#Threonine News

[chemanalystdata]

Threonine Price | Prices | Pricing | News | Database | Chart 

 Threonine is an essential amino acid with various applications in the pharmaceutical, animal feed, and food industries. Over the past few years, the price of threonine has fluctuated significantly due to a range of factors, including changes in production capacities, supply chain disruptions, raw material costs, and global demand. These fluctuations have been observed across multiple regions, influencing the strategies of businesses that depend on threonine as a critical input in their operations.

One of the primary drivers of threonine prices is the balance between supply and demand. When the demand for threonine increases, especially in high-demand sectors such as livestock feed, the prices tend to rise. This is because threonine is a key ingredient in enhancing the protein content in animal feed, particularly for pigs and poultry, making it an essential component of livestock production. As the global population continues to grow and consumer preferences shift toward protein-rich diets, the demand for animal protein and, consequently, threonine has been rising steadily. This growing demand often outstrips supply, causing upward pressure on prices.

Get Real Time Prices for Threonine : https://www.chemanalyst.com/Pricing-data/threonine-1510

Global trade dynamics also play a crucial role in influencing threonine prices. Threonine is traded internationally, and changes in trade policies, tariffs, or logistical challenges can significantly impact its price. For instance, disruptions in global shipping or the imposition of tariffs on key exporting countries can increase the landed cost of threonine in importing nations. These factors contribute to regional price variations, where countries with more favorable trade conditions might experience lower threonine prices, while those with trade barriers might face higher costs.

The price of threonine is also linked to the price of its feedstocks, such as corn and other starch-based inputs used in its fermentation process. When the prices of these raw materials increase, manufacturers face higher production costs, which may lead to an increase in the price of threonine. Additionally, fluctuations in energy prices can also affect threonine production costs, particularly in energy-intensive processes such as fermentation and drying. In recent years, energy prices have been volatile due to geopolitical tensions, supply chain disruptions, and policy shifts toward greener energy sources, all of which can contribute to fluctuations in threonine prices.

Moreover, the impact of currency exchange rates cannot be overlooked in the threonine market. Since threonine is a globally traded commodity, the strength or weakness of a country’s currency can affect its competitiveness in the international market. For instance, if the Chinese yuan weakens against the US dollar, threonine exports from China may become more competitive in the global market, potentially leading to lower prices in regions that import threonine. On the other hand, a stronger dollar or euro could make imports more expensive for countries dealing with weaker currencies, thereby pushing up local prices.

Innovation in production technology and processes has also been a contributing factor to threonine price changes. As manufacturers adopt more efficient methods of production, such as optimizing fermentation processes or using genetically engineered bacteria to increase yields, production costs can be reduced. These technological advancements can help stabilize prices or even bring them down over time, making threonine more affordable for industries that rely on it. However, these innovations require substantial investment, and not all manufacturers are quick to adopt them, leading to a mixed pricing environment.

Another important consideration when analyzing threonine prices is the role of alternative products and substitutes. As the cost of threonine rises, industries, particularly those involved in animal feed, may look for alternative amino acids or protein sources that can fulfill similar nutritional needs. This shift in demand can place downward pressure on threonine prices if substitutes become more widely available or more cost-effective. However, due to threonine's unique role in certain biological functions, the substitution potential is somewhat limited, especially in high-performance feed formulations.

In the long term, the outlook for threonine prices is subject to several uncertainties, including future production capacities, regulatory changes, and global economic conditions. On one hand, continued innovation in production methods and the expansion of manufacturing facilities, particularly in Asia, could help stabilize or even reduce threonine prices. On the other hand, rising environmental concerns and stricter regulatory frameworks may impose additional costs on producers, potentially driving prices up. Additionally, the ongoing geopolitical landscape, including trade tensions between major economies, could further complicate the global trade of threonine, leading to more price volatility.

Overall, threonine prices are influenced by a complex interplay of factors, ranging from supply and demand dynamics to raw material costs, production technology, and global trade policies. Businesses that rely on threonine must stay informed about these trends and consider hedging strategies or alternative sourcing options to manage price risks. Understanding the factors that drive threonine prices can help businesses make better-informed decisions and navigate the challenges of a volatile market, ensuring a stable and cost-effective supply of this critical amino acid.

Get Real Time Prices for Threonine : https://www.chemanalyst.com/Pricing-data/threonine-1510

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[covid-safer-hotties]

Also preserved on our archive (Thousands of reports, sources, and resources! Daily updates!)

By Robert Stevens

A COVID wave fuelled by the XEC variant is leading to hospitalisations throughout Britain.

According to the UK Health Security Agency (UKHSA), the admission rate for patients testing positive for XEC stood at 4.5 per 100,000 people in the week to October 6—up significantly from 3.7 a week earlier. UKHSA described the spread as “alarming”.

Last week, Dr. Jamie Lopez Bernal, consultant epidemiologist at the UKHSA, noted of the spread of the new variant in Britain: “Our surveillance shows that where Covid cases are sequenced, around one in 10 are the ‘XEC’ lineage.”

The XEC variant, a combination of the KS.1.1 and KP.3.3 variants, was detected and recorded in Germany in June and has been found in at least 29 countries—including in at least 13 European nations and the 24 states within United States. According to a New Scientist article published last month, “The earliest cases of the variant occurred in Italy in May. However, these samples weren’t uploaded to an international database that tracks SARS-CoV-2 variants, called the Global Initiative on Sharing All Influenza Data (GISAID), until September.”

The number of confirmed cases of XEC internationally exceeds 600 according to GISAID. This is likely an underestimation. Bhanu Bhatnagar at the World Health Organization Regional Office for Europe noted that “not all countries consistently report data to GISAID, so the XEC variant is likely to be present in more countries”.

Another source, containing data up to September 28—the Outbreak.info genomic reports: scalable and dynamic surveillance of SARS-CoV-2 variants and mutations—reports that there have been 1,115 XEC cases detected worldwide.

Within Europe, XEC was initially most widespread in France, accounting for around 21 percent of confirmed COVID samples. In Germany, it accounted for 15 percent of samples and 8 percent of sequenced samples, according to an assessment from Professor Francois Balloux at the University College London, cited in the New Scientist.

Within weeks of those comments the spread of XEC has been rapid. Just in Germany, it currently accounts for 43 percent of infections and is therefore predominant. Virologists estimate that XEC has around twice the growth advantage of KP.3.1.1 and will be the dominant variant in winter.

A number of articles have cited the comments made to the LA Times by Eric Topol, the Director of the Scripps Research Translational Institute in California. Topol warns that XEC is “just getting started”, “and that’s going to take many weeks, a couple months, before it really takes hold and starts to cause a wave. XEC is definitely taking charge. That does appear to be the next variant.”

A report in the Independent published Tuesday noted of the make-up of XEC, and its two parent subvariants: “KS.1.1 is a type of what’s commonly called a FLiRT variant. It is characterised by mutations in the building block molecules phenylalanine (F) altered to leucine (L), and arginine (R) to threonine (T) on the spike protein that the virus uses to attach to human cells.

“The second omicron subvariant KP.3.3 belongs to the category FLuQE where the amino acid glutamine (Q) is mutated to glutamic acid (E) on the spike protein, making its binding to human cells more effective.”

Covid cases are on the rise across the UK, with recent data from the UK Health Security Agency (UKHSA) indicating a 21.6 percent increase in cases in England within a week.

There is no doubt that the spread of XEC virus contributed to an increase in COVID cases and deaths in Britain. In the week to September 25, there were 2,797 reported cases—an increase of 530 from the previous week. In the week to September 20 there was a 50 percent increase in COVID-related deaths in England, with 134 fatalities reported.

According to the latest data, the North East of England is witnessing the highest rate of people being hospitalised, with 8.12 people per 100,000 requiring treatment.

Virologist Dr. Stephen Griffin of the University of Leeds has been an active communicator of the science and statistics of the virus on various public platforms and social media since the start of the pandemic. He was active in various UK government committees during the height of the COVID-19. In March 2022, he gave an interview to the World Socialist Web Site.

This week Griffin spoke to the i newspaper on the continuing danger of allowing the untrammelled spread of XEC and COVID in general. “The problem with COVID is that it evolves so quickly,” he said.

He warned, “We can either increase our immunity by making better vaccines or increasing our vaccine coverage, or we can slow the virus down with interventions, such as improving indoor air quality. But we’re not doing those things.”

“Its evolutionary rate is something like three or four times faster than that of the fastest seasonal flu. So you’ve got this constant change in the virus, which accelerates the number of susceptible people.

“It’s creating its own new pool of susceptibles every time it changes to something that’s ‘immune evasive’. Every one of these subvariants is distinct enough that a whole swathe of people are no longer immune to it and it can infect them. That’s why you see this constant undulatory pattern which doesn’t look seasonal at all.”

There are no mitigations in place in Britain, as is the case internationally, to stop the spread of this virus. Advice for those with COVID symptoms is to stay at home and limit contact with others for just five days. The National Health Service advises, “You can go back to your normal activities when you feel better or do not have a high temperature”, despite the fact that the person may well still be infectious. Families are advised that children with symptoms such as a runny nose, sore throat, or mild cough can still “go to school or childcare' if they feel well enough.

The detection and rapid spread of new variants disproves the lies of governments that the pandemic is long over and COVID-19 should be treated no differently to influenza.

Deaths due to COVID in the UK rose above 244,000 by the end of September. It is only a matter of time before an even deadlier variant emerges. Last month, Sir Chris Whitty, England’s chief medical officer, told the ongoing public inquiry into COVID-19 “We have to assume a future pandemic on this scale [the global pandemic which began in 2020] will occur… That’s a certainty.”

[aobnutritionblog]

Protein's Value and Benefit in a healthy, Balanced Diet and Nutrition.

Beginning: Why are people so interested in proteins when it comes to fitness and nutrition? In fitness, building strong muscles is a big focus. That's why there are many gym supplements for sale that promise to help give your body what it needs. Protein powder, shakes, bars, and other things are some of the most popular products. But why are proteins so important?

The Fundamental Role of Proteins in the Human Body

(a). For a Healthy and Balanced Diet and Nutrition.

Proteins play a big role in our body. They're made up of long chains of amino acids that are held together by special bonds. Having a diet that includes enough protein can help our body work better in many ways.

(b). Protein and Muscle Growth

Proteins play a crucial role in muscle growth. When we exercise, our muscle fibers are broken down. The body then uses proteins to repair and rebuild these fibers, making them stronger and bigger. This is why it's important to consume enough protein in our diets, especially for those who engage in regular physical activity. Proteins provide the building blocks for muscle growth and help to support muscle recovery and repair. Consuming protein sources such as lean meats, dairy products, beans, and nuts can help ensure that our muscles have the nutrients they need to grow and become stronger.

(c). Empower and Enhance Immunity at All Times.

Fighting off minor and major infections needs all bodily organs to be fully nourished and equipped with basic structural elements to function optimally. Proteins carry structures that help build antibodies efficiently and are vital in stronger and resilient immunity.

(d). Repair and Enhance New Cell Growth in the Body.

Proteins play a huge role in all the cells in our body. They help fix old cells and make new ones. Proteins are made up of long chains of amino acids. Some of these amino acids are important for our body to work right and are called "essential" amino acids. There are essential, nonessential, and common amino acids that help power our bodies. The essential amino acids are composed of histidine, isoleucine, leucine, lysine, methionine, valine, tryptophan, threonine, and phenylalanine.

(e). Keep Proper pH in the Body at all Times.

What is pH, and why is it significant in the human body at all times? pH is the potential for hydrogen in the human body. It is a measure of the level of acids and bases at any stage in the blood. The human body must maintain a certain level of alkalinity and acidity in order to function well and optimally at all times.

(f). Source of Energy and Vitality for the Muscles and Organs.

Every body organ benefits and derives benefits from the use of proteins. You cannot expect to see a vibrant, healthy, and strong human body with less of the essential nutrients in the body.   

(g). For the Formation of Enzymes Vital in Chemical Reactions.

The fundamental role to know is that protein exists in several parts of the body, including muscle, bones, skin, hair, and bodily tissues. It’s vital in the enzymes that regulate and control chemical reactions and in the haemoglobin. Protein, whether in the format of protein shakes or protein bars, can be metabolised to support an evolved, balanced, and healthy diet.

In the End: In that sense, having a balanced diet rich in proteins from optimum nutrition Ireland, enhances the benefits of good health and overall immunity. It empowers the recipient to enjoy good health for extended good periods of time without any worries of sickness or weakness. This is because the body finds and receives all its basic and essential food requirements in a single food intake. And with that protein powder Ireland is an avenue to ramp up the overall intake of the proteins in your diet.

[paletalegear]

Bluey fun in the car with New Orleans Sain

Bluey fun in the car with New Orleans Saints football shirt

The N-terminal half of Bluey fun in the car with New Orleans Saints football shirt binds FMN ,and C-terminal domain has characteristics of a serine-threonine kinase.The photosensory domain ,located at N-terminal, has two LOV domains,which exhibit protein sequence phonology to motifs found in a diverse range of eukaryotic and prokaryotic proteins involved in sensing Light,Oxygen or Voltage, hence the acronym LOV. Blue light irradiation of protein bound FMN causes a conformational change of phototropin that triggers auto phosphorylation and starts the sensory transduction cascade.There’re two different types of phototropins (PHOT 1 and PHOT 2) in Arabidopsis that exhibits overlapping function in addition to having unique physiological roles. In absence of light,FMNs are non covalently bonded to LOV domains.But in presence of blue light,they become covalently bonded to Cysteine residues in the polypeptides. Photoexcitaton of LOV results in activation of C- terminal kinase domain,leads to auto phosphorylation on multiple serine residues.

ts football shirt

[sunaleisocial]

Protein study could help researchers develop new antibiotics

New Post has been published on https://sunalei.org/news/protein-study-could-help-researchers-develop-new-antibiotics/

Protein study could help researchers develop new antibiotics

A bacterial enzyme called histidine kinase is a promising target for new classes of antibiotics. However, it has been difficult to develop drugs that target this enzyme, because it is a “hydrophobic” protein that loses its structure once removed from its normal location in the cell membrane.

Now, an MIT-led team has found a way to make the enzyme water-soluble, which could make it possible to rapidly screen potential drugs that might interfere with its functions.

The researchers created their new version of histidine kinase by replacing four specific hydrophobic amino acids with three hydrophilic ones. Even after this significant shift, they found that the water-soluble version of the enzyme retained its natural functions.

No existing antibiotics target histidine kinase, so drugs that disrupt these functions could represent a new class of antibiotics. Such drug candidates are badly needed to combat the growing problem of antibiotic resistance.

“Each year, more than 1 million people die from antibiotic-resistant infections,” says Shuguang Zhang, a principal research scientist in the MIT Media Lab and one of the senior authors of the new study. “This protein is a good target because it’s unique to bacteria and humans don’t have it.”

Ping Xu and Fei Tao, both professors at Shanghai Jiao Tong University, are also senior authors of the paper, which appears today in Nature Communications. Mengke Li, a graduate student at Shanghai Jiao Tong University and a former visiting student at MIT, is the lead author of the paper.

A new drug target

Many of the proteins that perform critical cell functions are embedded in the cell membrane. The segments of these proteins that span the membrane are hydrophobic, which allows them to associate with the lipids that make up the membrane. However, once removed from the membrane, these proteins tend to lose their structure, which makes it difficult to study them or to screen for drugs that might interfere with them.

In 2018, Zhang and his colleagues devised a simple way to convert these proteins into water-soluble versions, which maintain their structure in water. Their technique is known as the QTY code, for the letters that represent the hydrophilic amino acids that become incorporated into the proteins. Leucine (L) becomes glutamine (Q), isoleucine (I) and valine (V) become threonine (T), and phenylalanine (F) becomes tyrosine (Y).

Since then, the researchers have demonstrated this technique on a variety of hydrophobic proteins, including antibodies, cytokine receptors, and transporters. Those transporters include a protein that cancer cells use to pump chemotherapy drugs out of the cells, as well as transporters that brain cells use to move dopamine and serotonin into or out of cells.

In the new study, the team set out to demonstrate, for the first time, that the QTY code could be used to create water-soluble enzymes that retain their enzymatic function.

The research team chose to focus on histidine kinase in part because of its potential as an antibiotic target. Currently most antibiotics work by damaging bacterial cell walls or interfering with the synthesis of ribosomes, the cell organelles that manufacture proteins. None of them target histidine kinase, an important bacterial protein that regulates processes such as antibiotic resistance and cell-to-cell communication.

Histidine kinase can perform four different functions, including phosphorylation (activating other proteins by adding a phosphate group to them) and dephosphorylation (removing phosphates). Human cells also have kinases, but they act on amino acids other than histidine, so drugs that block histidine kinase would likely not have any effect on human cells.

After using the QTY code to convert histidine kinase to a water-soluble form, the researchers tested all four of its functions and found that the protein was still able to perform them. This means that this protein could be used in high-throughput screens to rapidly test whether potential drug compounds interfere with any of those functions.

A stable structure

Using AlphaFold, an artificial intelligence program that can predict protein structures, the researchers generated a structure for their new protein and used molecular dynamics simulations to investigate how it interacts with water. They found that the protein forms stabilizing hydrogen bonds with water, which help it keep its structure.

They also found that if they only replaced the buried hydrophobic amino acids in the transmembrane segment, the protein would not retain its function. The hydrophobic amino acids have to be replaced throughout the transmembrane segment, which helps the molecule maintain the structural relationships it needs to function normally.

Zhang now plans to try this approach on methane monooxygenase, an enzyme found in bacteria that can convert methane into methanol. A water-soluble version of this enzyme could be sprayed at sites of methane release, such as barns where cows live, or thawing permafrost, helping to remove a large chunk of methane, a greenhouse gas, from the atmosphere.

“If we can use the same tool, the QTY code, on methane monooxygenase, and use that enzyme to convert methane into methanol, that could deaccelerate climate change,” Zhang says.

The QTY technique could also help scientists learn more about how signals are carried by transmembrane proteins, says William DeGrado, a professor of pharmaceutical chemistry at the University of California at San Francisco, who was not involved in the study.

“It is a great advance to be able to make functionally relevant, water-solubilized proteins,” DeGrado says. “An important question is how signals are transmitted across membranes, and this work provides a new way to approach that question.”  

The research was funded, in part, by the National Natural Science Foundation of China. 

[jcmarchi]

Protein study could help researchers develop new antibiotics

New Post has been published on https://thedigitalinsider.com/protein-study-could-help-researchers-develop-new-antibiotics/

Protein study could help researchers develop new antibiotics

A bacterial enzyme called histidine kinase is a promising target for new classes of antibiotics. However, it has been difficult to develop drugs that target this enzyme, because it is a “hydrophobic” protein that loses its structure once removed from its normal location in the cell membrane.

Now, an MIT-led team has found a way to make the enzyme water-soluble, which could make it possible to rapidly screen potential drugs that might interfere with its functions.

The researchers created their new version of histidine kinase by replacing four specific hydrophobic amino acids with three hydrophilic ones. Even after this significant shift, they found that the water-soluble version of the enzyme retained its natural functions.

No existing antibiotics target histidine kinase, so drugs that disrupt these functions could represent a new class of antibiotics. Such drug candidates are badly needed to combat the growing problem of antibiotic resistance.

“Each year, more than 1 million people die from antibiotic-resistant infections,” says Shuguang Zhang, a principal research scientist in the MIT Media Lab and one of the senior authors of the new study. “This protein is a good target because it’s unique to bacteria and humans don’t have it.”

Ping Xu and Fei Tao, both professors at Shanghai Jiao Tong University, are also senior authors of the paper, which appears today in Nature Communications. Mengke Li, a graduate student at Shanghai Jiao Tong University and a former visiting student at MIT, is the lead author of the paper.

A new drug target

Many of the proteins that perform critical cell functions are embedded in the cell membrane. The segments of these proteins that span the membrane are hydrophobic, which allows them to associate with the lipids that make up the membrane. However, once removed from the membrane, these proteins tend to lose their structure, which makes it difficult to study them or to screen for drugs that might interfere with them.

In 2018, Zhang and his colleagues devised a simple way to convert these proteins into water-soluble versions, which maintain their structure in water. Their technique is known as the QTY code, for the letters that represent the hydrophilic amino acids that become incorporated into the proteins. Leucine (L) becomes glutamine (Q), isoleucine (I) and valine (V) become threonine (T), and phenylalanine (F) becomes tyrosine (Y).

Since then, the researchers have demonstrated this technique on a variety of hydrophobic proteins, including antibodies, cytokine receptors, and transporters. Those transporters include a protein that cancer cells use to pump chemotherapy drugs out of the cells, as well as transporters that brain cells use to move dopamine and serotonin into or out of cells.

In the new study, the team set out to demonstrate, for the first time, that the QTY code could be used to create water-soluble enzymes that retain their enzymatic function.

The research team chose to focus on histidine kinase in part because of its potential as an antibiotic target. Currently most antibiotics work by damaging bacterial cell walls or interfering with the synthesis of ribosomes, the cell organelles that manufacture proteins. None of them target histidine kinase, an important bacterial protein that regulates processes such as antibiotic resistance and cell-to-cell communication.

Histidine kinase can perform four different functions, including phosphorylation (activating other proteins by adding a phosphate group to them) and dephosphorylation (removing phosphates). Human cells also have kinases, but they act on amino acids other than histidine, so drugs that block histidine kinase would likely not have any effect on human cells.

After using the QTY code to convert histidine kinase to a water-soluble form, the researchers tested all four of its functions and found that the protein was still able to perform them. This means that this protein could be used in high-throughput screens to rapidly test whether potential drug compounds interfere with any of those functions.

A stable structure

Using AlphaFold, an artificial intelligence program that can predict protein structures, the researchers generated a structure for their new protein and used molecular dynamics simulations to investigate how it interacts with water. They found that the protein forms stabilizing hydrogen bonds with water, which help it keep its structure.

They also found that if they only replaced the buried hydrophobic amino acids in the transmembrane segment, the protein would not retain its function. The hydrophobic amino acids have to be replaced throughout the transmembrane segment, which helps the molecule maintain the structural relationships it needs to function normally.

Zhang now plans to try this approach on methane monooxygenase, an enzyme found in bacteria that can convert methane into methanol. A water-soluble version of this enzyme could be sprayed at sites of methane release, such as barns where cows live, or thawing permafrost, helping to remove a large chunk of methane, a greenhouse gas, from the atmosphere.

“If we can use the same tool, the QTY code, on methane monooxygenase, and use that enzyme to convert methane into methanol, that could deaccelerate climate change,” Zhang says.

The QTY technique could also help scientists learn more about how signals are carried by transmembrane proteins, says William DeGrado, a professor of pharmaceutical chemistry at the University of California at San Francisco, who was not involved in the study.

“It is a great advance to be able to make functionally relevant, water-solubilized proteins,” DeGrado says. “An important question is how signals are transmitted across membranes, and this work provides a new way to approach that question.”  

The research was funded, in part, by the National Natural Science Foundation of China. 

[rnomics]

CIMB, Vol. 46, Pages 2598-2619: Bio-Chemoinformatics-Driven Analysis of nsp7 and nsp8 Mutations and Their Effects on Viral Replication Protein Complex Stability

The nonstructural proteins 7 and 8 (nsp7 and nsp8) of SARS-CoV-2 are highly important proteins involved in the #RNA-dependent polymerase (RdRp) protein replication complex. In this study, we analyzed the global mutation of nsp7 and nsp8 in 2022 and 2023 and analyzed the effects of mutation on the viral replication protein complex using bio-chemoinformatics. Frequently occurring variants are found to be single amino acid mutations for both nsp7 and nsp8. The most frequently occurring mutations for nsp7 which include L56F, L71F, S25L, M3I, D77N, V33I and T83I are predicted to cause destabilizing effects, whereas those in nsp8 are predicted to cause stabilizing effects, with the threonine to isoleucine mutation (T89I, T145I, T123I, T148I, T187I) being a frequent mutation. A conserved domain database analysis generated critical interaction residues for nsp7 (Lys-7, His-36 and Asn-37) and nsp8 (Lys-58, Pro-183 and Arg-190), which, according to thermodynamic calculations, are prone to destabilization. Trp-29, Phe-49 of nsp7 and Trp-154, Tyr-135 and Phe-15 of nsp8 cause greater destabilizing effects to the protein complex based on a computational alanine scan suggesting them as possible new target sites. This study provides an intensive analysis of the mutations of nsp7 and nsp8 and their possible implications for viral complex stability. https://www.mdpi.com/1467-3045/46/3/165?utm_source=dlvr.it&utm_medium=tumblr

[lalsingh228-blog]

Amino Acids Market Size, Share, Growth, Trends, Analysis 2028

Global Amino Acids Market Report from AMA Research highlights deep analysis on market characteristics, sizing, estimates and growth by segmentation, regional breakdowns & country along with competitive landscape, player’s market shares, and strategies that are key in the market. The exploration provides a 360° view and insights, highlighting major outcomes of the industry. These insights help the business decision-makers to formulate better business plans and make informed decisions to improved profitability. In addition, the study helps venture or private players in understanding the companies in more detail to make better informed decisions. Major Players in This Report Include, Ajinomoto Co., Inc. (Japan), Adisseo France S.A.S (France), Archer Daniels Midland Company (United States), Chongqing Unisplendour Chemical Co., Ltd. (China), CJ CheilJedang Corporation (South Korea), Daesang Corporation (South Korea), Evonik Industries AG (Germany), Fufeng Group Company Limited (China), Global Bio-Chem Technology Group Company Limited (Hong Kong), Hebei Donghua Chemical Group (China). Free Sample Report + All Related Graphs & Charts @: https://www.advancemarketanalytics.com/sample-report/19302-global-amino-acids-market Amino Acids is one of the vital chemical used in manufacturing variety of products  including animal feed, food & beverages, pharma & health care, nutraceuticals, cosmetics & personal care, and many others. The human body is contains almost 20% of proteins and amino acids plays an important role in building blocks of protein, the amino acids will significantly assist animal food as well as foods & beverage manufacturing. Market Drivers

Minimizes Volatility in Human Body Protein Contents

Increasing Health-Consciousness among Consumers

Market Trend

Increasing Demand Low Calorie Artificial Sweeteners in Food and Beverage Industry

Growing Applications in Pharmaceutical Industry

Opportunities

Introduction to Protein Rich Food, Beverages as well as Animal Foods

Growing Opportunities for Amino Acids in Aquaculture Industry

Challenges

Increasing Prices of Protein Contained Foods

Enquire for customization in Report @: https://www.advancemarketanalytics.com/enquiry-before-buy/19302-global-amino-acids-market In this research study, the prime factors that are impelling the growth of the Global Amino Acids market report have been studied thoroughly in a bid to estimate the overall value and the size of this market by the end of the forecast period. The impact of the driving forces, limitations, challenges, and opportunities has been examined extensively. The key trends that manage the interest of the customers have also been interpreted accurately for the benefit of the readers. The Amino Acids market study is being classified by Type (L-Glutamic Acid/MSG, L-Lysine, Methionine, L-Threonine, L-Tryptophan, Glycine, L-Phenylalanine, L-Aspartic Acid), Application (Animal Feed, Food & Beverages, Pharma & Health Care, Nutraceuticals, Cosmetics & Personal Care, Others), Source (Plant-Based, Animal-Based, Microbial-Based) The report concludes with in-depth details on the business operations and financial structure of leading vendors in the Global Amino Acids market report, Overview of Key trends in the past and present are in reports that are reported to be beneficial for companies looking for venture businesses in this market. Information about the various marketing channels and well-known distributors in this market was also provided here. This study serves as a rich guide for established players and new players in this market. Get Reasonable Discount on This Premium Report @ https://www.advancemarketanalytics.com/request-discount/19302-global-amino-acids-market Extracts from Table of Contents Amino Acids Market Research Report Chapter 1 Amino Acids Market Overview Chapter 2 Global Economic Impact on Industry Chapter 3 Global Market Competition by Manufacturers Chapter 4 Global Revenue (Value, Volume*) by Region Chapter 5 Global Supplies (Production), Consumption, Export, Import by Regions Chapter 6 Global Revenue (Value, Volume*), Price* Trend by Type Chapter 7 Global Market Analysis by Application ………………….continued This report also analyzes the regulatory framework of the Global Markets Amino Acids Market Report to inform stakeholders about the various norms, regulations, this can have an impact. It also collects in-depth information from the detailed primary and secondary research techniques analyzed using the most efficient analysis tools. Based on the statistics gained from this systematic study, market research provides estimates for market participants and readers. Contact US : Craig Francis (PR & Marketing Manager) AMA Research & Media LLP Unit No. 429, Parsonage Road Edison, NJ New Jersey USA – 08837 Phone: +1 201 565 3262, +44 161 818 8166 sales@advancemarketanalytics.com

[omkarpatel]

Ornithine Transcarbamylase (OTC) Deficiency Treatment

Ornithine transcarbamylase (OTC) deficiency is an inherited genetic disorder that affects the body's ability to break down ammonia during protein metabolism. If not treated properly, OTC deficiency can cause serious medical issues and even death. Today, there are several effective treatment options available that can help people with OTC deficiency live healthier lives. Let’s take a closer look at OTC deficiency and its treatment: What is OTC deficiency? OTC deficiency occurs due to mutations in the OTC gene which provides instructions for making the ornithine transcarbamylase (OTC) enzyme. This enzyme helps convert ammonia, which is a byproduct of protein breakdown, into urea that can then be safely excreted from the body through urine. With OTC deficiency, the body is unable to effectively remove ammonia due to malfunctioning or non-existent OTC enzyme. This causes excess levels of ammonia, also known as hyperammonemia, in the blood. If left untreated, hyperammonemia can damage the brain and cause complications like intellectual disabilities, coma and even death. Symptoms of OTC deficiency vary from mild to severe depending on the levels of ammonia in the blood. Babies usually present symptoms within the first week of life which may include vomiting, lack of energy, seizures and breathing problems. In some cases, individuals may experience milder symptoms like headaches, nausea and confusion that only emerge during periods of stress or fasting later in life. Treatment Options While there is no cure for OTC deficiency, early detection and lifelong treatment can help manage the condition effectively. The main goals of treatment are to: - Reduce ammonia production by restricting dietary protein intake - Enable removal of ammonia through alternative pathways - Prevent catabolism that breaks down protein - Supplement essential amino acids that are restricted - Treat episodes of hyperammonemia promptly Some of the major treatment options for OTC deficiency include: Low-protein diet: Restricting protein intake is the primary treatment approach as it reduces the production of excess ammonia during protein metabolism. Foods are assigned point values based on their protein content and individuals follow a careful diet plan tailored to their needs and age. Carglumic acid: This drug helps activate an alternative pathway to remove ammonia from the body. It works by stimulating the N-acetylglutamate synthase enzyme which is necessary for urea cycle function. Sodium phenylbutyrate: This medication helps elimnate excess amino acids and allows nitrogen to be excreted in forms other than ammonia. It is often taken with carglumic acid for added benefit. Protein substitutions: Essential amino acids like lysine, threonine and tryptophan that are otherwise restricted for their protein content are supplemented. This prevents deficiency while maintaining a low protein intake. Drugs for hyperammonemia: Episodes of extremely high ammonia levels are treated promptly with medications like sodium benzoate or sodium phenylacetate to enhance ammonia removal along with other supportive measures. Liver transplantation: For patients who do not respond well to dietary and drug therapies, liver transplantation may be considered as it provides a new organ capable of efficient urea cycle function. However, it carries risks and lifelong immune suppression. Proper treatment protocol and diligence Adhering strictly to the prescribed treatment protocol is very important for effectively managing OTC deficiency over a lifetime. Some key points regarding protocol and diligence include:

[marketinsight1234]

Food Amino Acid Market: Global Industry Analysis and Forecast 2023 – 2030

The Food Amino Acid market estimated at USD 7.18 Billion in the year 2022, is projected to reach a revised size of USD 12.90 Billion by 2030, growing at a CAGR of 7.6% over the analysis period 2023-2030.

Food Amino Acids are molecules combined and used by all living things to form proteins. Essential amino acids include isoleucine, histidine, leucine, methionine, lysine, phenylalanine, threonine, valine, and tryptophan. Major foods that contain amino acids are meat, poultry, soy, black beans, cheese, mushroom, peanuts, dairy, beans, legumes, fish, chicken, quinoa, grains, and nuts.

The Food Amino Acid Market has witnessed significant growth in recent years, driven by increasing consumer awareness about the health benefits of amino acids and their essential role in the human diet. Amino acids are the building blocks of proteins and play a crucial role in various physiological functions.

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The latest research on the Food Amino Acid market provides a comprehensive overview of the market for the years 2023 to 2030. It gives a comprehensive picture of the global Food Amino Acid industry, considering all significant industry trends, market dynamics, competitive landscape, and market analysis tools such as Porter's five forces analysis, Industry Value chain analysis, and PESTEL analysis of the Food Amino Acid market. Moreover, the report includes significant chapters such as Patent Analysis, Regulatory Framework, Technology Roadmap, BCG Matrix, Heat Map Analysis, Price Trend Analysis, and Investment Analysis which help to understand the market direction and movement in the current and upcoming years. The report is designed to help readers find information and make decisions that will help them grow their businesses. The study is written with a specific goal in mind: to give business insights and consultancy to help customers make smart business decisions and achieve long-term success in their particular market areas.

Leading players involved in the Food Amino Acid Market include:

Kemin Industries, Inc. (USA), Pacific Rainbow International Inc. (US), Kingchem LLC (US), Sigma-Aldrich, Co. LLC. (US), Prinova Group LLC. (US), Phibro Animal Health Corporation (USA), ANGUS Chemical Company (USA), Rochem International Inc. (New York), Evonik Industries AG (Germany), Taiyo International (Germany), Brenntag AG (Germany), Azelis S.A (Europe) 

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Segmentation of Food Amino Acid Market:

By Type

Glutamic Acid

Lysine

Tryptophan

Methionine

By Application

Dietary Supplements

Infant Formula

Food Fortification

Convenience Foods

By Source

Plant-Based

Animal-Based

Synthetic

By Regions: -

North America (US, Canada, Mexico)

Eastern Europe (Bulgaria, The Czech Republic, Hungary, Poland, Romania, Rest of Eastern Europe)

Western Europe (Germany, UK, France, Netherlands, Italy, Russia, Spain, Rest of Western Europe)

Asia Pacific (China, India, Japan, South Korea, Malaysia, Thailand, Vietnam, The Philippines, Australia, New Zealand, Rest of APAC)

Middle East & Africa (Turkey, Bahrain, Kuwait, Saudi Arabia, Qatar, UAE, Israel, South Africa)

South America (Brazil, Argentina, Rest of SA)

What to Expect in Our Report?

(1) A complete section of the Food Amino Acid market report is dedicated for market dynamics, which include influence factors, market drivers, challenges, opportunities, and trends.

(2) Another broad section of the research study is reserved for regional analysis of the Food Amino Acid market where important regions and countries are assessed for their growth potential, consumption, market share, and other vital factors indicating their market growth.

(3) Players can use the competitive analysis provided in the report to build new strategies or fine-tune their existing ones to rise above market challenges and increase their share of the Food Amino Acid market.

(4) The report also discusses competitive situation and trends and sheds light on company expansions and merger and acquisition taking place in the Food Amino Acid market. Moreover, it brings to light the market concentration rate and market shares of top three and five players.

(5) Readers are provided with findings and conclusion of the research study provided in the Food Amino Acid Market report.

Our study encompasses major growth determinants and drivers, along with extensive segmentation areas. Through in-depth analysis of supply and sales channels, including upstream and downstream fundamentals, we present a complete market ecosystem.

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[themarketinsights]

Mitogen Activated Protein Kinase 8 Market – Major Technology Giants in Buzz Again

Latest released the research study on Global Mitogen Activated Protein Kinase 8 Market, offers a detailed overview of the factors influencing the global business scope. Mitogen Activated Protein Kinase 8 Market research report shows the latest market insights, current situation analysis with upcoming trends and breakdown of the products and services. The report provides key statistics on the market status, size, share, growth factors of the Mitogen Activated Protein Kinase 8 The study covers emerging player’s data, including: competitive landscape, sales, revenue and global market share of top manufacturers are Bristol Myers Squibb Company (Celgene Corp) (United States), Eisai Co., Ltd. (Japan), OPKO Health (United States), Xigen SA (Switzerland), Fulcrum Therapeutics (United States)

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Mitogen Activated Protein Kinase 8 Market Definition:

MAPK8 (Mitogen-Activated Protein Kinase 8) is a Protein Coding gene. Diseases like Fatty Liver Disease and Hepatitis C are associated with MAPK8. Serine/threonine-protein kinase is involved in various processes such as cell proliferation, differentiation, migration, transformation, and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. The MAP kinases act as an integration point for multiple biochemical signals involved with a variety of cellular processes, the activation of this kinase by tumor necrosis factor-alpha if required for TNF-alpha induced apoptosis.

Market Trend:

Increasing Number Cases Related to The Breast Cancer

High Adoption of CC-90001

Market Drivers:

Rising Demand due to Growing Prevalences of the Cancer and Gene Study

Increasing Investment in Healthcare Sector

Market Opportunities:

High Demand From the Developing Countries

Growing Demand due to Ongoing Research and Development activities across the World

The Global Mitogen Activated Protein Kinase 8 Market segments and Market Data Break Down are illuminated below:

by Type (CC-90001, SR-3306, ER-358063, WBZ-4, Others), Application (Breast Cancer, Alzheimer's Disease, Acute Renal Failure, Liver Failure, Others)

Region Included are: North America, Europe, Asia Pacific, Oceania, South America, Middle East & Africa

Country Level Break-Up: United States, Canada, Mexico, Brazil, Argentina, Colombia, Chile, South Africa, Nigeria, Tunisia, Morocco, Germany, United Kingdom (UK), the Netherlands, Spain, Italy, Belgium, Austria, Turkey, Russia, France, Poland, Israel, United Arab Emirates, Qatar, Saudi Arabia, China, Japan, Taiwan, South Korea, Singapore, India, Australia and New Zealand etc.

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Strategic Points Covered in Table of Content of Global Mitogen Activated Protein Kinase 8 Market:

Chapter 1: Introduction, market driving force product Objective of Study and Research Scope the Mitogen Activated Protein Kinase 8 market

Chapter 2: Exclusive Summary – the basic information of the Mitogen Activated Protein Kinase 8 Market.

Chapter 3: Displayingthe Market Dynamics- Drivers, Trends and Challenges of the Mitogen Activated Protein Kinase 8

Chapter 4: Presenting the Mitogen Activated Protein Kinase 8 Market Factor Analysis Porters Five Forces, Supply/Value Chain, PESTEL analysis, Market Entropy, Patent/Trademark Analysis.

Chapter 5: Displaying market size by Type, End User and Region 2015-2020

Chapter 6: Evaluating the leading manufacturers of the Mitogen Activated Protein Kinase 8 market which consists of its Competitive Landscape, Peer Group Analysis, BCG Matrix & Company Profile

Chapter 7: To evaluate the market by segments, by countries and by manufacturers with revenue share and sales by key countries (2021-2026).

Chapter 8 & 9: Displaying the Appendix, Methodology and Data Source

Finally, Mitogen Activated Protein Kinase 8 Market is a valuable source of guidance for individuals and companies in decision framework.

Data Sources & Methodology The primary sources involves the industry experts from the Global Mitogen Activated Protein Kinase 8 Market including the management organizations, processing organizations, analytics service providers of the industry’s value chain. All primary sources were interviewed to gather and authenticate qualitative & quantitative information and determine the future prospects.

In the extensive primary research process undertaken for this study, the primary sources – Postal Surveys, telephone, Online & Face-to-Face Survey were considered to obtain and verify both qualitative and quantitative aspects of this research study. When it comes to secondary sources Company's Annual reports, press Releases, Websites, Investor Presentation, Conference Call transcripts, Webinar, Journals, Regulators, National Customs and Industry Associations were given primary weight-age.

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Latest industry influencing trends and development scenario

Open up New Markets

To Seize powerful market opportunities

Key decision in planning and to further expand market share

Identify Key Business Segments, Market proposition & Gap Analysis

Assisting in allocating marketing investments

Definitively, this report will give you an unmistakable perspective on every single reality of the market without a need to allude to some other research report or an information source. Our report will give all of you the realities about the past, present, and eventual fate of the concerned Market.

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[chemanalystdata]

Threonine Prices | Pricing | News| Database | Index | Chart | Forecast

 Threonine Prices, an essential amino acid critical for protein synthesis and various metabolic processes, has seen considerable fluctuations in its market price over recent years. As a key component in animal feed, particularly for livestock like pigs and poultry, threonine's demand is closely tied to the agricultural sector. The price of threonine can be influenced by numerous factors, including global agricultural trends, production costs, and supply chain dynamics. In recent times, the price of threonine has been subject to volatility, reflecting broader trends in the commodity markets. The global demand for high-quality animal protein has driven the need for effective feed additives, including threonine, which has consequently impacted its market value.

One significant factor affecting threonine prices is the cost of raw materials and production. Threonine is synthesized through a fermentation process, which requires specific strains of microorganisms and substantial quantities of nutrients. Variations in the availability and cost of these raw materials can directly impact the production cost of threonine, thereby influencing its market price. Additionally, fluctuations in energy prices can affect the overall cost of manufacturing threonine, as energy is a critical input in the fermentation process.

Economic conditions play a crucial role in shaping threonine prices as well. During periods of economic growth, increased consumer spending can lead to higher demand for meat and dairy products, subsequently boosting the need for threonine in animal feed. Conversely, economic downturns can lead to reduced demand for animal products, impacting the threonine market negatively. Moreover, trade policies and international relations also contribute to price fluctuations. Tariffs, trade agreements, and geopolitical tensions can disrupt supply chains and influence the cost of threonine, as countries navigate the complexities of global trade.

Get Real Time Prices for Threonine : https://www.chemanalyst.com/Pricing-data/threonine-1510Supply chain disruptions have become increasingly relevant in recent years, exacerbating price volatility in the threonine market. Events such as natural disasters, pandemics, and logistical challenges can impede the production and distribution of threonine, leading to temporary shortages and price increases. For instance, disruptions in shipping routes or delays in raw material supply can create bottlenecks in production, causing prices to rise. Manufacturers and distributors must navigate these challenges to maintain a steady supply of threonine, which can affect market stability.

Furthermore, technological advancements and innovations in production processes can influence threonine prices. Ongoing research and development efforts aim to improve the efficiency of fermentation processes and reduce production costs. As technology advances, manufacturers may be able to produce threonine more cost-effectively, potentially leading to price reductions. However, the initial investment in new technologies can be significant, and the benefits of such advancements may take time to materialize in the market.

The regulatory environment is another important factor impacting threonine prices. Governments and regulatory bodies often impose standards and regulations related to the use of additives in animal feed, which can affect production processes and costs. Compliance with these regulations may require additional investments in quality control and safety measures, influencing the overall price of threonine. Furthermore, changes in regulatory policies or the introduction of new guidelines can have both short-term and long-term effects on the threonine market.

Consumer preferences and dietary trends also play a role in shaping threonine prices. As awareness of nutrition and animal welfare grows, there is increasing demand for sustainable and high-quality animal feed. This trend can drive up the demand for threonine, particularly in markets where consumers are willing to pay a premium for products that meet specific quality standards. Consequently, the price of threonine can be influenced by shifts in consumer behavior and preferences.

In conclusion, the pricing of threonine is influenced by a complex interplay of factors, including production costs, economic conditions, supply chain dynamics, technological advancements, regulatory environments, and consumer trends. As a vital component in animal feed, threonine's market value reflects broader trends in the agricultural and commodity sectors. Understanding these factors is essential for stakeholders in the threonine market to navigate price fluctuations and make informed decisions. The ongoing evolution of the threonine market highlights the need for continued attention to these variables to maintain stability and address challenges effectively.

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[covid-safer-hotties]

Also preserved on our archive

By Jabed Ahmed

A new Covid variant has been reported across the globe with fears it will soon be the dominant strain of the illness.

Cases of the XEC variant, first detected in Germany in June, have since been reported in the UK, United States, Denmark and other countries. Experts say the strain is now “taking charge” and will likely continue to spread globally.

Researchers predicted in August this variant could take anywhere from few weeks to a couple months to take off and spread more rapidly.

The strain has now been detected in at least 29 countries and 24 US states.

XEC, a sublineage of the omicron variant, was first reported in Berlin, Germany, in June and is now spreading “quite rapidly” across Europe, North America and Asia, according to Covid data analyst Mike Honey.

The Czech Republic had the highest prevalence of the variant as 16 per cent of Covid case samples from the country contained XEC.

The strain, a combination of the KS.1.1 and KP.3.3 variants, presents symptoms similar to those of other Covid variants including tiredness, headaches, a sore throat and high temperatures. However, researchers have called for monitoring the XEC variant more closely to better understand its symptoms.

Prof Francois Balloux, Director of the Genetics Institute at University College London told the BBC that the XEC variant is more contagious but that vaccines should still offer good protection as it is from the Omicron family. He says it is possible XEC will become the dominant subvariant over the winter though.

KS.1.1 is a type of what’s commonly called a FLiRT variant.

It is characterised by mutations in the building block molecules phenylalanine (F) altered to leucine (L), and arginine (R) to threonine (T) on the spike protein that the virus uses to attach to human cells.

The second omicron subvariant KP.3.3 belongs to the category FLuQE where the amino acid glutamine (Q) is mutated to glutamic acid (E) on the spike protein, making its binding to human cells more effective.

As the novel coronavirus continues to evolve, data suggests XEC is growing steadily each day with an advantage over previously known subvariants.

Its symptoms are similar to those of previous Covid variants, including fever, sore throat, cough, loss of sense of smell, loss of appetite, and body aches.

But since it is still only a sub-family of the same omicron lineage, experts say keeping up to date with vaccines and booster shots would offer sufficient protection against severe illness and hospitalisation.

The US Centers for Disease Control & Prevention also advises people to practise good hygiene and to take steps for cleaner air.

Researchers have called for monitoring the XEC variant more closely to better understand its symptoms.

[firstmoveronline]

Is 14-3-3 the Combination to Unlock New Pathways to Improve Metabolic Homeostasis and β-Cell Function?

Since their discovery nearly five decades ago, molecular scaffolds belonging to the 14-3-3 protein family have been recognized as pleiotropic regulators of diverse cellular and physiological functions. With their ability to bind to proteins harboring specific serine and threonine phosphorylation motifs, 14-3-3 proteins can interact with and influence the function of docking proteins, enzymes,…

[paletalegear]

Bluey fun in the car with New Orleans Saints football shirt The N-terminal half of Bluey fun in the car with New Orleans Saints football shirt binds FMN ,and C-terminal domain has characteristics of a serine-threonine kinase.The photosensory domain ,located at N-terminal, has two LOV domains,which exhibit protein sequence phonology to motifs found in a diverse range of eukaryotic and prokaryotic…

[sunaleisocial]

“Rosetta Stone” of cell signaling could expedite precision cancer medicine

New Post has been published on https://sunalei.org/news/rosetta-stone-of-cell-signaling-could-expedite-precision-cancer-medicine/

“Rosetta Stone” of cell signaling could expedite precision cancer medicine

A newly complete database of human protein kinases and their preferred binding sites provides a powerful new platform to investigate cell signaling pathways.

Culminating 25 years of research, MIT, Harvard University, and Yale University scientists and collaborators have unveiled a comprehensive atlas of human tyrosine kinases — enzymes that regulate a wide variety of cellular activities — and their binding sites.

The addition of tyrosine kinases to a previously published dataset from the same group now completes a free, publicly available atlas of all human kinases and their specific binding sites on proteins, which together orchestrate fundamental cell processes such as growth, cell division, and metabolism.

Now, researchers can use data from mass spectrometry, a common laboratory technique, to identify the kinases involved in normal and dysregulated cell signaling in human tissue, such as during inflammation or cancer progression.

“I am most excited about being able to apply this to individual patients’ tumors and learn about the signaling states of cancer and heterogeneity of that signaling,” says Michael Yaffe, who is the David H. Koch Professor of Science at MIT, the director of the MIT Center for Precision Cancer Medicine, a member of MIT’s Koch Institute for Integrative Cancer Research, and a senior author of the new study. “This could reveal new druggable targets or novel combination therapies.”

The study, published in Nature, is the product of a long-standing collaboration with senior authors Lewis Cantley at Harvard Medical School and Dana-Farber Cancer Institute, Benjamin Turk at Yale School of Medicine, and Jared Johnson at Weill Cornell Medical College.

The paper’s lead authors are Tomer Yaron-Barir at Columbia University Irving Medical Center, and MIT’s Brian Joughin, with contributions from Kontstantin Krismer, Mina Takegami, and Pau Creixell.

Kinase kingdom

Human cells are governed by a network of diverse protein kinases that alter the properties of other proteins by adding or removing chemical compounds called phosphate groups. Phosphate groups are small but powerful: When attached to proteins, they can turn proteins on or off, or even dramatically change their function. Identifying which of the almost 400 human kinases phosphorylate a specific protein at a particular site on the protein was traditionally a lengthy, laborious process.

Beginning in the mid 1990s, the Cantley laboratory developed a method using a library of small peptides to identify the optimal amino acid sequence — called a motif, similar to a scannable barcode — that a kinase targets on its substrate proteins for the addition of a phosphate group. Over the ensuing years, Yaffe, Turk, and Johnson, all of whom spent time as postdocs in the Cantley lab, made seminal advancements in the technique, increasing its throughput, accuracy, and utility.

Johnson led a massive experimental effort exposing batches of kinases to these peptide libraries and observed which kinases phosphorylated which subsets of peptides. In a corresponding Nature paper published in January 2023, the team mapped more than 300 serine/threonine kinases, the other main type of protein kinase, to their motifs. In the current paper, they complete the human “kinome” by successfully mapping 93 tyrosine kinases to their corresponding motifs.

Next, by creating and using advanced computational tools, Yaron-Barir, Krismer, Joughin, Takegami, and Yaffe tested whether the results were predictive of real proteins, and whether the results might reveal unknown signaling events in normal and cancer cells. By analyzing phosphoproteomic data from mass spectrometry to reveal phosphorylation patterns in cells, their atlas accurately predicted tyrosine kinase activity in previously studied cell signaling pathways.

For example, using recently published phosphoproteomic data of human lung cancer cells treated with two targeted drugs, the atlas identified that treatment with erlotinib, a known inhibitor of the protein EGFR, downregulated sites matching a motif for EGFR. Treatment with afatinib, a known HER2 inhibitor, downregulated sites matching the HER2 motif. Unexpectedly, afatinib treatment also upregulated the motif for the tyrosine kinase MET, a finding that helps explain patient data linking MET activity to afatinib drug resistance.

Actionable results

There are two key ways researchers can use the new atlas. First, for a protein of interest that is being phosphorylated, the atlas can be used to narrow down hundreds of kinases to a short list of candidates likely to be involved. “The predictions that come from using this will still need to be validated experimentally, but it’s a huge step forward in making clear predictions that can be tested,” says Yaffe.

Second, the atlas makes phosphoproteomic data more useful and actionable. In the past, researchers might gather phosphoproteomic data from a tissue sample, but it was difficult to know what that data was saying or how to best use it to guide next steps in research. Now, that data can be used to predict which kinases are upregulated or downregulated and therefore which cellular signaling pathways are active or not.

“We now have a new tool now to interpret those large datasets, a Rosetta Stone for phosphoproteomics,” says Yaffe. “It is going to be particularly helpful for turning this type of disease data into actionable items.”

In the context of cancer, phosophoproteomic data from a patient’s tumor biopsy could be used to help doctors quickly identify which kinases and cell signaling pathways are involved in cancer expansion or drug resistance, then use that knowledge to target those pathways with appropriate drug therapy or combination therapy.

Yaffe’s lab and their colleagues at the National Institutes of Health are now using the atlas to seek out new insights into difficult cancers, including appendiceal cancer and neuroendocrine tumors. While many cancers have been shown to have a strong genetic component, such as the genes BRCA1 and BRCA2 in breast cancer, other cancers are not associated with any known genetic cause. “We’re using this atlas to interrogate these tumors that don’t seem to have a clear genetic driver to see if we can identify kinases that are driving cancer progression,” he says.

Biological insights

In addition to completing the human kinase atlas, the team made two biological discoveries in their recent study. First, they identified three main classes of phosphorylation motifs, or barcodes, for tyrosine kinases. The first class is motifs that map to multiple kinases, suggesting that numerous signaling pathways converge to phosphorylate a protein boasting that motif. The second class is motifs with a one-to-one match between motif and kinase, in which only a specific kinase will activate a protein with that motif. This came as a partial surprise, as tyrosine kinases have been thought to have minimal specificity by some in the field.

The final class includes motifs for which there is no clear match to one of the 78 classical tyrosine kinases. This class includes motifs that match to 15 atypical tyrosine kinases known to also phosphorylate serine or threonine residues. “This means that there’s a subset of kinases that we didn’t recognize that are actually playing an important role,” says Yaffe. It also indicates there may be other mechanisms besides motifs alone that affect how a kinase interacts with a protein.

The team also discovered that tyrosine kinase motifs are tightly conserved between humans and the worm species C. elegans, despite the species being separated by more than 600 million years of evolution. In other words, a worm kinase and its human homologue are phosphorylating essentially the same motif. That sequence preservation suggests that tyrosine kinases are highly critical to signaling pathways in all multicellular organisms, and any small change would be harmful to an organism.

The research was funded by the Charles and Marjorie Holloway Foundation, the MIT Center for Precision Cancer Medicine, the Koch Institute Frontier Research Program via L. Scott Ritterbush, the Leukemia and Lymphoma Society, the National Institutes of Health, Cancer Research UK, the Brain Tumour Charity, and the Koch Institute Support (core) grant from the National Cancer Institute.