TheGIST Issue 18 by TheGIST

GIST The

THE GLASGOW INSIGHT INTO SCIENCE AND TECHNOLOGY

A MOSAIC OF

science

SEPTEMBER 2026 | ISSUE 18

Editorial note Over the past year, our team has worked behind the scenes to bring together yet another exciting collection of pieces that showcase the breadth of science and technology. It has been my absolute privilege to see our writers explore new subjects, turning complex ideas into features and snippets that we hope spark curiosity in our readers.

Across our snippets, we delve into timely topics, from semaglutide and the weightloss revolution to cancer reprogramming, personalised medicine, ribosomal collisions, and the evolutionary potential of the nitroplast. Together, these pieces offer a glimpse into some of the fascinating developments shaping modern science. Our features take a broader look at the connections between science and society. From the pressures of athletic performance and the biophysical roots of ALS to understanding complex scientific ideas, nanomedicine, and sustainable alternatives to antibiotics, these articles explore the diverse ways in which science continues to shape our understanding of the world. What makes this issue particularly exciting is the variety of perspectives it brings together. Each piece approaches science through its own lens, but together highlight the quest for continuing to discover, question and understand the world around us. We are always keen to welcome new voices to theGIST. We are currently looking for new members to join our editorial team, as well as writers interested in contributing to our online web publication and future print editions. If you have an interest in writing, editing, designing or simply a topic you are passionate about, we would love to hear from you! -editor@the-gist.org. If you’d like to read more or stay updated visit – the-gist.org and our Instagram page – @glasgowgist. Putting an issue together is a true team effort, I would like to thank everyone on the editorial team – submissions, snippets, copy-editing to our design and social media team for contributing their time, creativity and enthusiasm. Most importantly a thank you to our readers for continuing to support us. Whether you are already familiar with theGIST or are picking up our magazine for the first time, we hope this issue introduces you to something new, sparks your curiosity, and leaves you with a question worth exploring. Welcome to the latest issue of theGIST. We hope you enjoy reading it as much as we enjoyed putting it together!

Editor-in-Chief: University of Glasgow: Bavishya Tata University of Strathclyde: Khachonphat leesahatsawat Submission Editor: Vi Amara Head of Copy-Editing: Cameron McKeddie Head of Design: Hebatalla Kamaluddin Nurdin Deputy Head of Design: Aliah Tabasam Afzal

about us h n more ere! lear

CONTENTS articles

Sustainable Alternatives to Antibiotics: A battle against the AMR crisis By Kate Walter

By Matthieu Silbermann

Nanomedicine: fighting cancer at the nanoscale By Hebatalla Kamaluddin Nurdin

Beyond the Headline: how to truly own complex ideas

Targeting the Biophysical Roots of ALS By Veneta Salyahetdinova

Built to Compete, Expected to Cope: the price of the play By Holland Morris

snippets

03 08

Reprogramming Cancer Reversal: discovery of switch that resets cell fate

Could the nitroplast be the new powerhouse of the cell?

By Holland Morris

By Jennifer Ann Black

The Ozempic Revolution: how semaglutide is reshaping weight loss

Fighting the Deadliest Skin Cancer: the potential of personalised medicine

By Liam Butler

By Emma Nelson

When Ribosome Collide: how cells detect danger before it’s too late By Eleanor Dickson-Murray

You can access all references through the QR code at the end of each article to explore more about the topic discussed!

reprogra

ing m m

CANCER REVERSAL discovery of switch that resets cell fate

BY GRACE WHELAN EDITED BY DAISY LINTS COPY-EDITED BY BAVISHYA TATA

The team validated their findings in lab-grown organoids, which are miniature, simplified versions of organs grown from stem cells (6). These 3D models mimic the architecture and function of real tissues more closely than traditional flat cell cultures, providing a more realistic environment for testing. By controlling the expression of SOX2 and SOX10 in colon cancer organoids — and later in mouse models — the researchers were able to induce a shift back towards normal cellular behaviour (1).

Despite decades of progress in cancer treatment, therapies such as chemotherapy, radiation, and targeted drugs still face major limitations for example,— toxicity to healthy cells, drug resistance, and the inability to eradicate all malignant cells. One of the fundamental challenges in oncology is the irreversible nature of the cancer cell state: once a cell becomes cancerous, it rarely returns to normal. But what if that transformation could be undone? A new study by the Korea Advanced Institute of Science and Technology offers a striking alternative. The researchers, led by Professor Kwang-Hyun Cho, have identified a molecular "switch" that can revert cancer cells to a normal-like phenotype but only if triggered during a fleeting, unstable phase in their transformation.

This research challenges the dogma that cancerous transformation is a one-way process and introduces the possibility of novel therapies based on cellular reprogramming rather than destruction. Though still in its early stages, if this approach proves scalable and effective across a broader range of tumour types, it could revolutionise cancer treatment, offering options that are more targeted and less toxic, but capable of restoring healthy tissue function rather than just eliminating it.

This phase, known as the critical transition state,— is a tipping point where a cell’s identity is not yet fully fixed as cancerous. To capture and study this rare moment, the team used single-cell RNA sequencing — a powerful method that tracks gene activity in individual cells, revealing subtle differences that bulk methods, which examine several cells at once (3).

Their analysis pointed to two key transcription factors, SOX2 and SOX10, as central players in the decisionmaking process of cell fate (1). Transcription factors act like molecular switches, turning specific genes on or off to control how a cell behaves. SOX2 and SOX10 are particularly well-known for their roles in development and cellular plasticity — the ability of cells to change identity — which makes them prime candidates for reprogramming cancer cells

References

Could the nitroplast be the new powerhouse of the cell? NEW ORGANELLE DISCOVERED IN A MARINE ALGA REWRITES THE EUKARYOTIC RELATIONSHIP WITH NITROGEN BY JENNIFER ANN BLACK EDITED BY DAISY LINTS COPYEDITED BY BAVISHYA TATA

Did you know that Earth’s atmosphere is largely composed of a gaseous element nitrogen? Nitrogen, discovered in 1772, accounts for around 78% of the chemical elements in our air, followed by 21% oxygen, approximately 1% argon and a handful of other gases.

According to these findings, around 100 million years ago, a nitrogen-fixing prokaryote lost independence and became incorporated into B. bigeloweii, remaining as an organelle capable of fixing nitrogen.

But why could this discovery be so important?

Nitrogen sustains our life on Earth, acting as a key ingredient for biological molecules like amino acids (the building blocks of proteins) and DNA (which stores our genetic blueprint). In plants and some bacteria, nitrogen makes up a green pigment called chlorophyll which plants use during photosynthesis, a process that converts light to energy.

It’s estimated that the production of ammonia fertilisers from fossil fuels generates 1.3% of the world’s CO2 emissions, or 450 million metric tons! Now we know a eukaryote can host an organelle capable of nitrogen fixation, dissecting the relationship between B. bigelowii and its nitroplast further may help researchers to harness the power of the nitroplast for use in other eukaryotes and, in time, develop more sustainable and natural agricultural practices.

Ironically, despite the importance of nitrogen, we have little use for it as a gas. Two nitrogen atoms joined together (‘N2’) are very stable and need a huge amount of energy to break apart, so we just breathe it in and out unchanged. If you pick up a traditional biology textbook, you will read that animals and plants (otherwise known as eukaryotes) require nitrogen gas to be chemically converted to ammonia (‘NH3’) via a process known as nitrogen fixation. Until recently, scientists believed that only bacteria (prokaryotes) could ‘fix’ nitrogen. Soil bacteria absorb nitrogen from the air, break it apart with an enzyme called a nitrogenase and then add hydrogen, converting it into ammonia in the soil. Some plants even house nitrogen-fixing bacteria in their roots, for example, peas, soybeans and beans. In the agricultural industry, atmospheric nitrogen can be combined with hydrogen in a factory to generate ammonia for fertilisers that farmers use to grow crops. Scientists based at University of California, Santa Cruz have recently described the astonishing discovery of a novel organelle, the ‘nitroplast’, within a eukaryotic organism called Braarudosphaera bigelowii, a type of single-cell marine algae. Evidence suggests that this organelle was acquired by B. bigelowii through a process of endosymbiosis, the same process that happened billions of years ago leading to the acquisition of the mitochondria, the famous ‘powerhouse’ of the cell, and the chloroplasts that plants use for photosynthesis.

References

Sust

l e b a Alternatives n i a

BY KATE WALTER COPY-EDITED BY CAMERON MCKEDDIE

A Battle Against the AMR Crisis What emerging therapeutic strategies are being developed to combat multidrug‑resistant bacteria, and what are the potential consequences if this global challenge remains unaddressed?

The world is at risk of returning to a preantibiotic era due to the growing threat posed by antimicrobial resistance (AMR). Many bacteria have evolved strong resistance to the drugs that once reliably treated fatal infections and, as a result, annual deaths due to AMR are predicted to rise to 10 million by 2050. Our dependence on last line drugs, such as carbapenems, has increased, however resistance to these is also rising. Following the ‘Golden Era’ of antibiotic discovery in the mid-20th century, the current lack of new antibiotic discovery has left a gap in our ability to respond to infection. The significant economic cost of AMR is estimated to have reached $66 billion per year on treatments alone. This is not a sustainable way of countering the growing threat to public health and, to protect the future of global health, novel therapeutics must be developed.

Predatory Bacteria Bdellovibrio bacteriovorus, a free living bacteria in the Deltaproteobacteria phylum, is a promising example of a predatory bacteria which could be used as an alternative to antibiotics. These natural predators are harmless to humans but attack a diverse array of Gram negatives through specialized invasion and lysis mechanisms. B. bacteriovorus, which is non-toxic to mammals, causes minimal damage to the host by interacting specifically with prey bacteria. The innocuous nature of B. bacteriovorus may be enhanced by its neutral lipopolysaccharide (LPS) layer, which differs from the typical negatively charged LPS layer of pathogenic bacteria. Furthermore, inflammatory responses in the body are avoided through sealing the cell membrane once a bdelloplast has formed inside the prey, thus preventing the release of pathogenic components to the environment.

A major advantage of B. bacteriovorus is its potential to target and disrupt biofilms. Around 80% of bacterial infections involve biofilm formation, including those caused by E. coli in urinary tract infections (UTI) and Pseudomonas aeruginosa in wound and burn infections. These are difficult to treat with antibiotics due to the protective barrier formed which can prevent antibiotic penetration, however B. bacteriovorus possesses a range of proteolytic enzymes which enhance its ability to degrade biofilms and treat these infections. This allows the B. bacteriovorus to prey on bacteria with thick polysaccharide capsules, which are common in biofilms, and to hunt in viscous environments. Tang et al. found that B. bacteriovorus applied to wounds on mice inhibited the development of an E. coli biofilm, compared to in untreated mice where biofilms were established. Research suggests that B. bacteriovorus is more effective against localised infections than in bloodstream infections. In mouse infection models, Russo et al. showed that treatment with B. bacteriovorus following a Yersinia pestis infection of the lungs resulted in an 86% reduction in Y. pestis population within 24 hours. A similar study investigated the effect of the predatory bacteria against Klebsiella pneumoniae infection of the lungs of rats. An 83% reduction in K. pneumoniae colonies was observed in rats treated with B. bacteriovorus, again indicating that the predator can be used successfully to help clear local infections. However, systemic bloodstream infections of K. pneumoniae in rats were unable to be controlled with B. bacteriovorus in a study by Shatzkes et al. Despite the apparent therapeutic benefits of B. bacteriovorus to treat bacterial infections, its use still faces notable limitations. Most importantly, this predator is exclusive to Gram negative bacteria, leaving a potential gap in our efforts to

develop new treatments for Gram positive pathogens. Some of the most concerning drug resistant bacteria include. Methicillin-resistant Staphylococcus aureus and Vancomycin-resistant Enterococci, both of which are Gram positive and therefore unaffected by B. bacteriovorus. Furthermore, complete eradication of pathogenic bacteria is difficult to achieve, and no studies have shown a 100% decrease in prey populations.

Bacteriophages Antimicrobial Peptides Antimicrobial peptides (AMPs) are small, naturally occurring or synthetically produced proteins that act as a rapid first line of defense against pathogens. These oligopeptides play an important role in preventing most infections before symptoms arise and are able to disrupt biofilm formation. In the search for alternatives to conventional antibiotics, AMPs show potential against a wide range of pathogenic bacteria. Naturally occurring AMPs, such as defensin, cathelicidin and protegrin, are produced by lymphocytes and epithelial cells as part of the innate immune system. They exhibit rapid, potent activity against a broad spectrum of pathogens by interacting with specific molecular targets. However, AMPs can also be produced artificially through chemical synthesis or recombinant expression systems.

AMPs employ a broad range of mechanisms to inhibit bacterial growth, classified into membrane-active AMPs and cellular AMPs. As most AMPs are cationic, they bind well to anionic structures on bacterial cell surfaces, making membrane disruption the most common mechanism of action. Bacteria express a variety of molecules on their cell wall such as lipopolysaccharide (LPS) in Gram negatives and lipoteichoic acid in Gram positives, which are negatively charged and serve as targets for AMPs. After binding to the surface, AMPs insert into the membrane, resulting in pore formation and cell lysis. In addition to disrupt bacterial membranes, some AMPs act by targeting intracellular pathways: this includes inhibiting the synthesis of DNA, RNA, proteins and peptidoglycan, as well as enzymes such as proteases. Because AMPs work alongside the immune system as immunomodulators, they are able to enhance the ability of macrophages to recognize and phagocytose pathogens. Several AMPs are currently undergoing clinical trials as treatments for multi-drug resistant bacteria. One example is NNS56, an AMP produced by Paenibacillus thiaminolyticus.

Mussel adhesive protein (MAP), when fused with functional peptides (FP), has demonstrated antimicrobial effects against multiple Gram negative species. A study by Kim et al. tested the susceptibility of four Gram negatives to MAP-FPs, all of which were eradicated after 180 minutes. MAP-FP-2 and -5 showed particular efficacy against E. coli, S. typhimurium, and K. pneumoniae, killing these strains in only 10 minutes. Another interesting possibility involves using AMPs alongside existing antibiotics; Nisin and Ramoplanin (a cell wall inhibiting antibiotic) as a combination therapy has been shown to effectively kill MRSA. This demonstrates the potential of AMPs to enhance antibiotic efficacy and provide new strategies against resistant infections. However, AMPs are not a single sustainable solution to the AMR crisis. Biofilm resistance can arise through interactions with exopolysaccharides, which form a protective matrix that prevents AMP action through electrostatic repulsion. Additional resistance mechanisms have been observed in P aeruginosa and S enterica, including LPS modification to decrease net negative charge and the expression of AMP efflux pumps. Although recent research has highlighted the broad therapeutic potential of novel AMPs, their use in clinical settings remains challenging: high production costs, difficulties in isolation and the need for stable delivery systems all present issues that must be overcome.

Bacteriophages are viruses which infect and kill bacterial cells and represent another potential alternative to antibiotics. Phages are naturally occurring predators of bacteria, responsible for killing 2040% of marine surface bacteria in 24 hours, highlighting their potential clinical application. The specificity of phages for bacteria eliminates any risk to mammals, but maintains their ability to target a broad spectrum of Gram positive and Gram negative bacteria. Advances in modern biotechnology have helped overcome challenges in phage isolation and purification, including the development of bioengineered phages, and as a result, multi-stage clinical trials have demonstrated the successful treatment outcomes for certain infections. The lifecycle of bacteriophages, classified as lytic or lysogenic, ultimately results in the destruction of the bacterial host by exploiting its cellular machinery to replicate and spread. In both pathways, the virus initiates infection by binding to a specific receptor on the bacterial cell surface and injecting its genetic material into the cytoplasm. Specificity of the virus for a particular bacteria is driven by receptors on the cell wall which are not found in eukaryotic cells, thereby preventing human infection. Lytic phages hijack the replication mechanisms of the bacteria to replicate viral DNA and proteins, which then assemble into new virions within the cell. Once a critical mass of phage particles have been produced, enzymes are used to break down the host cell wall, causing lysis which releases new viruses to the environment. These phages are able to infect many new bacteria, repeating the cycle. In contrast, lysogenic phages integrate their genetic material into the bacterial chromosome to form a prophage, which is passed vertically to daughter cells through replication or horizontal. Temperate phages can also contribute to horizontal gene transfer between bacteria, particularly through phage-mediated transduction. Environmental stressors trigger the excision of the prophage, initiating a transition to the lytic cycle and subsequent bacterial death. Recently, an increased number of successful human phage‑therapy treatments have been documented in countries such as France, which has authorised the use of phage therapy for difficult to treat MDR infections. Reported cases include: a patient with systemic Acinetobacter infection who recovered following systemic phage therapy; the effective treatment of a Mycobacterium abscessus infection using a triple phage combination therapy; and the eradication of a resistant Klebsiella infection after a six‑day phage treatment following two years of unsuccessful antibiotic therapy. Another notable example is the use of predatory viruses to clear urinary tract infections,

demonstrated by Ujmajuridze et al. in a multi-stage trial. Pyo bacteriophage was administered to patients with UTIs caused by E coli, Streptococcus spp, Enterococcus spp, and P aeruginosa, and in six out of the nine patients investigated, Pyo phage therapy reduced pathogen titres with no adverse viral effects recorded. This increasing range of positive phage-therapy outcomes highlights their potential as viable alternatives to antibiotics. Although clinical interest in bacteriophages has grown in recent years, their routine use still faces several challenges. The high specificity of a phage for its host bacteria, while beneficial in preventing human infection, results in difficulty matching the infecting strain of bacteria with an effective viral predator. Furthermore, bacteria can evolve resistance to phages through multiple mechanisms, including receptor modification, prevention of DNA injection and inhibition of phage replication and release. These potential adaptations threaten to result in the emergence of widespread phage resistance if not used correctly. Despite not targeting human cells, the immune system can still recognise phages as foreign. As a result, immune responses to bacteriophages have been observed in humans, which potentially lead to the rapid eradication the phage and reduced efficacy against pathogens.

Multiple compounds have been isolated from endophytic fungi and successfully tested against bacteria. For example, extracts from Papulaspora immersa which inhibited the growth of numerous bacteria including P aeruginosa, S aureus and E coli. These same bacteria were also susceptible metabolites produced by Colletotrichum gloeosporioides, which additionally demonstrated activity against drug-resistant strains such as MRSA. Significant inhibition zones were reported by Xing et al when endophytic fungi within the genera Fusarium, Phoma, and Epicoccum were co-cultured with Bacillus subtilis and Staphylococcus aureus. Other Gram positive bacteria, including Staphylococcus epidermidis and Enterococcus faecalis, were found to be sensitive to extracts from Talaromyces wortmannii by Pretch et al. Collectively, these findings illustrate the broad antimicrobial capabilities of endophytic fungi and highlight their potential to target a wide spectrum of pathogenic bacteria.

Endophytic Fungi Endophytic fungi live in plant tissue asymptomatically and protect their host from disease through symbiotic interactions. The antimicrobial compounds produced by endophytes primarily function to shield plants from pathogenic microbes and have been shown to possess antimicrobial, antiparasitic, anticancer and anti‑inflammatory activities, with the vast array of potential antibiotics being described as a ‘reservoir’ by Deshmukh et al. In vitro studies have demonstrated the ability of endophytic metabolites to inhibit the growth of pathogenic bacteria; however, as of April 2026, no in vivo trials have been performed.

References

Irrespective of their broad potential against pathogenic bacteria, research on endophytic fungi is still at an early stage and there is still much to be discovered. Due to the absence of in vivo studies, it is unclear whether endophytes will exhibit the same biological activity in mammals, and their potential side effects remain unknown. In addition, more efficient and cost‑effective isolation techniques must be developed to facilitate their practical application. Our limited understanding of endophytic fungi presents several challenges that must be addressed before they can be safely and effectively used as therapeutic agents in humans.

The Ozempic Revolution How semaglutide is reshaping weight loss BY LIAM BUTLER EDITED BY DAISY LINTS COPY-EDITED BY CAMERON MCKEDDIE

In the world of weight loss and diabetes, one name keeps making headlines: semaglutide. Marketed as Ozempic and Wegovy (among other names), this game-changing medication is revolutionising how we manage conditions such as obesity and type 2 diabetes. But what makes it so effective, and why is it suddenly so popular? Originally developed as a treatment for diabetes, semaglutide mimics a hormone called glucagon-like peptide-1 (otherwise known as GLP-1), which regulates blood sugar and appetite. By slowing digestion and increasing feelings of fullness, semaglutide not only helps control blood sugar levels, but can also lead to significant weight loss. While Ozempic is approved for diabetes, Wegovy is specifically approved for weight loss, with results from clinical trials suggesting that users could lose more than 10% of their body weight after a year on the treatment (combined with diet changes, exercises, and behavioural support).

With celebrity endorsements from the likes of Elon Musk, the demand for Ozempic and Wegovy has skyrocketed [3]. Many see it as a ‘miracle-drug’, offering a solution for those struggling with obesity. Unlike fad diets or unsustainable weight loss programmes, semaglutide offers a pharmacological approach that directly affects both hunger levels and metabolism. Despite its benefits, the surge in popularity has led to supply shortages, leaving some diabetes patients struggling to access their medication. Unfortunately, some users also report side effects like nausea, vomiting, and even abdominal pain. There’s also concern that once the medication is stopped that weight regain is common, raising questions about long-term use. Semaglutide represents a shift in how we approach obesity. Nowadays, the condition is framed less as people simply eating too much, but more as a medical condition requiring treatment. As more research emerges, the debate is less about whether or not semaglutide works; but more about how to make it accessible, sustainable, and safe for those who need it.

medical necessity or miracle weight loss drug?

References

Beyond the How to truly Headline: own complex ideas

BY MATTHIEU SILBERMANN EDITED BY VI AMARA COPY-EDITED BY BAVISHYA TATA

Every time I read an article on TheGIST, whether it is about the intricate dance of nanoparticles in immunology or the dizzying implications of cosmological models, I feel a familiar tug. It is the excitement of encountering something genuinely new, something that reshapes my understanding of the world. But then there is the second, quieter feeling: the challenge of making that complex information stick. It is one thing to read about DNA origami; it is another to internalize its principles so deeply that you can explain it clearly to someone else, or connect it meaningfully to other fields.

The truth is, our brains are lazy, in a good way. They seek efficiency. If we do not signal that a piece of information is important enough to encode deeply, they will treat it as transient, something that can be discarded to make room for the next shiny thing. For the kind of rich, detailed science found here, that means a significant portion of what we read may never fully consolidate into our long-term knowledge base without a bit more effort.

I have found myself nodding along to brilliant explanations, only to realize a few hours later that the fine details have blurred, or the precise mechanisms have escaped me. This is not a failure of intelligence; it is a common human experience. Our brains are incredible at absorbing novelty, but they are equally adept at letting information slip away if we do not engage with it in specific ways. For an audience as curious and committed to understanding as TheGIST's readers, merely skimming the surface feels like a missed opportunity. We want to do more than just *know about* the latest breakthroughs; we want to *understand* them.

Why your brain needs to sweat a little True understanding is not a passive act. It is a demanding, active process. Think of your brain not just as a storage unit, but as a workshop. When you are genuinely trying to understand something, you are not just putting information into storage; you are actively manipulating it, comparing it, and integrating it with what you already know. This is where our working memory comes into play – it is the mental workspace where we temporarily hold and manage information to complete tasks. Reading about the precise mechanisms of a CRISPR gene edit, for instance, requires you to hold multiple steps and components in mind simultaneously.

The Illusion of Knowing It is easy to mistake familiarity for understanding. I have caught myself doing this countless times. I read an article, recognize the terms, and follow the logical flow. My internal monologue says, "Yes, I get this." But then, if someone asks me to elaborate, to describe the innovative aspect of a new biomedical approach, I might stumble. The words are there, but the deep, interconnected knowledge is not. This superficial grasp comes from how our brains process information. When we read something for the first time, especially complex scientific material, our cognitive system is working hard to take in the sheer volume of new concepts. We are operating primarily on what is known as fluid intelligence – our ability to reason, analyze, and solve novel problems. This is vital for initially grasping new ideas, but it is not enough for long-term retention. Our brain is handling a lot of novel input, and it takes time to process it all effectively. Research points to a general slowdown in processing speed with age (Salthouse, 1996), meaning that the sheer rate at which we can absorb and organize new information might change, making strategies for deeper engagement even more crucial.

What works for me, and what I have seen backed by cognitive science, is active engagement. Instead of just rereading a paragraph about quantum entanglement when it feels fuzzy, I try to explain it out loud in my own words. Even better, I try to explain it to an imaginary, skeptical friend. Can I define the key terms without looking them up? Can I articulate the core idea, its significance, and its challenges? If I cannot, that is a clear signal that I need to go back and wrestle with the material some more. This process forces my brain to retrieve the information, not just recognize it, which significantly strengthens the neural pathways associated with that knowledge. It is a little frustrating, I admit, especially when I just want to glide through an article, but the payoff is immense.

Your variety

mind

craves

How many times have I been halfway through explaining something, only to realize I have missed a critical nuance because I did not probe my own understanding deeply enough?

Sometimes, the best way to understand one complex topic is to step away from it for a moment and engage with another. This might sound counterintuitive. We are often told to focus intensely on one thing. But for learning, mixing things up can be incredibly powerful. This technique, known as interleaved practice, involves alternating between different types of problems or topics within a study session, rather than focusing on one until it is mastered.

This self-assessment is especially important given what we know about how memory can change over time. Studies have shown that our ability to retain rapidly changing information can differ with age, highlighting the need for active strategies to solidify our grasp on new concepts rather than assuming passive absorption is enough.

Building a mental model

Consider TheGIST's diverse content. You might read about the structural biology behind a new vaccine, then switch to an article on black holes, and then move to the cognitive science of decision-making. Instead of hindering your learning, this type of varied exposure can actually enhance it. When you return to the vaccine article after a brief detour into cosmology, your brain is forced to retrieve that specific knowledge from memory, rather than simply relying on its short-term familiarity. This makes the knowledge more durable and more accessible in the long run.

Ultimately, the goal is not just to fleetingly understand a single article, but to build a rich, durable mental model of how the world works – a robust crystallized intelligence (Cattell, 1963). This is the cumulative knowledge and skills we acquire over a lifetime. It is what allows you to read a new article on quantum computing and immediately connect it to your existing understanding of physics, mathematics, and even philosophy. This deeper engagement with science is not about brute force memorization. It is about cultivating habits that encourage your brain to integrate new information effectively. It is about treating every GIST article not just as something to read, but as a challenge to understand, to explain, and to connect. When we put in this effort, the incredible insights shared here become not just fleeting facts, but integral parts of our own intellectual landscape. The reward is a deeper, more resilient understanding of the scientific frontiers that define our age.

I still fail at this sometimes. I get absorbed in one topic and spend hours deep-diving. And while deep-diving has its place, I find that when I interleave, even if it is just switching between two or three different science articles, the connections I make across them are richer, and my overall recall improves. It is about building a more robust and interconnected mental framework, rather than just isolated pockets of information.

The honest check

durable

self-

A crucial skill in navigating complex information is metacognition – the ability to think about your own thinking (Nelson & Narens, 1990). It is about honestly assessing your understanding. When I read something truly mind-bending, like a new theory on the origins of life, I pause and ask myself: do I *really* understand this, or am I just familiar with the words? Do I understand the experimental evidence that backs this up, or just the conclusion? This internal dialogue prevents me from falling into the trap of overconfidence. It is about identifying the specific gaps in my knowledge, rather than just vaguely feeling confused. Sometimes, it means admitting I need to reread a section, or look up a foundational concept I thought I knew. It is an act of intellectual humility, and it makes all the difference. I ask myself this weekly, especially when tackling a new domain or trying to summarize a cuttingedge paper.

References

by Hebatalla Kamaluddin Nurdin Edited by Rui Ling Lee Copy-edited by Bavishya Tata

From precision drug delivery to tackling drug resistance, nanomedicine is offering a new approach in cancer therapy.

Cancer has been one of humanity’s most relentless diseases, claiming millions of lives annually. For decades, scientists have sought the potential cure, but the complexity and heterogeneity of cancer make this a formidable challenge. Unlike bacterial infections, which oftentimes can often be treated with specific choices of antibiotics targeting bacteria-specific structures and processes, cancer is a multifaceted disease driven by uncontrolled cell division, genetic mutations, and an ability to evade the body’s natural defences. Furthermore, as cancer cells originate from healthy cells, traditional chemotherapy innately damages healthy tissues. The complexity of cancer therefore demands increasingly selective and targeted approaches to treatment. Every moment, our cells divide in a highly regulated manner, controlled by precise checkpoints in the cell cycle. Proteins such as p53 and p21 act as cellular guardians, ensuring that DNA damage is repaired immediately before proceeding with the cell division cycle. However, when these regulatory mechanisms malfunction due to genetic mutations, cells may begin to divide uncontrollably, leading to the formation of tumours. These malignant growths create their own blood supply, enabling them to not only consume vital nutrients required by the local healthy cells, but also invade surrounding tissues. The ability to proliferate uncontrollably and metastasise makes cancer treatment extremely challenging and necessitates innovative therapeutic approaches. Established therapies such as surgery, chemotherapy, radiotherapy and immunotherapy have substantially improved cancer treatment, but important limitations remain, particularly regarding treatment specificity and side effects. In recent years, nanomedicine has emerged as a promising tool in oncology, offering new ways to make cancer treatment more precise.

Fighting Cancer at the

How Nanomedicine is Transforming Cancer Therapy? Nanomedicine involves the application of engineered nanoparticles (NPs) to improve drug delivery, enhance therapeutic efficacy, and minimise side effects. These carriers are typically on the nanometre scale and can be engineered to alter how drugs circulate, accumulate and are released within the body. Several mechanisms make these systems particularly interesting for cancer therapy.

Enhanced drug delivery and tumour targeting One of the biggest challenges in cancer treatment is achieving precise drug delivery. Traditional chemotherapy can affect both cancerous and healthy cells, contributing to side effects such as hair loss, immune suppression and damage to healthy tissues. Some nanocarriers can take advantage of the Enhanced Permeability and Retention (EPR) effect. Abnormal and relatively permeable blood vessels in some solid tumours can allow nanoparticles to enter and remain within tumour tissue more readily than in many healthy tissues. However, the extent of the EPR effect can vary considerably between tumour types and individual patients. One well-established example of cancer nanomedicine is Doxil®, a PEGylated liposomal formulation of the chemotherapy drug doxorubicin. Encapsulating doxorubicin within liposomes changes its pharmacokinetics and distribution within the body and can reduce some toxicities associated with conventional doxorubicin, particularly cardiotoxicity, while maintaining antitumour activity in appropriate clinical settings.

ale

nanomedicine

Nano

Controlled and sustained drug release Another advantage of nanocarriers is their potential to control how therapeutic compounds are released. Nanoparticles can be incorporated into delivery systems designed to release drugs gradually rather than all at once. For example, nanoparticlehydrogel systems can act as local drug reservoirs, allowing sustained or stimulusresponsive release of therapeutic compounds. Such approaches may help maintain drug exposure at the target site while reducing unnecessary exposure elsewhere.

Delivering multiple therapies at once Many cancer treatments require combinations of therapeutic agents to achieve optimal results. However, differences in physicochemical properties, pharmacokinetics and biodistribution can make simultaneous delivery challenging. Multifunctional nanocarriers can be designed to co-deliver different therapeutic agents within a single platform.

In cancer chemoimmunotherapy, for example, nanoparticle-based systems have been investigated as a way to deliver chemotherapy together with immunomodulatory agents, potentially improving coordination between the different treatments.

Overcoming drug resistance Cancer cells are also notorious for developing resistance to chemotherapy, rendering treatments ineffective over time. This phenomenon is called multidrug resistance (MDR). MDR is often linked to the tumour microenvironment and the presence of cancer stem cells (CSCs), which often mutate the ability to pump drugs out of the cells through the drug efflux mechanism.

Nanocarriers offer solutions to bypass this resistance through designing effective tumourpenetration and modifying surface of NPs.

nanoparticles and irradiation appropriately targeted.

are

Nanoparticles can also contribute to cancer imaging. Magnetic nanoparticles, including iron oxide-based nanoparticles, have been investigated as contrast agents for magnetic resonance imaging (MRI). Their magnetic properties can alter MRI signals and potentially improve the visualisation and localisation of malignant tissue.

As research continues to advance, the versatility of nanomedicine opens possibilities for increasingly personalised cancer therapies, in which treatments could one day be tailored more closely to the characteristics of an individual patient’s tumour.

Together, these applications demonstrate that nanoparticles can do more than simply transport conventional drugs: they can contribute to emerging strategies for drug delivery, imaging and cancer treatment.

By improving drug delivery, enabling controlled release, facilitating combination therapies and offering strategies to address drug resistance, nanomedicine may help overcome some of the limitations of conventional cancer treatments.

challenges

However, challenges involving safety, scalability, cost, tumour heterogeneity and clinical translation still need to be addressed before many experimental nanotechnologies can become part of routine cancer care.

Despite these advances, several important challenges remain. The design and largescale manufacturing of nanocarriers can be technically complex, and small changes in particle size, composition or surface properties can influence their behaviour in the body. the

Other applications of NPs Beyond the role as drug carriers, NPs can be exploited for different purposes in cancer treatment and diagnosis. For instance, gold nanoparticles have been extensively studied in photothermal therapy (PTT). In this approach, nanoparticles exposed to appropriate wavelengths of light absorb electromagnetic energy and convert it into heat. This localised heating can damage tumour cells and may help limit thermal injury to surrounding tissues when the

The future of nanomedicine in cancer therapy

Safety must also be carefully evaluated. The biodistribution, degradation and clearance of nanoparticles depend strongly on their size, material and surface chemistry. Some nanoparticle formulations may accumulate in organs or interact unexpectedly with proteins and immune cells, making detailed assessment of their biological behaviour essential. Tumour heterogeneity presents another major challenge. Tumours can differ considerably not only between patients but also between regions of the same tumour, meaning that a nanomedicine that accumulates effectively in one tumour may behave differently in another. Manufacturing, reproducibility, tumour biology and our still-incomplete understanding of nanoparticle–biological interactions therefore remain major obstacles to the clinical translation of many experimental nanomedicines Continued research is essential to refine nanoparticle design, improve manufacturing and cost-effectiveness, and ensure safe and reliable clinical applications.

Rather than replacing existing cancer treatments, nanomedicine may increasingly complement them, helping therapies become more targeted, effective and tolerable. As researchers continue to refine these technologies, tiny particles could play an increasingly significant role in the future of cancer treatment.

References

Targeting the Biophysical Roots of ALS Veneta explores how some of the devastating cellular effects of ALS may actually be governed by the laws of electrostatic attraction inside our protein factories — ribosomes.

BY VENETA SALYAHETDINOVA EDITED BY CAMERON MCKEDDIE

Amyotrophic lateral sclerosis (ALS) is a progressive neurological disorder which destroys motor neurons in the brain and central nervous system, and eventually causes the devastating prognosis of complete paralysis. ALS can be caused by genetic mutations. One of the genes that can be affected is C9orf72, which encodes a protein that shares the same name and is involved in autophagy — clearance of cellular waste in the cytoplasm. Of particular interest is the hexanucleotide expansion mutation in this gene, which in essence is a six-letter DNA sequence GGGGCC, repeated many times . The cellular manifestation of this mutation begins once the repeat-containing RNA is translated by the ribosome. The process of translation encapsulates the synthesis of a final product (the protein) by the cellular protein factories (the ribosomes). In this important biological event, mRNA serves as the recipe by which the ribosome builds the correct protein. This leads to the production of highly basic arginine-rich proteins, poly-GR (glycine-arginine) and poly-PR (proline-arginine). It is only then that the genetic mutation takes form in the cell, and this form is a polypeptide (protein) that contains highly basic residues such as arginine (Arg). Due to the charged nature of these polypeptides at bodily pH, it is not surprising that they interfere with normal cellular activity, especially because many components in the cell are charged. This is where the physical manifestation of ALS becomes directly relevant to physical chemistry and intermolecular interactions in the cell. The toxicity is not only genetic in origin, but also expressed through electrostatic interactions involving the ribosome and other charged species. Kriachkov et al. provide one of the most insightful studies on repeats resulting from the C9orf72 mutation. They made several observations. Firstly, stalling during translation was more likely with longer mutated protein products, with some forms of mutation causing nearcomplete stalling at around 75 repeats. Dipeptide repeats containing charged residues such as Arg caused the largest decrease in translation. Kriachkov et al. identified Arg-rich dipeptide repeat (DPR) stalling as a characteristic inducer of translational stress, while also acknowledging that the mechanism remains unclear. In this article, we will explore how charged interactions between the newlyformed polypeptide and the ribosome could influence ALS development.

Independent studies, outside the direct scope of ALS but strongly relevant to it, have explored the effect of charged repeats on the interaction between the newly synthesised protein and the ribosome, and more specifically the ribosome exit tunnel — the structural compartment through which the protein chain is ejected. An important cellular event is co-translational folding, which refers to the process of the protein adopting its three-dimensional structure as it is emerging from the ribosome. One study by Nissley et al. explored how the dynamics of this event are influenced by the ribosome, again highlighting the importance of specific electrostatic interactions. To understand the exact mode of toxicity in ALS, it is worth considering these studies which had a different purpose in mind, but whose findings are highly relevant.

Nissley et al. simulated the ejection of 122 E. coli proteins from the ribosome and compiled their ejection times. This study gives results that are highly coherent with the biophysical manifestation of ALS. One key finding directly relevant to ALS is that newly-formed proteins containing negatively charged residues near one of their ends eject the fastest, while those enriched with positive charge eject the slowest. A direct parallel can be drawn with the arginine-rich nature of DPR repeats in ALS. A highly basic protein in their study, 4DCM, exhibited complete ejection from the exit tunnel in only 23 out of 50 simulation trajectories.

If arginine-rich DPRs in ALS behave as extremely slowejecting newly-formed proteins, their prolonged residence in the ribosomal exit tunnel could increase ribosome density, delay recycling, and create conditions for stalling, subsequent collisions and hence disease progression. A direct parallel to ALS can be drawn here too. Stress granules are often discussed in relation to ALS and other neurodegenerative diseases, and they can be connected to translational inhibition and ribosome-associated stress. Stress granules are RNA-protein condensates found in the cell that form when translation initiation is suppressed, which allows cells to adapt to stress. However, when stress is chronic or unresolved, persistent stress granules become part of the pathological landscape of neurodegeneration in ALS. This is where ribosome recycling becomes relevant. Ribosome-associated quality control (RQC) in healthy cells detects stalled or collided ribosomes, and in turn promotes splitting of ribosomal subunits, and tags incomplete newly-formed proteins for degradation. If ribosomes however remain stalled, collided, or fail to recycle efficiently, broader stress signalling pathways are activated, including the integrated stress response (ISR). In a mouse model, some patterns of ribosome stalling were linked to integrated stress response hallmarks, such as phosphorylated eIF2α. This is highly relevant here because it suggests that stalled ribosomes interacting with arginine-rich newly-formed proteins cause wider cellular stress. Since ISR activation suppresses translational initiation, and stress granules form under conditions of translational inhibition, unresolved ribosome stalling may indirectly feed into stress granule formation. Hence, repeat mutations may contribute to toxicity in more than one way. This is another reason to think that charged interactions involving mutated repeats may drive cellular toxicity through mechanisms similar to those explained by Nissley and colleagues. Unresolved ribosome collisions and unrecycled ribosomes have the potential to be even more detrimental if the standard RQC and ribosome rescue machinery does not work efficiently. There is strong indication that this may be the case in ALS, as reported by Kriachkov and his team. They pointed out that poly-K, a well-known RQC-related stalling substrate, induces a different pattern of RQC gene expression compared to 102xPR. These differential and poorly managed ribosome collisions are worth exploring further, as finding ways to support the natural RQC support system of the cell might be one way to reduce ALS-associated cellular stress.

This is striking evidence that basic residues, through their charged nature, can and do participate in favourable interactions with the ribosomal surface that interfere with healthy translational dynamics. This is a crucial process, because it allows for the ribosomal machinery to be reused in new translational events. Their key finding was that slow ejectors have, on average, 3.3-times higher ribosome density at a particular point in the protein compared with fast ejecting proteins.

Switching gears now, because the centre of the minireview comprises interactions between the basic nature of the protein and the ribosome, thermodynamics should also be taken into account. Streit et al. have emphasised how the thermodynamics of protein folding are affected by the interaction between the ribosome and the mutated protein. They show, through experimental and computational approaches, that the energetics of folding (a key component of forming a functional protein) differ depending on whether a newly-formed protein folds in isolation or folds while emerging from the ribosome.

In a nutshell, the entropic penalty (aka the energy tax) that a protein needs to pay in order to fold into its native form is lower once it is ejected from the ribosome.

This study added additional evidence that basic residues as in ALS are of critical importance in these interactions. To prove this, the researchers used an advanced technique called Nuclear Magnetic Resonance (NMR) spectroscopy. NMR essentially tracks how a molecule’s local environment changes, producing a signature spectrum of signals. When parts of the emerging FLN5 protein interact with the ribosome, their specific signals change — a phenomenon known as line broadening.

This is mainly because while still bound to the exit vestibule of the ribosome in the unfolded state, the protein gets more heavily solvated, which means that a high number of water molecules are in a highly ordered state around it. Upon ejection, the protein is freed from the ribosomal constraints, allowing it to fully collapse and release these trapped water molecules back into the bulk. This massive release of ordered water is very energetically favourable and provides a powerful entropic drive for post-ejection folding of the protein. If we take a look at protein folding in the absence of the ribosome, the protein is less heavily solvated. Hence, the retention of the protein on the ribosome for a certain time serves an entropically important function. These studies might not seem directly related to ALS at first sight, but the energetics of folding dictate whether a polypeptide chain will potentially misfold, which is also a direct route of toxicity in ALS. The ejection times of highly basic residues is abnormally long, which may alter the thermodynamics of folding even more. While still bound to the ribosome, the protein may form intermediate conformations which are not its true native functional state. Streit et al. found that interactions between the ribosome and the nascent chain stabilise the unfolded state entropically. Essentially, the long-range electrostatic interactions between the negatively charged ribosomal surface, largely caused by rRNA, and the protein side residues are responsible for the retention of the nascent chain on the ribosome. In the case of ALS, these basic repeats render those times longer compared to normal proteins, due to the enhanced nature of these electrostatic interactions. The longer the chain stays on the ribosome, the higher the likelihood of either partially folded inactive or toxic conformations forming, or translational stalling of the ribosome and subsequent ribotoxicity through collisions or faulty recycling.

This in turn confirms that the basic parts of FLN5 protein were actively sticking to the ribosome. Interestingly, the team discovered that these changes can be reversed by increasing ionic strength (salt concentration) of the surrounding fluid. Because salt disrupts electrical charges, this observation confirms the electrostatic nature of the interaction between the ribosome and the FLN5 protein. Most excitingly, this proves that these cellular interactions are highly dynamic and could potentially be modified by future medical interventions. Further clarification of what makes these electrostatic interactions favourable in ALS would allow for new approaches to tilt the equilibrium away from stabilisation of the basic chain on the ribosome and hence away from stalling and collisions. A small-molecule approach could be one way through which these interactions can be shielded. On the other hand, modulating stress granule formation dynamics and supporting the natural RQC of the cell may also present viable approaches. Overall, this article proposes that ALS toxicity, at least in the context of C9orf72 arginine-rich DPRs can be viewed not only as a biochemical problem, but also as a physical manifestation inside the cell. The mutation creates a product whose charge, repetition, and supramolecular behaviour alter how it interacts with the ribosome and the wider intracellular environment. If the pathological consequences are a result partly from these interactions, then targeting the biophysical manifestation of the disease may become an additional way of future intervention.

Another insightful study relevant to ALS biophysical manifestation is done by Cassaignau et al., who found that the folding of proteins as they are being made can be interrupted by interactions between the newly-formed protein and the ribosome. To investigate these interactions they studied a specific part (domain) of a protein called FLN5 while it was still tethered to the ribosome. This study again proves the significance of long-range electrostatic interactions. Interestingly, even though 31 residues is the minimum required linker length for the entire FLN5 domain to span outside the exit tunnel of the ribosome, the protein does not fully fold into its native form at this length and remains partially unfolded. This indicates that interactions with the ribosome stay in the way of folding. It is only at a linker length of 41 residues that complete FLN5 folding can be observed.

References

e h t g n Fighti Deadliest D

r e c n a C n Ski

TIAL OF N E T O P THE ALISED PERSON MEDICINE

BY EMMA NELSON

SPECIALIST EDITED BY SAMIYA DASH COPY-EDITED BY BAVISHYA TATA

Melanoma is the deadliest form of skin cancer, claiming 57,000 lives annually. Current treatment focuses on surgery removing the cancerous tumour, followed by radiotherapy and chemotherapy. However, mRNA-4157 offers a more personalised treatment option with reduced side effects and greater effectiveness.

Moderna and Merck have developed this novel treatment particularly for high-risk stage III/IV melanoma, which involves administering mRNA-4157 in combination with KEYTRUDA, an immune checkpoint inhibitor that targets PD-1 (Programmed Cell Death protein 1) increasing its activity towards cancer cells. Therefore, KEYTRUDA enhances the immune response towards cancer cells. mRNA-4157 works by identifying the mutated regions of DNA in a patient’s tumour which form neoantigens. Neoantigens are a type of antigen specific to tumour cells that are a result of somatic mutations in the DNA. These are tumour specific and not normally found in healthy cells, making them ideal targets for immunotherapy.

In clinical trials, mRNA-4157 is provided alongside KEYTRUDA, a monoclonal antibody that binds to and blocks the PD-1/ PD-L1 pathway. By doing this it prevents suppression of the immune response, enhancing the action of mRNA-4157. When used together these drugs have reduced mortality and distant metastasis by 49% and 62% respectively.

This sequence of DNA encoding neoantigens can be transcribed into mRNA and amplified to be used as a prophylactic or vaccine treatment. These neoantigens which are unique to that patient’s tumour cells can then be identified by the innate immune systems cells like dendritic cells which process these neoantigens and present the resulting peptides on MHC class I molecules as they are derived from endogenous antigens. This activates the adaptive immune system's T cells resulting in a specific T-cell response. The immune system generates a primary immune response, training the body to recognise tumour cells so it can now either go on to attack tumour cells in the body or have the immunological memory to attack these cells in the future. Due to this being a targeted immune response there are minimal off target effects, resulting in reduced side effects.

While this treatment has only recently entered Phase 3 clinical trials, it has shown promising results of a future where melanoma might not be as deadly allowing individuals to receive treatment with fewer side effects. This technology has the potential to be applied to other cancers and even serve as a preventative vaccine for high-risk individuals. With continued research, this approach could revolutionise cancer treatment and prevention worldwide.

References

COMPETE

BY HOLLAND MORRIS SPECIALIST EDITED BY SAMIYA DASH COPY-EDITED BY CAMERON MCKEDDIE

Built

Holland explores how studentathletes navigate mental and physical burnout in a system that prioritises performance over wellbeing, revealing how performative strength becomes a survival strategy, and the hidden cost of maintaining it.

The stadium falls silent.

For a moment everything slows; the pass, the set, the swing. The rally stretches longer than usual. The ball comes flying back to your side. Your coach is shouting, teammates on their feet. The only message is to finish. u take one more approach, one more jump, one more swing.

The ball drops to the floor. The game is over. The crowd goes wild and your team rushes to the court. You finally exhale only to feel the soreness set in, sharper now that the adrenaline is gone. That winning feeling is short-lived. For many student-athletes this is the reality behind the performance of a game. A culture that celebrates "toughness". Hidden behind the visible triumph are physical exhaustion and emotional strain, inflamed by the unspoken expectation to keep going no matter how your body or mind feels. When signing up to be a collegiate athlete, it is easy to overlook the physical and emotional distress that quietly becomes part of the job description. As a fresher you arrive feeling like you have something to prove; that you deserve to be there, all while trying to find yourself within a new environment. As a fresher, you are expected to push through all of the mental, emotional, and physical obstacles that you encounter and that push never stops until you are officially done with your sport(s).

EXPECTED TO COPE: THE PRICE OF THE PLAY

For some, reporting their struggles risks opportunities to compete as well as the trust of their team that they worked so hard to earn. They may feel like they are being looked upon as weak, or end up feeding the insecurity of not being good enough to be there at all. Because of this, athletes hesitate to approach their coaches to ask a question or reconsider whether they should be honest about how they are actually doing. Over time, this mindset becomes automatic.

“For the first two years of my collegiate athlete experience, my coach wouldn’t respond kindly to questions or concerns that I had. I ended up struggling to go up to them asking for feedback on what I can do better or what I should do differently. I would have panic attacks before going into their office because of how scared I was” (anonymous). The mental, emotional, and physical distress is real, and unfortunately normalised in collegiate athletics. National research reflects this experience. A 2021 NCAA StudentAthlete Well-Being Survey found that many athletes reported feeling mentally exhausted, overwhelmed, and unable to balance sport with other demands, highlighting how performance pressures often outpace recovery and support structures.

Playing through injury and emotional exhaustion happens more often than most people realise. The fear of falling behind can discourage athletes to be honest with trainers and seek rest. In competitive environments where positions are never guaranteed, a short break or a missed practice can feel like a big risk. A teammate can step into your role and prove that they can do the job just as well or better than you can. This fear is the main reason for many decisions that student-athletes need to make throughout their college careers. An athlete explained, “Coming back from an injury, my teammates would start to make fun of me for taking more time off to make sure I was fully ready. Instead of taking more time off, I went back before I was fully ready and injured myself even more” (anonymous). Another anonymous athlete shared,

“I kept running on a stress fracture for four days before going to the athletic trainer, all because of the pressure forcing me to keep going.” Instead of stopping to recover, athletes often convince themselves that their injury is not serious enough, or the exhaustion is just part of “the grind”. What starts as pushing through discomfort, can deteriorate to constant strain. To accompany this article, a survey was distributed to several student athletes at different universities, with a sample size of 45 athletes. From this survey, approximately 91% of respondents report high personal expectations for themselves being the primary factor driving them to continue even whilst injured, while 43% say they fear losing playing time when reporting an injury. Practices, games, travel, and schoolwork all accumulate, leaving little time to physically, emotionally, and mentally reset. “I was the only setter on my club team so there were times I was extremely exhausted or sometimes sick but I had to play and push through. Otherwise my team wouldn’t have a setter” (anonymous).

Figure 1. Personal expectations were the most abundantly reported factor driving athletes to push through challenges, followed by fear of losing playing time and cultural norms, while external pressures were cited less often.

Over time, the constant pushing through injuries leads to more than physical wear and tear. Studentathletes may feel burnt out from a sport they once loved so dearly. “I was lacking motivation and consistently dreading practice. I had to push through to stay in shape, headed into our championship season” (anonymous). The expectation to always be ready can make exhaustion feel normal, rather than a sign that something needs to change for the better. Mental and emotional health is a growing consideration in collegiate athletics. Resources to support athletes are available, yet many studentathletes struggle to use these services due to limited time, difficulty of access, and lack of trust. As NCAA Champion Magazine notes, many athletes hesitate to seek help because they fear appearing weak, losing their role, or being judged within the competitive culture of college sports. Between early morning practices, lift, classes, treatment, travel, and games, there isn’t much space in athletes' schedules to step away and seek help, even if it is needed. Many schools promote wellness for these athletes and encourage them to ‘take care of themselves’, but athletes often ask the question:

When every minute of your day is structured around a sport, taking time for mental health can feel like falling behind rather than wellbeing. From the conducted survey, approximately 40% of respondents reported that they don’t have the time to get the help that they need, and 17% are answered ‘other’ meaning they are scared to get help and they end up trying to fix it themselves. Others worry about who will know if they asked for help, or whether being honest about stress or anxiety could change how they are being viewed by their team or coaches. The result of getting help is a disconnect between what is being offered and what is actually used. Support systems that are present are not always reachable when athletes need them most. Suppressing struggle has long-term psychological costs. Burnout, anxiety, depression, and identity loss are all consequences that can build over time, and often go unnoticed. When athletes are constantly expected to appear strong, they learn soon enough to disconnect from what they are actually feeling. Pushing through becomes automatic, but so does emotional exhaustion. The sport that once brought excitement can start to feel like an obligation instead of something they love.

“when would I have time?”

Figure 2. Lack of time and doubts about effectiveness were the leading barriers to student-athletes seeking support, with accessibility, scheduling issues, and stigma reported less frequently.

Over time, many athletes begin to tie their entire sense of self to how they perform. When performance drops — because of injuries, fatigue, or mental strain — it can feel like losing not just a role on the team, but a part of who they are. Without the space to acknowledge struggle, athletes are left managing the pressure on their own, carrying the weight of expectation long after the final whistle. One athlete described this shift:

“I have played my sport for almost 12 years now. Ever since I started, I have loved the game. After a couple seasons in college, I started to get burnt out. While I still love my sport, I also started hating it, and I’m still struggling with it now. I dread going to practice, even though it used to be my escape from anxiety. I hate feeling like this, but I don’t know how to get help” (anonymous).

Figure 3. Loss of motivation, burnout, and performance anxiety were the most commonly reported challenges, with sleep disruption and identity struggles also affecting many athletes. Conversation around college athletics has begun to shift. The current expectation asks athletes to prove their strength by ignoring pain, staying silent, and pushing past their limits, while it leaves little room for the real wellbeing of the athlete. The ability to perform should not be a consequence of physical health or personal identity. Strength could be redefined as recognising when to recover, when to speak up, and when to prioritise wellbeing over short-term performance.

References

Some organisations are already starting to move in that direction. Programmes from UK Sport and the English Institute of Sport focus on supporting athletes beyond physical performance by providing mental health education and access to professionals when athletes need help. Campaigns like State of Mind Sport and the Mental Health Charter for Sport and Recreation also work to reduce stigma and encourage more open conversations across sport. Efforts like these reflect a growing understanding that athletes are more than just performers.

Toughness is not merely the ability to play through an injury or exhaustion; toughness is making it possible for athletes to put their best efforts on the court. Means to do so include but are not limited to developing schedules that allow recovery, encouraging conversations about mental health, and valuing athletes as people first and performers second. The final score may show who won the match, but it does not show the cost it took to get there. Redefining what strength means could be the first step to ensure that cost is no longer invisible

When

R ibosome Collide How cells detect danger before it’s too late

BY ELEANOR DICKSON-MURRAY

EDITED BY CAMERON MCKEDDIE

Your body is composed of thousands of different types of proteins that serve a vast range of different functions. In human cells, organelles called ribosomes are responsible for building all of these different types of proteins. Ribosomes bind to messenger RNA (mRNA) and translate this mRNA into a new protein using building blocks called amino acids.

Particularly promising is the overall reduction in PTSD and depressive symptoms, increased happiness and the neurophysiological specificity i.e., only the targeted regions in the brain were affected by neurofeedback. However, these studies could adopt certain improvements including larger sample sizes, controlling for participation motivation, behavioral, and external stimuli effects, and finally using double blinded trials, where neither the participants nor the researchers know which group is receiving the neurofeedback and which are the control group. Through imaging techniques, the scientists found that ZAK, a protein known to sense cell stress, binds to specific parts of ribosomes. When ribosomes collide, two ZAK proteins come together. This pairing up of ZAK proteins initiates a signalling cascade that is protective to the cell, allowing the cell to adapt to stressors rather than succumbing to them.

Think of ribosomes like a chef, where the recipe is the mRNA, the ingredients are the amino acids and the finished dish is the new protein. Hopefully you can now understand just how important ribosomes are to ensuring cells, and your body, continue functioning as normal.

Therefore, these ribosome chefs don’t just make the proteins, they can also help the kitchen run smoothly by acting as an early warning system when things are going wrong. This prevents the kitchen (your cell) from having to close completely and instead means that adaptive and preventative measures can be taken to ensure that proteins continue to be made, and your body is kept happy.

Recent research by Professor Roland Beckmann’s group at the Ludwig Maximilian University of Munich uncovered a further role of ribosomes in sensing when something is wrong within the cell. When making a new protein, like cooking, lots of things can go wrong, such as not having enough amino acids (ingredients) and/or damaged mRNA (recipe). When these issues arise, the ribosome cannot smoothly translate (read) along the mRNA to produce the protein and instead begins to stall. This causes ribosomes to collide with one another and emit a stress signal which ultimately leads to programmed cell death. This new research has found that this collision event acts as an early danger sign to trigger a protective response, like a fire alarm going off when detecting smoke.

References

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ISSUE NO. 18

2026

theGIST

SEPTEMBER 2026