Introduction – Company Background
GuangXin Industrial Co., Ltd. is a specialized manufacturer dedicated to the development and production of high-quality insoles.
With a strong foundation in material science and footwear ergonomics, we serve as a trusted partner for global brands seeking reliable insole solutions that combine comfort, functionality, and design.
With years of experience in insole production and OEM/ODM services, GuangXin has successfully supported a wide range of clients across various industries—including sportswear, health & wellness, orthopedic care, and daily footwear.
From initial prototyping to mass production, we provide comprehensive support tailored to each client’s market and application needs.
At GuangXin, we are committed to quality, innovation, and sustainable development. Every insole we produce reflects our dedication to precision craftsmanship, forward-thinking design, and ESG-driven practices.
By integrating eco-friendly materials, clean production processes, and responsible sourcing, we help our partners meet both market demand and environmental goals.


Core Strengths in Insole Manufacturing
At GuangXin Industrial, our core strength lies in our deep expertise and versatility in insole and pillow manufacturing. We specialize in working with a wide range of materials, including PU (polyurethane), natural latex, and advanced graphene composites, to develop insoles and pillows that meet diverse performance, comfort, and health-support needs.
Whether it's cushioning, support, breathability, or antibacterial function, we tailor material selection to the exact requirements of each project-whether for foot wellness or ergonomic sleep products.
We provide end-to-end manufacturing capabilities under one roof—covering every stage from material sourcing and foaming, to precision molding, lamination, cutting, sewing, and strict quality control. This full-process control not only ensures product consistency and durability, but also allows for faster lead times and better customization flexibility.
With our flexible production capacity, we accommodate both small batch custom orders and high-volume mass production with equal efficiency. Whether you're a startup launching your first insole or pillow line, or a global brand scaling up to meet market demand, GuangXin is equipped to deliver reliable OEM/ODM solutions that grow with your business.



Customization & OEM/ODM Flexibility
GuangXin offers exceptional flexibility in customization and OEM/ODM services, empowering our partners to create insole products that truly align with their brand identity and target market. We develop insoles tailored to specific foot shapes, end-user needs, and regional market preferences, ensuring optimal fit and functionality.
Our team supports comprehensive branding solutions, including logo printing, custom packaging, and product integration support for marketing campaigns. Whether you're launching a new product line or upgrading an existing one, we help your vision come to life with attention to detail and consistent brand presentation.
With fast prototyping services and efficient lead times, GuangXin helps reduce your time-to-market and respond quickly to evolving trends or seasonal demands. From concept to final production, we offer agile support that keeps you ahead of the competition.
Quality Assurance & Certifications
Quality is at the heart of everything we do. GuangXin implements a rigorous quality control system at every stage of production—ensuring that each insole meets the highest standards of consistency, comfort, and durability.
We provide a variety of in-house and third-party testing options, including antibacterial performance, odor control, durability testing, and eco-safety verification, to meet the specific needs of our clients and markets.
Our products are fully compliant with international safety and environmental standards, such as REACH, RoHS, and other applicable export regulations. This ensures seamless entry into global markets while supporting your ESG and product safety commitments.
ESG-Oriented Sustainable Production
At GuangXin Industrial, we are committed to integrating ESG (Environmental, Social, and Governance) values into every step of our manufacturing process. We actively pursue eco-conscious practices by utilizing eco-friendly materials and adopting low-carbon production methods to reduce environmental impact.
To support circular economy goals, we offer recycled and upcycled material options, including innovative applications such as recycled glass and repurposed LCD panel glass. These materials are processed using advanced techniques to retain performance while reducing waste—contributing to a more sustainable supply chain.
We also work closely with our partners to support their ESG compliance and sustainability reporting needs, providing documentation, traceability, and material data upon request. Whether you're aiming to meet corporate sustainability targets or align with global green regulations, GuangXin is your trusted manufacturing ally in building a better, greener future.
Let’s Build Your Next Insole Success Together
Looking for a reliable insole manufacturing partner that understands customization, quality, and flexibility? GuangXin Industrial Co., Ltd. specializes in high-performance insole production, offering tailored solutions for brands across the globe. Whether you're launching a new insole collection or expanding your existing product line, we provide OEM/ODM services built around your unique design and performance goals.
From small-batch custom orders to full-scale mass production, our flexible insole manufacturing capabilities adapt to your business needs. With expertise in PU, latex, and graphene insole materials, we turn ideas into functional, comfortable, and market-ready insoles that deliver value.
Contact us today to discuss your next insole project. Let GuangXin help you create custom insoles that stand out, perform better, and reflect your brand’s commitment to comfort, quality, and sustainability.
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One-stop OEM/ODM solution provider Taiwan
Are you looking for a trusted and experienced manufacturing partner that can bring your comfort-focused product ideas to life? GuangXin Industrial Co., Ltd. is your ideal OEM/ODM supplier, specializing in insole production, pillow manufacturing, and advanced graphene product design.
With decades of experience in insole OEM/ODM, we provide full-service manufacturing—from PU and latex to cutting-edge graphene-infused insoles—customized to meet your performance, support, and breathability requirements. Our production process is vertically integrated, covering everything from material sourcing and foaming to molding, cutting, and strict quality control.Memory foam pillow OEM factory Vietnam
Beyond insoles, GuangXin also offers pillow OEM/ODM services with a focus on ergonomic comfort and functional innovation. Whether you need memory foam, latex, or smart material integration for neck and sleep support, we deliver tailor-made solutions that reflect your brand’s values.
We are especially proud to lead the way in ESG-driven insole development. Through the use of recycled materials—such as repurposed LCD glass—and low-carbon production processes, we help our partners meet sustainability goals without compromising product quality. Our ESG insole solutions are designed not only for comfort but also for compliance with global environmental standards.Eco-friendly pillow OEM factory Taiwan
At GuangXin, we don’t just manufacture products—we create long-term value for your brand. Whether you're developing your first product line or scaling up globally, our flexible production capabilities and collaborative approach will help you go further, faster.Taiwan graphene product OEM factory
📩 Contact us today to learn how our insole OEM, pillow ODM, and graphene product design services can elevate your product offering—while aligning with the sustainability expectations of modern consumers.Flexible manufacturing OEM & ODM China
According to new research, a simple two-carbon compound may have been a crucial player in the evolution of metabolism before the advent of cells. An early step in metabolic evolution set the stage for emergence of ATP as the universal energy carrier. A simple two-carbon compound may have been a crucial player in the evolution of metabolism before the advent of cells. This is according to a new study by Nick Lane and colleagues of University College London, UK that was published in the open-access journal PLOS Biology on October 4th. The discovery may provide key insight into the earliest stages of prebiotic biochemistry. In addition, the finding suggests how ATP (adenosine triphosphate) came to be the universal energy carrier of all cellular life today. Adenosine triphosphate (ATP) is an organic compound that provides energy to drive many processes in living cells, such as nerve impulse propagation, muscle contraction, condensate dissolution, and chemical synthesis. ATP is found in all known forms of life and isoften referred to as the “molecular unit of currency” of intracellular energy transfer. ATP is used by all cells as an energy intermediate. During cellular respiration, energy is captured when a phosphate is added to ADP (adenosine diphosphate) to generate ATP. Cleavage of that phosphate releases energy to power most types of cellular functions. However, building ATP’s complex chemical structure from scratch is energy intensive and requires six separate ATP-driven steps. While convincing models do allow for prebiotic formation of the ATP skeleton without energy from already-formed ATP, they also indicate that ATP was likely quite scarce. This means that some other compound may have played a central role in the conversion of ADP to ATP at this stage of evolution. Acetyl Phosphate as a Prebiotic Phosphorylator The most likely candidate, Lane and colleagues believed, was the two-carbon compound acetyl phosphate (AcP), which functions today in both bacteria and archaea as a metabolic intermediate. AcP has been shown to phosphorylate ADP to ATP in water in the presence of iron ions, but a host of questions remained after that demonstration, including whether other small molecules might work as well, whether AcP is specific for ADP or instead could function just as well with diphosphates of other nucleosides (such as guanosine or cytosine), and whether iron is unique in its ability to catalyze ADP phosphorylation in water. Molecular dynamic simulation of ADP and acetyl phosphate Credit: Aaron Halpern, UCL (CC-BY 4.0) The authors explored all these questions in their new study. Drawing on data and hypotheses about the chemical conditions of the Earth before life arose, they tested the ability of other ions and minerals to catalyze ATP formation in water; none were nearly as effective as iron. Next, they tested a panel of other small organic molecules for their ability to phosphorylate ADP; none were as effective as AcP, and only one other (carbamoyl phosphate) had any significant activity at all. Finally, they showed that none of the other nucleoside diphosphates accepted a phosphate from AcP. Combining these results with molecular-dynamic modeling, the authors propose a mechanistic explanation for the specificity of the ADP/AcP/iron reaction, hypothesizing that the small diameter and high charge density of the iron ion, combined with the conformation of the intermediate formed when the three come together, provide a “just right” geometry that allows AcP’s phosphate to switch partners, forming ATP. The Significance of AcP in the Origin of Life “Our results suggest that AcP is the most plausible precursor to ATP as a biological phosphorylator,” Lane says, “and that the emergence of ATP as the universal energy currency of the cell was not the result of a ‘frozen accident,’ but arose from the unique interactions of ADP and AcP. Over time, with the emergence of suitable catalysts, ATP could eventually displace AcP as a ubiquitous phosphate donor, and promote the polymerization of amino acids and nucleotides to form RNA, DNA, and proteins.” Lead author Silvana Pinna adds, “ATP is so central to metabolism that I thought it might be possible to form it from ADP under prebiotic conditions. But I also thought that several phosphorylating agents and metal ion catalysts would work, especially those conserved in life. It was very surprising to discover the reaction is so selective – in the metal ion, phosphate donor, and substrate – with molecules that life still uses. The fact that this happens best in water under mild, life-compatible conditions is really quite significant for the origin of life.” Reference: “A prebiotic basis for ATP as the universal energy currency” by Silvana Pinna, Cäcilia Kunz, Aaron Halpern, Stuart A. Harrison, Sean F. Jordan, John Ward, Finn Werner and Nick Lane, 4 October 2022, PLOS Biology. DOI: 10.1371/journal.pbio.3001437 Funding: We are grateful to the Biotechnology and Biological Sciences Research Council to NL, FW and JW (BB/V003542/1) and HR (LIDo Doctoral Training Program), to Gates Ventures (formerly bgc3) to NL, and to the Natural Environment Research Council to AH and NL (2236041). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
After examining two large databases of traits in spouses, researchers discovered that the tendency for individuals to mate with others who possess similar traits (known as cross-trait assortative mating) is strongly linked to genetic correlation estimates and likely plays a significant role in these estimates. According to researchers, mating patterns may be able to explain many of the relationships between traits that were previously thought to be biological. A new study led by the University of California, Los Angeles suggests that current methods for evaluating the genetic connections between traits often overlook the influence of mating patterns, leading to inflated estimates of the strength of the genetic link between traits and diseases. Scientists have been using powerful genome sequencing technology to try to uncover the genetic connections between traits and disease risk in recent years, hoping that this knowledge could lead to new disease treatments. However, a study conducted by UCLA and published in the journal Science warns against relying too heavily on genetic correlation estimates, as these estimates may be distorted by non-biological factors that have not been fully taken into account. Impact of Cross-Trait Assortative Mating Genetic correlation estimates typically assume that mating is random. But in the real world, partners tend to pair up because of many shared interests and social structures. As a result, some genetic correlations in previous work that have been attributed to shared biology may instead represent incorrect statistical assumptions. For example, previous estimates of genetic overlap between body mass index (BMI) and educational attainment are likely to reflect this type of population structure, induced by “cross-trait assortative mating,” or how individuals of one trait tend to partner with individuals of another trait. The study authors said genetic correlation estimates deserve more scrutiny since these estimates have been used to predict disease risk, glean for clues for potential therapies, inform diagnostic practices, and shape arguments about human behavior and societal issues. The authors said some in the scientific community have placed too much emphasis on genetic correlation estimates based on the idea that studying genes, because they are unalterable, can overcome confounding factors. “If you just look at two traits that are elevated in a group of people, you can’t conclude that they’re there for the same reason,” said lead author Richard Border, a postdoctoral researcher in statistical genetics at UCLA. “But there’s been a kind of assumption that if you can track this back to genes, then you would have the causal story.” Findings on Spousal Traits and Psychiatric Disorders Based on their analysis of two large databases of spousal traits, researchers found that cross-trait assortative mating is strongly associated with genetic correlation estimates and plausibly accounts for a “substantial” portion of genetic correlation estimates. “Cross-trait assortative mating has affected all of our genomes and caused interesting correlations between DNA you inherit from your mother and DNA you inherit from your father across the whole genome,” said study co-author Noah Zaitlen, a professor of computational medicine and neurology at UCLA Health. The researchers also examined genetic correlation estimates of psychiatric disorders, which have sparked debate in the psychiatric community because they appear to show genetic relationships among disorders that seemingly have little similarities, such as attention-deficit hyperactivity disorder and schizophrenia. The researchers found that genetic correlations for a number of unrelated traits could be plausibly attributed to cross-trait assortative mating and imperfect diagnostic practices. On the other hand, their analysis found stronger links for some pairs of traits, like anxiety disorders and major depression, suggesting that there truly is at least some shared biology. “But even when there is a real signal there, we’re still suggesting that we’re overestimating the extent of that sharing,” Border said. Reference: “Cross-trait assortative mating is widespread and inflates genetic correlation estimates” by Richard Border, Georgios Athanasiadis, Alfonso Buil, Andrew J. Schork, Na Cai, Alexander I. Young, Thomas Werge, Jonathan Flint, Kenneth S. Kendler, Sriram Sankararaman, Andy W. Dahl and Noah A. Zaitlen, 17 November 2022, Science. DOI: 10.1126/science.abo2059 The study was funded by the National Institutes of Health, the Chan Zuckerberg Initiative, the National Science Foundation, Open Philanthropy, and the Wellcome Trust.
Scientists are deciphering the nuclear pore complex in incredible detail. Credit: Valerie Altounian Scientists have mapped the nuclear pore complex, revealing its structure and role in disease, paving the way for new research and treatments. Many of us learned the basic cell structure at some point and will recall components like the cell membrane, cytoplasm, mitochondrion, and nucleus. However, the structure of our cells is actually vastly more complicated than you may have thought. In fact, because we have been discovering so much over the years, we now know that cells are far more complex than even expert biologists realized not too long ago. One element of particular complexity is the nuclear pore complex. Surrounding the eukaryotic cell nucleus is a double membrane, the nuclear envelope, which encloses the genetic material of the cell nucleus. Spanning that nuclear envelope is the nuclear pore complex, which though microscopic in size, is incredibly complex molecular machinery comprised of a vast number of different proteins. 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 cell’s nucleus, the membrane-bound region inside a cell that holds that cell’s genetic material. Anything going in or out of the nucleus has to pass through the NPC on its way. A molecular model of the outside (cytoplasmic) face of the nuclear pore complex. Reprinted with permission from C.J. Bley et al., Science 376, eabm9129 (2022). Credit: Hoelz Laboratory/Caltech The NPC’s role as a gatekeeper of the nucleus means it is vital for the operations of the cell. Within the nucleus, DNA, the cell’s 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 nucleus and enabling the RNA to leave the nucleus after it has been made. “It’s a little like an airplane hangar where you can repair 747s, and the door opens to let the 747 come in, but there’s a person standing there who can keep a single marble from getting out while the doors are open,” says Caltech’s André 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 them piece by piece by piece by piece. 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 journal Science, 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. A Very Tiny 3D Jigsaw Puzzle 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 with Escherichia coli bacteria (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 in E. coli cells, break those cells open, and chemically purify each protein component.” Once that purification—which can require as much as 1,500 liters of bacterial culture to get enough material for a single experiment—was 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 NPC—for which we determined the atomic structures—had 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 NPC’s linker-scaffold—the 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. The nuclear pore complex (NPC) is able to expand and contract to adapt to the needs of the cell. Reprinted with permission from S. Petrovic et al., Science 376, eabm9798 (2022). Credit: Hoelz Laboratory/Caltech “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 cell’s NPCs when those defective proteins were introduced. If the cell’s 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 NPC’s 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 Hoelz’s team understood the structure of the NPC’s 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 team’s discoveries open the door for much more research. “Having determined its structure, we can now focus on working out the molecular bases for the NPC’s 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 journal Science. References: “Architecture of the cytoplasmic face of the nuclear pore” by Christopher J. Bley, Si Nie, George W. Mobbs, Stefan Petrovic, Anna T. Gres, Xiaoyu Liu, Somnath Mukherjee, Sho Harvey, Ferdinand M. Huber, Daniel H. Lin, Bonnie Brown, Aaron W. Tang, Emily J. Rundlet, Ana R. Correia, Shane Chen, Saroj G. Regmi, Taylor A. Stevens, Claudia A. Jette, Mary Dasso, Alina Patke, Alexander F. Palazzo, Anthony A. Kossiakoff and André Hoelz, 10 June 2022, Science. DOI: 10.1126/science.abm9129 “Architecture of the linker-scaffold in the nuclear pore” by Stefan Petrovic, Dipanjan Samanta, Thibaud Perriches, Christopher J. Bley, Karsten Thierbach, Bonnie Brown, Si Nie, George W. Mobbs, Taylor A. Stevens, Xiaoyu Liu, Giovani Pinton Tomaleri, Lucas Schaus and André Hoelz, 10 June 2022, Science. DOI: 10.1126/science.abm9798 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 Hoelz’s 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 Hoelz’s lab; Aaron W. Tang, a former research technician in Hoelz’s lab; Emily J. Rundlet, now of St. Jude Children’s 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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