Category: 7. Science

The first hexagonal-structured diamond was discovered in 1967 within the Canyon Diablo meteorite that hit Arizona 49,000 years ago. It was widely believed to have formed from graphite under the intense heat and pressure generated by the impact with Earth.

While all diamonds consist of carbon atoms, they are not limited to the better-known cubic structure. Research teams from around the world have been trying for years to recreate the hexagonally arranged variant with its distinct atomic stacking.

In an article published on July 30 by the peer-reviewed journal Nature, the Chinese researchers detailed how they achieved high-purity hexagonal diamond crystals of 100 micrometres in size, providing definitive proof of the material’s macroscopic existence.

The team combined expertise from the Centre for High Pressure Science and Technology Advanced Research and the Chinese Academy of Sciences’ Xian Institute of Optics and Precision Mechanics.

While other teams around the world claimed to have synthesised the material, previous attempts typically yielded cubic diamonds or mixed-phase samples rather than pure hexagonal structures, according to the paper’s corresponding author Luo Duan.

It’s been a space-heavy week for science news, with a team of engineers winning a design competition for a spaceship that could carry 2,400 passengers on a one-way trip to Alpha Centauri. The craft’s designers say it could be built in as little as 25 years.

The downside? The journey will take roughly 400 years, and the first generations of the ship’s inhabitants will have to live in Antarctica for 80 years to get used to interstellar isolation (so most of them won’t even get to go into space). It’s a shame humans can’t just hibernate — although, according to another study this week, our species does appear to carry dormant genes that give us untapped “superpowers” related to this torpor state.

The spore is ten times thinner than a human hair, but that is enough to make it a lethal threat. It only needs an ant to walk over it. The insect has no way of knowing, but at that very moment the tiny cell has attached itself to its exoskeleton, penetrated it, and now a parasite is developing inside, growing until it reaches the nervous system. No one can explain how it does this, but in a very short time the fungus takes control of the ant and bends it to its will.

Days later, in a completely unusual move, the little worker ant leaves the path that connects its anthill with the rest of the jungle. It climbs up a tree trunk until it finds a leaf — not too high, not too low — and bites into it with its mandibles. The ant dies, and its executioner finally reveals itself: from the insect’s head sprouts the imposing stalk of an Ophiocordyceps unilateralis, which now releases spores that will patiently disperse until they find new victims.

This infectious fungus, specialized in attacking ants, altering their behavior, and using them to reproduce, exists in the real world but became famous through fiction. In the video game and TV series The Last of Us, there are fungi that parasitize and zombify humans. These are the Cordyceps, relatives of the ones that target ants. But it’s not the only parasite capable of controlling its host. In fact, there is a name for the victims: zombie insects.

American science journalist Mindy Weisberger has just published Rise of the Zombie Bugs, a book that explores the unsettling phenomenon of zombification in nature, far from the Hollywood spectacle.

“There’s something about zombies that I find particularly intriguing,” Weisberger says in a video interview with EL PAÍS from New York, where he lives and collaborates with museums and science documentaries. “The idea of losing free will, of something external controlling your body while you’re still technically alive, is unsettling,” he adds. Parasites reproduce by rewriting the neurochemistry of their victims, transforming them into “the living dead.” Viruses, worms, fungi, and wasps: the list of zombie-like species in the real world is long and varied.

Although these unsettling relationships between species have existed for millions of years, entomology still doesn’t fully understand how they work. “Scientists are just beginning to unravel the details. How they manipulate, what chemical pathways they use, what neural mechanisms are involved — it’s all very mysterious and fascinating,” explains Weisberger. But to understand zombification, we must first understand parasitism.

The term “parasite” was first used in the 16th century, and its origins can be traced back to ancient Greek, where parasitos means “person who eats at the table of another.” “It’s different from a symbiotic relationship,” Weisberger writes, “because in those cases, both living beings enjoy the benefits. When it comes to a parasite, it’s the only one who benefits from the arrangement.”

The most cinematic example — and the favorite of the science communicator — is that of the so-called “zombie snail.” The worm Leucochloridium paradoxum begins its life in bird droppings, where its eggs are accidentally ingested by a snail.

Once inside, the larvae hatch and travel to the mollusk’s tentacles, swelling and shaking them to resemble a caterpillar. The parasite takes control and forces the snail to leave the shadows and expose itself in broad daylight. Birds, attracted by the caterpillar-like appearance, peck at it, allowing the worms to enter the bird’s digestive system. And so, the cycle begins again. “It’s a complex cycle, but visually impressive and evolutionarily fascinating,” notes Weisberger.

Millions of years of parasitic relationships

The first evidence of a parasitic relationship comes from the sea and dates back 500 million years. These are the remains of small invertebrates called brachiopods that inhabited an ocean that occupied present-day southern China. Preserved parts of their shells reveal mineralized tubes constructed by tiny worms that likely stole food from their hosts.

“The parasitologists I interviewed for the book joke that the first life form was free, and the second was parasitic,” says the author. Of the approximately 7.7 million known animal species, an estimated 40% are parasitic. And the strategy has evolved independently at least 223 times throughout history.

When asked how these various controlling strategies developed, Weisberger responds that for researchers, “it’s difficult to know because parasitic behavior is complex, and many relationships cannot be replicated in a laboratory.” But there are clues.

It is known, for example, that many zombifying parasites do not introduce new substances into their victims but rather manipulate the chemistry already present in their hosts and use it to their advantage. In other cases, it is almost as if they “drug” them, as happens with jewel wasps. These insects turn cockroaches into functional zombies that serve as living shelters for their larvae.

The process is surgical: the wasp first stings the cockroach in the thorax, paralyzing its front legs. Then, it delivers a second sting directly into the brain, where it takes control of decision-making and the escape instinct, causing the cockroach to obey and ultimately become fresh food for the wasp larvae, which eat it alive. “Although this is exceptional, and in most cases there is no chemical silver bullet explaining the behavioral change,” the author notes.

The case of mammals

The hit TV adaptation of The Last of Us, in which a fictional species of fungi triggers an apocalypse, reopened a debate that occasionally resurfaces in some corners of the internet. Could a parasite zombify a person? “No, I don’t think we have to worry about a fungal zombie pandemic,” Weisberger says.

Fungi don’t thrive inside bodies with high temperatures like those of mammals. “In fact, it’s thought that one of the reasons we evolved with such a high body temperature was precisely to protect ourselves against fungal infections,” the author explains.

For now, insects are the only ones who should worry about these fungi. Oscar Soriano, researcher at the Department of Biodiversity and Evolutionary Biology at the National Museum of Natural Sciences in Madrid, agrees. “I find it more complicated for one of these parasites to manage to control more complex structures, like the brain of a mammal,” he says. Although he adds a caveat: “Still, look at the effect drugs have. Some manipulate the human brain by producing hallucinations and making it act accordingly. Maybe it’s just a matter of the right molecule appearing.”

The relationships between parasites and zombie insects are highly specialized. They are very precise mechanisms that have taken millions of years of evolutionary trial and error. “To think that such a unique parasite could suddenly jump in and take over a human brain doesn’t make much sense from an evolutionary perspective. It would be like trying to use one key for a completely different lock,” says Weisberger.

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The Expedition 73 crew briefly grew to 11 members last Saturday (Aug. 2) but then quickly receded back to seven with the departure on Friday (Aug. 8) of SpaceX’s four-person Crew-10 mission. Most of this week was spent familiarizing the new arrivals with their home for the next six to eight months and preparing for the departure of Endurance, Crew-10’s Dragon capsule.

Orbital observation

“Want to go to the moon or even Mars? I do!”

For more than 30 years, scientists have studied how the myogenic determination gene number 1 (MYOD) protein binds DNA to modify the gene expression of muscle stem cells. Similar to the instant kung fu education Keanu Reeves downloaded in “The Matrix,” MYOD plugs into muscle stem cell DNA and reprograms the cells to build muscle.

MYOD also comes to the rescue when muscle tissue needs to be repaired after injury or to restore minor damage that occurs with athletic training or other physical activity. The transcription factor rallies nearby muscle stem cells to expand in number and become muscle cells capable of regenerating harmed muscle fibers.

Like Spiderman hiding in plain sight as the unassuming photojournalist Peter Parker, this activator of genes specific to muscle has been harboring a secret identity. Scientists at Sanford Burnham Prebys and their international colleagues published findings August 6, 2025, in Genes and Development demonstrating that MYOD has its own Jekyll-and-Hyde twist, turning from a gene activator to a gene silencer.

“If you think of a cell like a house, then gene expression can be seen as the furniture that plays a major part in defining its unique identity,” said Pier Lorenzo Puri, MD, professor in the Center for Cardiovascular and Muscular Diseases at Sanford Burnham Prebys and the senior and co-corresponding author of the study.

“We focus a lot on MYOD’s traditional role of bringing in the new furniture appropriate for a muscle cell, but there is a critical first step of clearing out the old furniture to reset the cell’s identity.”

The research team examined MYOD binding events in human fibroblast cells during the process of MYOD reprogramming them into skeletal muscle cells. This experimental setting mimics the physiological process of muscle stem cells reprogramming into the myogenic lineage that occurs during muscle regeneration, and indeed the results were validated within the context of muscle regeneration following myotrauma in a mouse model. 

One-third of the binding events were found at the conventional MYOD binding sites (the myogenic E-box motifs) at regulatory elements of the genome, consistent with MYOD’s traditional role as a gene activator. More than one-half of the binding events, however, occurred at the regulatory elements of downregulated genes, where DNA is packaged in such a way as to be less accessible to being transcribed into proteins, and coincided with the presence of DNA binding sites other than the E-box motifs. This finding challenges the dogma that historically restricts MYOD DNA binding properties to the E-box motifs.

Furthermore, the scientists observed that the MYOD binding events associated with gene repression were found at genes involved in cell growth, cell proliferation, cell-of-origin as well as alternative cell lineages. This observation fits into the proposed new role of MYOD as a driver of cell reprogramming by removing the cell’s prior gene expression “furniture.”

“We discovered that MYOD has the ability to promiscuously bind the DNA at previously unexpected places,” said Puri. “These locations were occupied by transcription factors that were promoting the expression of the cell’s origin lineage genes, so MYOD is binding there to erase the previous lineage prior to turning cells into the myogenic lineage.”

Puri and the team see their findings as an opportunity to expand current ideas about how transcription factors operate.

“We have provided seminal evidence that the same transcriptional activator can also play a repressor role at the very beginning of the process of cell transdifferentiation or reprogramming,” said Puri. “Transcription factors are way more versatile than we thought, and this newfound versatility is dictated by where and how they bind to DNA.”

Puri says that the group’s findings regarding cellular reprogramming may help advance efforts to develop regenerative medicine therapies and to better understand the process of cellular reprogramming itself.

“In regenerative medicine, we hope to treat certain medical conditions by turning one cell type into another, one pathological cell into one physiologically normal or even therapeutic cell,” said Puri. “And now we know that an important task is the repression of the previous lineage’s gene expression furniture.”

Puri also emphasized MYOD’s role in filtering out competing biochemical signals during cellular reprogramming.

“There are a variety of growth factors or regeneration cues that typically encounter these cells during the regeneration period,” said Puri. “MYOD is able to be very selective in repressing most of the gene expression that would be activated by these cues in order to curate the proper program for building muscle.”

Next, the research team plans to explore what happens when MYOD’s repression of the cell’s prior identity is incomplete. This phenomenon may help explain why some athlete’s muscles recover better as they get older or why some people suffer from the age-related muscle mass deterioration and frailty known as sarcopenia at a younger age.

“It may be that small alterations in MYOD’s silencing role are tolerated by the body but progressively impair muscle function,” said Puri. “Better understanding this concept may have an enormous impact in terms of biomedical applications for regenerative and sports medicine for athletes and sarcopenia patients.”

Puri shared that children suffering from muscular dystrophy experience a transition period called the honeymoon. For a length of time that varies with each child, their bodies can still deal with the disease by regenerating their muscle.

“If we can better understand this honeymoon period, then we may be able to use regenerative medicine approaches to extend it for as long as possible,” said Puri.

New computer simulations that model every atom of a protein as it folds into its final three-dimensional form support the existence of a recently identified type of protein misfolding. Proteins must fold into precise three-dimensional shapes – called their native state – to carry out their biological functions. When proteins misfold, they can lose function and, in some cases, contribute to disease. The newly spotted misfolding results in a change to a protein’s structure – either a loop that traps another section of the protein forms when it shouldn’t or doesn’t when it should – that disrupts its function and can persist in cells by evading the cell’s quality control system. The simulated misfolds also align closely with structural changes inferred from experiments that track protein folding using mass spectrometry, according to the team led by researchers at Penn State.

“Protein misfolding can cause disease, including Alzheimer’s and Parkinson’s, and is thought to be one of the many factors that influence aging,” said Ed O’Brien, professor of chemistry in the Eberly College of Science, a co-hire of the Institute for Computational and Data Sciences at Penn State and the leader of the research team. “This research represents another step forward in our attempt to document and understand the mechanisms of protein misfolding. Our aim is to translate these fundamental discoveries into therapeutic targets that could help mitigate the impacts of these disorders and even aging.”

A paper describing the research appeared today (Aug. 8) in the journal Science Advances.

Proteins are composed of long strings of units called amino acids. A protein’s function relies on the sequence of those amino acids along the string, which determines how the string will fold into a three-dimensional structure. Sections of the protein can fold into helices, loops, sheets and various other structures which allows them to interact with other molecules and perform their functions. Any mistake during this folding process can disrupt these functions.

The new class of misfolding, recently identified by the O’Brien Lab, involves a change in entanglement status in the protein’s structure. Entanglement refers to sections of the string of amino acids looping around each other like a lasso or a knot. Sometimes an entanglement can form when it shouldn’t be there and sometimes an entanglement that is part of the protein’s native structure doesn’t form when it should.

“In our previous study, we used a coarser-grained simulation that only modeled the protein at the amino acid level not the atomic level,” said Quyen Vu, first author of the paper and a postdoctoral researcher in chemistry at Penn State who started the research as a graduate student at the Polish Academy of Sciences. “But there was concern in the community that such a model might not be realistic enough, as the chemical properties and bonding of the atoms that make up amino acids influence the folding process. So, we wanted to make sure we still saw this class of entanglement misfolding with higher-resolution simulations.”

The team first used all-atom models of two small proteins and simulated their folding. They found that both small proteins could form the misfolds just like in their coarser-grained simulations. However, unlike in their previous simulations, which modeled normal-sized proteins, the misfolds in these small proteins lasted only a short time. 

“We think that the misfolds in our previous simulations persisted for two main reasons,” Vu said. “First, to fix the misfold required backtracking and unfolding several steps to correct to entanglement status, and second, the misfold can be buried deep inside the protein’s structure and essentially invisible to the cell’s quality control system. With the small proteins there were fewer steps and less to hide behind so the mistakes could be quickly fixed. So, we simulated a normal size protein at the atomic scale and saw misfolding that persisted.”

The team also tracked folding of the proteins used in their simulations experimentally. While they couldn’t directly observe the misfolds in the experiments, structural changes inferred using mass spectrometry occurred in the locations that misfolded in their simulations.

“Most misfolded proteins are quickly fixed or degraded in cells,” O’Brien said. “But this type of entanglement presents two major problems. They are difficult to fix as they can be very stable, and they can fly under the radar of the cell’s quality control systems. Coarse-grain simulations suggest that this type of misfolding is common. Learning more about the mechanism can help us understand its role in aging and disease and hopefully point to new therapeutic targets for drug development.”

In addition to Vu and O’Brien, the research team includes Ian Sitarik, graduate student in chemistry; Yang Jiang, assistant research professor in chemistry; and Hyebin Song, assistant professor of statistics, at Penn State; Yingzi Xia, Piyoosh Sharma, Divya Yadav, and Stephen D. Fried at Johns Hopkins University; and Mai Suan Li at the Polish Academy of Sciences.

The U.S. National Science Foundation, the U.S. National Institutes of Health and the Polish National Science Centre funded the research. The research was supported in part by the TASK Supercomputer Center in Gdansk, Poland; the PLGrid Infrastructure in Poland; and the Roar supercomputer in the Institute for Computational and Data Sciences at Penn State.

Fighting off pathogens is a tour de force that must happen with speed and precision. A team of researchers at CeMM and MedUni Vienna led by Christoph Bock and Matthias Farlik has investigated how macrophages-immune cells that are the body’s first responders-master this challenge. Their study, published in Cell Systems (DOI: 10.1016/j.cels.2025.101346), offers a time-resolved analysis of the molecular processes that unfold when these cells encounter various pathogens. They developed a new method that combines gene editing and machine learning, which identified key regulators of macrophage immune responses.

Macrophages (Greek for “big eaters”) deserve their name: their job is to recognize invading pathogens such as bacteria or viruses, engulf them and break them down into their biochemical building blocks. Macrophages are also messengers: they release various signals to recruit other immune cells, trigger inflammation, and present digested fragments of pathogens on their surface, guiding the adaptive immune system to develop long-term immunity.

Macrophages encountering a pathogen are under immense pressure. If they react too late or not decisively enough, an infection may become fatal. But an overshooting immune response is equally damaging. Within a very short time, a tailored immune response must be initiated: cascades of biochemical reactions triggered, thousands of genes activated, and an arsenal of substances produced-each response tailored to the specific pathogen encountered.

Network of regulators uncovered

To understand how macrophages coordinate this multitude of tasks, the team led by Christoph Bock (CeMM Principal Investigator and Professor at MedUni Vienna) and Matthias Farlik (Principal Investigator at the MedUni Vienna) exposed macrophages from mice to various immune stimuli that mimic bacterial or viral infections. They tracked the changes inside the cells by measuring gene activity and DNA accessibility every few hours, establishing a molecular timeline of how the regulatory programs unfold step by step.

Next, the team identified regulatory proteins that orchestrate these programs, using CRISPR genome editing to produce hundreds of gene knockouts and single-cell RNA sequencing to characterize the genetically perturbed cells. This innovative method uncovered a network of several dozen regulators that share the responsibility of triggering the most appropriate immune response. The identified regulators include many “usual suspects” such as the JAK-STAT signaling pathway, but also splicing factors and chromatin regulators whose role in immune regulation is not well understood.

It is impressive how much complexity there is in this ancient part of our immune system, which we share with sponges, jellyfish and corals. Thanks to the advances in CRISPR screening technology, we can systematically study the underlying regulatory programs.”

Christoph Bock, senior author

In this review, the authors present recent findings that uncover a previously unappreciated nuclear signaling hub: the PIPn-p53 signalosome. This complex not only modulates AKT activation within the nucleus but also integrates two major oncogenic pathways-p53 dysregulation and PI3K-AKT amplification-into a unified mechanism driving cancer cell migration and invasion.

Key points of the review include:

1. Nuclear PIPn signaling expands beyond classical models: Phosphoinositides, long thought to be confined to plasma and endomembranes for cytoplasmic signaling, are now shown to form active signaling complexes in the nucleus, reshaping our understanding of lipid-mediated regulation.
2. Wild-type and mutant p53 serve as nuclear scaffolds: Both forms of p53 anchor nuclear PIPns and facilitate the assembly of lipid-protein complexes (signalosomes), directly influencing gene expression, chromatin remodeling, and cytoskeletal dynamics.
3. De novo AKT activation in the nucleus: Unlike canonical membrane-bound activation, nuclear AKT is activated by PtdIns(3,4,5)P₃ generated by the PIPn-p53 complex. This activation promotes cancer cell survival and migration-particularly under stress.
4. Therapeutic implications: Disruption of the nuclear PIPn-p53 signalosome, especially in mutant p53-driven cancers, could impair metastasis. Targeting nuclear-specific PIPn enzymes or restoring p53 function may synergize with PI3K/AKT inhibitors to suppress cancer dissemination.

This review highlights the nuclear PIPn-p53 signalosome as a central regulator of cancer cell motility and a promising target for metastasis therapy. The work entitled “The Nuclear Phosphoinositide-p53 Signalosome in the Regulation of Cell Motility” was published in Protein & Cell (Advance access May 26, 2025).

An international research team involving the Leibniz Institute on Aging – Fritz Lipmann Institute (FLI) in Jena, the Scuola Normale Superiore Pisa, and Stanford University has discovered that in the aging brain, certain proteins are lost even though their mRNA blueprints remain intact. The reason for the loss is not increased degradation, but rather a manufacturing error: ribosomes get stuck on sections rich of basic amino acids, preventing the production of important proteins needed for DNA repair and ribosome assembly. This finding provides new insights into brain aging and neurodegenerative diseases.

Proteostasis describes the balance of proteins in cells, which includes the continuous production of new proteins, their correct folding, and the degradation of damaged or redundant proteins. This balance is essential for cell health; if it is out of balance, misfolded or redundant proteins can accumulate—with potentially harmful consequences. Such dysfunctions are a typical feature of aging and are closely linked to diseases such as Alzheimer’s and Parkinson’s.

An international research team from the Leibniz Institute on Aging – Fritz Lipmann Institute (FLI) in Jena, the Scuola Normale Superiore in Pisa, and Stanford University has now investigated how the aging process influences proteostasis in the brain. In the process, they identified a central mechanism that disrupts proteostasis in the aging brain—with far-reaching consequences. The results have now been published in the journal “Science”.

Model organism killifish provides precise insights

The brain of the short-lived killifish (Nothobranchius furzeri), an established model organism in aging research that shows typical age-related changes in the brain, such as neurodegenerative processes, was investigated.

The team comprehensively analyzed how gene expression is regulated during aging—from the transcription of genetic information (transcriptome) to protein production by ribosomes (translatome) to the actual composition of the proteins formed (proteome). “This multi-step approach allowed us to determine very precisely at which level age-related changes occur and which mechanisms are disrupted,” explains Domenico Di Fraia, former graduate student of the FLI and co-first author of the study.

Protein loss despite intact blueprint

The study focused on a remarkable observation: many proteins, especially those with numerous basic amino acids (e.g., arginine, lysine), decreased significantly in the aging brain. These proteins play a central role in DNA and RNA processing and in the formation of ribosomes. Their absence can have far-reaching cellular consequences.

Surprisingly, the mRNA, i.e., the corresponding blueprint for these proteins, was present in normal amounts. “This was a clear sign to us that the problem lay not in the degradation but in the production of the proteins,” explains Alessandro Ori, associated research group leader at the FLI and senior author of the study.

Further analyses showed that the ribosomes—the cell’s “protein factories” that produce proteins from mRNA blueprints—became stuck on sequences containing basic amino acids. The ribosomes “paused” or even collided, preventing the corresponding protein from being completed correctly or even formed initially. This is an indication of a specific disorder of translation in the aging brain.

These disorders mainly affected proteins responsible for important central tasks such as DNA repair, RNA processing, cell division, and energy production in the mitochondria. They are therefore closely linked to many already known “hallmarks of aging”—typical biological characteristics of aging.

Translation disrupted – not protein degradation

To rule out the possibility that the protein loss was not based on increased degradation, the team specifically blocked the proteasome—the cellular “waste disposal system.” This ensures the quality of proteins by breaking down damaged, misfolded, or no longer needed proteins, thereby helping to maintain the function and stability of cellular processes.

“Although this changed the proteome, the loss of basic proteins remained. So, they were not degraded, but apparently not produced correctly in the first place. This confirmed our assumption that the cause lies at the level of translation— i.e., protein biosynthesis,” continued Antonio Marino, former graduate student of the FLI and co-first author of the study.

Chain reaction in the aging brain

Using an integrative model, it was also shown that reduced ribosome function during aging affects the production of certain proteins more than others. Some mRNAs are even read more efficiently because there are fewer “traffic jams,” while others are hardly read at all. This results in a kind of chain reaction: missing ribosomes promote further changes in translation and further contribute to modify the protein composition of old brains.

“Proteins in the mitochondria and nervous system are particularly affected,” adds Alessandro Ori. “This imbalance disrupts the balance of proteins in the brain and could be a possible trigger for age-related diseases such as Alzheimer’s or Parkinson’s.”

Groundbreaking findings for aging and dementia research

The study provides the first conclusive explanation for the phenomenon of mRNA and protein levels often no longer matching in the aging brain, which is also known to occur in humans. The reason is a malfunction in protein synthesis, in which ribosomes become stuck. “We have identified a weak point in the cellular machinery that increasingly fails with aging, “This malfunction could play a central role in the development of neurodegenerative diseases.”

These findings extend previous observations from studies in nematodes and show that translation disorders are a major factor in the decline of proteostasis in aging vertebrate brains.

In the long term, the findings could open up new possibilities for therapies that specifically prevent the loss of important proteins—and thus counteract neurodegenerative diseases.