Heterotopic ossification affects a substantial fraction of people with spinal cord injury, with estimates in clinical literature ranging from around 20 percent to more than 60 percent depending on how aggressively patients are screened. The condition typically emerges below the level of the lesion, most often around the hips, knees and elbows, and produces swelling, stiffness, progressive joint immobility and, in severe cases, complete ankylosis of the affected joint. For individuals already coping with paralysis, the added loss of joint range can devastate independence, interfering with seating, transfers, dressing and the ability to use a wheelchair comfortably. Current treatment options are limited and unsatisfying: nonsteroidal anti-inflammatory drugs and bisphosphonates are used prophylactically with mixed evidence, radiation therapy is occasionally deployed in high-risk cases, and surgical excision remains the definitive intervention, despite high recurrence rates and considerable operative risk.

What has been missing is a coherent account of how a wound in the spinal cord communicates with skeletal muscle distant from the injury site. Inflammation at the muscle level has long been implicated, and macrophages, the versatile immune cells that flood damaged tissue, have been suspected participants. Bone morphogenetic protein signaling, particularly through BMP2 and related ligands, is known to be a powerful inducer of ectopic bone. Yet none of these observations explained the striking temporal and anatomical link to the central nervous system injury itself. The new work addresses that gap by identifying adrenomedullin as the long-range signal, and by showing that it does not act alone but through a choreographed interaction between the nervous system, the immune system and mesenchymal progenitors residing in muscle.

Adrenomedullin is a 52-amino-acid peptide first isolated from human pheochromocytoma tissue in the early 1990s and subsequently recognized as a near-universal stress messenger. It is produced by vascular smooth muscle, endothelial cells, epithelia and neurons, and it participates in vasodilation, angiogenesis, immune modulation and tissue repair. Its receptors, composed of the calcitonin receptor-like receptor paired with receptor activity-modifying proteins, are widely distributed. In the context of spinal cord injury, the researchers found that adrenomedullin expression rises markedly in the injured cord, and that the peptide reaches the circulation and downstream tissues at levels capable of instructing cells far from the lesion. This elevation is not a passive byproduct of tissue damage; the study demonstrates that it is functionally required for the ectopic bone program to begin.

The mechanistic core of the paper lies in what adrenomedullin does once it arrives in muscle. Using rodent models of spinal cord injury combined with pharmacological blockade and genetic approaches, the team showed that adrenomedullin recruits and polarizes macrophages toward a pro-inflammatory, pro-osteogenic state. These macrophages, in turn, become a rich local source of bone morphogenetic protein 2, the master osteoinductive cue. Meanwhile, adrenomedullin acts directly on mesenchymal stromal cells and muscle-resident progenitors, sensitizing them to the BMP2 signal and pushing them along an osteoblastic differentiation pathway. The result is a feed-forward circuit: the neural signal summons and shapes the immune response, the immune response supplies the osteogenic ligand, and the sensitized progenitors execute the bone-forming program. The authors describe this as a neuro–immune–bone axis, a three-node signaling architecture in which each node is necessary for the pathology to unfold.

The experimental evidence supporting this model is notably multi-layered. In mice subjected to spinal cord injury, heterotopic bone formed in paralyzed limbs on a timeline consistent with the human clinical course, and the extent of ossification correlated with circulating adrenomedullin. Neutralizing the peptide with antibodies, antagonizing its receptors, or depleting macrophages each substantially reduced ectopic bone formation. Conversely, administering exogenous adrenomedullin to animals with otherwise insufficient neural drive promoted macrophage accumulation and osteogenic differentiation in muscle. Conditional genetic strategies further clarified the cellular division of labor: macrophage-derived BMP2 proved essential, while the osteogenic competence of the mesenchymal compartment depended on adrenomedullin receptor signaling. Transcriptional profiling of the affected muscle revealed enrichment of inflammatory, angiogenic and osteogenic gene programs, consistent with a tissue being actively converted from a muscle identity toward a bone-forming niche.

Perhaps the most clinically resonant finding concerns timing and reversibility. The adrenomedullin-driven cascade was shown to be active during a defined window after cord injury, and interventions that blocked the axis during that window prevented or markedly attenuated heterotopic ossification. This reframes the condition not as an inevitable consequence of paralysis but as a targetable signaling disease, one that could in principle be intercepted in the days to weeks following injury, before the first radiographic sign of bone appears. Because adrenomedullin antagonists and anti-BMP2 strategies already exist in various experimental and clinical forms, the pathway offers a plausible translational route. The caveat, which the authors acknowledge, is that adrenomedullin performs beneficial functions in vascular integrity, wound healing and immune regulation, so systemic blockade carries risks. Local delivery strategies, short treatment windows, or agents tuned to the specific receptor subtype involved may be needed to separate therapeutic benefit from collateral harm.

The study also carries broader implications beyond spinal cord medicine. Heterotopic ossification arises in other settings, including traumatic brain injury, severe burns, blast injuries in military personnel, and genetic conditions such as fibrodysplasia ossificans progressiva. In several of these contexts, central nervous system trauma or systemic inflammatory storms are part of the clinical picture, raising the possibility that neuro–immune–bone communication is a general principle of ectopic bone formation rather than a peculiarity of cord injury. If adrenomedullin or related neural signals contribute to ossification after burns or brain injury, the therapeutic horizon widens considerably. Even in fibrodysplasia ossificans progressiva, where an activating ACVR1 mutation provides the primary osteogenic driver, inflammatory flares are known to precipitate bone episodes, and understanding how neural and immune signals amplify that driver could inform combination therapies.

From a basic science perspective, the work adds to a growing recognition that the nervous system is not merely a bystander in regenerative and pathological processes but an active endocrine organ whose injury products reshape distant tissues. The concept of a neuro–immune–bone axis echoes earlier discoveries of neuroimmune interactions in pain, cachexia and bone homeostasis, but here the axis is shown to operate in a pathologically constructive direction, building ectopic skeleton rather than maintaining existing bone. It also underscores the macrophage’s dual identity: the same cells that clear debris and support repair can be commandeered by a circulating peptide into serving as local factories for osteoinductive ligands. Dissecting which macrophage subsets respond to adrenomedullin, and whether their polarization can be selectively redirected, represents an obvious next step.

For the millions of people worldwide living with spinal cord injury, and for the clinicians who manage the secondary complications of paralysis, the identification of a single, druggable molecular trigger for heterotopic ossification is a genuine advance. It converts a decades-old clinical observation, that paralyzed limbs sometimes grow bone, into a defined signaling pathway with named nodes, testable intermediates and established pharmacological levers. Clinical translation will require careful validation in human tissue and trials that respect the peptide’s physiological roles, but the conceptual shift is already complete: heterotopic ossification after spinal cord injury is now understood as a systemic endocrine event, initiated in the damaged cord, amplified by the immune system, and executed by progenitors in muscle that never asked to become bone cells.

Subject of Research: Adrenomedullin-driven heterotopic ossification after spinal cord injury via a neuro–immune–bone axis

Article Title: Adrenomedullin from spinal cord injury drives heterotopic ossification in skeletal muscle via a neuro–immune–bone axis

Article References: Chen, J., Wang, Z., Zeng, X., Wu, X., Li, G., Miao, N., Deng, Y., Zhang, D., Chen, X., Lai, H., Wan, Y., Wang, L., & Li, X. (2026). Adrenomedullin from spinal cord injury drives heterotopic ossification in skeletal muscle via a neuro–immune–bone axis. Experimental & Molecular Medicine. https://doi.org/10.1038/s12276-026-01836-7

Image Credits: AI Generated

DOI: 10.1038/s12276-026-01836-7

Keywords: spinal cord injury, heterotopic ossification, adrenomedullin, macrophages, BMP2, neuro–immune–bone axis, mesenchymal progenitors, ectopic bone, osteogenesis, Experimental & Molecular Medicine, spinal, cord

Thrombospondin-1 has historically been studied through the lens of its anti-angiogenic activity, particularly its ability to inhibit new blood vessel formation through interactions with endothelial cell receptors. But the protein is large, structurally complex, and released into the extracellular space by many cell types, and accumulating evidence has hinted that its domains may carry out distinct, even opposing, functions. The new work focuses on the N-terminal portion, the segment at the beginning of the protein chain, and asks what happens when this region is elevated in the circulation at a time when the body is being pushed to perform.

The central experimental strategy was to deliver the N-terminal fragment of thrombospondin-1 and then challenge animals with treadmill exercise or with cold exposure, two interventions that tax energy metabolism in fundamentally different ways. Exercise demands sustained contractile work from skeletal muscle and drives adaptations such as mitochondrial expansion, enhanced oxidative fiber recruitment, and improved glucose handling. Cold exposure, by contrast, activates thermogenesis, drawing on brown and beige adipose tissue and on shivering and non-shivering muscle heat production to defend core body temperature. The researchers reasoned that if a circulating factor could enhance adaptation to both stresses, it would be a strong candidate for a systemic coordinator of metabolic flexibility.

That is broadly what the data showed. Animals receiving the N-terminal fragment displayed greater muscle function, reflected in improved performance and force-generating capacity relative to controls undergoing the same exercise regimen. Histological and molecular analyses of the treated muscle pointed toward hallmarks of beneficial remodeling: shifts in fiber type composition toward a more oxidative profile and changes in gene expression consistent with enhanced mitochondrial and metabolic capacity. In the context of cold exposure, the fragment appeared to support tissue-specific adaptation, including responses in thermogenic fat, helping the animals meet the thermal challenge more effectively.

A key conceptual takeaway is the phrase tissue-specific metabolic adaptation. Rather than acting as a blunt metabolic accelerant, the N-terminal fragment seems to be interpreted differently by different tissues, evoking a pro-performance program in skeletal muscle during exercise and a pro-thermogenic program during cold stress. This kind of context dependence is characteristic of matricellular proteins and circulating signaling factors, whose effects depend on receptor expression patterns, local extracellular matrix composition, and concurrent physiological signals such as adrenergic tone and calcium flux. The study thus adds to a growing appreciation that exercise biology is not confined to muscle; it involves an endocrine-like dialogue among muscle, liver, adipose tissue, and the vasculature.

Mechanistically, the authors connect the fragment’s effects to established metabolic signaling hubs. Exercise adaptation is widely understood to flow through energy-sensing and transcriptional control pathways, including AMP-activated protein kinase, the master regulator of cellular energy status, and the PGC-1α coactivator that drives mitochondrial biogenesis. Enhancement of these pathways would plausibly explain both the improved contractile endurance observed in exercised animals and the greater thermogenic readiness observed under cold challenge. The fragment’s extracellular origin also raises questions about which cell-surface receptors mediate its uptake and signaling, an area where thrombospondin biology offers several candidates but no single obvious answer.

The timing of the discovery is notable. In recent years, the field has identified a parade of exercise-induced circulating factors, sometimes called exerkines, that mediate the systemic benefits of physical activity, from brain-derived neurotrophic effects to hepatic metabolic shifts. Identifying an N-terminal thrombospondin-1 fragment as a positive modulator of both exercise capacity and cold tolerance expands this catalog in an unexpected direction, because thrombospondin-1 has more often been cast as a negative regulator, for example in contexts of vascular injury, fibrosis, and tumor angiogenesis suppression. The work underscores a recurring lesson in protein biology: cleaved or independently folded domains of one protein can carry physiological meanings entirely distinct from the parent molecule.

Translational implications follow naturally, though with appropriate caveats. If the N-terminal fragment can be produced, stabilized, and safely delivered, it might one day serve as a therapy for conditions defined by muscle weakness or impaired metabolic adaptation, including sarcopenia of aging, prolonged disuse, and certain metabolic diseases. The cold-exposure component of the study adds a second, less obvious application space: enhancing thermogenic capacity could theoretically support metabolic health by increasing energy expenditure, a strategy many laboratories are pursuing through different targets. At the same time, the authors’ findings are preclinical, and the gap between improved performance in animal models and a safe, effective human intervention is notoriously wide. Dosing, receptor-mediated off-target effects, and the protein’s established roles in vascular biology would all require careful evaluation.

There are also intriguing physiological questions raised but not fully resolved. Is the endogenous N-terminal fragment released in response to exercise in humans, and if so, from which tissues? Could its levels serve as a biomarker of training status or metabolic health? And how do its effects interact with well-characterized exercise signals such as lactate, myostatin inhibitors, and the growing list of myokines and hepatokines? Answering these questions will require longitudinal studies in larger animals and, ultimately, human cohorts, as well as a more precise molecular dissection of the fragment’s receptor interactions and downstream signaling.

For now, the study offers a compelling proof of concept: a defined fragment of a familiar extracellular matrix protein can act as a systemic metabolic enhancer, amplifying the body’s own adaptive responses to exercise and to cold. As the exerkine field matures, discoveries of this kind move the conversation from cataloging what exercise does to understanding how the body broadcasts those instructions across tissues, and they hint at a future where the benefits of a hard workout or a cold morning might be partially recaptured, under medical guidance, by molecules the body already knows how to make.

Subject of Research: The role of the N-terminal fragment of thrombospondin-1 in enhancing muscle function and tissue-specific metabolic adaptation during exercise and cold exposure

Article Title: N-terminal thrombospondin-1 enhances muscle function and tissue-specific metabolic adaptation in response to exercise and cold exposure

Article References: N-terminal thrombospondin-1 enhances muscle function and tissue-specific metabolic adaptation in response to exercise and cold exposure. (n.d.). https://doi.org/10.1038/s12276-026-01830-z

Image Credits: AI Generated

DOI: 10.1038/s12276-026-01830-z

Keywords: thrombospondin-1, exercise, metabolic adaptation, skeletal muscle, cold exposure, thermogenesis, mitochondrial biogenesis, exerkines, AMPK, PGC-1alpha, brown adipose tissue, Experimental & Molecular Medicine

The research, led by investigators working to improve experimental models of the MASH-to-cancer transition, addresses a persistent gap in liver disease research. Existing animal models of MASH-driven hepatocellular carcinoma often fail to reproduce the slow, inflammation-heavy sequence of events seen in patients, in which fatty liver disease, chronic immune activation, fibrosis and eventually tumor formation unfold over years or decades. Without faithful models, researchers have struggled to identify the molecular switches that convert a wound-healing response into a cancer-promoting environment.

To close that gap, the team refined an experimental MASH–HCC model designed to capture the inflammatory milieu more accurately, combining metabolic stress with the kind of sustained immune signaling that characterizes human disease. The goal was not simply to make tumors appear faster, but to recreate the biological context in which inflammation actively reshapes the liver’s cellular landscape and drives pre-malignant cells toward full neoplastic transformation.

Using this refined platform, the researchers systematically examined the roles of immune cell populations within the tumor microenvironment. Macrophages, long recognized as versatile players that can either restrain or support tumor growth, emerged as central figures. Their internal molecular machinery, rather than their mere presence, appeared to determine the trajectory of disease. At the heart of that machinery sat Gadd45b, a protein belonging to the growth arrest and DNA damage-inducible family, best known for its involvement in cellular stress responses, DNA repair signaling and the regulation of inflammatory pathways.

Gadd45b has previously been implicated in immune regulation in several contexts, but its function inside tumor-associated macrophages during liver cancer development had remained poorly defined. The new work positions it as a key orchestrator of inflammation-driven neoplastic progression. According to the study’s findings, macrophage Gadd45b helps shape the signaling environment that fuels the proliferation and survival of pre-cancerous liver cells, effectively linking chronic inflammatory stimulation to the cellular events that culminate in hepatocellular carcinoma.

From a technical standpoint, the study’s strength lies in its integrated approach. By coupling a physiologically relevant disease model with mechanistic interrogation of macrophage biology, the researchers could move beyond correlation. Altering Gadd45b function in macrophages changed the course of neoplastic progression in the refined model, supporting the interpretation that this protein is not a passive bystander but an active regulator of the inflammatory program that drives cancer formation. The findings suggest that the epigenetic and transcriptional state of macrophages may be a decisive factor in whether a chronically inflamed liver progresses to malignancy.

The broader significance of this work rests on the biology of MASH itself. As obesity and metabolic syndrome rates climb worldwide, MASH has become one of the fastest-growing liver diseases and a rapidly expanding risk factor for hepatocellular carcinoma. Patients with MASH-related liver cancer often present at advanced stages, and therapeutic options remain limited. Understanding the immune-mediated mechanisms that connect steatohepatitis to tumor formation is therefore considered a priority for developing preventive strategies and earlier interventions.

Macrophages are particularly attractive targets in this context. Unlike malignant cells, which accumulate mutations that make them unstable therapeutic targets, macrophages are genetically stable and highly responsive to their environment. If a single intracellular factor such as Gadd45b controls whether these cells adopt a tumor-promoting state, it opens the possibility of reprogramming the inflammatory microenvironment before cancer takes hold. Such an approach would not attack tumor cells directly but would instead dismantle the ecological niche they depend upon, an increasingly popular strategy in modern cancer research.

The study also underscores the value of model refinement in biomedical research. Many promising findings in liver cancer biology have failed to translate because standard mouse models compress or bypass key stages of human disease. By building a system that more faithfully reproduces the inflammatory architecture of MASH-associated cancer, the researchers have created a tool that can be used to test candidate mechanisms and therapies under conditions that better mirror the clinical reality. This methodological contribution may prove as consequential as the Gadd45b finding itself, offering the field a more reliable framework for studying inflammation-driven carcinogenesis.

Looking ahead, the identification of macrophage Gadd45b as a key orchestrator of the MASH–HCC transition raises a series of testable questions. Researchers will need to determine whether Gadd45b expression in macrophages correlates with disease progression in human liver samples, whether it can serve as a biomarker of elevated cancer risk in patients with MASH, and whether pharmacological modulation of the Gadd45b pathway can safely dampen tumor-promoting inflammation without impairing the liver’s essential wound-healing responses. The answers could shape a new generation of therapies aimed not at the tumor itself, but at the inflammatory soil in which it grows, marking a meaningful step toward interrupting one of the most consequential disease trajectories in modern hepatology.

Subject of Research: The role of macrophage Gadd45b in inflammation-driven progression from MASH to hepatocellular carcinoma

Article Title: A refined MASH–HCC model identifies macrophage Gadd45b as a key orchestrator of inflammation-driven neoplastic progression

Article References: Kim, H., Kim, G., Yeon, H., Yang, D.-Y., Lee, S. G., An, T. H., Oh, S. Y., Yoon, S., Kim, J., Choi, J., Park, H.-J., Lee, E.-W., Han, B.-S., Lee, C.-H., Kim, I. Y., Kim, W. K., Bae, K.-H., Park, J. W., Oh, S. H., … Oh, K.-J. (2026). A refined MASH–HCC model identifies macrophage Gadd45b as a key orchestrator of inflammation-driven neoplastic progression. Experimental & Molecular Medicine. https://doi.org/10.1038/s12276-026-01838-5

Image Credits: AI Generated

DOI: 10.1038/s12276-026-01838-5

Keywords: MASH, hepatocellular carcinoma, macrophages, Gadd45b, inflammation, liver cancer, tumor microenvironment, metabolic dysfunction-associated steatohepatitis, neoplastic progression, cancer immunology, disease models, Experimental & Molecular Medicine

The study, whose findings are summarized under the title describing how HDAC1 maintains metabolic homeostasis in nucleus pulposus cells via post-translational modification interactions with YBX1, adds a significant piece to the puzzle of intervertebral disc degeneration, a condition that affects a large proportion of the adult population and is a leading contributor to chronic low back pain. By identifying a molecular axis that links chromatin-modifying enzymes to metabolic regulation, the work suggests that disc degeneration may be driven not only by mechanical loading and aging but also by specific, potentially targetable, biochemical failure points inside the cells themselves.

To appreciate why this matters, it helps to understand the harsh environment in which nucleus pulposus cells operate. The disc interior is poorly supplied with blood vessels, meaning nutrients such as glucose and oxygen arrive only by diffusion through surrounding tissue, while metabolic waste products such as lactate accumulate locally. Cells in this avascular niche must survive on comparatively little energy while simultaneously producing and maintaining an abundant extracellular matrix rich in proteoglycans and collagen, which gives the disc its ability to absorb compressive forces. When the metabolic balance tips — whether through nutrient deprivation, oxidative stress, or the cumulative damage of aging — the cells shift toward catabolic behavior, producing matrix-degrading enzymes and inflammatory mediators that accelerate tissue breakdown.

HDAC1 belongs to a family of enzymes that remove acetyl groups from histone proteins, the spools around which DNA is wound. By deacetylating histones, HDAC1 generally compacts chromatin and represses gene expression, but the enzyme also acts on many non-histone proteins, influencing their stability, activity, and interactions. This dual capacity makes HDAC1 a candidate regulator of programs that must respond quickly to cellular stress, including the metabolic adaptations that nucleus pulposus cells require to survive their nutrient-poor surroundings. Previous work across multiple tissues has implicated HDAC enzymes in cell survival, differentiation, and inflammatory signaling, but their specific role in disc cells has remained incompletely defined.

The new study centers on the interaction between HDAC1 and YBX1, a so-called cold-shock protein that functions as both a DNA- and RNA-binding factor and as a coordinator of stress responses. YBX1 has been linked to cell proliferation, survival under stress, and the regulation of metabolic gene expression in several biological systems. Crucially, both HDAC1 and YBX1 are subject to post-translational modifications — chemical tags such as acetylation, phosphorylation, ubiquitination, and others that are appended to proteins after translation and that can dramatically alter protein behavior. The researchers report that the functional relationship between HDAC1 and YBX1 is governed by such modifications, meaning that the enzymes and tagging systems that install or remove these marks effectively control how the two proteins work together.

According to the findings, when this HDAC1–YBX1 axis is intact, nucleus pulposus cells maintain metabolic homeostasis: their energy-generating pathways remain balanced, their matrix-producing functions are preserved, and degenerative signaling is held in check. When HDAC1 activity or its interaction with YBX1 is disrupted, the cells lose this equilibrium. The consequence, as described in the study, is a drift toward metabolic dysfunction of the kind observed in degenerated disc tissue, providing a mechanistic explanation for how epigenetic changes can translate into the structural failure of the disc over time.

The emphasis on post-translational modification crosstalk is perhaps the most technically significant aspect of the work. Post-translational modifications rarely act in isolation; a single protein may carry multiple marks that compete or cooperate with one another, and enzymes that install one mark can influence the deposition or removal of another. In the case of HDAC1 and YBX1, the study indicates that the acetylation state of the proteins shapes their physical interaction and, by extension, the downstream metabolic programs they regulate. This kind of modification crosstalk provides a rapid, reversible layer of control that operates alongside transcriptional regulation, allowing cells to adjust metabolism on short timescales in response to stress.

For the field of disc biology, the results help connect several previously parallel strands of research. Investigators have long documented that degenerated discs show altered gene expression, mitochondrial dysfunction, increased oxidative stress, and shifts in glucose and lactate metabolism. Separately, epigenetic studies have catalogued changes in histone modifications and DNA methylation in disc disease. By showing that a chromatin-associated enzyme directly maintains metabolic homeostasis through a modification-dependent interaction with a stress-response protein, the new work provides a causal bridge between these observations: epigenetic regulation is not merely a readout of degeneration but an active participant in keeping disc cells metabolically fit.

The translational implications are cautiously encouraging. If the HDAC1–YBX1 axis can be measured or modulated, it could inform strategies aimed at slowing or preventing disc degeneration, from biomarkers that identify early metabolic failure in disc cells to therapies designed to restore the interaction or its downstream protective programs. However, the study also underscores a central challenge in targeting epigenetic enzymes: HDAC1 performs essential functions in many cell types throughout the body, so any therapeutic approach would need to achieve specificity for the disc environment or exploit the modification crosstalk in a way that spares other tissues. The authors’ mechanistic framework offers a starting point for designing such selective interventions, but considerable preclinical work would be required before any clinical application.

Beyond the disc, the findings speak to a broader principle in cell biology: the insulation of tissue-specific metabolism by epigenetic machinery operating through networks of post-translational modifications. Cells in harsh niches — cartilage, the lens of the eye, the avascular regions of tumors — face analogous metabolic constraints, and similar enzyme-partner axes may govern their resilience. As the tools for mapping protein modifications become more powerful, studies of this kind are likely to reveal additional examples in which a single deacetylase, acting through a modification-dependent partnership, secures the metabolic foundations of long-lived cells. For the millions of people whose lives are affected by degenerative disc disease, the demonstration that HDAC1 and YBX1 jointly safeguard the metabolic health of the disc’s core cells represents a meaningful step toward understanding — and eventually intervening in — one of the most common forms of chronic musculoskeletal deterioration.

Subject of Research: The role of HDAC1 and YBX1 post-translational modification interactions in maintaining metabolic homeostasis of nucleus pulposus cells

Article Title: HDAC1 maintains metabolic homeostasis in nucleus pulposus cells via post-translational modification interactions with YBX1

Article References: HDAC1 maintains metabolic homeostasis in nucleus pulposus cells via post-translational modification interactions with YBX1. (n.d.). https://doi.org/10.1038/s12276-026-01843-8

Image Credits: AI Generated

DOI: 10.1038/s12276-026-01843-8

Keywords: HDAC1, YBX1, nucleus pulposus cells, intervertebral disc degeneration, metabolic homeostasis, post-translational modification, epigenetics, histone deacetylase, low back pain, disc biology, chromatin regulation, Experimental & Molecular Medicine