The phenomenon at the center of the study is the Warburg effect, a metabolic behavior first described nearly a century ago. Even when oxygen is available, many cancer cells rely heavily on glycolysis—the stepwise breakdown of glucose in the cell’s cytoplasm—and convert much of the resulting pyruvate into lactate. This is less efficient than mitochondrial oxidative phosphorylation in terms of ATP produced per molecule of glucose, but it can provide rapidly dividing cells with metabolic intermediates needed to build DNA, proteins and membranes. Glycolysis also allows cells to maintain energy production under fluctuating oxygen conditions. In breast cancer, the degree to which this metabolic program is engaged has been associated with disease behavior and patient outcomes, but the molecular switches that connect glycolysis to the cell’s transcriptional machinery have remained incompletely understood.

The investigators focused on AKR1B10, an enzyme involved in cellular metabolism whose abnormal overexpression has been observed in cancer. Enzymes of this kind can influence the balance of aldehydes, carbonyl compounds and other metabolic molecules, but AKR1B10’s precise relationship with glucose metabolism in breast cancer was unclear. To investigate it, the team combined bioinformatics with analyses of breast-cancer tissues and cell lines, measuring gene and protein activity using quantitative reverse-transcription polymerase chain reaction and western blotting. They also used metabolomics to survey changes in small molecules, glucose-metabolism assays to track the behavior of cancer cells, and mass spectrometry to examine protein modifications. This multi-layered approach allowed the researchers to follow the pathway from AKR1B10 expression to metabolic output and, ultimately, cell proliferation.

The experiments indicated that AKR1B10 is not simply correlated with aggressive cancer-cell behavior but is functionally important for it. When researchers reduced AKR1B10 activity, breast-cancer cells showed impaired glycolysis and reduced proliferation. Conversely, experiments designed to increase its activity supported the metabolic and growth-associated phenotype. The researchers tested these gain- and loss-of-function effects both in cultured cells and in animal models, providing evidence beyond a single laboratory system. Their results identified elevated AKR1B10 as a driver of the Warburg effect in the models examined, with increased glucose use and lactate generation accompanying the enzyme’s overexpression. The findings do not establish that AKR1B10 alone determines the course of human breast cancer, but they place the protein at a critical control point within the tumor’s metabolic network.

The mechanistic breakthrough came when the team examined how AKR1B10 communicates with other proteins. The study found that AKR1B10 acts as a molecular bridge between IGF2R and PGK1. IGF2R is a receptor involved in the trafficking and handling of insulin-like growth factor 2, while PGK1 catalyzes a reversible step in glycolysis, transferring a phosphate group from 1,3-bisphosphoglycerate to ADP and generating ATP. According to the researchers, the AKR1B10-linked interaction enables IGF2R to promote phosphorylation of PGK1 at the amino-acid position tyrosine 324, designated Y324. Phosphorylation can alter a protein’s activity, location or interactions, and in this case the modification appears to push PGK1 toward a state that supports stronger glycolytic flux. The resulting rise in lactate becomes the signal for the next stage of the cascade.

Lactate is often treated as a metabolic waste product, the acidic end point of glycolysis that must be exported from cells. Increasing evidence, however, shows that it can also act as a signaling molecule and a source of chemical groups used to modify proteins. The study links the lactate produced through the AKR1B10–IGF2R–PGK1 circuit to a process called histone lactylation. Histones are proteins around which DNA is wrapped, and chemical marks on histones can make particular genomic regions more or less accessible to transcriptional machinery. The researchers detected dynamic lactylation at lysine 12 of histone H4, referred to as H4K12la. In effect, the cancer cell’s altered metabolism appears to leave a chemical imprint on its chromatin. This provides a direct route by which excess glycolysis can influence gene expression rather than merely supplying energy.

The researchers then used RNA sequencing and chromatin immunoprecipitation sequencing to determine which genes were affected by this metabolic-to-epigenetic connection. Their results implicated transcriptional activation of mTOR, a master regulator of cell growth, protein synthesis, nutrient sensing and survival. The mechanistic sequence proposed by the study is therefore unusually long but tightly connected: increased AKR1B10 supports an interaction involving IGF2R and PGK1; IGF2R-dependent phosphorylation activates PGK1; enhanced PGK1 activity increases glycolysis and lactate production; lactate promotes H4K12 lactylation; and this chromatin modification helps activate mTOR transcription. Once engaged, mTOR signaling can encourage the synthesis of cellular components and the growth programs required for proliferation. The pathway illustrates how cancer metabolism and gene regulation can operate as a feedback system, with a biochemical change in the cytoplasm reshaping activity in the nucleus.

The therapeutic experiments offered an early test of whether this pathway could be disrupted. Knockdown of AKR1B10 suppressed the signaling axis and reprogrammed the metabolism of breast-cancer cells, reducing their proliferative capacity. The researchers also examined oleanolic acid, or OA, as an AKR1B10 inhibitor in combination with 2-deoxy-D-glucose, a glycolysis inhibitor commonly abbreviated 2-DG. The combination inhibited the AKR1B10-centered pathway more effectively in the reported experiments than leaving the metabolic circuit unchallenged, while also restraining cell proliferation. The logic behind the pairing is complementary: blocking AKR1B10 may weaken the upstream molecular bridge, while 2-DG limits glucose breakdown itself. Together, the compounds could attack both the regulatory trigger and the metabolic output. However, these findings remain preclinical. The study does not show that OA and 2-DG are safe or effective treatments for patients, nor does it establish how the proposed strategy would interact with standard breast-cancer therapies.

The work also highlights why metabolic targets can be difficult to translate into medicines. Glycolysis and mTOR signaling are used by healthy cells as well as tumors, so inhibiting them broadly could produce toxicity or affect immune, muscle and other tissues. AKR1B10 may offer a more selective point of intervention if its overexpression or pathway activity distinguishes particular breast-cancer subtypes, but that possibility will require detailed validation in larger patient cohorts. The study used clinical tissue samples collected with informed consent and approvals from institutional ethics committees, along with animal experiments conducted under approved guidelines. Even so, questions remain about which molecular breast-cancer subtypes depend most strongly on the pathway, whether tumors can bypass it through alternative glycolytic enzymes, and whether resistance emerges after prolonged treatment. Future studies will need to test the biomarkers that could identify responsive tumors and assess the pathway in clinically relevant treatment settings.

The significance of the findings lies less in presenting an immediate cancer cure than in revealing a form of molecular entanglement that may help tumors thrive. AKR1B10 appears to connect a metabolic enzyme, a receptor, a glycolytic catalyst, a histone modification and a growth pathway into one circuit. That architecture helps explain how breast-cancer cells can convert their demand for glucose into a durable proliferative advantage: nutrients are processed into lactate, lactate modifies chromatin, and chromatin activates signals that support further growth. By combining metabolic inhibition with targeted disruption of this signaling axis, researchers may eventually be able to interrupt the feedback loop at several points. For now, the study provides a mechanistic blueprint—and a potentially shareable target—for understanding why some breast tumors are so metabolically aggressive.

Anaplastic thyroid carcinoma, or ATC, is rare but exceptionally aggressive. Unlike many differentiated thyroid cancers, ATC can grow rapidly, invade nearby structures, and spread before treatment has had time to take effect. The BRAF V600E mutation is one of the most important genetic alterations in a subset of these tumors. It changes the BRAF protein so that it remains abnormally active, driving the MAPK signaling pathway, a molecular chain that regulates proliferation, survival, and cellular behavior. Dabrafenib is designed to inhibit mutant BRAF, cutting off this signal at a critical point. Yet cancer cells are not passive targets. Under therapeutic pressure, they can adapt, rewire signaling networks, and alter the way they process nutrients.

The central insight of the new work is that drug resistance is not solely a matter of changing receptors or acquiring additional mutations. It can also involve a shift in the cell’s internal economy. Cancer cells require a continuous supply of ATP for energy, reducing equivalents to control chemical reactions, and carbon-based molecules for constructing DNA, proteins, membranes, and other cellular components. Glucose is a major source of these materials, but its carbon can be redirected into multiple biochemical pathways. PHGDH sits at the entrance to one such branch: the serine synthesis pathway. It diverts the glycolytic intermediate 3-phosphoglycerate away from energy production and toward the generation of serine and related metabolites.

Serine is more than a simple amino acid. It contributes to the production of glycine, nucleotides, phospholipids, and glutathione, an important antioxidant system. Through these connections, the serine synthesis pathway can influence how cells replicate their genomes, build new membranes, and withstand oxidative stress. PHGDH also participates in the cell’s management of redox balance, helping shape the availability of molecules required for maintaining chemical stability during rapid growth. In tumors exposed to a BRAF inhibitor, these functions may become particularly valuable. If dabrafenib suppresses the signaling program that normally supports proliferation, a resistant cell may compensate by strengthening metabolic pathways that preserve survival and biosynthetic capacity.

Kim and You’s study identifies PHGDH inhibition as a means of disrupting that compensation. The reported effect is described as metabolic rewiring: rather than simply adding another brake to the same signaling pathway, PHGDH inhibition changes the flow of nutrients through the cancer cell. This distinction matters because resistant tumors often survive by routing around a blocked pathway. A second drug that targets the same route may have limited impact if the cancer has already activated a parallel mechanism. By interfering with serine-related metabolism, however, PHGDH inhibition may remove the raw materials or redox support that resistant BRAF-mutant cells require to remain viable under dabrafenib treatment.

The approach also illustrates why combination therapies are increasingly being designed around the relationship between signaling and metabolism. Oncogenic BRAF signaling can alter glucose uptake, mitochondrial activity, amino-acid use, and the expression of metabolic enzymes. At the same time, metabolic changes can feed back into signaling by modifying the cellular energy state and the chemical environment in which proteins operate. A tumor treated with dabrafenib may therefore not be understood as a static collection of mutated cells. It is a dynamic system responding to stress. The combination of BRAF blockade and PHGDH inhibition aims to attack both the growth command and the adaptive fuel network that can help cancer cells survive its suppression.

From a technical perspective, the strategy may produce several layers of stress at once. Restricting PHGDH activity can reduce the ability of cells to generate serine through glucose-derived intermediates. That shortage may affect nucleotide synthesis, limiting the materials needed for DNA replication and repair. It may also weaken phospholipid production, which is essential for expanding cellular membranes during division. At the same time, reduced support for glutathione production could leave tumor cells more exposed to reactive oxygen species. These chemically reactive molecules arise naturally during metabolism and can increase when cells are under therapeutic pressure. A cancer cell that can no longer buffer oxidative damage may cross a threshold leading to growth arrest or cell death.

The findings are especially notable because dabrafenib resistance remains a major obstacle even when a tumor carries a mutation that appears directly druggable. Targeted therapies can produce striking responses, but those responses may be temporary. Some resistant cells reactivate MAPK signaling through alterations elsewhere in the pathway, while others engage receptor tyrosine kinases, change cell identity, or enter a slower-growing state that tolerates treatment. Metabolic rewiring adds another dimension to this problem. It suggests that the cells surviving therapy may not merely be genetically different; they may also be physiologically different, using nutrients in a way that makes them less dependent on the pathway originally targeted.

The study’s implications extend beyond thyroid cancer, although its immediate focus is BRAF V600E anaplastic thyroid carcinoma. PHGDH is overexpressed or relied upon in several cancer contexts, and the serine synthesis pathway has attracted attention as a potential therapeutic target. Still, an experimental result in a cancer model does not automatically establish a safe or effective treatment for patients. Serine metabolism is also important in normal tissues, and the therapeutic challenge will be to determine whether PHGDH can be inhibited strongly enough to affect resistant tumor cells without causing unacceptable toxicity. Future work will need to clarify which tumors are most dependent on PHGDH, identify biomarkers that predict response, and establish the appropriate dose, timing, and sequence for combining a PHGDH inhibitor with dabrafenib.

The broader message is that cancer resistance may be defeated by targeting not only what tumors signal, but also how they survive. In BRAF V600E anaplastic thyroid carcinoma, the work by Kim and You positions PHGDH as a metabolic pressure point that becomes important when dabrafenib pushes cancer cells into an adaptive state. If these findings are confirmed in additional models and ultimately in clinical studies, the combination could help convert a resistant tumor’s survival strategy into a liability. The research offers a vivid example of modern oncology’s expanding battlefield: the fight is no longer confined to mutated genes and signaling proteins, but includes the intricate metabolic networks that keep malignant cells alive.

Subject of Research: PHGDH inhibition and metabolic rewiring as a strategy to overcome dabrafenib resistance in BRAF V600E anaplastic thyroid carcinoma.

Article Title: PHGDH inhibition overcomes dabrafenib resistance through metabolic rewiring in BRAF V600E anaplastic thyroid carcinoma.

Article References: Kim, S.Y., You, MH. “PHGDH inhibition overcomes dabrafenib resistance through metabolic rewiring in BRAF V600E anaplastic thyroid carcinoma.” Cell Death Discovery (2026). https://doi.org/10.1038/s41420-026-03293-7

Image Credits: AI Generated

DOI: https://doi.org/10.1038/s41420-026-03293-7

Keywords: PHGDH, dabrafenib resistance, metabolic rewiring, BRAF V600E, anaplastic thyroid carcinoma, serine synthesis pathway, targeted therapy, cancer metabolism

KRAS mutations are notorious drivers in approximately 30% of all human cancers, with an overwhelming 90% incidence in pancreatic ductal adenocarcinoma (PDAC), a malignancy characterized by dismal prognosis and limited treatment options. KRAS inhibitors have been hailed as potential game-changers, yet their clinical efficacy is frequently undermined by acquired drug resistance. This research addresses a critical gap: the role of metabolic rewiring and mitochondrial quality control, particularly mitophagy, in mediating resistance to KRAS-targeted therapies.

The study centers on the observation that KRAS inhibitors, specifically MRTX1133 targeting the KRAS(G12D) mutant and the pan-RAS inhibitor RMC-6236, lead to a significant reduction in ATP citrate lyase (ACLY) expression and consequently decrease cytosolic AcCoA levels in both murine KPC cells and human PDAC AsPC-1 cells harboring KRAS(G12D) mutations. This metabolic suppression initiates a cascade culminating in elevated mitophagy, a selective autophagic process for mitochondrial turnover. Importantly, the induction of mitophagy by KRAS inhibition was effectively antagonized by exogenous acetate supplementation, underscoring the centrality of the ACLY-AcCoA axis in controlling this process.

Delving deeper, the researchers demonstrated that mitophagy triggered by KRASi is strikingly dependent on NLRX1, a mitochondrial NOD-like receptor previously implicated in innate immune signaling and mitochondrial homeostasis. NLRX1-deficient cells exhibited a near-complete abrogation of KRASi-induced mitophagy, illuminating its indispensable role as a mediator of mitochondrial quality control in this context. The absence of NLRX1 not only hindered mitophagy but also resulted in pronounced accumulation of reactive oxygen species (ROS) and heightened cellular oxidative stress, as evidenced by increased NADP⁺/NADPH ratios.

The functional consequences of these molecular events were profound. NLRX1 deficiency sensitized cancer cells to KRAS inhibition, augmenting cytotoxicity in both murine and human KRAS-mutant PDAC and lung cancer models. This finding was further bolstered by experiments involving the antioxidant N-acetyl-L-cysteine (NAC), which rescued the viability of NLRX1-deficient cells exposed to KRASi by mitigating oxidative stress. It became evident that the mitophagy pathway represents a cellular defensive maneuver that mitigates ROS-induced damage to sustain tumor cell survival during KRAS-targeted therapy.

Complementing the in vitro analyses, in vivo studies employing a subcutaneous KPC tumor model in NSG mice cemented the therapeutic relevance of the ACLY–AcCoA–NLRX1 axis. Mice receiving the KRAS inhibitor MRTX1133 exhibited notable tumor regression, an effect amplified in the absence of NLRX1. Moreover, immunoblot and histological analyses revealed that while Acly suppression occurred uniformly across conditions, mitochondrial protein levels—indicative of mitophagy—were preserved in NLRX1-deficient tumors, affirming the disrupted mitophagic response. Consistently, ROS levels were reduced in control tumors following KRASi but escalated in NLRX1-lacking specimens, reinforcing the interplay between mitophagy, redox balance, and therapy resistance.

These revelations shift the paradigm by identifying mitophagy not merely as a housekeeping process but as a vital resistance mechanism exploited by cancer cells under pharmacologic assault. The study’s insights suggest that targeting the metabolic regulation of mitophagy—specifically through the ACLY-AcCoA-NLRX1 signaling axis—may enhance the efficacy of KRAS inhibitors and suppress tumor adaptation.

Intriguingly, this research also reports synergistic antitumor effects when combining KRAS inhibitors with mitophagy inhibitors like Mdivi-1, which exacerbates mitochondrial dysfunction and oxidative stress in cancer cells. This dual targeting strategy presents a compelling therapeutic avenue, potentially circumventing the resilience conferred by mitophagy-mediated mitochondrial clearance.

From a mechanistic viewpoint, the intimate connection between decreased ACLY activity and mitophagy induction underscores the broader concept that metabolic state functions as a signaling nexus. Cytosolic AcCoA emerges as more than a metabolic intermediate; it acts as a signaling metabolite communicating cellular energy and nutrient status to the mitophagy machinery. This axis elegantly illustrates how metabolic rewiring can intersect with organelle quality control to govern cell fate decisions during oncogenic stress.

Beyond immediate therapeutic implications, these findings raise significant questions about mitophagy’s role across diverse KRAS-mutant tumor types and contexts of therapy resistance. As chronic KRAS inhibition becomes more prevalent in clinical oncology, understanding how tumor cells engage mitochondrial quality control pathways could guide the design of combinatorial regimens that preempt or reverse resistance.

Moreover, this study highlights the vital importance of ROS homeostasis in malignancies driven by KRAS mutations. The intricate balance between mitochondrial removal and redox signaling revealed here may represent a universal vulnerability exploitable across cancers characterized by oxidative stress adaptations.

In conclusion, the elucidation of the ACLY–AcCoA–NLRX1 axis as a regulator of mitophagy in KRAS inhibitor-mediated drug resistance broadens the framework of cancer metabolism and organelle dynamics in oncogenesis. It opens exciting pathways for innovative treatments that disrupt tumor adaptive mechanisms, potentially transforming outcomes for patients afflicted with some of the deadliest KRAS-driven cancers.

Subject of Research:
KRAS-mutant cancer metabolism, mitophagy, and drug resistance mechanisms

Article Title:
Cytosolic acetyl-coenzyme A is a signalling metabolite to control mitophagy

Article References:
Zhang, Y., Shen, X., Shen, Y. et al. Cytosolic acetyl-coenzyme A is a signalling metabolite to control mitophagy. Nature (2025). https://doi.org/10.1038/s41586-025-09745-x

Image Credits: AI Generated

DOI:
https://doi.org/10.1038/s41586-025-09745-x

Bladder cancer remains one of the most prevalent and deadly malignancies affecting the urinary tract, characterized by high rates of recurrence and mortality. Despite advances in clinical treatment, the molecular mechanisms underpinning its progression and interaction with the host immune environment remain incompletely understood. SLC16A7, belonging to the solute carrier family 16, encodes a class of monocarboxylate transporters responsible for the proton-coupled translocation of key metabolites such as lactate, pyruvate, and ketone bodies. These metabolites are critical for cellular metabolism and energy homeostasis, particularly within the tumor microenvironment where metabolic rewiring is a hallmark of cancer.

The team implemented a comprehensive pan-cancer analysis utilizing data from 33 distinct tumor types curated in The Cancer Genome Atlas (TCGA). This approach enabled them to systematically assess SLC16A7’s expression levels and correlate these with diverse clinical parameters including tumor stage, mutation burden, microsatellite instability (MSI), immune cell infiltration, and survival outcomes. The study revealed that SLC16A7 expression was consistently downregulated in the majority of analyzed cancers, including bladder cancer, underscoring a potential universal tumor-suppressive function that transcends cancer subtypes.

One of the most compelling findings was the dichotomous relationship between SLC16A7 expression and patient prognosis, which varied depending on the cancer type. In bladder cancer, elevated SLC16A7 levels were robustly associated with better overall survival, a finding confirmed through Kaplan-Meier survival analyses using independent patient cohorts. This prognostic association affirms the gene’s potential utility both as a diagnostic marker and a predictor of treatment response, offering clinicians a new molecular handle to stratify patient risk more accurately.

Genomic investigations further exposed significant correlations between SLC16A7 expression and tumor mutation burden (TMB) in 13 cancer types, as well as with microsatellite instability in 11 cancers. These genetic instability measures are critical in cancer biology, often affecting how tumors evolve and respond to immunotherapies. The association suggests that SLC16A7 may influence not only metabolic homeostasis but also the mutational landscape, possibly through mechanisms impacting DNA repair or cellular stress responses.

To unravel the functional implications of SLC16A7, the researchers delved into pathway analyses utilizing hallmark gene set enrichment (Hallmark-GSEA) and Kyoto Encyclopedia of Genes and Genomes (KEGG-GSEA) databases. The results illuminated strong links between SLC16A7 and pathways governing immune response and tumor progression. These pathways include those involved in T-cell activation, cytokine signaling, and inflammatory responses, implicating SLC16A7 as a key modulator within the tumor microenvironment’s complex immunological network.

Immune infiltration analyses, employing CIBERSORT computational deconvolution methods, depicted a nuanced relationship between SLC16A7 and various immune cell subtypes populating the tumor microenvironment. Notably, SLC16A7 expression positively correlated with resting memory CD4+ T cells, eosinophils, monocytes, and memory B cells, which are generally associated with immune surveillance and anti-tumor activities. Conversely, it was negatively correlated with activated memory CD4+ T cells, M1 macrophages, follicular helper T cells, and CD8+ T cells in certain cancer contexts, suggesting complex immunomodulatory roles that may vary across tumor types.

Experimental validation through in vitro and ex vivo methods confirmed the diminished expression of SLC16A7 in bladder cancer tissues and cell lines compared to normal counterparts. Functional assays demonstrated that restoring SLC16A7 expression significantly inhibited bladder cancer cell proliferation, highlighting its direct role in curbing tumor growth. Moreover, co-culture experiments with activated CD8+ T cells revealed that SLC16A7 enhances the chemotactic attraction of cytotoxic lymphocytes toward tumor cells and boosts their tumor-killing efficacy, underscoring its pivotal role in orchestrating anti-tumor immunity within the bladder cancer microenvironment.

The mechanistic insights gleaned from this study present SLC16A7 as a multifaceted tumor suppressor. By regulating metabolite transport, it appears to influence cellular energy balance and metabolic crosstalk that are essential for both cancer cell viability and immune cell functionality. The enhanced recruitment and activation of CD8+ cytotoxic T cells driven by SLC16A7 suggest it acts as a bridge linking metabolism to immune surveillance, a crucial axis in the fight against cancer.

Given the growing emphasis on immunotherapy as a transformative approach to cancer treatment, these findings have profound clinical relevance. The ability of SLC16A7 to facilitate immune cell infiltration and activation within the tumor microenvironment may enhance responses to checkpoint inhibitors and other immunomodulatory treatments. Thus, therapeutic strategies aimed at restoring or mimicking SLC16A7 functions offer an exciting avenue to potentiate existing therapies and overcome resistance mechanisms.

Beyond bladder cancer, the pan-cancer perspective of this study provides a valuable framework for understanding SLC16A7’s context-dependent roles in diverse oncological settings. Its downregulation across most cancers and association with improved survival metrics reinforce the importance of metabolic transporters as crucial regulators of tumor biology. The dual role observed – protective in some cancers, complex in others – also sheds light on the intricate tumor heterogeneity that continues to challenge precision oncology.

This research further enriches the landscape of cancer biomarker discovery by positioning SLC16A7 as a potential candidate for diagnostic panels and therapeutic targeting. Given the gene’s influence on immune modulation and tumor progression, integrating SLC16A7 expression profiling into clinical workflows could improve the granularity of patient stratification, helping to tailor treatments more effectively and avoid unnecessary therapeutic burdens.

In conclusion, the elucidation of SLC16A7’s tumor-suppressing function provides a compelling narrative linking cancer metabolism, immune regulation, and clinical outcomes. The study’s integration of large-scale bioinformatics, robust experimental models, and clinical validation exemplifies modern oncology research’s multidisciplinary approach. Moving forward, deeper mechanistic studies and clinical trials will be vital to translate these insights into tangible benefits for patients battling bladder cancer and potentially other malignancies.

With cancer incidence on the rise globally, innovative biomarkers such as SLC16A7 offer hope for earlier diagnosis, better prognostic assessments, and more effective treatments. This research underscores the necessity of exploring metabolic transporters within the tumor microenvironment as therapeutic targets, opening new frontiers in the quest to outsmart cancer’s adaptive resilience.

The findings reported here lay a foundation for future investigations into the molecular interplay between metabolism and immunity in cancer. As scientists continue deciphering the complex web of tumor-host interactions, discoveries like SLC16A7 bring us closer to personalized medicine approaches that harness the body’s own defenses while starving tumors of their metabolic lifelines.

Subject of Research: Tumor-suppressing role of SLC16A7 in bladder cancer and pan-cancer analysis involving tumor progression, immune regulation, and prognosis.

Article Title: Tumor suppressing function of SLC16A7 in bladder cancer and its pan-cancer analysis

Article References:
Xu, M., Zhou, J., Lv, J. et al. Tumor suppressing function of SLC16A7 in bladder cancer and its pan-cancer analysis. BMC Cancer 25, 932 (2025). https://doi.org/10.1186/s12885-025-14345-z

Image Credits: Scienmag.com

DOI: https://doi.org/10.1186/s12885-025-14345-z