Category Archives: Biochemistry

Plant-based testosterone in pine pollen could be a goldmine for forestry – New Zealand Herald

Pine pollen is the fine yellow powder released by pine trees every spring that forms part of the reproductive life cycle of the tree. Photo / Supplied

Pine pollen containing a rare natural source of plant-based testosterone could prove a goldmine for New Zealand's forestry sector.

Pine Pollen New Zealand Limited, trading under the name Bio Gold, has received $288,500 in Government funding through the Ministry for Primary Industries' Sustainable Food and Fibre Futures fund (SFF Futures) to lay the foundations for a pine pollen industry in New Zealand.

"Pine pollen has been consumed for health and wellbeing in China, South Korea and Japan for more than 3000 years," Bio Gold founder Carl Meyer said.

"It's been found to contain a naturally occurring testosterone, and lately there's been a new wave of interest from the natural health industry in the United States and Canada."

Common reasons for taking pine pollen as a dietary supplement include supporting energy levels, hormonal balance, immune function, and overall wellbeing.

"We've furthered our research and development work for the past 18 months with the help of SFF Futures funding to understand how the biochemistry of New Zealand pine pollen differs in relation to factors such as species, genetics, location, and more," Meyer said.

"We've also compared our pollen to that from overseas and it's looking very promising."

Pine pollen is the fine yellow powder released by pine trees every spring that forms part of the reproductive life cycle of the tree.

The powder is produced inside the catkin (male flowers) of pine trees.

"We've spent years working out which specific type of Pinus radiata yields the best pollen it's not a matter of using any old pine tree," Meyer said.

"It's very complex, and you've got to really know what you're doing. Safety and quality are our top priorities."

Meyer said the final product was expensive because the seasonal window for pine pollen was often less than three weeks.

Bio Gold's pollen was currently harvested near Hanmer Springs and Kaikura from trees on land owned and operated by Ngi Tahu Forestry, he said.

"However, we're also open to exploring additional partnerships with other forest owners across New Zealand, as well as connecting with entrepreneurs, investors, and health companies to help scale things up. We encourage people to reach out to us.

Callaghan Innovation had helped with research, including providing funding for a top Master's student to investigate biochemistry and extraction on an even deeper level, Meyer said.

"The University of Canterbury has also assisted with harvesting trials, and we're developing technology that's able to do large-scale harvesting."

Bio Gold has developed two prototype products so far.

One is a concentrated liquid "Supercharge" extract to support energy levels, sports and exercise performance, libido, and vitality.

The other is a raw powder that can be added to smoothies and drinks for overall wellbeing.

"Establishing this industry means New Zealanders will be able to enjoy any benefits that pine pollen offers," Meyer said.

"Our local customers love the pollen, and we're getting excellent feedback from them. We're also looking at high-value export opportunities."

Steve Penno, MPI's director of investment programmes, said Bio Gold had identified an opportunity to increase the value of New Zealand's forestry industry, and create new jobs in regional communities.

"Investing in this high-value product is helping Bio Gold fast-track their research and take this initiative to a full-scale operation."

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Plant-based testosterone in pine pollen could be a goldmine for forestry - New Zealand Herald

Researchers Develop Next-Gen Cancer Therapy – University of Houston

Oncolytic viruses are those that can kill cancer cells while leaving nearby healthy cells and tissues intact. Image of cancer cells courtesy: GettyImages

Shaun Zhang, director of the Center for Nuclear Receptors and Cell Signaling at the University of Houston and M.D. Anderson Professor in the Department of Biology & Biochemistry, has created a new oncolytic virus, pushing oncolytic cancer therapy forward.

Among the most promising anti-cancer treatments in recent years, oncolytic virotherapy (OV) has emerged at the top of the pack of immunotherapy. Oncolytic viruses are those that can kill cancer cells while leaving nearby healthy cells and tissues intact. In oncolytic virotherapy, the treatment also exerts its influence by activating an antitumor immune response made of immune cells such as natural killer (NK) cells.

But sometimes those natural killers limit the oncolytic viruses, and so despite the exciting development in the OV field in recent years, there is room for improvement to tackle some limitations, including the relatively weak therapeutic activity and lack of means for effective systemic delivery.

Those improvements are now being made in the lab of Shaun Zhang, director of the Center for Nuclear Receptors and Cell Signaling at the University of Houston and M.D. Anderson Professor in the Department of Biology & Biochemistry. Zhang has received a $1.8 million grant from the National Institutes of Health to support his work.

We have developed a novel strategy that not only can prevent NK cells from clearing the administered oncolytic virus, but also goes one step further by guiding them to attack tumor cells. We took an entirely different approach to create this oncolytic virotherapy by deleting a region of the gene which has been shown to activate the signaling pathway that enables the virus to replicate in normal cells, said Zhang.

The different approach consists of Zhangs lab creating a new oncolytic virus called FusOn-H2, based on the Herpes simplex 2 virus, (HSV-2, commonly known as genital herpes). Its the first of its kind. They arm the virus with a NK cell engager, resulting in what Zhang calls the two birds with one stone strategy to enhance therapeutic effect of the new oncolytic virus. This engager forms a bridge between NK cells and tumor cells, resulting in the killing of the engaged tumor cells.

Our recent studies showed that arming FusOn-H2 with a chimeric NK engager (C-NK-E) that can engage the infiltrated natural killer cells with tumor cells could significantly enhance the effectiveness of this virotherapy, said Zhang. Most importantly, we observed that tumor destruction by the joint effect of the direct oncolysis and the engaged NK cells led to a measurable elicitation of neoantigen-specific antitumor immunity.

Zhang and team believe that this armed FusOn-H2 will produce a three-pronged effect to enhance the antitumor efficacy against solid tumors in colon and lung cancer, which they expect to come in waves.

The first wave comes immediately after the armed virus is administered and it derives primarily from administration of the virus. The second wave comes from the natural killer cells doing their work while the third wave is the outcome of a series of chain events that ultimately result in inducing neoantigen-specific antitumor immunity.

We hypothesize that the combination of the high potency of the three-pronged therapy with the improved systemic delivery will lead to effective treatment of metastatic diseases, said Zhang.

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Researchers Develop Next-Gen Cancer Therapy - University of Houston

Researchers use rapid antibody test to gauge immune response to SARS-CoV-2 variants – University of Toronto

COVID-19 infections are once again on the rise as our immune systems struggle to combat new variants.

Thats according to a University of Toronto study that foundthe antibodies generated by people who were vaccinated and/or recovered from COVID-19prior to 2022 failed to neutralize the variants circulating today.

Furthermore, the researchers expect that the antibody test they developed to measure immunity in the studys participants will become a valuable tool for deciding who needs a booster and when,helping to save lives and avoid future lockdowns.

The truth is we dont yet know how frequent our shots should be to prevent infection, saidIgor Stagljar, a professor of biochemistry and molecular geneticsat theDonnelly Centre for Cellular and Biomolecular Research andat the Temerty Faculty of Medicine. To answer these questions, we need rapid, inexpensive and quantitative tests that specifically measure Sars-CoV-2 neutralizing antibodies, which are the ones that prevent infection.

The study was led byStagljarand Shawn Owen, an associate professor of pharmaceutics and pharmaceutical chemistry, at the University of Utah.

The journalNature Communications recentlypublished their findings.

Many antibody tests have been developed over the past two years. But only a few of the authorized ones are designed to monitor neutralizing antibodies, which coat the viral spike protein so that it can no longer bind its receptor and enter cells.

It's an important distinction, as only a fraction of all Sars-CoV-2 antibodies generated during infection are neutralizing. And while most vaccines were specifically designed to produce neutralizing antibodies, its not clear how much protection they give against variants.

Our method, which we named Neu-SATiN, is as accurate as but faster and cheaper than the gold standard, and it can be quickly adapted for new variants as they emerge, Stagljar said.

Neu-SATiN stands forNeutralizationSerologicalAssay based on splitTri-partNanoluciferase, and it is a newer version ofSATiN, which monitors the complete IgG poolthey developed last year.

The development of Neu-SATiN was spearheaded byZhong Yao, a senior research associate in Stagljars lab, and Sun Jin Kim, a post-doctoral researcherin Owens lab, who are the co-first authors on the paper.

The pinprick test is powered by the fluorescent luciferase protein from a deepwater shrimp. It measures the binding between the viral spike protein and its human ACE2 receptor, each of which is attached to a luciferase fragment. The engagement of the spike protein with ACE2 pulls the fragments close, catalyzing reconstitution of the full length luciferasewith a concomitant glow of light captured by the luminometer instrument. When a patients blood sample is added into the mixture, the neutralizing antibodies bind to and mop up all spike protein, while ACE2 remains in unengaged state. Consequentially, the luciferase remains in piecesand the light signal drops. The researchers say the plug-and-play design of the test means it can be adapted to emerging variants by engineering mutations in the spike protein.

The researchers applied Neu-SATiN to blood samples collected from 63 patients with different histories of COVID-19 and vaccinationup to November 2021. Patient neutralizing capacity was assessed against the original Wuhan strainand the following variants:Alpha, Beta, Gamma, Delta and Omicron.

We thought it would be important to monitor people that have been vaccinated to see if they still have protection and how long it lasts, said Owen, who did his post-doctoral training in the Donnelly Centre with distinguished bioengineer and University Professor Molly Shoichet of the Faculty of Applied Science & Engineering.But we also wanted to see if you were vaccinated against one variant, does it protect you against another variant?

The neutralizing antibodies were found to last about three to four months beforetheir levels would drop by about 70 per cent irrespective of infection or vaccination status. Hybrid immunity, acquired through both infection and vaccination, produced higher antibody levels at first, but these too dropped significantly four months later.

Most worryingly, infection and/or vaccination provided good protection against the previous variants, but not Omicronor its sub-variantsBA.4 and BA.5.

The data match those from arecent U.K. study thatshowed that both neutralizing antibodies and cellular immunity a type of immunity provided by memory T cellsfrom either infection, vaccination, or both, offered no protection from catching Omicron. In a surprising twist, the U.K. group also found that infections with Omicron boosted immunity against earlier strains, but not against Omicron itselffor reasons that remain unclear.

It's important to stress that vaccines still confer significant protection from severe disease and death, said Stagljar. Still, he added that the findings from his team and others call for vigilance in the coming periodgiven that the more transmissible BA.4 and BA.5 sub-variants can escape immunity acquired from earlier infections with Omicron, as attested by rising reinfections.

There will be new variants in the near future for sure, Stagljar said. Monitoring and boosting immunity with respect to circulating variants will become increasingly important and our method could play a key role in this since it is fast, accurate, quantitative and cheap.

He is already collaborating with the Canadian vaccine maker Medicago to help determine the efficacy of their candidates against Omicron and its sub-variants.Meanwhile, U of T is negotiating to license Neu-SATiN to a company which will scale it up for real world usessuch as population immunosurveillance and vaccine development.

The research was supported with funding from the Toronto COVID-19 Action Fund,Division of the Vice-President, Research & Innovation and the 3i Initiative at the University of Utah.

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Researchers use rapid antibody test to gauge immune response to SARS-CoV-2 variants - University of Toronto

Clemson research could advance key understanding of cell mutation, pave way to new cancer treatments – Greenville Journal

A number of Clemson University research projects are designed to advance critical understanding of how cancer cells function, but one project seeks to unlock some of the mysteries behind the most common type of cancer and lead to more effective treatments.

Jennifer Mason, assistant professor of genetics and biochemistry and a researcher in Clemsons Center for Human Genetics, has received more than $2.6 million in grant funding to investigate how cells repair DNA damage and what happens when those processes go wrong.

Such breakdowns can lead to mutations, according to Mason, a process at the heart of most cancers and increasingly tied to many diseases. Her research aims to answer many important questions about a particular DNA repair protein, known as FBH1, tied to the most common form of cancer, skin cancer, and its most deadly variant, melanoma.

Cancer is a disease of mutation, Mason says. The majority of cancers have an underlying defect that causes the cells to increase their mutation rate.

Masons work is being funded in part by a $792,000 research scholar grant from the American Cancer Society. Her research was inspired by a study that found missing or defective FBH1 in a majority of melanoma cases.

DNA damage is a natural process that happens in human cells, and one of the most common causes of such damage is ultraviolet light from exposure to sunlight. UV light is a major cause for melanoma, according to the American Cancer Society, and states with a high UV index, like South Carolina, tend to have higher incidences of melanoma in their populations.

Among the aims of Masons research is to find out why missing or defective FBH1 is resistant to DNA-destroying compounds, a property at the heart of most chemotherapies. Cracking that puzzle could lead to more effective cancer treatments.

Thats the hope of where someday this research will lead, she says.

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Clemson research could advance key understanding of cell mutation, pave way to new cancer treatments - Greenville Journal

Dihydropyridine (DHP) Market Insights 2022 And Analysis By Top Keyplayers Shenzhen Simeiquan Biotechnology, Boc Sciences, Weifang Union Biochemistry,…

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University of Utah Health Biochemist Matt Miller Named Pew Scholar – University of Utah Health Care

Jun 14, 2022 8:00 AM

Matthew Miller, Ph.D., an assistant professor of biochemistry at University of Utah Health, was named as a 2022 Pew Scholar for his exploration of the cellular machines that help accurately divide and separate chromosomes during cell division. This work is critical as even the smallest errors in this process can have harmful consequences, including birth defects, miscarriages, and cancer.

Miller is one of 22 scientists nationwide to receive the honor from the Pew Charitable Trusts. The Pew Scholars Program in the Biomedical Sciences provides funding to early-career investigators of outstanding promise in science that is relevant to the advancement of human health.

Millers research focuses on a key phase of cell division, or mitosis, when protein-based machines called kinetochores help chromosomes correctly maneuver between parent and newly forming daughter cells. This process ensures that each cell receives a complete set of accurately replicated chromosomes.

Better understanding of how kinetochores work could lead to the development of genetic interventions or other treatments to reduce the risk of these disorders, Miller says.

Matt Miller is studying a truly fascinating and red-hot area of research, says Wes Sundquist, Ph.D., a former Pew Scholar and chair of the Department of Biochemistry at the University of Utah Health. To address this problem, Matt uses an amazingmulti-disciplinary combination of biochemistry, biophysics, genetics, and cell biology for which he is almost uniquely qualified owing to his wonderful breadth, insight, and creativity.

Understanding the process of chromosome separation during mitosis is a difficult challenge, according to Miller. Thats because of its dynamic nature and the inability to precisely replicate the physical forces that regulate these activities in cells.

To overcome this difficulty, Miller and his colleagues purify the protein machines involved and have developed techniques which allow them to reestablish their complex activities outside of a cell. This allows the researchers to experimentally control things such as applied physical force and ultimately understand how these factors carry out this process so reliably.

Kinetochores are incredible protein machines, Miller says. They move chromosomes within an ever-changing environment and are signaling hubs that help regulate the cell cycle. Biologists have been fascinated with this process for more than 100 years, yet we still dont know how kinetochores achieve their remarkable feats.

In fact, according to Miller, scientists still dont have a complete parts list for the inner workings of kinetochores. Its like knowing that an internal combustion engine makes a car run but not understanding that under the hood it is a collection of pistons, spark plugs, and other vital moving parts, he says.

Despite this, Miller and his colleagues are unraveling several key aspects of kinetochores and their role in cell division.

During cell division, the cells genetic information, or DNA, is packaged into structures known as chromosomes, which need to be copied and then partitioned equally between resulting daughter cells. To facilitate this process, kinetochores assemble on chromosomes and attach themselves to the mitotic spindle, a molecular machine that forms thin, thread-like strands called microtubules. Once they do this, the duplicated chromosomes can move to opposite ends of the parent cell in preparation for cell division.

If kinetochores dont do their job correctly, then the chromosomes wont divide evenly, and one cell could end up with too many or too few of them. As a result, harmful imbalances and mutations can occur, Miller says.

Fortunately, these types of errors are rare. So what keeps the chromosomes attached to the right microtubules? It all boils down to tension, Miller says.

To accurately segregate replicated chromosomes to daughter cells, the chromosome must attach to microtubules from opposite sides of the cell. This pulling from opposite sides generates tension, telling the cell it has the correct attachment configuration and can proceed with cell division. Miller and colleagues recently discovered that kinetochores have an intrinsic mechanism that senses this tension. It acts, Miller says, like a childs finger trap, a simple puzzle that traps fingers in both ends of a small cylinder woven from bamboo. The harder a person tries to pull their fingers out, the tighter the device gets.

In much the same way, the tension created by the force of opposing microtubule pulling keeps the chromosomes aligned properly. When the kinetochores sense the right amount of tension, they give the go-ahead signal and then move each of their chromosomes to opposite sides of the parent cell, enabling accurate cell division.

Using an array of cutting-edge tools in biochemistry, biophysics, and gene editing, Miller hopes to determine which parts of the protein machines are responsible forchromosomal attachment and segregation.

We will then reconstitute the activities of these protein machines in a test tube to discover the mechanisms these protein machines use to carry out this process, Miller says. This work could lead to novel strategies for reducing the chromosomal segregation defects that give rise to many human diseases, including cancer and developmental disorders such as Down syndrome.

The 2022 class of Pew scholarsall early-career, junior facultywill receive four years of funding to explore some of the most pressing questions in health and medicine. They were chosen from 197 applicants nominated by leading academic institutions and researchers across the United States.

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Research News Biochemistry Pew Scholar

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University of Utah Health Biochemist Matt Miller Named Pew Scholar - University of Utah Health Care

Online Biochemistry Course | MCAT or Med School Prep | Arizona Online

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Caltech Professor of Chemistry and Biochemistry Decodes a Key Part of the Cell, Atom by Atom Pasadena Now – Pasadena Now

Credit: Valerie Altounian

Whatever you are doing, whether it is driving a car, going for a jog, or even at your laziest, eating chips and watching TV on the couch, there is an entire suite of molecular machinery inside each of your cells hard at work. That machinery, far too small to see with the naked eye or even with many microscopes, creates energy for the cell, manufactures its proteins, makes copies of its DNA, and much more.

Among those pieces of machinery, and one of the most complex, is something known as the nuclear pore complex (NPC). The NPC, which is made of more than 1,000 individual proteins, is an incredibly discriminating gatekeeper for the cells nucleus, the membrane-bound region inside a cell that holds that cells genetic material. Anything going in or out of the nucleus has to pass through the NPC on its way.

The NPCs role as a gatekeeper of the nucleus means it is vital for the operations of the cell. Within the nucleus, DNA, the cells permanent genetic code, is copied into RNA. That RNA is then carried out of the nucleus so it can be used to manufacture the proteins the cell needs. The NPC ensures the nucleus gets the materials it needs for synthesizing RNA, while also protecting the DNA from the harsh environment outside the nucleusandenabling the RNA to leave the nucleus after it has been made.

Its a little like an airplane hangar where you can repair 747s, and the door opens to let the 747 come in, but theres a person standing there who can keep a single marble from getting out while the doors are open, says CaltechsAndr Hoelz, professor of chemistry and biochemistry and a Faculty Scholar of the Howard Hughes Medical Institute. For more than two decades, Hoelz has been studying and deciphering the structure of the NPC in relation to its function. Over the years, he has steadily chipped away at its secrets, unraveling thempiecebypiecebypiecebypiece.

The implications of this research are potentially huge. Not only is the NPC central to the operations of the cell, it is also involved in many diseases. Mutations in the NPC are responsible for some incurable cancers, for neurodegenerative and autoimmune diseases such as amyotrophic lateral sclerosis (ALS) and acute necrotizing encephalopathy, and for heart conditions including atrial fibrillation and early sudden cardiac death. Additionally, many viruses, including the one responsible for COVID-19, target and shutdown the NPC during the course of their lifecycles.

Now, in a pair of papers published in the journalScience,Hoelz and his research team describe two important breakthroughs: the determination of the structure of the outer face of the NPC and the elucidation of the mechanism by which special proteins act like a molecular glue to hold the NPC together.

In their paper titled Architecture of the cytoplasmic face of the nuclear pore, Hoelz and his research team describe how they mapped the structure of the side of the NPC that faces outward from the nucleus and into the cells cytoplasm. To do this, they had to solve the equivalent of a very tiny 3-D jigsaw puzzle, using imaging techniques such as electron microscopy and X-ray crystallography on each puzzle piece.

Stefan Petrovic, a graduate student in biochemistry and molecular biophysics and one of the co-first authors of the papers, says the process began withEscherichia colibacteria (a strain of bacteria commonly used in labs) that were genetically engineered to produce the proteins that make up the human NPC.

If you walk into the lab, you can see this giant wall of flasks in which cultures are growing, Petrovic says. We express each individual protein inE. colicells, break those cells open, and chemically purify each protein component.

Once that purificationwhich can require as much as 1,500 liters of bacterial culture to get enough material for a single experimentwas complete, the research team began to painstakingly test how the pieces of the NPC fit together.

George Mobbs, a senior postdoctoral scholar research associate in chemistry and another co- first author of the paper, says the assembly happened in a stepwise fashion; rather than pouring all the proteins together into a test tube at the same time, the researchers tested pairs of proteins to see which ones would fit together, like two puzzle pieces. If a pair was found that fit together, the researchers would then test the two now-combined proteins against a third protein until they found one that fit with that pair, and then the resulting three-piece structure was tested against other proteins, and so on. Working their way through the proteins in this way eventually produced the final result of their paper: a 16-protein wedge that is repeated eight times, like slices of a pizza, to form the face of the NPC.

We reported the first complete structure of the entire cytoplasmic face of the human NPC, along with rigorous validation, instead of reporting a series of incremental advances of fragments or portions based on partial, incomplete, or low-resolution observation, says Si Nie, postdoctoral scholar research associate in chemistry and also a co-first author of the paper. We decided to patiently wait until we had acquired all necessary data, reporting a humungous amount of new information.

Their work complemented research conducted by Martin Beck of the Max Planck Institute of Biophysics in Frankfurt, Germany, whose team used cryo-electron tomography to generate a map that provided the contours of a puzzle into which the researchers had to place the pieces. To accelerate the completion of the puzzle of the human NPC structure, Hoelz and Beck exchanged data more than two years ago and then independently built structures of the entire NPC. The substantially improved Beck map showed much more clearly where each piece of the NPCfor which we determined the atomic structureshad to be placed, akin to a wooden frame that defines the edge of a puzzle, Hoelz says.

The experimentally determined structures of the NPC pieces from the Hoelz group served to validate the modeling by the Beck group. We placed the structures into the map independently, using different approaches, but the final results completely agreed. It was very satisfying to see that, Petrovic says.

We built a framework on which a lot of experiments can now be done, says Christopher Bley, a senior postdoctoral scholar research associate in chemistry and also co-first author. We have this composite structure now, and it enables and informs future experiments on NPC function, or even diseases. There are a lot of mutations in the NPC that are associated with terrible diseases, and knowing where they are in the structure and how they come together can help design the next set of experiments to try and answer the questions of what these mutations are doing.

This elegant arrangement of spaghetti noodles

In the other paper, titled Architecture of the linker-scaffold in the nuclear pore, the research team describes how it determined the entire structure of what is known as the NPCs linker-scaffoldthe collection of proteins that help hold the NPC together while also providing it with the flexibility it needs to open and close and to adjust itself to fit the molecules that pass through.

Hoelz likens the NPC to something built out of Lego bricks that fit together without locking together and are instead lashed together by rubber bands that keep them mostly in place while still allowing them to move around a bit.

I call these unstructured glue pieces the dark matter of the pore,' Hoelz says. This elegant arrangement of spaghetti noodles holds everything together.

The process for characterizing the structure of the linker-scaffold was much the same as the process used to characterize the other parts of the NPC. The team manufactured and purified large amounts of the many types linker and scaffold proteins, used a variety of biochemical experiments and imaging techniques to examine individual interactions, and tested them piece by piece to see how they fit together in the intact NPC.

To check their work, they introduced mutations into the genes that code for each of those linker proteins in a living cell. Since they knew how those mutations would change the chemical properties and shape of a specific linker protein, making it defective, they could predict what would happen to the structure of the cells NPCs when those defective proteins were introduced. If the cells NPCs were functionally and structurally defective in the way they expected, they knew they had the correct arrangement of the linker proteins.

A cell is much more complicated than the simple system we create in a test tube, so it is necessary to verify that results obtained from in vitro experiments hold up in vivo, Petrovic says.

The assembly of the NPCs outer face also helped solve a longtime mystery about the nuclear envelope, the double membrane system that surrounds the nucleus. Like the membrane of the cell within which the nucleus resides, the nuclear membrane is not perfectly smooth. Rather, it is studded with molecules called integral membrane proteins (IMPs) that serve in a variety of roles, including acting as receptors and helping to catalyze biochemical reactions.

Although IMPs can be found on both the inner and outer sides of the nuclear envelope, it had been unclear how they actually traveled from one side to the other. Indeed, because IMPs are stuck inside of the membrane, they cannot just glide through the central transport channel of the NPC as do free-floating molecules.

Once Hoelzs team understood the structure of the NPCs linker-scaffold, they realized that it allows for the formation of little gutters around its outside edge that allow the IMPs to slip past the NPC from one side of the nuclear envelope to the other while always staying embedded in the membrane itself.

It explains a lot of things that have been enigmatic in the field. I am very happy to see that the central transport channel indeed has the ability to dilate and form lateral gates for these IMPs, as we had originally proposed more than a decade ago, Hoelz says.

Taken together, the findings of the two papers represent a leap forward in scientists understanding of how the human NPC is built and how it works. The teams discoveries open the door for much more research. Having determined its structure, we can now focus on working out the molecular bases for the NPCs functions, such as how mRNA gets exported and the underlying causes for the many NPC-associated diseases with the goal of developing novel therapies, Hoelz says.

The papers describing the work appear in the June 10 issue of the journalScience.

Additional co-authors of the paper, Architecture of the cytoplasmic face of the nuclear pore, are Anna T. Gres; now of Worldwide Clinical Trials; Xiaoyu Liu, now of UCLA; Sho Harvey, a former grad student in Hoelzs lab; Ferdinand M. Huber, now of Odyssey Therapeutics; Daniel H. Lin, now of the Whitehead Institute for Biomedical Research; Bonnie Brown, a former research technician in Hoelzs lab; Aaron W. Tang, a former research technician in Hoelzs lab; Emily J. Rundlet, now of St. Jude Childrens Research Hospital and Weill Cornell Medicine; Ana R. Correia, now of Amgen; Taylor A. Stevens, graduate student in biochemistry and molecular biophysics; Claudia A. Jette, graduate student in biochemistry and molecular biophysics; Alina Patke, research assistant professor of biology; Somnath Mukherjee and Anthony A. Kossiakoff of the University of Chicago; Shane Chen, Saroj G. Regmi, and Mary Dasso of the National Institute of Child Health and Human Development; and Alexander F. Palazzo of the University of Toronto.

Additional co-authors of the paper, Architecture of the linker-scaffold in the nuclear pore, are Dipanjan Samanta, postdoctoral scholar fellowship trainee in chemical engineering; Thibaud Perriches, now of Care Partners; Christopher J. Bley; Karsten Thierbach; now of Odyssey Therapeutics; Bonnie Brown, Si Nie, George W. Mobbs, Taylor A. Stevens, Xiaoyu Liu, now of UCLA; Giovani Pinton Tomaleri, graduate student in biochemistry and molecular biophysics; and Lucas Schaus, graduate student in biochemistry and molecular biophysics.

Funding for the research was provided by the National Institutes of Health, the Howard Hughes Medical Institute, and the Heritage Medical Research Institute.

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Caltech Professor of Chemistry and Biochemistry Decodes a Key Part of the Cell, Atom by Atom Pasadena Now - Pasadena Now

New cryo-electron microscopy centers help UW researchers uncover mysteries of life – University of Wisconsin-Madison

At the Steenbock Symposium on June 7 and 8, 2022, the University of WisconsinMadison Department of Biochemistry opened its doors in celebration of two new research centers that bring to campus advanced biomolecular imaging technology called cryo-electron microscopy.

The technology allows scientists to capture detailed information about the smallest components of living cells to understand everything from more effective drug development to how viruses infect cells. It relies on ultra-cold temperatures during biomolecular specimen preservation and imaging and requires the right combination of expertise and highly specialized equipment.

The UWMadison Cryo-Electron Microscopy Research Center and the NIH-sponsored Midwest Center for Cryo-Electron Tomography represent a continuation of UWMadisons long history of contributions to structural biology. The event featured tours of the centers and scientific talks and posters about cryo-EM.

Both centers provide instrumentation, training, technical assistance and support to UWMadison researchers, as well as access to cryo-EM. The centers are also open to other universities and to private industry.

1 Thomas Anderson, a cellular and molecular biology graduate student working in the lab of biochemistry professor Robert Kirchdoerfer, and Anil Kumar, a research specialist in the cryo-EM centers, explain the inner workings of the Titan Krios cryo-electron microscope to their tour group at the Cryo-Electron Microscopy Research Center. Photo by Michael P. King/UW-Madison CALS

2 Industry and campus partnerships are critical to the centers' construction and operation. Zoltan Metlagel, a senior applications engineer at ThermoFisher Scientific, shared his knowledge about tomographic imaging alongside Parrell during one of five interactive workshops held during the open house. Photo by Michael P. King/UW-Madison CALS

3 Joseph Kim, a graduate student in the chemistry department, leads scientists through one of five interactive workshops held during the open house. Dedicated on-site training by center users and staff is available to scientists across campus and beyond. Photo by Michael P. King/UW-Madison CALS

4 Postdoctoral researcher Daniel Parrell explains how to use cryo-electron tomography data to produce an image known as a 3D tomogram. The montage shows biological structures in a thin layer of human cells and was collected using remote access capabilities and a focused ion beam. Remote training and operation of equipment are both features of the new centers. Photo by Michael P. King/UW-Madison CALS

5 Biochemistry professor and Morgridge Institute for Research investigator Elizabeth Wright directs the UWMadison Cryo-Electron Microscopy Research Center, led by a coalition of campus partners, and the NIH-sponsored Midwest Center for Cryo-Electron Tomography. Photo by Robin Davies

6 Open house attendees learned what can be achieved with cryo-EM during scientific talks and poster sessions held in the Discovery Building. Approximately 200 people attended the open house in-person, while another 200 viewed talks and workshops online. Photo by Robin Davies

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New cryo-electron microscopy centers help UW researchers uncover mysteries of life - University of Wisconsin-Madison

UMass Amherst’s Up-and-coming Biochemists Are Already Recruiting the Next GenerationWith Strawberries – UMass News and Media Relations

Many students love their undergraduate major. But for students in the UMass Amherst Biochemistry Club, spending extra hours in the lab isnt enough. Thanks to a grant from the American Society for Biochemistry and Molecular Biology (ASBMB), club members spent this past spring semester working with high school students in the Holyoke Public Schools to help plant the seeds for the next generation of up-and-coming biochemists. Their secret? Strawberries.

The Holyoke Public School system is currently under state receivership after being designated in 2015 as chronically underperforming. The district has been working to increase graduation rates, and as part of this goal, Holyoke High School has been redesigned to let each student choose a pathway that will prepare them for success in college, in a career or in community leadership. One of these pathways is the Medical and Life Sciences Pathway, designed to develop problem solving, critical thinking and communication skills for students interested in the biological sciences and healthcare. The UMass Biochem Club worked specifically with this cohort, performing experiments with them and conducting Q-and-A panels.

One of these experiments involved extracting DNA from strawberries. Michael Cotto, chair of the science department at Holyoke High School, said that having the opportunity for a hands-on experiment was a great way to welcome students back from their spring vacation. Students were engaged and excited by the science!

Anna Gorfinkel 22 and Ashley Sheehan 22, co-presidents of the Biochem Club, said that Western Massachusetts is a hub of educational opportunities and STEM careers. As students at the University of Massachusetts Amherst, the commonwealths flagship public university, we have a great opportunity to use our proximity to Holyoke to serve as role models for students interested in continuing their education and pursuing careers in the life sciences.

The Biochem Club is the ASBMB Student Chapter for UMass Amherst, and their mission is to help young people foster curiosity and interest in STEM. They have done extensive outreach to local communities since their inception in 2012, including programs at the Amherst-Pelham Regional High School, Girls Inc. of the Valley, and the Holyoke High School.

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UMass Amherst's Up-and-coming Biochemists Are Already Recruiting the Next GenerationWith Strawberries - UMass News and Media Relations