Biochemistry – Definition, Careers and Major | Biology Dictionary

Biochemistry Definition

Biochemistry is the study of the chemical reactions that take place inside organisms. It combines elements from both biology and chemistry. Biochemistry became a separate discipline in the early 20th Century. Biochemists study relatively large molecules like proteins, lipids, and carbohydrates, which are important in metabolism and other cellular activities; they also study molecules like enzymes and DNA.

Biochemistry research has been done for around the past 400 years, although the term biochemistry itself was only coined in 1903 by the German chemist Carl Neuberg. The study of biochemistry essentially began with the invention of the microscope in 1665 by Robert Hooke. He was the first person to observe cells under a microscope, but they were dead cells; later on in 1674, Anton van Leeuwenhoek saw live plant cells under a microscope. Now that scientists had seen cells for the first time, they were eager to study them and discover more about the processes that occurred inside them. In the 18th Century, the French scientist Antoine Lavoisier proposed a reaction mechanism for photosynthesis, which is the process by which plants make their own food out of carbon dioxide, water, and sunlight, releasing oxygen in the process. He also was the first person to investigate the process of cell respiration, the process of making the energy molecule adenosine triphosphate (ATP) in the mitochondria of the cell.

In the 19th Century, a prevailing belief was that protoplasm, the jelly-like inside of the cell, carried out all of the processes involved with breaking down food molecules. It was believed that the chemistry of living organisms was inherently different from that of non-living ones. In 1897, Eduard Buchner performed an experiment that would change this view. He prepared an extract from yeast that he called zymase. Although zymase did not contain any living yeast cells, it could still ferment glucose to produce carbon dioxide and ethanol. Following Buchners convention, enzymes began to be named for the reaction they carried out; for example, DNA polymerase polymerizes DNA. (Zymase was later found to be multiple enzymes.)

In the 20th Century, further advancements were made. Hans Krebs discovered the citric acid cycle (which would also become known as the Krebs cycle), a series of chemical reactions during cellular respiration where glucose and oxygen are converted to ATP, carbon dioxide, and water. Also, DNA became known as the genetic material of the cell and its structure was identified by James Watson and Francis Crick from previous research done by Rosalind Franklin. Presently, newer technology such as recombinant DNA, gene splicing, radioisotopic labelling, and electron microscopy are advancing scientific knowledge further than ever before.

Topics in biochemistry research include enzyme mechanisms and kinetics, the making of proteins from DNA, RNA, and amino acids through the processes of transcription and translation, and the metabolic processes of cells. Biochemistry is closely related to molecular biology, which is the study of biological molecules such as DNA, proteins, and other macromolecules. Molecular biology techniques are often used to study biochemistry, along with techniques from other fields like immunology and physics. Since all life can be broken down into small molecules and chemical reactions, biochemistry is a broad science that is used in studying all types of biology, from botany to molecular genetics to pharmacology. Chemical reactions in cells are emphasized, but specific research topics can vary widely. For example, biochemists may be interested in researching the chemical reactions that occur in the brain (thereby connecting biochemistry with neurochemistry), how cells divide and differentiate, cell communication, the chemical basis of genetic inheritance, or how diseases such as cancer spread.

This is an image of a biochemist working in a laboratory.

Biochemistry is a laboratory science. To work in the field of biochemistry, an individual must be interested in conducting research, and should obtain at least a bachelors degree. Many biochemists teach and are principal investigators of research laboratories at universities; these positions require PhDs. While most biochemists with PhDs conduct research, some are academic lecturers and solely teach at universities. However, these biochemists also had to do research throughout graduate school in order to complete their PhD thesis. Other biochemists are lab managers, which requires a masters degree. With a bachelors degree, one may become a scientific research technician. The more education an individual has, generally the more independence they will have in a lab. Technicians carry out bench work and help perform experiments that a principal investigator designs. A lab manager has more responsibilities than a technician and may do independent research projects under the guidance of a principal investigator. Aside from academia, biochemists also work in industry positions. They may work in government laboratories or for a variety of companies including agricultural, pharmaceutical, public health, or biotechnology companies. Others provide specific services such as toxicology or forensics.

In order to be a competent biochemist, one must be interested in biology or chemistry research and learn proper laboratory skills and safety procedures. It is also important to have an aptitude for mathematics and statistics, and be able to analyze the data generated from experiments. The ability to think outside the box and brainstorm new ideas is important for designing experiments. Biochemists must also keep up with the scientific literature by reading recent publications in scientific journals and attending conferences. Although it takes a lot of hard work, training, and study, biochemists are able to uncover new information about the chemistry of living things and contribute to advancing scientific knowledge.

Students interested in becoming biochemists need to take many science courses during their time as an undergraduate. General knowledge of both biology and chemistry is essential. Many schools offer biochemistry as a specific major. It is also possible to become a biochemist after obtaining a biology or chemistry bachelors degree, but one needs to make sure that they have a good background in the subject they are not majoring in; i.e., an undergraduate majoring in biology needs to take chemistry courses (this is usually a requirement of all undergraduate biology majors), and an undergraduate majoring in chemistry should also take biology courses. Of course, there are also specifically biochemistry courses that students should take. Additionally, it is important to be well versed in mathematics and physics.

As students advance in their undergraduate career, they will take more specific science courses based on their specific interests. For example, they could take classes in botany, molecular biology, biophysics, biomedical sciences, or structural biology (how molecules are organized into cells and tissues), depending on where their research interests lie.

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Biochemistry - Definition, Careers and Major | Biology Dictionary

Biochemistry | UC San Diego Extension

Saborio, Jose

Jose has conducted research in Academic Institutions in the USA, Mexico, and Sweden, focused on viral gene expression in cells infected with Poliovirus, Adenovirus, and of cytoskeletal and contractile proteins in cultures cells and in skeletal and smooth muscle tissues. While at the University of California, Irvine, Jose discovered and characterized two paraflagellar proteins, and the corresponding genes, of Trypanosoma cruzi , the causative agent of Chagas Disease, a parasitosis endemic in several South American countries. In the Biotechnology industry, for ten years, Jose worked as a scientist and as quality assurance manager for the Molecular Biology product line.

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Biochemistry | UC San Diego Extension

Researchers discover antibodies that neutralize omicron and other SARS-CoV-2 variants – News-Medical.Net

An international team of scientists have identified antibodies that neutralize omicron and other SARS-CoV-2 variants. These antibodies target areas of the virus spike protein that remain essentially unchanged as the viruses mutate.

By identifying the targets of these "broadly neutralizing" antibodies on the spike protein, it might be possible to design vaccines and antibody treatments that will be effective against not only the omicron variant but other variants that may emerge in the future, said David Veesler, investigator with the Howard Hughes Medical Institute and associate professor of biochemistry at the University of Washington School of Medicine in Seattle. "This finding tells us that by focusing on antibodies that target these highly conserved sites on the spike protein, there is a way to overcome the virus' continual evolution," Veesler said.

Veesler led the research project with Davide Corti of Humabs Biomed SA, Vir Biotechnology, in Switzerland. The study's findings were published Dec. 23 in the journal Nature. The lead authors of the study were Elisabetta Cameroni and Christian Saliba (Humabs), John E. Bowen (UW Biochesmistry) and Laura Rosen (Vir).

The omicron variant has 37 mutations in the spike protein, which it uses to latch onto and invade cells. This is an unusually high number of mutations. It is thought that these changes explain in part why the variant has been able to spread so rapidly, to infect people who have been vaccinated and to reinfect those who have previously been infected.

The main questions we were trying to answer were: how has this constellation of mutations in the spike protein of the omicron variant affected its ability to bind to cells and to evade the immune system's antibody responses."

David Veesler, Study Investigator with the Howard Hughes Medical Institute and Associate Professor of Biochemistry, School of Medicine in Seattle, University of Washington

[Veesler and his colleagues speculate that omicron's large number of mutations might have accumulated during a prolonged infection in someone with a weakened immune system or by the virus jumping from humans to an animal species and back again.]

To assess the effect of these mutations, the researchers engineered a disabled, nonreplicating virus, called a pseudovirus, to produce spike proteins on its surface, as coronaviruses do. They then created pseudoviruses that had spike proteins with the omicron mutations and those found on the earliest variants identified in the pandemic.

The researchers first looked to see how well the different versions of the spike protein were able to bind to protein on the surface of cells, that the virus uses to latch onto and enter the cell. This protein is called the angiotensin converting enzyme-2 (ACE2) receptor.

They found the omicron variant spike protein was able to bind 2.4 times better than spike protein found in the virus isolated at the very beginning of the pandemic. "That's not a huge increase," Veesler noted, "but in the SARS outbreak in 2002-2003, mutations in the spike protein that increased affinity were associated with higher transmissibility and infectivity." They also found that the omicron version was able to bind to mouse ACE2 receptors efficiently, suggesting omicron might be able to "ping-pong" between humans and other mammals.

The researchers then looked at how well antibodies against earlier isolates of the virus protected against the omicron variant. They did this by using antibodies from patients who had previously been infected with earlier versions of the virus, vaccinated against earlier strains of the virus, or had been infected and then vaccinated.

They found that antibodies from people who had been infected by earlier strains and from those who had received one of the six most-used vaccines currently available all had reduced ability to block infection.

Antibodies from people who had previously been infected and those who had received the Sputnik V or Sinopharm vaccines as well as a single dose of Johnson & Johnson had little or no ability to block or "neutralize" the omicron variant's entry into cells. Antibodies from people who had received two doses of the Moderna, Pfizer/BioNTech, and AstraZeneca vaccines retained some neutralizing activity, albeit reduced by 20- to 40-fold, much more than any other variants.

Antibodies from people who had been infected, recovered, and then had two doses of vaccine also had reduced activity, but the reduction was less, about fivefold, clearly demonstrating that vaccination after infection is useful.

Antibodies from people, in this case a group of renal dialysis patients, who had received a booster with a third dose of the mRNA vaccines produced by Moderna and Pfizer/BioNTech showed only a 4-fold reduction in neutralizing activity. "This shows that a third dose is really, really helpful against omicron," Veesler said.

All but one antibody treatments currently authorized or approved to be used with patients exposed to the virus, had no or had markedly reduced activity against omicron in the laboratory. The exception was an antibody called sotrovimab, which had a two- to three-fold reduction of neutralizing activity, the study finds.

But when they tested a larger panel of antibodies that have been generated against earlier versions of the virus, the researchers identified four classes of antibodies that retained their ability to neutralize omicron. Members of each of these classes target one of four specific areas of the spike protein present in not only SARS-CoV-2 variants but also a group of related coronaviruses, called sarbecoviruses. These sites on the protein may persist because they play an essential function that the protein would lose if they mutated. Such areas are called "conserved."

The finding that antibodies are able to neutralize via recognition of conserved areas in so many different variants of the virus suggests that designing vaccines and antibody treatments that target these regions could be effective against a broad spectrum of variants that emerge through mutation, Veesler said.

Source:

Journal reference:

Cameroni, E., et al. (2021) Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift. Nature. doi.org/10.1038/d41586-021-03825-4.

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Researchers discover antibodies that neutralize omicron and other SARS-CoV-2 variants - News-Medical.Net

NASA hired 24 theologians to study reaction to aliens: book – New York Post

Between heaven and Earth, where do aliens fit in?

Thats the question that NASA hopes theologians at the Center for Theological Inquiry (CTI) in Princeton, New Jersey, can answer, in a recent effort to understand how humans will react to news that intelligent life exists on other planets.

University of Cambridge religious scholar Rev. Dr. Andrew Davison, who also holds a doctorate in biochemistry from Oxford, is one of the 24 theologians enlisted to help with the project, the Times UK reported last week.

In a recent statement on the University of Cambridges Faculty of Divinity blog, Davison says his research so far has already seen just how frequently theology-and-astrobiology has been topic in popular writing during the previous 150 years.

Davisons upcoming book, Astrobiology and Christian Doctrine, due out in 2022, according to the Times, will cover part of CTI and NASAs joint spiritual exploration, in which his most significant question is how theologians would respond to the notion of there having been many incarnations [of Christ] in the universe, he added in the blog post.

This is the latest dispatch to come in a partnership between the US space agency and the religious institute. In 2014, NASA awarded CTI a $1.1 million grant to study worshippers interest in and openness to scientific inquiry called the Societal Implications of Astrobiology study.

Studies have shown links between religiosity and belief in extraterrestrial intelligence. Research published in 2017 found that people with a strong desire to find meaning, but a low adherence to a particular religion, are more likely to believe aliens exist indicating that faith in either theory may come from the same human impulse.

With NASAs support, CTIs director Will Storrar said theyd hoped to see serious scholarship being published in books and journals to come out on the subject, answering to the profound wonder and mystery and implication of finding microbial life on another planet.

According to the Times, Davisons book notes that a large number of people would turn to their religions traditions for guidance if extraterrestrials were found, and what that means for the standing and dignity of human life.

Detection [of alien life] might come in a decade or only in future centuries or perhaps never at all, but if or where it does, it will be useful to have thought through the implications in advance, Davison writes.

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NASA hired 24 theologians to study reaction to aliens: book - New York Post

Peter Setlow, at 50 Years and Counting: ‘I Really Like Doing Research’ – UConn Today – UConn Today

Hes UConn Healths longest-serving employee. It was the summer of 1971 when Peter Setlow started working in a trailer as an assistant professor in what was then known as the Department of Biochemistry. Over the next five decades he would become assistant professor, then full professor, serve a seven-year stint as the chair of the Department of Biochemistry, and since 2005 hes held the title of Board of Trustees Distinguished Professor in the Department of Molecular Biology and Biophysics.

Setlow estimates that over his 50 years at UConn Health, the number of lab technicians, lab assistants, graduate assistants, students, and postdoctoral fellows whove worked in his lab is in the hundreds, and he conservatively estimates the amount of grant money hes brought in exceeds $20 million.

Earlier this year UConn Health recognized Setlow for his 50th-year-of-service milestone. UConn Today asked him to reflect on his time and share some of his observations.

What was it like when you got here in 1971?

This place was very different then. This building [the L building] wasnt open yet. When I came in, everything was down the hill where Jackson Labs is now. I was in a trailer. I was in there for a year, in a trailer that had been outfitted as a lab, very minimally, and I was separate from the rest of the department; they were in Butler buildings that were all sort of cobbled together. So if I wanted to go to the department where most of the equipment was, I had to go outside fine during the summer, but it was a pain in the winter. And the pipes froze in the winter because they werent insulated down below. But we survived.

You could walk outside and look up the hill and see this new building. The shell was all there. There was something up there; it was hope for the future.

And my department then it was biochemistry was the first one to move up here [L building] in the summer of 1972, and that was interesting because there were some things that hadnt been fixed, but it was a hell of a lot better than the Butler buildings, especially in the winter, because those Butler buildings were cold and very crowded. And so, it was really nice to get up here.

What brought you to UConn Health?

I wanted to run a lab. I had some things that I picked out to start working on. Thats changed a lot of course, over 50 years, but I wanted to work in a lab and climb those golden stairs and do all kinds of great things in science. I came from Stanford University, the biochemistry department, in the California Bay area, drove across the country with my wife, who was then pregnant, in a VW beetle, it was a good time.

I came here because I wanted to come back to the East Coast. My wife, who was from the Midwest, didnt want to go back to the Midwest for love nor money, and I didnt want to be in a big city. I wanted no part of a big-city school. I didnt even go look. I wanted to come back to the East Coast.

I was born in New Haven and I grew up in New Haven. I went to high school there, my father was at Yale on the faculty. And then we moved to Oak Ridge, Tennessee a little different than New Haven, but theres a big national lab there. My dad was offered a big position and my mother was also in science and she was going to have her lab there too. So it was a big deal for them.

I wanted to come here because I liked the place, I liked where I would be, where I could live, five minutes from the lab. We ended up buying a house in Farmington that is five minutes from the lab. We moved in in 1972, and were still there.

I like doing research, looking at data is still fun. Trying to puzzle out what the data mean and what to do next is fun. I enjoy it. Peter Setlow

How did those early years go for you?

I had five publications, not huge big papers, but they had my name numero uno on them, that were published from work that I did in that trailer, almost all by myself. The last few months I had a graduate student who had started in my lab and she helped. So I really felt good about it.

One of the things that I did caused quite a stir in the field. It shouldnt have, but it did. For a long time, it was one of the most cited things Id ever done, essentially saying that there is none of a particular compound (cyclic AMP), that was really a big thing in the bacterial world at that time, and me just saying, Nope, its not in this organism at all. And that went against the dogma. I was right as it turns out. So I professionally, I did quite well.

Before I left Stanford I had started a grant that was recommended for NIH funding. I had that to start essentially once I got up the hill, so I could hire a technician and on and on and on. So when I got up the hill, I had a graduate student and I had a technician and my career really took off.

If someone told you in 1971 youd still be here in 2021, how would you have reacted?

Oh, I would have laughed at that. When I came here, the only option we had in terms of retirement was the state retirement. It was something like, if you leave before 10 years, the states not going to give you their contributions. And I said, Im not going to be here in 10 years. Id been in college for four, graduate school for four, postdoctoral for three, three different places. Im not going to be here. So we didnt even sign up for it.

Then one day you look up and youve been here 50 years. Ive had opportunities to leave. I looked, there were some things here I was unhappy with. So when I looked, I looked at four different places, and always decided that the grass was not greener. I had offers from three and I turned them down.

How have you spent your time away from the office and lab?

I got very heavily involved in coaching soccer. I played soccer in college. Then I watched my daughters team get destroyed. I started coaching my son a little bit, but he wasnt really interested in playing. Then I started coaching my daughter and I coached her for 10 years, which was great. I got to know my daughter better than most fathers ever do. It was phenomenal. I enjoyed coaching her and being with her. We took a team to Scotland for an exchange program. We were there for two weeks and my daughter had a blast. And a number of the kids that I coached came and worked in the lab in the summer, which was really great. One became a graduate student here and is now teaching in the Farmington school system.

A big deal was just made because they named a field after me. Theres a group of outdoor fields called Tunxis Mead. A new turf field was put in and they named the field after me. There was a big dedication ceremony right in front of the field, and there were about 75 to 100 people there some people from here, a lot of former players and some people I coached with. It was really very touching to me. And my daughter actually flew up from Florida, where shes on the faculty at the University of Florida. My wife even came, and she has no interest in soccer. I did it for 44 years, recreational league initially, then travel, mostly girls, the last six or seven years with boys, but I wasnt a head coach anymore, I was an assistant for those teams. But Ive coached travel and won the state championship six times, a lot of tournaments. The great majority were wonderful kids. I had a wonderful time. And I still hear from a lot of them. It was a lot of fun. It was great to be here working here for eight, nine hours and then go down and coach and yell at a bunch of kids, great for stress relief.

What are you most proud of from your 50 years at UConn Health?

That Ive always done really good research, utilizing all kinds of new new to me technology. There are a lot of people that do the same thing over and over and over. And Ive done some of that. Everybody does the low-hanging fruit, but Ive consistently utilized new and upcoming technology for my research. I may not do it in my lab, but I find people to collaborate with to do it. And thats been a lot of fun because you suddenly can look at problems in ways that you never imagined. And doing science for 50 years, you see revolutions in science. When I started, there was no molecular biology, it was just coming, so I got to learn it myself, how to do it, how to apply it. And that was difficult because you have to learn new stuff on your own, which is fine, and apply it. Its phenomenal, and made the problems I was working on, now you can do them in a whole new way. So Im really proud of that.

Im also proud of so many of the graduate students Ive had who have gone on and done really well. And Im still in touch with so many of them, which is really gratifying, to see I had something to do with their success, and postdocs as well. Im really proud of them. I mean, not every graduate student Ive had is having that kind of success, but an awful lot of them have done well, found careers that were right for them.

What keeps you motivated?

I really like doing research. There are other things that we do here as part of this. I mean, I have to serve on some committees and one of them is very time consuming, but its a very important committee, which is the promotions committee. We make recommendations to the Dean.

I review papers. I review 40 to 50 every year and Im an editor for four or five journals or on the editorial board, either or both, because thats part of you giving back to the community of science and its also providing quality control over what makes it into the literature in my field. Theres a lot of trash. I enjoy reviewing papers, even if Im going to reject them. And I like doing research, looking at data is still fun. Trying to puzzle out what the data mean and what to do next is fun. I enjoy it.

And I dont know what Id do if I wasnt doing this.

Setlow, 77, lives in Farmington with his wife of 56 years, Barbara Setlow, who is retired from the UConn School of Medicine faculty. They have two children (one in science) and four grandchildren.

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Peter Setlow, at 50 Years and Counting: 'I Really Like Doing Research' - UConn Today - UConn Today

Yemeni students are the silent victims of Lebanons crisis – TRT World

Lebanon has kept its borders open for war-affected Yemenis, many of whom struggle to get by as the country grapples with economic chaos.

When Ahmed* travelled to Lebanon from Taiz in Yemen in 2014, he had high hopes for his career and future.

He enrolled for a degree in biochemistry at a Lebanese university, thanks to a government scholarship that covered his fees and accommodation. At the time, his parents were able to send him a basic maintenance stipend. But that came to an end two years later, despite the familys best efforts. Taiz, Yemens third-largest city, had become the theatre of some of the fiercest fighting in the seven-year war between Iran-aligned Houthi rebels and government forces backed by a Saudi-led coalition. He had to become a lifeline for his family back home.

After what happened in Yemen things became so tough for them, the 26-year-old told TRT World from Beirut, music blasting in the background of the shop where hes been working for the past few months. So I dropped out of college and started working. Illegally, of course.

Since then, Ahmed says hes been hopping from job to job in order to send the much-needed remittance money to his family in Yemen. But as Lebanons economic crisis grinds on, leaving 80 percent of its population living below the poverty line, keeping afloat has become a daily struggle. The Lebanese currency has lost as much as 90 percent of its value since 2019, while inflation has skyrocketed and the average cost of food increased by more than 400 percent between October 2019 and June 2021.

I am working on finding better opportunities to work in another place, as its so difficult in Lebanon, Ahmed says, We get paid so little, approximately 30 dollars a month. I used to be able to send money to my family, but now I am only covering my living expenses.

Every year, hundreds of students from Yemen study at Lebanese universities, accounting for the largest chunk of the Yemeni community in the country, estimated at around 500. But no one is keeping an official count and Lebanon has remained one of the few countries in the world that Yemen citizens can enter on a tourist visa they can get upon arrival at Beirut airport - provided they can show they are carrying $2,000 in cash and proof of a hotel booking.

Since the start of the war, Yemeni students in Lebanon have seen their sources of support dry up whether its government scholarship payments that no longer come in regularly, or family income sources depleted due to the ongoing economic crisis in the country, where millions are food insecure and at risk of famine.

Yemeni students have protested a number of times over the years to raise their concerns, but their voices have been largely ignored. The economic crisis in Lebanon has only contributed to a deterioration of the situation, as those, like Ahmed, who are forced to drop out and find work mostly have no choice but to join the informal labour force.

When you go apply for a student residence permit at the General Security Office, they ask you to sign an official document that you're not going to be working in Lebanon, says Ali Al-Dailami, a researcher at the Sanaa Center for Strategic Studies. Applying for a work permit is possible only upon meeting certain conditions including receiving pre-approval before arrival in Lebanon. And if you get caught, you can get deported, Al-Dailami says.

From student to unrecognized refugee

Al-Dailamis research into the Yemeni community in Lebanon found that some students have decided to approach the UNHCR instead to apply for asylum and resettlement.

When students find their families can't provide for them anymore, what they do is they go to apply because they need support, Al-Dailami says.

The number of Yemeni asylum seekers registered with the UNHCR in Lebanon remains negligible, however just 104 in 2020. An additional 25 had been recognised refugee status. Many, Al-Dailami says, see the process as daunting, long and leading nowhere, particularly as resettlement options are limited. While four million people have been uprooted due to the crisis in Yemen, Yemenis did not figure among the top ten nationalities resettled in the EU in 2020.

This country has placed more powerful and wealthier states to shame by opening the doors to lots of refugees from these war zones in the region, Al-Dailami says. A country of barely seven million, Lebanon hosts more refugees per capita than anywhere else in the world, the majority being Syrians.

Ahmed plans to find a way to resume his studies in biochemistry.

I dont know how many years its going to take me to graduate, he says, but I think leaving Lebanon at this time is better. I may find other opportunities for work that allow me to continue my studies.

We are not treated like Lebanese students, we have to pay [our student fees] in dollars now, he adds.

Going back to his worn-torn country is not an option either, particularly as, he says, having lived in Lebanon means hed be seen as taking sides.

Lebanon is safe, for now. You can live here, but you need fresh dollars from outside, he says. You work, you pay for your food and your stay. There is nothing much else you can do.

[Note: Ahmed* is a pseudonym used to protect his identity due to his status.]

Source: TRT World

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Yemeni students are the silent victims of Lebanons crisis - TRT World

Feeling stressed? This ‘weird’ technique can help – and here is how you can learn it easily – Economic Times

The technique is known as Emotional Freedom Techniques (EFT). It's commonly called tapping because the technique stimulates acupressure points on the face and body with a gentle two-finger tapping process.

What is the evidence for tapping?The evidence for this simple approach to stress reduction has been growing exponentially.

Research now shows tapping is beneficial for food cravings, depression, anxiety, phobias and post-traumatic stress disorder.

What is even more interesting is that tapping affects the body's biochemistry such as immunity and blood pressure. Just one hour of tapping decreases the stress hormone cortisol by 43%.

It's suggested tapping affects the stress centre in the brain (the amygdala) and the memory centre (the hippocampus). Both play a role in the decision-making process when someone decides if something is a threat.

Research has now examined primary school children who have used tapping in schools and found it helps with their focus and concentration.

So how can you get started?Usually tapping is done when you have a feeling you would like to reduce. If you feel stressed, this would be a perfect time to start tapping. There are five steps:

Step 1. Rate your level of stress out of ten, where ten is the highest level and zero would represent complete calm. You can guess this number as it is just a way of you rating your feeling.

Step 2. People should state their feeling out loud in order to engage with it and pay attention to how you feel. Typically, you would say:

Even though I feel really stressed at the moment because of ______, I accept this is how I feel.

It is important to be specific about why you feel stressed and think about that as you do the tapping process. As you say this statement out loud, tap on the point at the side of the hand, as shown below.

Saying your problem out loud will not reinforce it; you are actually being honest with yourself in this moment and acknowledging how you feel.

Step 3. Tap with two fingers through the eight acupoints shown below and just say the feeling (not the whole sentence). For example, you may say feel stressed while you think about what is making you feel stressed in that moment.

Step 4. When you finish tapping on the last acupoint (top of the head), pause and take a breath. Re-rate your level of stress after that single round.

Step 5. If your rating out of ten is still high, continue tapping as many rounds as you want until it feels lower in number, or you notice a shift. If you were to think of other feelings as you are tapping, you can change the words.

For example, you might start tapping on feeling stressed about a work task, but after a few rounds you notice you really feel overwhelmed and wishing you had support. You can change the words to reflect this and say I feel overwhelmed instead.

The underlying mechanism is that the tapping at these acupoints sends activating or deactivating signals to brain areas that have been aroused by the phrases. Tapping generates these electrical signals via the principle of mechanosensory transduction.

As a brief intervention that can be self-applied, tapping is now backed by more than 100 randomised clinical trials (the most accepted form of research).

It appears highly effective and rapid compared to conventional treatments.

So, while it may look a little strange, tapping is equivalent or comparable to gold-standard approaches such as Cognitive Behavioural Therapy (CBT). It's worth trying next time you feel stressed!

(This article is syndicated by PTI from The Conversation)

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Feeling stressed? This 'weird' technique can help - and here is how you can learn it easily - Economic Times

Researchers discover new function of protein tBID – News-Medical.net

The protein tBID can trigger programmed cell death (apoptosis) by inducing damage in the energy suppliers of the cells, the mitochondria. Apoptosis is essential for maintaining tissue balance. In addition, apoptosis plays a critical role as a defense mechanism and in the elimination of damaged or redundant cells in our bodies. Impaired apoptosis has been linked to many human diseases, from cancer and autoimmune diseases to neurological disorders and heart failure. The discovery by Professor Dr Ana Garcia-Saez and her collaborators and colleagues at the University of Cologne's CECAD Cluster of Excellence for Aging Research that tBID, previously thought to be a signal transducer, can also execute apoptosis could open up new therapies to treat malignant cells such as cancer cells. The article 'tBID can act as a BAX-like effector of apoptosis' has now been published in The EMBO Journal.

The protein tBID belongs to the family of BCL-2 proteins, which are fundamentally important for the self-determined apoptosis of cells and tissue balance. Because of the overlapping functions of this protein family, studying them individually is particularly challenging. Garcia-Saez and her team set out to characterize the roles of the various family members. Using cell lines lacking much of the BCL-2 proteins, they were able to determine the function of tBID. In addition, state-of-the-art microscopy (confocal, STED and electron microscopy) was used to analyze in detail the effects of tBID at the mitochondrial membrane in the cell. Activating tBID was also able to combat cellular infection with the bacterium Shigella flexneri and kill blood cancer cells (leukemia). In addition, the researchers showed that apoptosis triggered by tBID is independent of other known apoptosis induction pathways.

'For us, it was amazing to see that proteins which are quite well known still surprise us after four decades. The realization that a protein that was considered a signal transducer for twenty years has an effector function under certain conditions is mind-blowing,' Garcia-Saez remarked. This newly discovered function of tBID could in the future become useful in medicine.

For example, activating tBID could induce apoptosis when other known apoptosis signaling pathways fail or lack the proteins that carry it out. Activating tBID could also help with Shigella infections, where the proteins that usually induce apoptosis are not activated."

Professor Dr Ana Garcia-Saez, University of Cologne's CECAD Cluster of Excellence for Aging Research

The work for this study started at the IFIB (Interfaculty Institute of Biochemistry) in Tbingen and was further developed at the CECAD Research Center, Institute for Genetics, in Garcia-Saez's core laboratory, together with the laboratories of Professor Dr Hamid Kashkar und Dr Lukas Frenzel as well as external collaborators from the University of Nebraska and the laboratory of Andreas Villunger (University of Innsbruck and CeMM Research Center, Austria).

Source:

Journal reference:

Flores-Romero, H., et al. (2021) tBID can act as a BAX-like effector of apoptosis. The EMBO Journal. doi.org/10.15252/embj.2021108690.

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21 Interesting Knox Students and Alumni We Met in 2021 – Knox College

Cecilia Pinto 81 (1) is a fiction writer and teaching artist. Her novella, Imagine the Dog, won the 2020 Clay Reynolds Novella Prize. Severalcurrent students received prestigious awards this year.Becca Gadiel 22 (2) was chosen as Knox Colleges 2021-22 Student Laureate of the Lincoln Academy of Illinois.Sophia Bowley 22 (3)received the Faculty Scholarship Prize at Knoxs 2021 Opening Convocation ceremony, andKyle Williams 22 (4), was awarded a scholarship from the National Association of Black Journalists Chicago Chapter.

In the fall of 2021, new minors were introduced to the Knox academic programsone of them being Spanish translation and interpreting. Eric Espinoza 23 (5) is an exemplary student for the new minor, having volunteered for different projects and clinics, as well as being hired by Worldwide Languages as an interpreter.

In the always advancing world of technology, two alumni we met in 2021 have centered their careers around software. Ginny Graves 10 (6) leads a team with a start-up, Association Analytics, which provides business intelligence software to the association market. Harry Carpenter 18 (7) has been developing life insurance and annuities software for LIDP.

The business and management major is now a top program at Knox. Current students Elijah Crump 22 (8) and Andrew Hand 22 (9), are both majors and have had significant success and opportunities in the program. Crump connected with a Knox alumnus and worked in finance during a summer internship. Hand came to Knox as a transfer student, and found Knox was the perfect fit for him by working with the business and management faculty. While majoring in computer science, Kam Wells 17 (10) minored in business and management and a self-designed minor in the analytics of athletics. Wells is currently a data engineer for the Boston Red Sox, combining his interests in baseball and computer science.

Though they may not have majored in business at Knox, Khyati Shah 99 (11) and Pamela Hernandez 22 (12) both have successful careers in the corporate world. Shah is currently senior vice president of corporate communications at Kinara Capital, a company driving financial inclusion of small business entrepreneurs in India. The company was founded by Knox alumna Hardika Shah 99, Khyatis sister and CEO of Kinara Capital. As an entrepreneur, Hernandez has launched her own social science research firm, Educo Research.

The pandemic shone a light on how very important teachers are in ensuring future generations receive the education they need, even in almost impossible situations. Knox has accomplished alumni filling that need. Jason Maclin 07 (13) is currently the principal at Vista PEAK Preparatory in Colorado, and he finds his time of being a principal and educator during a pandemic to be enlightening. Recent graduate Katy Coseglia 20 (14) discovered the opportunity to teach in a school district in a village in Alaska and has enjoyed learning from the people in the village and teaching her students new skills.

Being as involved as possible is how Melvin Taylor 14 (15) describes his time since graduating from Knox. After working in several different roles and career paths, Taylor is currently working as a writer at Heavy.com, an online news platform that covers breaking news, sports, entertainment, and shopping.

In the sciences, Natalee Young Hau 13 (16), who majored in biology, reignited her passion for science when she started working as a medical laboratory technologist during the pandemic. Britney Salinas 22 (17) is majoring in biochemistry and is taking the opportunity to conduct research in a new collaborative program by working on the Solutions of Nature project on the Knox Farm. After graduating from Knox with a degree in biochemistry,Taliah Ellis 19 (18) attends medical school and plans on a career in orthopedic surgery and sports medicine.

Jessie Johnson 12 (19), and Jon Gripshover 06 (20) are in different careers than they pictured when they arrived at Knox. Johnson is the founder and CEO of a successful food blog called Life As A Strawberry. Gripshover has opened Accessibility Compliance Testing Services, which is a new program in California Prison Industry Authoritys digital services division.

Knox students are so dedicated to learning that some started coming to Knox even before they graduated high school. Emma Curry 24 (21) took advantage of the Early College program, leading her to her decision to attend Knox.

2021 was a year that showed us that nothing can keep the Knox community from reaching new heights on and off campus. The resilience and determination of our community continues to shine, as it has for almost 185 years.

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Lung Cancer Research Advocacy Driven by Heart – Curetoday.com

Upal Basu Roy is currently the senior director of LUNGevity Research at the LUNGevity Foundation. He holds a Ph.D. in molecular and cellular biology from the University of Arizona in Tucson and an M.P.H. in global health policy and management from New York University.

In his official capacity, he spearheads LUNGevitys Translational Science Research Programs and its Patient-Focused Research Center. The research programs he develops and manages, such as Project Transform and Project PEER, focus on capturing the experience and perspective of patients with lung cancer in a way that will improve treatment and patient care for all lung cancer types. His LUNGevity work also includes overseeing its research awards program, participating in the Health Equity Council, guiding the scientific program of its International Lung Cancer Survivorship Conference, tracking developments in lung cancer care and translating new research into patient-friendly materials. He also provides patient perspective to government agencies, academia and industry, such as exploring ways to make clinical trials more accessible to a wider variety of patients.

In addition to an in-depth understanding of lung cancer science and research, Upal has a real heart for patients. He has generously given his personal as well as professional time to serve on an institutional review board, address disparities in cancer care, educate individual patients and help them navigate cancer drug access issues in other countries, and facilitate several patient-driven initiatives. For example, he helped create Project PRIORITY a collaboration between LUNGevity Foundation and EGFR Resisters to capture the lived experience of patients who have EGFR-positive lung cancer and analyzed data for presentations. Another example is helping the patient group ALK Positive develop their research grant awards process. Additionally, he served as a volunteer mentor for the new International Association for the Study of Lung Cancers Supportive Training for Advocates on Research and Science (STARS) program, which helps lung cancer advocates evolve into research advocates, and he developed a STARS training module for small cell lung cancer.

Most of Upals work happens behind the scenes and does not get the same visibility as aware- ness campaigns and policy advocacy. However, his work is essential for improving outcomes for all patients with lung cancer. He deserves the highest appreciation and recognition from the entire lung cancer community.

For more news on cancer updates, research and education, dont forget tosubscribe to CUREs newsletters here.

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