Why can some people easily stop eating when they are full and others can’t, which can lead to obesity?
A Northwestern Medicine study has found one reason may be a newly discovered structural connection between two regions in the brain that appears to be involved in regulating feeding behavior. These regions involve the sense of smell and behavior motivation.
The weaker the connection between these two brain regions, the higher a person’s Body Mass Index (BMI), the Northwestern scientists report.
The investigators discovered this connection between the olfactory tubercle, an olfactory cortical region, which is part of the brain’s reward system, and a midbrain region called the periaqueductal gray (PAG), involved in motivated behavior in response to negative feelings like pain and threat and potentially in suppression of eating.
The study will be published May 16 in the Journal of Neuroscience.
Previous research at Northwestern by co-author Thorsten Kahnt, now at the National Institutes of Health, has shown the smell of food is appetizing when you’re hungry. But the smell is less appealing when you eat that food until you are full.
Odors play an important role in guiding motivated behaviors such as food intake, and — in turn — olfactory perception is modulated by how hungry we are.

Scientists have not fully understood the neural underpinnings of how the sense of smell contributes to how much we eat.
“The desire to eat is related to how appealing the smell of food is — food smells better when you are hungry than when you are full,” said corresponding author Guangyu Zhou, research assistant professor of neurology at Northwestern University Feinberg School of Medicine. “But if the brain circuits that help guide this behavior are disrupted, these signals may get confused, leading to food being rewarding even when you are full. If this happens, a person’s BMI could increase. And that is what we found. When the structural connection between these two brain regions is weaker, a person’s BMI is higher, on average.”
Though this study does not directly show it, the study authors hypothesize that healthy brain networks connecting reward areas with behavior areas could regulate eating behavior by sending messages telling the individual that eating doesn’t feel good anymore when they’re full. In fact, it feels bad to overeat. It’s like a switch in the brain that turns off the desire to eat.
But people with weak or disrupted circuits connecting these areas may not get these stop signals, and may keep eating even when they aren’t hungry, the scientists said.
“Understanding how these basic processes work in the brain is an important prerequisite to future work that can lead to treatments for overeating,” said senior author Christina Zelano, associate professor of neurology at Feinberg.
How the study worked
This study used MRI brain data — neurological imaging — from the Human Connectome Project, a large multi-center NIH project designed to build a network map of the human brain.

Northwestern’s Zhou found correlations to BMI in the circuit between the olfactory tubercle and the midbrain region, the periaqueductal gray. For the first time in humans, Zhou also mapped the strength of the circuit across the olfactory tubercle, then replicated these findings in a smaller MRI brain dataset that scientists collected in their lab at Northwestern.
“Future studies will be needed to uncover the exact mechanisms in the brain that regulate eating behavior,” Zelano said.
The research reported in this press release was supported by the National Institute on Deafness and Other Communication Diseases grants R01-DC-016364, R01-DC-018539, R01-DC-015426 and the Intramural Research Program at the National Institute on Drug Abuse grant ZIA DA000642, all of the National Institutes of Health. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

Chemotherapy kills cancer cells. But the way these cells die appears to be different than previously understood. Researchers from the Netherlands Cancer Institute, led by Thijn Brummelkamp, have uncovered a completely new way in which cancer cells die: due to the Schlafen11 gene. “This is a very unexpected finding. Cancer patients have been treated with chemotherapy for almost a century, but this route to cell death has never been observed before. Where and when this occurs in patients will need to be further investigated. This discovery could ultimately have implications for the treatment of cancer patients.” They publish their findings in Science.
Many cancer treatments damage cell DNA. After too much irreparable damage, cells can initiate their own death. High school biology teaches us that the protein p53 takes charge of this process. p53 ensures repair of damaged DNA, but initiates cell suicide when the damage becomes too severe. This prevents uncontrolled cell division and cancer formation.
Surprise: unanswered question
That sounds like a foolproof system, but reality is more complex. “In more than half of tumors, p53 no longer functions,” says Thijn Brummelkamp. “The key player p53 plays no role there. So why do cancer cells without p53 still die when you damage their DNA with chemotherapy or radiation? To my surprise, that turned out to be an unanswered question.”
His research group then discovered, together with the group of colleague Reuven Agami, a previously unknown way in which cells die after DNA damage. In the lab, they administered chemotherapy to cells in which they carefully modified the DNA. Thijn: “We were looking for a genetic change that would allow cells to survive chemotherapy. Our group has a lot of experience in selectively disabling genes, which we could perfectly apply here.”*
New key player in cell death
By switching off genes, the research group found a new pathway to cell death headed by the gene Schlafen11 (SLFN11). Principle investigator Nicolaas Boon: “In the event of DNA damage, SLFN11 shuts down the protein factories of cells: the ribosomes. This causes immense stress in these cells, which leads to their death. The new route we discovered completely bypasses p53.”
The SLFN11 gene is not unfamiliar in cancer research. It is often inactive in tumors of patients who do not respond to chemotherapy, says Thijn. “We can now explain this link. When cells lack SLFN11 they will not die in this manner in response to DNA damage. The cells will survive and the cancer persist.”

Impact on cancer treatment
“This discovery uncovers many new research questions, which is usually the case in fundamental research,” says Thijn. “We have demonstrated our discovery in lab-grown cancer cells, but many important questions remain: Where and when does this pathway occur in patients? How does it affect immunotherapy or chemotherapy? Does it affect the side effects of cancer therapy? If this form of cell death also proves to play a significant role in patients, this finding will have implications for cancer treatments. These are important questions to investigate further.”
*Turning off genes, one by one
People have thousands of genes, many of which have functions that are unclear to us. To determine the roles of our genes, researcher Thijn Brummelkamp developed a method using haploid cells. These cells contain only one copy of each gene, unlike the regular cells in our bodies that contain two copies. Handling two copies can be challenging in genetic experiments, because changes (mutations) often occur in just one of them. This makes it difficult to observe the effects of these mutations.
Together with other researchers, Brummelkamp has been unraveling processes that are crucial in disease for years using this versatile method. For example, his group recently discovered that cells can make lipids in a different way than previously known. They uncovered how certain viruses, including the deadly Ebola virus, manage to enter human cells. They delved into cancer cell resistance against specific therapies and identified proteins that act as brakes on the immune system, which is relevant to cancer immunotherapy. Over the last years, his team discovered two enzymes that had remained elusive for four decades, and that turned out to be vital for muscle function and brain development.
This research was financially supported by KWF Dutch Cancer Society, Oncode Institute, and Health Holland.

Artificial intelligence (AI) has numerous applications in healthcare, from analyzing medical imaging to optimizing the execution of clinical trials, and even facilitating drug discovery.
AlphaFold2, an artificial intelligence system that predicts protein structures, has made it possible for scientists to identify and conjure an almost infinite number of drug candidates for the treatment of neuropsychiatric disorders. However recent studies have sown doubt about the accuracy of AlphaFold2 in modeling ligand binding sites, the areas on proteins where drugs attach and begin signaling inside cells to cause a therapeutic effect, as well as possible side effects.
In a new paper, Bryan Roth, MD, PhD, the Michael Hooker Distinguished Professor of Pharmacology and director of the NIMH Psychoactive Drug Screening Program at the University of North Carolina School of Medicine, and colleagues at UCSF, Stanford and Harvard determined that AlphaFold2 can yield accurate results for ligand binding structures, even when the technology has nothing to go off of. Their results were published in Science.
“Our results suggest that AF2 structures can be useful for drug discovery,” said Roth, senior author who holds a joint appointment at the UNC Eshelman School of Pharmacy. “With a nearly infinite number of possibilities to create drugs that hit their intended target to treat a disease, this sort of AI tool can be invaluable.”
AlphaFold2 and Prospective Modeling
Much like weather forecasting or stock market prediction, AlphaFold2 works by pulling from a massive database of known proteins to create models of protein structures. Then, it can simulate how different molecular compounds (like drug candidates) fit into the protein’s binding sites and produce wanted effects. Researchers can use the resulting combinations to better understand protein interactions and create new drug candidates.
To determine the accuracy of AlphaFold2, researchers had to compare the results of a retrospective study against that of a prospective study. A retrospective study involves researchers feeding the prediction software compounds they already know bind to the receptor. Whereas, a prospective study requires researchers to use the technology as a fresh slate, and then feed the AI platform information about compounds that may or may not interact with the receptor.

Researchers used two proteins, sigma-2 and 5-HT2A, for the study. These proteins, which belong to two different protein families, are important in cell communication and have been implicated in neuropsychiatric conditions such as Alzheimer’s disease and schizophrenia. The 5-HT2A serotonin receptor is also the main target for psychedelic drugs which show promise for treating a large number of neuropsychiatric disorders.
Roth and colleagues selected these proteins because AlphaFold2 had no prior information about sigma-2 and 5-HT2A or the compounds that might bind to them. Essentially, the technology was given two proteins for which it wasn’t trained on — essentially giving the researchers a “blank slate.”
First, researchers fed the AlphaFold system the protein structures for sigma-2 and 5-HT2A, creating a prediction model. Researchers then accessed physical models of the two proteins that were produced using complex microscopy and x-ray crystallography techniques. With a press of a button, as many as 1.6 billion potential drugs were targeted to the experimental models and AlphaFold2 models. Interestingly, every model had a different drug candidate outcome.
Successful Hit Rates
Despite the models having differing results, they show great promise for drug discovery. Researchers determined that the proportion of compounds that actually altered protein activity for each of the models were around 50% and 20% for the sigma-2 receptor and 5-HT2A receptors, respectively. A result greater than 5% is exceptional.
Out of the hundreds of millions of potential combinations, 54% of the drug-protein interactions using the sigma-2 AlphaFold2 protein models were successfully activated through a bound drug candidate. The experimental model for sigma-2 produced similar results with a success rate of 51%.
“This work would be impossible without collaborations among several leading experts at UCSF, Stanford, Harvard, and UNC-Chapel Hill,” Roth said. “Going forward we will test whether these results might be applicable to other therapeutic targets and target classes.”

In an important step toward more effective gene therapies for brain diseases, researchers from the Broad Institute of MIT and Harvard have engineered a gene-delivery vehicle that uses a human protein to efficiently cross the blood-brain barrier and deliver a disease-relevant gene to the brain in mice expressing the human protein. Because the vehicle binds to a well-studied protein in the blood-brain barrier, the scientists say it has a good chance at working in patients.
Gene therapy could potentially treat a range of severe genetic brain disorders, which currently have no cures and few treatment options. But FDA-approved forms of the most commonly used vehicle for packaging and delivering these therapies to target cells, adeno-associated viruses (AAVs), aren’t able to efficiently cross the blood-brain barrier at high levels and deliver therapeutic cargo. The enormous challenge of getting therapies past this barrier — a highly selective membrane separating the blood from the brain — has stymied the development of safer and more effective gene therapies for brain diseases for decades.
Now researchers in the lab of Ben Deverman, an institute scientist and senior director of vector engineering at the Broad, have engineered the first published AAV that targets a human protein to reach the brain in humanized mice. The AAV binds to the human transferrin receptor, which is highly expressed in the blood-brain barrier in humans. In a new study published in Science, the team showed that their AAV, when injected into the bloodstream in mice expressing a humanized transferrin receptor, crossed into the brain at much higher levels than the AAV that is used in an FDA-approved gene therapy for the central nervous system, AAV9. It also reached a large fraction of important types of brain cells, including neurons and astrocytes. The researchers then showed that their AAV could deliver copies of the GBA1 gene, which has been linked to Gaucher’s disease, Lewy body dementia, and Parkinson’s disease, to a large fraction of cells throughout the brain.
The scientists add that their new AAV could be a better option for treating neurodevelopmental disorders caused by mutations in a single gene such as Rett syndrome or SHANK3 deficiency; lysosomal storage diseases like GBA1deficiency; and neurodegenerative diseases such as Huntington’s disease, prion disease, Friedreich’s ataxia, and single-gene forms of ALS and Parkinson’s disease.
“Since we came to the Broad we’ve been focused on the mission of enabling gene therapies for the central nervous system,” said Deverman, senior author on the study. “If this AAV does what we think it will in humans based on our mouse studies, it will be so much more effective than current options.”
“These AAVs have the potential to change a lot of patients’ lives,” said Ken Chan, a co-first author on the paper and group leader from Deverman’s group who has been working on solving gene delivery to the central nervous system for nearly a decade.
Mechanism first
For years, researchers developed AAVs for specific applications by preparing massive AAV libraries and testing them in animals to identify top candidates. But even when this approach succeeds, the candidates often don’t work in other species, and the approach doesn’t provide information about how the AAVs reach their targets. This can make it difficult to translate a gene therapy using these AAVs from animals to humans.

To find a delivery vehicle with a greater chance of reaching the brain in people, Deverman’s team switched to a different approach. They used a method they published last year, which involves screening a library of AAVs in a test tube for ones that bind to a specific human protein. Then they test the most promising candidates in cells and mice that have been modified to express the protein.
As their target, the researchers chose human transferrin receptor, which has long been the target of antibody-based therapies that aim to reach the brain. Several of these therapies have shown evidence of reaching the brain in humans.
The team’s screening technique identified an AAV called BI-hTFR1 that binds human transferrin receptor, enters human brain cells, and bypasses a human cell model of the blood-brain barrier.
“We’ve learned a lot from in vivo screens but it has been tough finding AAVs that worked this well across species,” added Qin Huang, a co-first author on the study and a senior research scientist in Deverman’s lab who helped develop the screening method to find AAVs that bind specific protein targets. “Finding one that works using a human receptor is a big step forward.”
Beyond the dish
To test the AAVs in animals, the researchers used mice in which the mouse gene that encodes the transferrin receptor was replaced with its human equivalent. The team injected the AAVs into the bloodstream of adult mice and found dramatically higher levels of the AAVs in the brain and spinal cord compared to mice without the human transferrin receptor gene, indicating that the receptor was actively ferrying the AAVs across the blood-brain barrier.

The AAVs also showed 40-50 times higher accumulation in brain tissue than AAV9, which is part of an FDA-approved therapy for spinal muscular atrophy in infants but is relatively inefficient at delivering cargo to the adult brain. The new AAVs reached up to 71 percent of neurons and 92 percent of astrocytes in different regions of the brain.
In work led by research scientist Jason Wu, Deverman’s team also used the AAVs to deliver healthy copies of the human GBA1 gene, which is mutated in several neurological conditions. The new AAVs delivered 30 times more copies of the GBA1 gene than AAV9 in mice and were delivered throughout the brain.
The team said that the new AAVs are ideal for gene therapy because they target a human protein and have similar production and purification yields as AAV9 using scalable manufacturing methods. A biotech company co-founded by Deverman, Apertura Gene Therapy, is already developing new therapies using the AAVs to target the central nervous system.
With more development, the scientists think it’s possible to improve the gene-delivery efficiency of their AAVs to the central nervous system, decrease their accumulation in the liver, and avoid inactivation by antibodies in some patients.
Sonia Vallabh and Eric Minikel, two researchers at the Broad who are developing treatments for prion disease, are excited by the potential of the AAVs to deliver brain therapies in humans.
“When we think about gene therapy for a whole-brain disease like prion disease, you need really systemic delivery and broad biodistribution in order to achieve anything,” said Minikel. “Naturally occurring AAVs just aren’t going to get you anywhere. This engineered capsid opens up a world of possibilities.”

In humans, the energetic cost of pregnancy is about 50,000 dietary calories — far higher than previously believed, a new study found.It takes a lot of energy to grow a baby — just ask anyone who has been pregnant. But scientists are only now discovering just how much.In a study published on Thursday in the journal Science, Australian researchers estimated that a human pregnancy demands almost 50,000 dietary calories over the course of nine months. That’s the equivalent of about 50 pints of Ben and Jerry’s Cherry Garcia ice cream, and significantly more than the researchers expected.Previous estimates were lower because scientists generally assumed that most of the energy involved in reproduction wound up stored in the fetus, which is relatively small.But Dustin Marshall, an evolutionary biologist at Monash University, and his students have discovered that the energy stored in a human baby’s tissues accounts for only about 4 percent of the total energy costs of pregnancy. The other 96 percent is extra fuel required by a woman’s own body.“The baby itself becomes a rounding error,” Dr. Marshall said. “It took us a while to wrap our heads around that.”This discovery emerged from Dr. Marshall’s long-running research on metabolism. Different species have to meet different demands for energy. Warm-blooded mammals, for example, can maintain a steady body temperature and stay active even when the temperature drops.We are having trouble retrieving the article content.Please enable JavaScript in your browser settings.Thank you for your patience while we verify access. If you are in Reader mode please exit and log into your Times account, or subscribe for all of The Times.Thank you for your patience while we verify access.Already a subscriber? Log in.Want all of The Times? Subscribe.

A deadlier version of the infectious disease is ravaging the Democratic Republic of Congo, while the type that caused a 2022 outbreak among gay and bisexual men is regaining strength.With Pride events scheduled worldwide over the coming weeks, U.S. officials are bracing for a return of mpox, the infectious disease formerly called monkeypox that struck tens of thousands of gay and bisexual men worldwide in 2022. A combination of behavioral changes and vaccination quelled that outbreak, but a majority of those at risk have not yet been immunized.On Thursday, the Centers for Disease Control and Prevention warned of a deadlier version of mpox that is ravaging the Democratic Republic of Congo and urged people at risk to be vaccinated as soon as possible. No cases of that subtype have been identified outside Africa so far. But the escalating epidemic in Congo nevertheless poses a global threat, just as infections in Nigeria set off the 2022 outbreak, experts said.“This is a very important example of how an infection anywhere is potentially an infection everywhere, and why we need to continue to improve disease surveillance globally,” said Anne Rimoin, an epidemiologist at the University of California, Los Angeles.Dr. Rimoin has studied mpox in Congo for more than 20 years, and first warned of its potential for global spread in 2010.The C.D.C. is focusing on encouraging Americans at highest risk to become vaccinated before the virus resurges. The agency’s outreach efforts include engaging with advocacy groups and social media influencers who have broad appeal among the L.G.B.T.Q. community. In December, the agency urged clinicians to remain alert for possible cases in travelers from Congo.There are two main types of mpox: Clade I, the type that is dominant in Congo, and Clade II, a version of which caused the 2022 global outbreak. (A clade is a genetically and clinically distinct group of viruses.) Both clades have circulated in Africa for decades, sporadically erupting into outbreaks.We are having trouble retrieving the article content.Please enable JavaScript in your browser settings.Thank you for your patience while we verify access. If you are in Reader mode please exit and log into your Times account, or subscribe for all of The Times.Thank you for your patience while we verify access.Already a subscriber? Log in.Want all of The Times? Subscribe.

Many people are concerned about residues of chemicals, contaminants or microplastics in their food. However, it is less well known that many foods also contain toxins of completely natural origin. These are often chemical compounds that plants use to ward off predators such as insects or microorganisms. These substances are found in beans and potatoes, for example, and can pose potential health risks. However, according to a recent representative survey by the German Federal Institute for Risk Assessment (BfR), only just under half of the respondents (47 per cent) were even aware of plant toxic substances.
The BfR Consumer Monitor Special on naturally occurring plant toxins also revealed that this risk worries 27 per cent. In contrast, residues in food (e.g. from plant protection products) and contaminants, i.e. substances that are not intentionally added to food (e.g. heavy metals), cause concern for 63 and 62 per cent of respondents respectively. “The survey results make it clear that risks of natural origin tend to be underestimated, while risks of synthetic origin tend to be overestimated,” says BfR President Professor Andreas Hensel.”
Raw plant-based foods are consumed frequently by 34 per cent, occasionally or rarely by 45 per cent and very rarely or not at all by 19 per cent.
Which foods with naturally occurring plant toxins do you already know? If this question is asked openly and without pre-selection, potatoes are named first (15 per cent), followed by tomatoes, raw beans (nine per cent each) and mushrooms (five per cent).
Naturally occurring toxic substances worry 27 per cent in the survey. More than half of the respondents (53 per cent) feel poorly informed about plant toxins in food, while only eight per cent feel well informed.
At 63 per cent and 62 per cent respectively, significantly more consumers are concerned about residues or contaminants.
Residues are residualamounts of substances that are used in the production of food. For example, residues can remain in fruit, vegetables or cereals even if plant protection products are used correctly.
Contaminants, on the other hand, are undesirable substances that unintentionally end up in food. They can occur naturally in the environment, arise during the processing of raw materials into food or be released into the environment as a result of human activities. Contaminants are undesirable because they can be harmful to health under certain circumstances.
The study also shed light on the related topic of “mouldy food.” Here, too, there is a clear need for education. Even small amounts of mould toxins can be harmful to the health of humans and animals. Mouldy jam, for example, should therefore always be disposed of completely. Nevertheless, 25 per cent of respondents stated that they only remove the mouldy part. Even in the case of mouldy berries, affected and surrounding fruit should no longer be eaten. Only 60 per cent adhere to this rule.

What features does a robotic guide dog need? Ask the blind, say the authors of an award-winning paper. Led by researchers at the University of Massachusetts Amherst, a study identifying how to develop robot guide dogs with insights from guide dog users and trainers won a Best Paper Award at CHI 2024: Conference on Human Factors in Computing Systems (CHI).
Guide dogs enable remarkable autonomy and mobility for their handlers. However, only a fraction of people with visual impairments have one of these companions. The barriers include the scarcity of trained dogs, cost (which is $40,000 for training alone), allergies and other physical limitations that preclude caring for a dog.
Robots have the potential to step in where canines can’t and address a truly gaping need — if designers can get the features right.
“We’re not the first ones to develop guide-dog robots,” says Donghyun Kim, assistant professor in the UMass Amherst Manning College of Information and Computer Science (CICS) and one of the corresponding authors of the award-winning paper. “There are 40 years of study there, and none of these robots are actually used by end users. We tried to tackle that problem first so that, before we develop the technology, we understand how they use the animal guide dog and what technology they are waiting for.”
The research team conducted semistructured interviews and observation sessions with 23 visually impaired dog-guide handlers and five trainers. Through thematic analysis, they distilled the current limitations of canine guide dogs, the traits handlers are looking for in an effective guide and considerations to make for future robotic guide dogs.
One of the more nuanced themes that came from these interviews was the delicate balance between robot autonomy and human control. “Originally, we thought that we were developing an autonomous driving car,” says Kim. They envisioned that the user would tell the robot where they want to go and the robot would navigate autonomously to that location with the user in tow.
This is not the case.

The interviews revealed that handlers do not use their dog as a global navigation system. Instead, the handler controls the overall route while the dog is responsible for local obstacle avoidance. However, even this isn’t a hard-and-fast rule. Dogs can also learn routes by habit and may eventually navigate a person to regular destinations without directional commands from the handler.
“When the handler trusts the dog and gives more autonomy to the dog, it’s a bit delicate,” says Kim. “We cannot just make a robot that is fully passive, just following the handler, or just fully autonomous, because then [the handler] feels unsafe.”
The researchers hope this paper will serve as a guide, not only in Kim’s lab, but for other robot developers as well. “In this paper, we also give directions on how we should develop these robots to make them actually deployable in the real world,” says Hochul Hwang, first author on the paper and a doctoral candidate in Kim’s robotics lab.
For instance, he says that a two-hour battery life is an important feature for commuting, which can be an hour on its own. “About 90% of the people mentioned the battery life,” he says. “This is a critical part when designing hardware because the current quadruped robots don’t last for two hours.”
These are just a few of the findings in the paper. Others include: adding more camera orientations to help address overhead obstacles; adding audio sensors for hazards approaching from the occluded regions; understanding ‘sidewalk’ to convey the cue, “go straight,” which means follow the street (not travel in a perfectly straight line); and helping users get on the right bus (and then find a seat as well).
The researchers say this paper is a great starting point, adding that there is even more information to unpack from their 2,000 minutes of audio and 240 minutes of video data.

Winning the Best Paper Award was a distinction that put the work in the top 1% of all papers submitted to the conference.
“The most exciting aspect of winning this award is that the research community recognizes and values our direction,” says Kim. “Since we don’t believe that guide dog robots will be available to individuals with visual impairments within a year, nor that we’ll solve every problem, we hope this paper inspires a broad range of robotics and human-robot interaction researchers, helping our vision come to fruition sooner.”
Other researchers who contributed to the paper include:
Ivan Lee, associate professor in CICS and a co-corresponding author of the article along with Donghyun, an expert in adaptive technologies and human-centered design; Joydeep Biswas, associate professor at the University of Texas Austin, who brought his experience in creating artificial intelligence (AI) algorithms that allow robots to navigate through unstructured environments; Hee Tae Jung, assistant professor at Indiana University, who brought his expertise in human factors and qualitative research to participatory study with people with chronic conditions; and Nicholas Giudice, a professor at the University of Maine who is blind and provided valuable insight and interpretation of the interviews.
Ultimately, Kim understands that robotics can do the most good when scientists remember the human element. “My Ph.D. and postdoctoral research is all about how to make these robots work better,” Kim adds. “We tried to find [an application that is] practical and something meaningful for humanity.”

Cerebrovascular accidents, or strokes, are the most common cause of aphasia, a speech disorder of cerebral origin. People with aphasia have a reduced ability to understand or produce speech or written language. An estimated 40% of people who have had a stroke have aphasia. As many as half of them experience aphasia symptoms even a year after the original attack.
Researchers at the University of Helsinki previously found that sung music helps in the language recovery of patients affected by strokes. Now, the researchers have uncovered the reason for the rehabilitative effect of singing. The recently completed study was published in the eNeuro journal.
According to the findings, singing, as it were, repairs the structural language network of the brain. The language network processes language and speech in our brain. In patients with aphasia, the network has been damaged.
“For the first time, our findings demonstrate that the rehabilitation of patients with aphasia through singing is based on neuroplasticity changes, that is, the plasticity of the brain,” says University Researcher Aleksi Sihvonen from the University of Helsinki.
Singing improves language network pathways
The language network encompasses the cortical regions of the brain involved in the processing of language and speech, as well as the white matter tracts that convey information between the different end points of the cortex.
According to the study results, singing increased the volume of grey matter in the language regions of the left frontal lobe and improved tract connectivity especially in the language network of the left hemisphere, but also in the right hemisphere.

“These positive changes were associated with patients’ improved speech production,” Sihvonen says.
A total of 54 aphasia patients participated in the study, of whom 28 underwent MRI scans at the beginning and end of the study. The researchers investigated the rehabilitative effect of singing with the help of choir singing, music therapy and singing exercises at home.
Singing is a cost-effective treatment
Aphasia has a wide-ranging effect on the functional capacity and quality of life of affected individuals and easily leads to social isolation.
According to Sihvonen, singing can be seen as a cost-effective addition to conventional forms of rehabilitation, or as rehabilitation for mild speech disorders in cases where access to other types of rehabilitation is limited.
“Patients can also sing with their family members, and singing can be organised in healthcare units as a group-based, cost-efficient rehabilitation,” Sihvonen says.

Today is International Celiac Day. Celiac disease is a chronic autoimmune condition that occurs in around one per cent of the world’s population. It is triggered by the consumption of gluten proteins from wheat, barley, rye and some oats. A gluten-free diet protects celiac patients from severe intestinal damage. Together with colleagues, chemist Dr Veronica Dodero from Bielefeld University was able to determine new details on how certain gluten-derived molecules trigger leaky gut syndrome in celiac disease.
The key finding of the study: a particular protein fragment formed in active celiac disease forms nanosized structures, the so-called oligomers, and accumulates in a gut epithelial cell model. The technical name of the molecule is 33-mer deamidated gliadin peptide (DGP). The study team has now discovered that the presence of DGP oligomers may open the tightly closed gut lining, leading to the leaky gut syndrome. The study has now been published in the journal ‘Angewandte Chemie’.
Wheat Peptides Causing Leaky Gut
When we eat wheat, our bodies cannot completely break down gluten proteins. This can lead to the formation of large gluten fragments (peptides) in our gut. In cases of active coeliac disease, researchers discovered that the enzyme tissue transglutaminase 2 (tTG2) present in humans modifies a specific gluten peptide, resulting in the formation of the 33-mer DGP. This usually happens in a part of our gut called the lamina propria. However, recent research has shown that this process can also occur in the gut lining.
‘Our interdisciplinary team characterized the formation of 33-mer DGP oligomers through high-resolution microscopy and biophysical techniques. We discovered the increased permeability in a gut cell model when DGP accumulates, reports Dr. Maria Georgina Herrera, the first author of the study. She is researcher at the University of Buenos Aires in Argentina and was a postdoctoral fellow at Bielefeld.
When the intestinal barrier is weakened
Leaky gut syndrome occurs when the lining of the intestine becomespermeable, allowing harmful substances to enter the bloodstream, leading to inflammatory responses and different diseases. In celiac disease, there’s debate about the early stages of increased permeability. The mainstream theory suggests that chronic inflammation in coeliac disease leads to a leaky gut. However, there is a second theory that proposes that gluten’s effects on gut lining cells are the primary cause. In this view, gluten directly damages the cells of the intestinal lining, making thempermeable, which triggers chronic inflammation and potentially leads to celiac disease in predisposed people.

However, since gluten is consumed daily, what molecular triggers lead to the leaky gut in celiac disease patients? If 33-merDGP oligomers are formed, they may damage the epithelial cell network, allowing gluten peptides, bacteria, and other toxins to pass massively into the bloodstream, leading to inflammation and, in celiac disease, autoimmunity.
‘Our findings reinforce the medical hypothesis that impairment of the epithelial barrier promoted by gluten peptides is a cause and not a result of the immune response in celiac patients,’ says the lead author of the study, Dr Veronica Dodero from the Bielefeld Faculty of Chemistry.
The relationship between 33-mer DGP and Celiac Disease
Human leukocyte antigens (HLAs) are proteins found on the surface of cells in the body. They play a crucial role in the immune system by helping it distinguish between self (the body’s own cells) and non-self (foreign substances like bacteria or viruses). In celiac disease, two specific HLA proteins, namely HLA-DQ2 and HLA-DQ8, are strongly associated with the condition. The 33-mer DGP fits perfectly with HLA-DQ2 or HLA-DQ8 and triggers an immune response, leading to inflammation and small intestine villous atrophy. This strong interaction turns the DGP into what scientists call a superantigen. For those affected, a gluten-free diet is the only lifelong therapy.