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SharecloseShare pageCopy linkAbout sharingImage source, ReutersA Japanese woman officially certified as the world’s oldest person has died aged 119. Kane Tanaka was born in 1903, the same year as George Orwell, at a time when Japan was emerging as a global power.She got married a century ago, and had four children. She spent her later years in a Japanese care home, where she enjoyed board games and chocolate.With her death, the world’s oldest person is now Lucile Randon, a 118-year-old French nun. What the Japanese can teach us about super-ageing gracefullyAlso in the year of her birth, Theodore Roosevelt was US president and Edward VII was British king. The Wright Brothers carried out the first controlled flight of their motor-driven airplane and the Tour de France was staged for the first time.The following year, Russia went to war against Japan, suffering a major defeat.Tanaka was the seventh of nine siblings. She married aged 19 and ran various businesses, including a noodle shop.Her husband, whom she hadn’t met before their wedding day, fought in the Second Sino-Japanese War in 1937 while her son fought in World War II, and was held as a captive by the Soviet Union.Tanaka had been due to take part in the torch relay at the Tokyo Olympics but the Covid pandemic prevented her from doing so. On top of having a sweet tooth, she is said to have risen early at her retirement home, spending time on mathematics and calligraphy.At a ceremony recognising her as the world’s oldest person in 2019, she said she was happier than she had ever been.The oldest-ever living person remains Frenchwoman Jeanne Louise Calment, who died aged 122 years and 164 days in 1997.Japan has the most elderly population in the world. More than a quarter of society are aged 65 or older, with diet, healthcare, and the fact many older people continue to work into their later years identified as reasons behind long life expectancies.

It is well known in physics and chemistry that equal charges repel each other, while opposite charges attract. It was long assumed that this principle also applies when enzymes — the biological catalysts in all living organisms — form or break chemical bonds. It was thought that enzymes place charges in their “active centres,” where the chemical reactions actually take place, in such a way that they repel similar charges from the other molecules around them. This concept is known as “electrostatic stress.” For example, if the substrate (the substance upon which the enzyme acts) carries a negative charge, the enzyme could use a negative charge to “stress” the substrate and thus facilitate the reaction. However, a new study by the University of Göttingen and the Max Planck Institute for Multidisciplinary Sciences in Göttingen has now shown that, contrary to expectations, two equal charges do not necessarily lead to repulsion, but can cause attraction in enzymes. The results were published in the journal Nature Catalysis.
The team investigated a well-known enzyme that has been studied extensively and is a textbook example of enzyme catalysis. Without the enzyme, the reaction is extremely slow: in fact, it would take 78 million years for half of the substrate to react. The enzyme accelerates this reaction by 1017 times, simply by positioning negative and positive charges in the active centre. Since the substrate contains a negatively charged group that is split off as carbon dioxide, it was assumed for decades that the negative charges of the enzyme serve to stress the substrate, which is also negatively charged, and accelerate the reaction. However, this hypothetical mechanism remained unproven because the structure of the reaction was too fast to be observed.
Professor Kai Tittmann’s group at the Göttingen Center for Molecular Biosciences (GZMB) has now succeeded for the first time in using protein crystallography to obtain a structural snapshot of the substrate shortly before the chemical reaction. Unexpectedly, the negative charges of enzyme and substrate did not repel each other. Instead, they shared a proton, which acted like a kind of molecular glue in an attractive interaction. “The question of whether two equal charges are friends or foes in the context of enzyme catalysis has long been controversial in our field, and our study shows that the basic principles of how enzymes work are still a long way from being understood,” says Tittmann. The crystallographic structures were analysed by quantum chemist Professor Ricardo Mata and his team from Göttingen University’s Institute of Physical Chemistry. “The additional proton, which has a positive charge, between the two negative charges is not only used to attract the molecule involved in the reaction, but it triggers a cascade of proton transfer reactions that further accelerate the reaction,” Mata explains.
“We believe that these newly described principles of enzyme catalysis will help in the development of new chemical catalysts,” says Tittmann. “Since the enzyme we studied releases carbon dioxide, the most important greenhouse gas produced by human activities, our results could help develop new chemical strategies for carbon dioxide fixation.”
The study involved scientists from the Göttingen Centre for Molecular Biosciences (GZMB), the Faculty of Biology and Psychology, and the Faculty of Chemistry at the University of Göttingen, as well as the Max Planck Institute for Multidisciplinary Sciences, the European Molecular Biology Laboratory (EMBL) Hamburg and the University of Toronto. The publication is dedicated to the memory of co-author Professor Ulf Diederichsen, who passed away last year.
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The human gut — or gastrointestinal system — where food is broken down into nutrients for the body, is an ecosystem that harbours thousands of bacteria species, whose interactions determine its health and susceptibility to diseases. While some microorganisms are harmful, many are beneficial and help keep the human body in good health. It is largely accepted that the more diverse the species of bacteria, the greater capacity the gut has in regulating its health and combating diseases.
Higher levels of certain types of bacteria, or parasites, can result in an unhealthy gut, which causes conditions like inflammation disorders, irritable bowel syndrome, stomach cramps, bloating, diarrhea, and constipation. However, in a study conducted by researchers from the NUS Yong Loo Lin School of Medicine (NUS Medicine), a common parasite that inhabits the gastrointestinal tracts of humans, Blastocystis subtype (ST) 4, was found to be associated with benefits for the gut.
Led by research fellows Dr Deng Lei, Dr Png Chin Wen and Dr Lukasz Wojciech from the Department of Microbiology and Immunology at NUS Medicine, the study showed that the parasite suppresses inflammation in the gut and displays properties of probiotics that keep the gut healthy. Published in the journal Cellular and Molecular Life Sciences, the series of experiments found that the parasite stabilised the bacteria ecosystem in the gut of laboratory models, and promoted quicker recovery from inflammation.
Dr Deng Lei, one of the authors of the study, said, “When one thinks of parasites, we do not normally associate them as beneficial organisms. However, the study proved that Blastocystis ST4is not a pathogen, butcould in fact promote better health of the gut.”
The ability of Blastocystis ST4in restructuring the state of the gut into a healthy composition of microorganisms could be a result of its ability to increase the types of bacteria that produce beneficial molecules, as well as increase immune cells that dampen inflammation. The findings of the study suggest that the detection of the parasite may in fact be linked to the presence of a healthy gut, and the microorganism could potentially be translated into probiotics to treat inflammation in patients.
Dr Png Chin Wen, another author of the study, added, “Our data indicates that Blastocystis ST4 behaves like an ‘ecosystem engineer’ that helps keep the bacterial environment of the gut diverse and versatile, to better combat potential diseases that may arise.”
“The common view of bacteria is that they are either good or bad. However, interactions between bacteria and the human body evolve over time, and the key is finding a balance that can cultivate a healthy environment for the gut,” said Dr Lukasz Wojciech, a co-author of the study.
While Blastocystis ST4 is shown to have beneficial properties, not all the subtypes of Blastocystis necessarily behave the same way, added the researchers. As found in an earlier study, a team from the School proved that another subtype could be harmful to the gut. Clinically, it is key for further studies to investigate the behaviour of the microorganism’s various subtypes, for a more complete assessment of their respective implications.

Peripheral membrane proteins have the particularity of temporarily binding to cell membranes, a necessary step for them to be able to fulfil their biological function. To do this, certain enzymes that catalyse their lipid modification come into action. This process is called “palmitoylation.” Some of these proteins can mutate and become oncogenic, such as the RAS proteins, which are responsible for about one third of cancers. In order to understand how palmitoylation works and to use it for therapeutic purposes, scientists from the University of Geneva (UNIGE), Switzerland, developed a novel tool to visualize this process in living cells. They have shown that, contrary to what was thought, palmitoylation is possible not only in the Golgi apparatus, the usual site for protein processing and delivery, but also at the very site where the protein must act, e.g. the plasma membrane. This discovery, to be read in the journal Nature Communications, paves the way to innovative drug discovery strategies to target very precisely the membrane binding — and therefore activity — of oncogenic proteins.
Palmitoylation consist in the introduction of fatty acids into certain proteins for them to be able to bind to cell membranes. This mechanism is governed by precise rules, which depend on the sequence of each type of protein, and on the presence of specialised enzymes. Until now, the scientific community believed that palmitoylation of peripheral membrane proteins could only take place in one place in the cell, the Golgi apparatus.
“Indeed, these proteins are produced in the cytosol — the cell fluid — and then ‘swim’ to the Golgi apparatus, where they are modified before being transported to where they need to act,” explains Gonzalo Solis, researcher in the Department of Cell Physiology and Metabolism at the UNIGE’s Faculty of Medicine, and lead author of this work. “Nevertheless, we hypothesised the possibility of local palmitoylation, without passing through the Golgi apparatus. If this is true, it opens up completely new possibilities for the intervention of this mechanism.”
Observing and manipulating proteins
To test this hypothesis, the research team led by Vladimir Katanaev, professor in the Department of Cell Physiology and Metabolism and at the Centre for Translational Research in Onco-Haematology at the UNIGE Faculty of Medicine, focused on a protein called Gαo, which is normally located at the plasma membrane and the Golgi apparatus.
The methodology used is completely new: “We brought the palmitoylating enzymes to a totally different compartment in the cell, the nuclear membrane,” explains Gonzalo Solis. “Gαo was recruited at the nuclear membrane, allowing us to identify the specific enzyme that palmitoylates them. We thus confirmed that this process can take place on the very site the protein is needed.”
Contrary to usual biochemical methodologies, the tool developed by Vladimir Katanaev and his team, which they named SwissKASH, is also the first to keep the cell alive and allows for the observation of the process dynamically. “Until now, there was no alternative to destroying the cell,” says Vladimir Katanaev. “Our method also makes it possible to determine exactly which protein reacts to which enzyme locally, which is essential if we want to control this mechanism for therapeutic purposes.”
A new drug target
Several peripheral membrane proteins, and in particular Gα subunit proteins and RAS proteins, are susceptible to mutation and thus acquire an aggressive oncogenic potential. Their oncogenicity depends on their ability to bind to the plasma membrane; palmitoylation thus plays a key role in the transformation of a healthy cell into a cancerous one.
“Inhibiting the enzyme that induces palmitoylation, and preventing the oncogenic protein from binding to the plasma membrane, could therefore defuse its pathogenicity,” points out Gonzalo Solis. “We can thus imagine blocking this specific reaction without unbalancing the whole system.” The scientists will now aim at automatizing this methodology to study the effect of a whole series of pharmaceutical products on the palmitoylation of selected oncoproteins, as well as testing their toxicity on the whole cell.
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Materials provided by Université de Genève. Note: Content may be edited for style and length.

Scientists from Kyoto University’s Institute for Integrated Cell-Material Sciences (iCeMS) and Wildlife Research Centre have produced stem cells from the endangered Grévy’s zebra using human reprogramming factors. Further comprehensive gene analyses identified key genes that are also found in human and mouse cells, providing insight into evolutionary conservation between mammals. The findings were published in the journal Stem Cells and Development.
Mammalian stem cells have drawn interest from researchers for their ability to change into multiple cell types, such as skin, muscle, egg and sperm. Pluripotent stem cells have the capacity for unlimited self-renewal and differentiation into any type of cell. Despite their potential to help researchers understand the genome, few studies have looked into pluripotent stem cells from endangered species. Ken-ichiro Kamei from iCeMS teamed up with Miho Murayama and Yoshinori Endo of the Wildlife Research Center to produce and analyse induced pluripotent stem cells (iPSCs) from Grévy’s zebras, which is on the Red List of Threatened Species.
The research group generated iPSCs by converting Grévy’s zebra skin cells using human reprogramming factors that tell the differentiated cells to revert back to their stem cell state. The iPSCs were then grown using the same methods as human iPSCs and demonstrated the potential to differentiate into different cell types. The zebra iPSCs exhibited characteristics similar to other mammalian iPSCs, such as their appearance, doubling rate and method of forming colonies. These similarities suggest that Grévy’s zebra iPSCs are good candidates to scale up for future research using similar methods as human iPSCs.
The researchers then performed RNA sequencing analyses to better understand and characterize the cells. By examining the genes that were turned on in the zebra iPSCs, the scientists were able to identify key genes, such as those associated with pluripotency and cell adhesion, that are also present in human and mouse stem cells, showing remarkable genetic conservation between these mammalian species.
The successful production of the zebra iPSCs could provide resources for functional research and the artificial reproduction of the endangered species. In the future, the researchers would like to build on their previous work and compare the zebra iPSCs with other species to help advance the understanding of the differences and similarities between mammalian pluripotent stem cells. “We would like to explore how to differentiate Grévy’s zebra iPSCs into other cells. This could provide new options for saving this species,” says Kamei.
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Antibiotics have once proclaimed the salvation of the world. Today, researchers fear that antibiotics could become a threat to public health and the natural environment.
Since its invention, we have used antibiotics in such large doses and so often that more and more of us become resistant, and thus otherwise common and harmless infections can become life-threatening for us.
In recent years, research has also shown that just being exposed to antibiotics can have a negative effect; both on the organism being exposed and on the offspring of the organism.
Always in our water
And we are many, both humans and animals, who are exposed to antibiotics. Antibiotics are often found in wastewater, groundwater, surface water, and even bottled water and are thus difficult not to come into contact with.
“The half-life of antibiotics is quite short — it is out of the water again after hours or days — but since large amounts are continuously released into our water, we consider antibiotics as pseudo persistent water pollution,” says Elvis Genbo Xu, who is an expert in ecotoxicology and assistant professor at the Department of Biology, University of Southern Denmark.
He is the co-corresponding author of a new study on the undesirable effects of antibiotics, published in Environmental Science & Technology The background for the study is that in recent years, researchers have discovered that antibiotics can have a detrimental effect on the descendants of the individuals exposed to the drugs.
“In this study, we examined the offspring of zebrafish that were exposed to CTC, which is a common antibiotic. The CTC concentrations of the experiment corresponded to the concentrations that wild organisms may encounter in nature. We can see that the young generations, ie the offspring, are less effective at fighting bacteria and in general have a weaker immune system than the parent generation,” explains Elvis Genbo Xu.
More specifically, the study shows that the first generation of zebrafish, born to CTC-exposed parents, had weakened antibacterial defenses and that the number of their immune cells decreased. The latter also applied to the third generation. When an organism’s immune system is weakened, the organism becomes less able to fight viruses and bacteria and thus more prone to diseases.
Previous research has also shown that males among so-called false scorpions (Cordylochernes scorpioides) have poorer sperm quality when their fathers have been exposed to the antibiotic tetracycline: the number of viable sperm cells fell by 25 percent.
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Materials provided by University of Southern Denmark. Original written by Birgitte Svennevig. Note: Content may be edited for style and length.

Fearful events negatively impact the brain. For instance, war veterans often go through post-traumatic stress disorder months after the cessation of the triggering event. Now, in a study led by Tokyo University of Science researchers, the precise mechanism of suppression of such fearful memories has been uncovered. Using a mouse model, the researchers identified the associated biochemical pathways, thus paving the way for the development and clinical evaluation of therapeutic compounds such as KNT-127.
Tragic events like wars, famines, earthquakes, and accidents create fearful memories in our brain. These memories continue to haunt us even after the actual event has passed. Luckily, researchers from Tokyo University of Science (TUS) have recently been able to understand the hidden biochemical mechanisms involved in the selective suppression of fearful memories, which is called fear extinction. The researchers, who had previously demonstrated fear extinction in mice using the chemically synthesized compound “KNT-127,” have now identified the underlying mechanism of this compound’s action. Their findings have been published recently in Frontiers in Behavioral Neuroscience.
Prof. Akiyoshi Saitoh, lead author of the study, and Professor at TUS, muses, “Drugs that treat fear-related diseases like anxiety and posttraumatic stress disorder must be able to help extinguish fear. We previously reported that KNT-127, a selective agonist of the d-opioid receptor or DOP, facilitates contextual fear extinction in mice. However, its site of action in the brain and the underlying molecular mechanism remained elusive. We therefore investigated brain regions and cellular signaling pathways that we assumed would mediate the action of KNT-127 on fear extinction.”
“We investigated the molecular mechanism of KNT-127-mediated suppression of fearful memories. We administered KNT-127 to specific brain regions and identified the brain regions involved in promoting fear extinction via delta receptor activation,” elaborates Dr. Daisuke Yamada, co-author of the study, and Assistant Professor at TUS.
Using a mouse model, the research team performed fear conditioning test on laboratory mice. During fear conditioning, mice learn to associate a particular neutral conditioned stimulus with an aversive unconditioned stimulus (e.g., a mild electrical shock to the foot) and show a conditioned fear response (e.g., freezing).
After the initial fear conditioning, the mice were re-exposed to the conditioning chamber for six minutes as part of the extinction training. Meanwhile, the fear-suppressing therapeutic “KNT-127” was microinjected into various regions of the brain, 30 minutes prior to re-exposure. The treated brain regions included the basolateral nucleus of the amygdala (BLA), the hippocampus (HPC), and the prelimbic (PL) or infralimbic subregions (IL) of the medial prefrontal cortex. The following day, the treated mice were re-exposed to the chamber for six minutes for memory testing. The fear-suppressing “KNT-127” that infused into the BLA and IL, but not HPC or PL, significantly reduced the freezing response during re-exposure. Such an effect was not observed in mice that did not receive the KNT-127 treatment, thus confirming the fear-suppressing potential of this novel compound.
Chemical compounds known to inhibit the actions of key intracellular signaling pathways like PI3K/Akt and MEK/ERK pathways reversed the therapeutic effect, thereby suggesting the key roles of these two pathways in influencing KNT-127-mediated fear extinction.
The first author of the study, Ayako Kawaminami, who is currently pursuing research at TUS, says, “The selective DOP antagonist that we used for pretreatment antagonized the effect of KNT-127 administered into the BLA and IL. Further, local administration of MEK/ERK inhibitor into the BLA and of PI3K/Akt inhibitor into the IL abolished the effect of KNT-127. These findings strongly indicated that the effect of KNT-127 is mediated by MEK/ERK signaling in the BLA, by PI3K/Akt signaling in the IL, and by DOPs in both brain regions. We have managed to show that DOPs play a role in fear extinction via distinct signaling pathways in the BLA and IL.”
PTSD and phobias are thought to be caused by the inappropriate or inadequate control of fear memories. Currently, serotonin reuptake inhibitors and benzodiazepines are prescribed during therapy. However, many patients do not derive significant therapeutic benefits from these drugs. Therefore, there is an urgent need for the development of new therapeutic agents that have a different mechanism of action from existing drugs.
Dr. Hiroshi Nagase, a Professor at University of Tsukuba and a coauthor of the study, concludes, “We have succeeded in creating KNT-127 by successfully separating convulsion- and catalepsy-inducing actions, which has so far been extremely difficult. Our findings will provide useful and important information for the development of evidence-based therapeutics with a new mechanism of action, that is targeting DOP.”
Fighting fear with the right therapeutic is the need of the hour, as anxiety and stress increase globally, and the findings of this study could help us achieve this objective. We have our fingers crossed.

The risk of major complications for people who donate a kidney via laparoscopic surgery is minimal. That is the conclusion of a 20-year Mayo Clinic study of more than 3,000 living kidney donors. Only 2.5% of patients in the study experienced major complications, and all recovered completely.
“The results of this study are extremely reassuring for individuals who are considering being living kidney donors. We found that this lifesaving surgery, when performed at experienced transplant centers, is extremely safe,” says Timucin Taner, M.D., Ph.D., chair of the Division of Transplant Surgery at Mayo Clinic’s William J. von Liebig Center for Transplantation and Clinical Regeneration in Minnesota. Dr. Taner is a co-author of the study.
The study was published in Mayo Clinic Proceedings.
The results are significant, given that nearly 90,000 people in the U.S. are waiting for a lifesaving kidney transplant. Patients who receive a kidney from a living donor generally have better outcomes. Living donor kidneys usually function longer than those from deceased donors.
The retrospective, single-center study is believed to be the largest research study to date to examine the risks associated with living kidney donation via laparoscopic surgery. The study involved 3,002 living kidney donors who underwent laparoscopic living kidney donor surgery at the transplant center from Jan. 1, 2000, to Dec. 31, 2019. The study tracked complications that occurred up to 120 days after surgery.
Overall, 12.4% of patients had postsurgical complications, with most of them experiencing an infection or hernia related to the incision. Most of these complications occurred in the earlier era of the study. No patients died. Researchers discovered 76% of those complications happened after the patient was discharged.
“While this study reinforces the safety of this surgical procedure, it does highlight the importance of following up with the donors after donation. That ensures any complications can be treated quickly without any long-term damage,” Dr. Taner says.
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Materials provided by Mayo Clinic. Original written by Heather Carlson Kehren. Note: Content may be edited for style and length.

Proper function of the kidney is critical for concentrating urine, regulating blood pressure, and for the tight control of electrolyte levels in the blood. The kidney achieves these important functions through many microscopic functional units, called nephrons. These nephrons consist of different segments with distinct functions. How these segments form during development and how their function is maintained in the adult is only partially understood.
A team of MGH investigators has now investigated which factors control the formation and function of specific segments of the nephron, called the distal nephron.
The distal nephron is particularly important for the ability of the kidney to concentrate urine, regulate blood pressure, and control calcium and magnesium blood levels. Parts of the distal nephron have specific salt transporters, which are the main targets of medicine’s most effective diuretics, used in the treatment of hypertension and chronic kidney disease. Thus, understanding how their function is regulated has important implications for these common diseases.
Alexander G. Marneros, MD, PhD, a physician-scientist at Mass General’s Cutaneous Biology Research Center and an associate professor of Dermatology at Harvard Medical School, and colleagues set out to identify key regulators of distal nephron function. In a new research article published in the journal Nature Communications, he and his team show that two very similar proteins, the transcription factors AP-2α and AP-2β, regulate the function of two distinct segments of the distal nephron in mice.
Previously, Marneros showed in work published in Developmental Cell in 2020 that AP-2β is required for the formation of the segment of the distal nephron that is targeted by thiazide diuretics: the distal convoluted tubule. This prompted him to ask whether the closely related protein AP-2α also has a function in the kidney. His team found that while AP-2β function in the kidney is required for survival by regulating the development and function of distal convoluted tubules, AP-2α is important for the proper function of a different segment of the distal nephron, called the collecting duct, which is involved in the kidney’s ability to concentrate urine. Notably, loss of even only half of AP-2β levels causes progressive kidney disease, whereas complete loss of AP-2α resulted in less severe kidney abnormalities.
“These findings show that AP-2α and AP-2β are important regulators of distinct segments of the distal nephron. These new observations in genetic mouse models are important contributions to our understanding of how specific segments of the kidney are regulated on a molecular level,” says Marneros.
“A detailed understanding of the mechanisms that not only lead to the formation of distal nephron segments but also that maintain the proper function of these segments in the adult is important for future novel therapeutic approaches in the management of various kidney diseases,” he adds.
This study was supported by the National Institutes of Health and institutional funding from Massachusetts General Hospital.
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Visionaries is a limited series that looks at figures who are trying to transform the way we live.Dr. Rachel Hardeman’s journey to understanding community health care began in Cuba, where she studied medicine and public health at the Latin American School of Medicine from 2002 to 2004. “That’s really where I learned not just what public health was, but how powerful it could be,” she said. “I saw that there’s a different model for caring for people than what we know and what I’d been exposed to in the United States.”In February 2021, Dr. Hardeman, who is now a reproductive health equity researcher and associate professor at the University of Minnesota, founded the Center for Anti-Racism Research for Health Equity, which seeks health care solutions to the effects of policies and attitudes that work against people of color. Dr. Hardeman is the first to acknowledge that balancing her academic work and the center can be a challenge. “I feel like I’m building a plane while also flying the plane,” she said. “The work can’t stop while I build the infrastructure for the center.”While the subjects and data-driven results of her research — survival rates of Black infants who are cared for by Black doctors versus white doctors after difficult deliveries, for example — sometimes garner controversy, Dr. Hardeman believes they are necessary for understanding the Black experience in the United States.She has also partnered with the Roots Community Birth Center in Minneapolis, one of the first Black birthing centers in the United States. Her work has shown the difference that Roots and similar centers can make for both mothers and their babies, revealing more positive outcomes than many hospital systems.Government involvement, Dr. Hardeman said, is also key. While she tries to get congressional support, she is leading up a work group with the Centers for Disease Control and Prevention as well as the American College of Obstetricians and Gynecologists, where “we are tasked with developing a tool to help maternal mortality review committees identify racism as a contributing factor in maternal deaths,” she said.Dr. Hardeman hopes to inspire others to think bigger about policies that hamstring women of color, and in turn, to think of solutions that protect mothers and babies: “We have to be thinking about the complexities of how this all shows up right to be able to have the impact.” (The following interview has been condensed and edited.)When and how did you determine where you wanted to focus?At Xavier University of Louisiana, a historically Black college in New Orleans. I was actually on the pre-med path. I talked a lot about health disparities, but I didn’t have the language for what I was seeing, right within my family and my community and certainly in New Orleans. Xavier is surrounded by some really poor and underresourced neighborhoods and a lot of marginalized folks, and so I knew — even in undergrad I knew — that I was really interested in asking: How do we change this reality?And your path to that was through academia?I went into my Ph.D. program with the intention of getting the training I needed to go work for a policy institute to use evidence to inform policy. And somewhere along the way, I started looking around at who I learned from and who taught me as a doctoral student, who was saying the words that I wanted and needed to hear about racial inequities and health and who wasn’t.What did you learn from that assessment?I realized that as a doctoral student or in the School of Public Health that I’d never taken a class from someone who was Black. So I thought to myself, “If not me, then who?” What could my place be in academia? What would that look like? Can I occupy space in academia and still be true to who I am?And it seems that you’ve found quite a few roles that accomplish that. Do you feel as if you have to do it all?I feel like you have to be working at multiple places along the spectrum to actually get the work done. It’s all related, and I’m a big thinker. I like to think big and bold and broadly about this work and the ways that it can be connected. So everything I do is very intentional. I deeply feel the urgency. It’s a matter of life and death.Do you have any free time?[Laughs] I don’t. Work has been really interesting and important because we’ve sounded the alarm on the impact of racism on maternal health outcomes. Now we’re trying to sort of see how we collect these data and identify what’s happening and these maternal deaths, so both of the maternal deaths — mother and child — aren’t in vain. Also, statistically, we need to be able to, either from a quantitative or a research perspective, name what’s happening, and also map out how we intervene.Does your identity as a Black woman play into your feeling as if you need to do everything in this space?You’re familiar with the narrative of Black women taking on the caregiver role. My daughter and I both have shirts that say “Black girls save the world.” I think that phenomenon is hard to move away from, especially when I think about the Black role models that came before me who did incredible things: my mom and both my grandmothers, who were just incredible people who cared for their families and their communities and did what they could to affect change in the spaces that they were in. I come from a family where it was very clear to me from a young age that to whom much is given, much is required. I’ve always had this sense of responsibility, in addition to just caring deeply about people — my people — and caring deeply about liberation.With all of that in mind, how do you care for yourself to prevent burnout?In the past couple of years, I’ve become more intentional about self-care. I found an amazing Black female therapist who helps me a great deal. I intentionally take time off to go away with my family. Recently, my husband and I booked airfare and we went someplace warm for a few days to relax and get some vitamin D, some sunshine. I’m also trying to shift my thinking. I can’t show up if I’m not taking care of myself.I think it was [the sociologist and New York Times contributing opinion writer] Tressie McMillan Cottom who said: “These institutions do not love you or they will not love you back. They’re still there to generate knowledge and generate capital, and you have to recognize that you are someone who’s helping to make that happen. But you don’t owe them anything.” This is advice I need to take personally. We’re all replaceable.What would you tell another Black woman who’s maybe starting out in her career and feels like she needs to do it all?I always want to encourage them to be clear about why they’re there and what they want to do. They also have to make sure that’s what’s driving them. I always say my purpose in being here is to manifest racial justice so that Black women and girls can live their full greatness and glory that they can achieve and have the opportunities for health equity. I think you have to know that and be clear about that to be able to be in the space of spaces that I am in and thrive.