophobic core of MAO-B and ultimately induced higher binding affinities of both F1 and MO10. Conclusion: These insights present useful structural perspectives of the extended double bond conjugation associated with the experimentally reported enhanced inhibitory activity of F1 and MO10 against MAO-B.
MeSH term(s)	Chalcone/chemistry ; Chalcone/pharmacology ; Chalcones/chemistry ; Chalcones/pharmacology ; Membrane Proteins ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Monoamine Oxidase/metabolism ; Monoamine Oxidase Inhibitors/chemistry ; Monoamine Oxidase Inhibitors/pharmacology ; Structure-Activity Relationship ; Sulfur
Chemical Substances	Chalcones ; Membrane Proteins ; Monoamine Oxidase Inhibitors ; Chalcone (5S5A2Q39HX) ; Sulfur (70FD1KFU70) ; Monoamine Oxidase (EC 1.4.3.4)
Language	English
Publishing date	2022-02-13
Publishing country	United Arab Emirates
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2064785-2
ISSN	1875-5402 ; 1386-2073
ISSN (online)	1875-5402
ISSN	1386-2073
DOI	10.2174/1386207325666220214110717
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