5-Amino 1MQ: A Comprehensive Research Monograph

Overview

5-Amino 1MQ (5-amino-1-methylquinolinium) is a small molecule inhibitor of nicotinamide N-methyltransferase (NNMT), a cytosolic enzyme that catalyzes the methylation of nicotinamide (vitamin B3) to produce 1-methylnicotinamide (1-MNA) using S-adenosylmethionine (SAM) as the methyl donor. Unlike the peptides that comprise most research compounds in this class, 5-Amino 1MQ is a low molecular weight organic molecule (173.21 g/mol) that acts through a highly specific enzymatic inhibition mechanism rather than receptor agonism. Its quinolinium-based structure was identified through systematic structure-activity relationship studies as a potent and selective NNMT inhibitor with favorable drug-like properties, including cell permeability and aqueous solubility.

The rationale for NNMT inhibition as a metabolic intervention stems from the discovery that NNMT is significantly upregulated in white adipose tissue and liver during obesity, where it depletes intracellular NAD+ pools by consuming its precursor nicotinamide. Because NAD+ is an essential cofactor for sirtuins (particularly SIRT1 and SIRT3), mitochondrial function, and cellular energy metabolism, excessive NNMT activity creates a metabolic bottleneck that impairs fat cell energy expenditure and promotes lipid storage. By inhibiting NNMT, 5-Amino 1MQ restores NAD+ availability, reactivates sirtuin-dependent metabolic pathways, and reprograms adipocyte metabolism from a storage to an oxidative phenotype. This mechanism positions NNMT inhibition as a fundamentally different approach to metabolic research compared to NAD+ precursor supplementation (nicotinamide riboside, NMN), which increases substrate supply rather than addressing the enzymatic drain.

The broader significance of NNMT as a drug target has expanded considerably since the initial metabolic studies. NNMT sits at a critical junction of NAD+ metabolism and the methionine cycle, giving it the capacity to simultaneously influence cellular energy status, epigenetic regulation through the SAM/SAH ratio, and signaling through the 1-MNA product. This multifaceted metabolic impact has made NNMT and its inhibitors relevant not only to obesity and metabolic syndrome research but also to cancer biology, aging, hepatic steatosis, and neurodegenerative disease. The enzyme’s tissue-specific expression patterns — with particularly high levels in adipose tissue, liver, and certain tumor types — offer the prospect of interventions with relatively focused metabolic effects, a desirable property for any pharmacological tool.

Mechanism of Action

NNMT Enzyme Biology

NNMT belongs to the family of SAM-dependent methyltransferases and was originally characterized as a hepatic drug-metabolizing enzyme involved in the biotransformation of nicotinamide and other pyridine compounds. However, research over the past decade has revealed that NNMT plays a far more significant role in cellular metabolism than previously appreciated. The enzyme sits at a critical metabolic intersection: it simultaneously consumes nicotinamide (depleting the NAD+ salvage pathway), consumes SAM (depleting the cellular methyl donor pool), and produces 1-MNA and S-adenosylhomocysteine (SAH). The dual depletion of both NAD+ precursors and methyl donors makes NNMT a powerful regulator of cellular metabolic and epigenetic states.

NNMT is expressed across a broad range of tissues, with the highest basal expression levels found in the liver, where it was first characterized. Significant expression is also found in white adipose tissue, skeletal muscle, kidney, lung, and brain. In the context of metabolic disease, NNMT expression in white adipose tissue and liver is of particular importance, as upregulation of the enzyme in these compartments during obesity creates a metabolic environment that promotes energy storage and impairs oxidative metabolism. The tissue-specific regulation of NNMT expression is driven by nutritional signals, inflammatory cytokines, and hormonal inputs, with high-fat diet feeding producing robust upregulation in adipose tissue that correlates with the severity of metabolic dysfunction.

Ruf et al. (2012) elucidated the crystal structure of human NNMT, providing critical insights into the enzyme’s active site architecture and the structural basis for substrate recognition. The enzyme adopts a two-domain fold common to SAM-dependent methyltransferases, with a catalytic pocket that accommodates both the SAM methyl donor and the nicotinamide substrate. The structural data revealed key residues involved in substrate binding and catalysis, establishing the molecular framework that guided the rational design of inhibitors including the quinolinium-based series from which 5-Amino 1MQ was derived.

Kraus et al. (2014) published a seminal study in Nature demonstrating that NNMT expression is markedly elevated in white adipose tissue of obese mice and humans. Critically, antisense oligonucleotide knockdown of NNMT in adipose tissue protected mice from diet-induced obesity, increased energy expenditure by approximately 10-15%, improved glucose tolerance, and induced a gene expression profile characteristic of brown/beige adipocytes. This study established NNMT as a bona fide metabolic target and provided the biological rationale for developing pharmacological NNMT inhibitors.

NAD+ Restoration and Sirtuin Activation

The primary downstream consequence of NNMT inhibition is restoration of intracellular NAD+ concentrations. NAD+ is an indispensable cofactor for the sirtuin family of deacetylases (SIRT1-7), particularly SIRT1 and SIRT3, which regulate mitochondrial biogenesis, fatty acid oxidation, glucose metabolism, and cellular stress responses. When NNMT activity is elevated in obesity, excessive consumption of nicotinamide reduces NAD+ availability, impairing sirtuin function and creating a metabolic environment that favors energy storage over expenditure. This creates a vicious cycle: obesity upregulates NNMT, which depletes NAD+, which impairs sirtuin-mediated fat oxidation, which promotes further fat accumulation.

By blocking NNMT, 5-Amino 1MQ increases the pool of nicotinamide available for NAD+ biosynthesis through the salvage pathway enzyme NAMPT (nicotinamide phosphoribosyltransferase), thereby restoring NAD+ levels and reactivating sirtuin-mediated metabolic programs. Hong et al. (2015) demonstrated that NNMT regulates hepatic nutrient metabolism through SIRT1 protein stabilization, providing a direct mechanistic link between NNMT activity, NAD+ levels, and sirtuin-dependent metabolic regulation. SIRT1 activation by NNMT inhibition leads to deacetylation and activation of key metabolic transcription factors including PGC-1alpha (which drives mitochondrial biogenesis) and FOXO1 (which regulates gluconeogenesis and lipid metabolism).

The NAD+ salvage pathway represents the predominant route of NAD+ biosynthesis in most mammalian tissues, recycling nicotinamide generated by NAD+-consuming enzymes (sirtuins, PARPs, CD38) back into NAD+ through the sequential action of NAMPT and nicotinamide mononucleotide adenylyltransferases (NMNATs). NNMT diverts nicotinamide away from this recycling pathway by irreversibly methylating it to 1-MNA, which is subsequently excreted. The rate of NNMT-mediated nicotinamide consumption can be substantial in tissues with high NNMT expression, creating a significant drain on the NAD+ precursor pool that cannot be compensated by the de novo biosynthesis pathway from tryptophan, which operates at much lower flux rates in most tissues.

The broader importance of NAD+ metabolism in aging and disease has been extensively reviewed. Verdin (2015) provided a comprehensive overview of NAD+ in aging, metabolism, and neurodegeneration, establishing the central role of NAD+ decline as a driver of age-related metabolic dysfunction. Covarrubias et al. (2021) updated this framework to include the role of NAD+ in inflammatory aging (inflammaging), cellular senescence, and tissue repair. NNMT inhibition with 5-Amino 1MQ represents one approach within a growing pharmacological toolkit for addressing NAD+ decline, distinct from but complementary to precursor supplementation strategies.

SAM/SAH Ratio and Epigenetic Effects

NNMT inhibition also impacts the cellular SAM/SAH ratio, a critical determinant of methylation capacity. SAM is the universal methyl donor for essentially all cellular methylation reactions, including DNA methylation by DNMTs, histone methylation by histone methyltransferases, and small molecule methylation. By reducing NNMT-mediated consumption of SAM, 5-Amino 1MQ preserves methyl donor availability for other SAM-dependent methyltransferases, including those involved in histone and DNA methylation. Simultaneously, reduced SAH production shifts the SAM/SAH ratio in favor of methylation capacity, as SAH is a competitive inhibitor of most SAM-dependent methyltransferases.

This epigenetic dimension of NNMT inhibition has been extensively characterized. Sperber et al. (2015) positioned NNMT at the crossroads between cellular metabolism and epigenetic regulation, demonstrating that NNMT expression levels directly influence the global methylation landscape of the cell. In embryonic stem cells, NNMT acts as a metabolic regulator of the naive-to-primed pluripotency transition by modulating the SAM/SAH ratio and consequently the activity of histone methyltransferases. This finding broadened the understanding of NNMT from a purely metabolic enzyme to a key epigenetic regulator.

Adipocyte Metabolic Reprogramming

The combined effect of NAD+ restoration and epigenetic remodeling through NNMT inhibition produces a profound shift in adipocyte metabolism. Research has demonstrated that NNMT inhibition promotes characteristics associated with beige/brown adipocyte identity, including upregulation of uncoupling protein 1 (UCP1), increased mitochondrial density, enhanced oxygen consumption rate, and elevated expression of thermogenic gene programs including PRDM16, CIDEA, and DIO2. This white-to-beige adipocyte conversion represents a potentially important mechanism for increasing whole-body energy expenditure.

The SIRT1 activation resulting from restored NAD+ levels plays a central role in this reprogramming. SIRT1 deacetylates and activates PGC-1alpha, the master regulator of mitochondrial biogenesis and oxidative metabolism, driving increased mitochondrial content and respiratory capacity in adipocytes. Additionally, SIRT1 activity promotes the browning transcriptional program through interactions with PRDM16 and other brown fat transcription factors. Mouchiroud et al. (2013) demonstrated that the NAD+/sirtuin pathway modulates longevity through activation of mitochondrial UPR and FOXO signaling, establishing the broader anti-aging relevance of sirtuin activation through NAD+ restoration.

Pharmacokinetics

Absorption and Distribution

The pharmacokinetic profile of 5-Amino 1MQ has been characterized primarily in rodent models during the preclinical development of NNMT inhibitors. As a small molecule with a molecular weight of only 173.21 Da, 5-Amino 1MQ possesses pharmacokinetic properties fundamentally different from those of peptides, including greater metabolic stability, broader tissue distribution, and resistance to peptidase degradation.

Following intraperitoneal injection in mice, which was the primary route of administration in the pivotal obesity studies by Neelakantan et al. (2018), 5-Amino 1MQ is rapidly absorbed into the systemic circulation. The small molecular size facilitates efficient diffusion from the peritoneal cavity into the vasculature. The compound carries a permanent positive charge on the quinolinium nitrogen, which influences its pharmacokinetic behavior by enhancing aqueous solubility while potentially limiting passive diffusion across lipid bilayer membranes. Despite this charge, 5-Amino 1MQ has been demonstrated to be cell-permeable, likely utilizing organic cation transporters (OCTs) or other carrier-mediated transport systems to gain intracellular access.

The tissue distribution of 5-Amino 1MQ shows preferential accumulation in NNMT-expressing tissues, including white adipose tissue, liver, and kidney. This tissue tropism is advantageous for its intended metabolic applications, as these are the primary sites where NNMT overexpression contributes to metabolic dysfunction in obesity. The volume of distribution in rodent studies indicates broad tissue penetration, consistent with the compound’s small molecular size. Whether 5-Amino 1MQ crosses the blood-brain barrier in pharmacologically relevant concentrations has not been extensively characterized, though its permanent positive charge may limit CNS penetration.

Metabolism and Elimination

Metabolism of 5-Amino 1MQ differs fundamentally from peptide metabolism. As a quinolinium derivative rather than a peptide, it is not subject to degradation by the endogenous peptidases and proteases that rapidly clear peptide drugs from the circulation. Instead, its metabolic fate involves Phase I and Phase II biotransformation reactions in the liver, potentially including oxidation, reduction, and conjugation reactions. The charged quinolinium core may limit the extent of hepatic metabolism, as the cationic charge can reduce access to cytochrome P450 active sites. Detailed metabolite identification studies have not been published to date.

Renal excretion is a significant elimination pathway for 5-Amino 1MQ, facilitated by the compound’s aqueous solubility and cationic charge, which promotes active tubular secretion by renal organic cation transporters. The elimination half-life in rodent models has not been precisely reported in the published literature, but the dosing regimens used in the pivotal in vivo studies (daily intraperitoneal injections) suggest a half-life on the order of hours, requiring daily administration for sustained NNMT inhibition. Comprehensive pharmacokinetic parameters including oral bioavailability, protein binding, and human-relevant clearance estimates remain to be determined in formal pharmacokinetic studies.

Research Applications

Obesity and Weight Management

Neelakantan et al. (2018) conducted the key preclinical study establishing 5-Amino 1MQ as an effective anti-obesity agent in a diet-induced obesity (DIO) mouse model. C57BL/6 mice fed a high-fat diet (60% kcal from fat) were treated with 5-Amino 1MQ via daily intraperitoneal injection. The results demonstrated:

• Significant reduction in body weight gain compared to vehicle-treated controls, with treated animals gaining substantially less weight despite consuming the same high-fat diet
• Selective reduction in white adipose tissue mass without affecting lean body mass, indicating that the anti-obesity effect was due to reduced fat accumulation rather than generalized tissue wasting
• Improved glucose tolerance as measured by oral glucose tolerance test (OGTT), with treated animals showing faster glucose clearance and lower peak glucose levels
• Improved insulin sensitivity, consistent with the metabolic reprogramming of adipose tissue from a lipid-storing to a lipid-oxidizing phenotype
• Reduced plasma total cholesterol and LDL cholesterol levels, suggesting favorable effects on lipid metabolism beyond adipose tissue
• No observed adverse effects on liver or kidney function at therapeutic doses, as assessed by plasma markers of hepatic and renal injury

NNMT as a Drug Target

The development of 5-Amino 1MQ was guided by systematic structure-activity relationship (SAR) studies that identified the key pharmacophoric features required for potent and selective NNMT inhibition. Neelakantan et al. (2017) synthesized and evaluated a series of quinolinium-based compounds, establishing the SAR around the quinolinium scaffold. The key findings that led to the identification of 5-Amino 1MQ as the lead compound included:

• High selectivity for NNMT over other methyltransferases, a critical property given the large number of SAM-dependent methyltransferases in the human proteome
• Cell permeability despite the permanently charged quinolinium core, demonstrated by cellular NNMT activity assays
• Competitive inhibition with respect to the substrate nicotinamide, with the amino group at the 5-position providing critical hydrogen bonding interactions with active site residues
• Suitable pharmacokinetic profile for in vivo studies, including aqueous solubility and metabolic stability sufficient for daily dosing regimens

Hepatic Steatosis and Fatty Liver Research

NNMT has been identified as a contributor to hepatic steatosis (fatty liver disease), a condition that affects a substantial proportion of the obese population and is increasingly recognized as a major public health concern. Kannt et al. (2015) demonstrated that NNMT activation contributes to the development of fatty liver disease through depletion of hepatic NAD+ and SAM pools, which impairs fatty acid oxidation and promotes lipogenesis. In their experimental models, elevated hepatic NNMT activity was associated with increased triglyceride accumulation, impaired mitochondrial beta-oxidation capacity, and altered expression of key lipogenic transcription factors including SREBP-1c and ChREBP. NNMT inhibition with compounds such as 5-Amino 1MQ represents a potential research avenue for addressing the metabolic disturbances underlying non-alcoholic fatty liver disease (NAFLD) and its progressive form, non-alcoholic steatohepatitis (NASH). The convergence of NAD+ restoration, improved mitochondrial function, and SIRT1-mediated deacetylation of metabolic regulators provides a mechanistic rationale for NNMT inhibition in the context of hepatic lipid metabolism.

Cancer Metabolism Research

NNMT has been identified as overexpressed in multiple cancer types, where it may contribute to metabolic reprogramming and epigenetic dysregulation that supports tumor growth and survival. Ulanovskaya et al. (2013) characterized NNMT’s role as a metabolic regulator in cancer cells, demonstrating that NNMT overexpression creates a metabolic sink for SAM that broadly alters the cellular methylation landscape, reducing levels of histone methylation marks that regulate gene expression. This epigenetic remodeling can promote a more aggressive, treatment-resistant cancer phenotype.

Subsequent research has expanded the understanding of NNMT’s role across cancer types:

• Renal cell carcinoma: Tang et al. (2015) identified NNMT overexpression as a prognostic factor in clear cell renal cell carcinoma, where elevated NNMT levels correlated with more advanced disease stage and poorer clinical outcomes
• Breast cancer: Wang et al. (2019) demonstrated that NNMT enhances chemoresistance in breast cancer through SIRT1 protein stabilization, suggesting that NNMT inhibition could potentially sensitize resistant tumors to chemotherapy
• Metabolic vulnerability: The dependence of certain tumors on high NNMT activity for maintaining their epigenetic landscape creates a potential metabolic vulnerability that could be exploited by NNMT inhibitors
• Tumor microenvironment: Emerging research suggests that NNMT activity in tumor-associated stromal cells and immune cells may also contribute to the immunosuppressive tumor microenvironment, creating additional rationale for evaluating NNMT inhibition in immuno-oncology contexts

NAD+ Biology and Aging Research

The role of 5-Amino 1MQ in boosting intracellular NAD+ has made it relevant to the broader field of NAD+ biology and aging research. NAD+ levels decline with age across multiple tissues, and this decline is increasingly recognized as a driver of age-related metabolic dysfunction, mitochondrial impairment, and cellular senescence. The age-related decline in NAD+ is multifactorial, involving both increased consumption by enzymes such as CD38 (whose expression rises with inflammation and aging) and reduced biosynthetic capacity. NNMT upregulation in aged tissues may represent an additional mechanism of NAD+ depletion that has been underappreciated relative to other contributors.

NNMT inhibition represents an alternative strategy to boost NAD+, complementing other approaches such as supplementation with NAD+ precursors (nicotinamide riboside, nicotinamide mononucleotide) by addressing the enzymatic drain on nicotinamide rather than simply increasing precursor supply. This distinction is mechanistically important: if NNMT activity is elevated, simply providing more nicotinamide through precursor supplementation may be partially counteracted by increased NNMT-mediated methylation and clearance of the additional nicotinamide. Combining NNMT inhibition with precursor supplementation could therefore produce synergistic NAD+ elevation. Pissios (2017) provided a comprehensive review of NNMT at the intersection of NAD+ metabolism and health, articulating the rationale for targeting NNMT in age-related metabolic decline.

Safety Profile in Research

The safety profile of 5-Amino 1MQ has been evaluated in preclinical studies, primarily in the context of the rodent obesity models used to establish its metabolic efficacy. In the pivotal study by Neelakantan et al. (2018), daily intraperitoneal administration of 5-Amino 1MQ to diet-induced obese mice over the treatment period did not produce observable adverse effects on liver function (as measured by plasma ALT and AST levels), kidney function (as measured by plasma creatinine and BUN), or general health parameters including body condition, activity level, and food intake. The selectivity of body weight reduction — affecting adipose tissue mass without reducing lean body mass — suggests that the compound’s metabolic effects are targeted rather than resulting from generalized toxicity or appetite suppression.

The high selectivity of 5-Amino 1MQ for NNMT over other methyltransferases is an important contributor to its safety profile. The human genome encodes over 200 SAM-dependent methyltransferases, many of which perform essential cellular functions in DNA methylation, histone modification, and small molecule metabolism. A non-selective methyltransferase inhibitor would be expected to produce widespread and potentially toxic disruption of cellular methylation processes. The quinolinium-based design of 5-Amino 1MQ, which mimics the substrate nicotinamide rather than the cofactor SAM, provides the structural basis for selective NNMT inhibition while sparing other methyltransferases.

The permanent positive charge on the quinolinium nitrogen is relevant to the safety consideration of potential cardiac effects, as other cationic compounds are known to interact with cardiac ion channels (particularly hERG potassium channels), potentially causing QT interval prolongation. While no cardiac toxicity has been reported in the published 5-Amino 1MQ literature, formal hERG channel binding studies and in vivo cardiac safety pharmacology studies have not been published. This represents an important safety evaluation that would be required in any formal drug development program.

Regarding genotoxicity, 5-Amino 1MQ’s mechanism of action is enzymatic inhibition rather than direct DNA interaction, suggesting a low inherent genotoxic risk. However, the downstream effects on the SAM/SAH ratio and consequent changes in DNA and histone methylation could theoretically influence epigenetic regulation in ways that merit careful long-term safety evaluation. Formal genotoxicity testing (Ames test, micronucleus assay) results have not been published.

It is important to note that 5-Amino 1MQ remains in the preclinical stage of investigation. No Phase I human safety studies have been conducted, and the full safety profile — including rare adverse effects, drug interactions, and effects of long-term administration — remains to be determined through formal toxicology programs and clinical trials.

Dosing in Research Literature

The following table summarizes representative dosing approaches used across different 5-Amino 1MQ research applications:

Molecular Properties

Storage and Handling for Research

5-Amino 1MQ should be stored as a dry powder at -20 degrees C for long-term stability. As a small molecule with a stable quinolinium core, it is considerably more stable than peptides and is less susceptible to degradation from temperature fluctuations, hydrolysis, or oxidation. For short-term storage (weeks), room temperature storage in a desiccated container is acceptable. The compound should be protected from moisture during storage, as the hygroscopic nature of many salt forms of quinolinium derivatives can lead to weight inaccuracies if the powder absorbs atmospheric water. Storage containers should be tightly sealed with desiccant included.

Stock solutions can be prepared in sterile water or DMSO and stored at -20 degrees C as frozen aliquots. Aqueous solutions should be used within 7-14 days when stored at 2-8 degrees C. For longer-term storage of solutions, DMSO stocks are preferred over aqueous solutions, as the organic solvent provides better chemical stability for the compound. Aliquot concentrated stock solutions into single-use volumes to avoid repeated freeze-thaw cycles, although 5-Amino 1MQ is substantially more tolerant of freeze-thaw cycling than peptide solutions.

Current Research Landscape

5-Amino 1MQ and NNMT inhibition represent a growing area of metabolic research with expanding relevance across multiple disease domains. Key directions of ongoing investigation include:

1. Clinical translation: Efforts to advance NNMT inhibitors from preclinical models toward human clinical trials for obesity and metabolic syndrome. This requires formal pharmacokinetic studies in relevant preclinical species, comprehensive toxicology programs, and the establishment of manufacturing processes that meet Good Manufacturing Practice (GMP) standards. The favorable preclinical profile of 5-Amino 1MQ positions it as a candidate for further development, though the gap between preclinical proof-of-concept and clinical-stage programs remains substantial.

2. Tissue-specific NNMT biology: Characterizing the role of NNMT in specific tissues including liver, skeletal muscle, brain, and immune cells to understand organ-specific effects of inhibition. NNMT expression varies markedly across tissues, and the consequences of inhibition may differ depending on the tissue context. Understanding these tissue-specific roles is essential for predicting the full spectrum of effects of systemic NNMT inhibition.

3. Combination strategies: Research combining NNMT inhibition with NAD+ precursor supplementation (NR, NMN), exercise, caloric restriction, or other metabolic interventions to determine additive or synergistic effects. The mechanistic rationale for combining NNMT inhibition with NAD+ precursor supplementation is compelling: NNMT inhibition prevents the enzymatic drain on nicotinamide while precursor supplementation increases the substrate supply, potentially producing greater NAD+ elevation than either approach alone.

4. Cancer applications: Investigating NNMT inhibition as a metabolic intervention in cancers with high NNMT expression, potentially resensitizing tumor cells to methylation-dependent regulatory mechanisms or to conventional chemotherapeutic agents. The discovery that NNMT promotes chemoresistance in breast cancer has opened a new therapeutic avenue for combination strategies.

5. Next-generation inhibitors: Development of structurally diverse NNMT inhibitors with improved pharmacokinetic properties, oral bioavailability, and tissue-selective distribution for specific research and potential therapeutic applications. Several pharmaceutical and academic groups are pursuing alternative chemical scaffolds for NNMT inhibition, including non-quinolinium-based inhibitors that may offer different pharmacokinetic profiles.

6. Hepatic steatosis: Expanding the investigation of NNMT inhibition in models of NAFLD and NASH, where the combination of impaired NAD+ metabolism and dysregulated lipid handling in hepatocytes creates a metabolic environment that may be particularly amenable to NNMT inhibitor intervention.

7. Biomarker development: Identification of circulating biomarkers that can serve as pharmacodynamic indicators of NNMT inhibition in vivo, including plasma 1-MNA levels, NAD+ metabolomics, and histone methylation marks in accessible tissues. Such biomarkers would be essential for clinical development to confirm target engagement and guide dose selection.

References

The studies referenced throughout this monograph represent key publications in the emerging field of NNMT biology and pharmacological inhibition, spanning the period from the initial characterization of NNMT’s metabolic role through the development of selective inhibitors and their preclinical evaluation. For the most current research, search PubMed using the terms “NNMT inhibitor,” “5-amino-1-methylquinolinium,” “nicotinamide N-methyltransferase,” or “NNMT obesity” for the latest publications. Key journals that have published NNMT inhibitor research include Biochemical Pharmacology, Journal of Medicinal Chemistry, Nature, Nature Medicine, Nature Chemical Biology, and ACS Chemical Biology.