Tables have become a ubiquitous standard for capturing, storing, and sharing data on the web. This is primarily due to the semi-structured nature of tables, where relationships between data are often ambiguously encoded using locality. While this format can be easy for humans to interpret in simple cases, as table complexity increases, so does the difficulty in interpretability. To bridge this context gap, many data publishers provide a data dictionary to capture schema elements' meaning through text descriptions. Existing work compounds the need for data dictionaries to improve tabular interoperability, but few provide detailed requirements for data dictionary descriptions. This paper identifies and defines three common types of data dictionary descriptions in the biomedical domain. We then compare the effectiveness of each description type by normalizing data dictionary descriptions to a single type using large language models and measuring their performance using a semantic tabular interpretation algorithm. Our experiments show that intensional descriptions, which describe the general properties a column member should have, are most effective for tabular alignment and improve the reusability of data dictionaries.

Despite SH2 domains, being pivotal in protein interactions linked to various diseases like cancer, we lack specific research tools for intracellular assays. Understanding SH2-mediated interactions and creating effective inhibitors requires tools which target individual protein domains. Affimer reagents exhibit promise, yet their potential against the extensive SH2 domain family remains largely unexplored. Our study aimed to bridge this gap by identifying Affimer reagents that selectively bind to 22 out of 41 SH2 domains. These reagents enabled a medium-throughput screening approach resembling siRNA studies, shedding light on their functionality. Notably, select Affimers demonstrated the ability to curtail the nuclear translocation of pERK, with Grb2 being a prominent target. Further analyses revealed that these Grb2-specific Affimer reagents displayed competitive inhibition with impressive metrics: IC50s ranging from 270.9 nM to 1.22 µM, together with low nanomolar binding affinities. Moreover, they exhibited the ability to pull down endogenous Grb2 from cell lysates, illustrating their efficacy in binding the Grb2 SH2 domain. This comprehensive assessment underscores the potential of Affimer reagents as domain-specific inhibitors. Their viability for medium/high-throughput phenotypic screening presents a promising avenue via which to identify and characterize potential drug targets within the SH2 domain family.

Increasing emphasis is being placed by granting agencies on the need for specialists who support the translation of research into societal benefits. This societal benefit is often referred to as broader impacts (BI), and BI is important for acquiring grant funding and fulfilling land-grant university missions, among other benefits. However, few career paths lead directly to becoming a BI professional, so individuals moving into BI work need to transition from another career, which requires learning about BI. This case study examines the experiences of four former classroom teachers making the transition to both teacher educator (a teacher of teachers) and BI professional, and the ways in which their transition was supported using the Center for Advancing Research Impacts in Society (ARIS) BI Toolkit. Implications for onboarding using this toolkit are described and recommendations are made for how to use the ARIS BI Toolkit for transitioning BI professionals.

Knowledge graphs have become an essential technology for both businesses and governments. They enable a wide variety of critical tasks, such as aligning diverse datasets, improving the capabilities of search engines, supporting error checking, and generating explanations using inference engines. However, populating, augmenting, and/or validating a knowledge graph can be challenging because developers need domain knowledge to understand their data and experience in ontology modeling to align concepts properly as well as experience with conflict detection and truth maintenance tools. Previous efforts have explored automatically integrating simple tabular data into knowledge graphs to lower the barrier to entry. These methods heavily rely on named entity overlap and require that tables are similar to relational tables in third normal form. While these methods have been successful under competition, these limitations make them impractical for general usage. In this paper, we introduce the semantic data dictionary generator (SDD-Gen), an algorithm that aligns complex tabular data to ontological terms for knowledge graph generation. Our methodology leverages context information from data dictionaries to make alignments, enabling us to align complex tables with few named entities and multiple subject columns.

Supplementary Figure 4 from Milk Fat Globule EGF-8 Promotes Melanoma Progression through Coordinated Akt and Twist Signaling in the Tumor Microenvironment

Supplementary Figure Legends 1-4 from Milk Fat Globule EGF-8 Promotes Melanoma Progression through Coordinated Akt and Twist Signaling in the Tumor Microenvironment

Supplementary Figure 2 from Milk Fat Globule EGF-8 Promotes Melanoma Progression through Coordinated Akt and Twist Signaling in the Tumor Microenvironment

Supplementary Table 1 from Milk Fat Globule EGF-8 Promotes Melanoma Progression through Coordinated Akt and Twist Signaling in the Tumor Microenvironment

Supplementary Figure 4 from Milk Fat Globule EGF-8 Promotes Melanoma Progression through Coordinated Akt and Twist Signaling in the Tumor Microenvironment

Supplementary Figure 3 from Milk Fat Globule EGF-8 Promotes Melanoma Progression through Coordinated Akt and Twist Signaling in the Tumor Microenvironment

The joining process for oxide dispersion strengthened (ODS) alloys remains a key challenge facing the nuclear community. The microstructure and mechanical properties were characterized in the base material and friction stir welded ODS MA956 irradiated with 5 MeV Fe2+ ions from 400 to 500 degrees C up to 25 dpa. Nanoindentation was performed to assess changes in hardness and yield stress, and the dispersed barrier hardening (DBH) model was applied to described results. A combination of scanning transmission electron microscopy (STEM) and atom probe tomography (APT) were used to assess evolution of the microstructure including dispersoids, network dislocations and dislocation loops, nanoclusters, and solid solution concentrations. Overall, softening was observed as a result of increased dose, which was exacerbated at 500 degrees C. The formation and coarsening of new dispersoids was noted while nanoclusters tended to dissolve in the base material, and were not observed in the stir zone. Solute nanocluster evolution was identified as a primary driver of the changes in mechanical properties. Published by Elsevier B.V.

The remarkable success of SARS CoV-2 mRNA-based vaccines and the ensuing interest in mRNA vaccines and therapeutics have highlighted the need for a scalable clinical-enabling manufacturing process to produce such products, and robust analytical methods to demonstrate safety, potency, and purity. To date, production processes have either not been disclosed or are bench-scale in nature and cannot be readily adapted to clinical and commercial scale production. To address these needs, we have advanced an aqueous-based scalable process that is readily adaptable to GMP-compliant manufacturing, and developed the required analytical methods for product characterization, quality control release, and stability testing. We also have demonstrated the products produced at manufacturing scale under such approaches display good potency and protection in relevant animal models with mRNA products encoding both vaccine immunogens and antibodies. Finally, we discuss continued challenges in raw material identification, sourcing and supply, and the cold chain requirements for mRNA therapeutic and vaccine products. While ultimate solutions have yet to be elucidated, we discuss approaches that can be taken that are aligned with regulatory guidance.

RAS mutations are the most common oncogenic drivers across human cancers, but there remains a paucity of clinically-validated pharmacological inhibitors of RAS, as druggable pockets have proven difficult to identify. Here, we identify two RAS-binding Affimer proteins, K3 and K6, that inhibit nucleotide exchange and downstream signaling pathways with distinct isoform and mutant profiles. Affimer K6 binds in the SI/SII pocket, whilst Affimer K3 is a non-covalent inhibitor of the SII region that reveals a conformer of wild-type RAS with a large, druggable SII/α3 pocket. Competitive NanoBRET between the RAS-binding Affimers and known RAS binding small-molecules demonstrates the potential to use Affimers as tools to identify pharmacophores. This work highlights the potential of using biologics with small interface surfaces to select unseen, druggable conformations in conjunction with pharmacophore identification for hard-to-drug proteins.

Ferritic-martensitic alloys have emerged as candidates for structural and cladding applications in advanced reactors but are known to experience irradiation-induced changes to their microstructures (including solute clustering), leading to changes in their mechanical properties. Irradiation of three commercial alloys (HT9, HCM12A, and T91) with Fe2+ ions to 3 dpa is found to result in varying degrees of hardening of the materials, consistent with prior TEM- and APT-based microstructure observations. As irradiation dose is increased to 100 dpa, partial softening is observed in both HCM12A and T91. Matrix solute concentrations are observed to decline at higher dose and are likely contributing to the softening, with evidence of segregation of solutes to more stable sinks at higher dose. Analysis methods combining the dispersed barrier hardening and solid solution strengthening effects are successful at correlating microstructures to mechanical properties using a combined effective diameter approach to represent complex Cu-rich nanoclusters with Si-Mn-Ni-rich appendages.

BEST PIC I PAPER WINNER There is an exponential growth in the number of cyber-attack incidents resulting in significant financial loss and national security concerns. Secure cyberspace has been designated as one of the National Academy of Engineering (NAE) Grand Challenges in engineering. Broadly, the security threats are targeted on software programs, operating system and network with the intention to launch confidentiality, integrity and availability violations. Existing undergraduate and graduate-level cybersecurity education curriculum rely primarily on didactic teaching methods with little focus on student centered, inquiry-based teaching, known to improve student learning. With growing number of security incidents taking place, it is utmost important to prepare a workforce equipped with knowledge of the threat space and existing state-of-the-art solution. Such comprehensive understanding is only possible by a dedicated hands-on course on cybersecurity where students can learn the key concepts by editing the hardware, software and OS, and, network policies. Unfortunately, such extensive and deep flexibilities are not provided in current cybersecurity curriculum. In this paper, we introduce a hands-on and modular self-learning Cybersecurity Training (CST) Kit to advance cybersecurity education. Students can promptly apply newly acquired knowledge on the CST Kit as part of the learning process. This Kit accompanies Do-It-Yourself (DIY) training modules that is used to model and investigate cybersecurity issues and their prevention to all levels of the cybersecurity workforce, including undergraduate and graduate students and K-12 science and technology teachers. The Kit also covers various aspects of cybersecurity issues including, hardware, software, operating system and network security. A coursework is developed on hardware security for Senior undergraduate and graduate students. A preliminary survey conducted among students who were introduced to the modular board to implement hardware security threats such as, side-channel attack shows an 120% improvement in their understanding after the CST Kit based activities. The components of the CST Kit are also used in a 4-day summer workshop for K-12 teachers. Teachers took pre- and post- concept inventories to assess their learning of content throughout the workshop and the results indicated improvement of 58%. These assessments focused on vulnerabilities and specific types of attacks, system security, data transmission and encryption, permutations and combinatorics, and binary numbers.

Machine learning allows computers to learn a model for a given task, such as face recognition, with a high degree of accuracy, using data. However, after these models are generated, they are often treated as black boxes by developers and the limitations of a model are often unknown to end-users. To address these issues, this paper introduces the Face Recognition Model Analyzer (FRMA) ontology and a semantically enabled Result-set viewer. Together these resources describe image features relevant to face recognition and allow users to explore how well a face recognition model does at classifying images that contain an image feature. We evaluated the ontology and Result-set viewer by loading in the Labeled Faces in the Wild [1] dataset, enriching the images with image tags [2], and exploring two popular face recognition models, Facenet [3] and DLib [4]. Using the FRMA ontology and the Result-set viewer, we discovered several classic face recognition model limitations, such as trouble classifying images with occlusions. This evaluation shows that these resources can discover model limitations which can make face recognition model reuse easier for future users.

BioanalysisVol. 12, No. 3 EditorialFree AccessHarnessing anti-idiotypic antibody alternatives to advance biotherapeutic pharmacokinetic assaysMatt JohnsonMatt Johnson*Author for correspondence: E-mail Address: affimers@avacta.comAvacta Life Sciences, Ash Way, Thorp Arch Estate, Wetherby, LS23 7FA, UKPublished Online:24 Jan 2020https://doi.org/10.4155/bio-2019-0291AboutSectionsPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareShare onFacebookTwitterLinkedInReddit Keywords: affimerantibodyassay developmentbinding reagentsbiotherapeutics drug developmentELISApharmacokinetic assaystherapeuticsPharmacokinetics (PK) is the branch of pharmacology dedicated to determining the fate of substances in the body. PK assays are, therefore, an essential element in the development of new drugs, with favorable PK profiles essential to promising leads progressing to the later stages of development. In combination with pharmacodynamic (PD) assays, PK assays are vital to understanding a drug's mechanism of action, and it is increasingly recommended that they be carried out throughout the drug-development process for a more efficient pipeline [1]. PK assays can also be used as companion diagnostics at the point-of-care by determining the concentration of a therapeutic in a patient's blood; it is possible to assess whether the patient is getting the right dose; and a clinician can use this information to make personalized adjustments where appropriate [2].To be effective, PK assays must accurately measure a drug's concentration in complex biological matrices such as blood plasma. This requires a reliable supply of reagents that can bind to different drug molecules with the highest possible specificity. The most commonly used platforms for PK assays are ligand-binding assays, and in particular, enzyme-linked immunosorbent assay (ELISA) formats employing tagged antibodies to bind to the drug of interest. The validity of PK readouts is largely determined by both the assay format, and the quality of the reagents used. Although antibodies are traditionally the preferred binding reagents, questions have been raised by some about their suitability in a number of situations. This generally stems from antibodies' inherent structural complexity, which can lead to associated issues with stability, development speed, production costs, lot-to-lot variability and target specificity [3,4]. These issues can be so problematic that erroneous conclusions may be drawn from biochemical assays, leading some to blame antibodies for the 'reproducibility crisis' currently being seen across the life science research sector [4].If the drug being measured by the PK assay is itself an antibody, then this can complicate matters even further. In such cases the PK binding reagent must be anti-idiotypic (anti-ID), which means it must bind to the unique complementarity-determining region of the therapeutic antibody in a highly selective manner. The challenge here is ensuring the PK reagent is specific to the therapeutic antibody, and exhibits minimal cross-reactivity to the excess of antibodies found in human blood plasma [5].Anti-ID reagents bind to therapeutic antibodies in three ways:Competing: used to measure free drug concentration, unbound to the target;Noncompeting: used to measure total drug concentration (free and bound);Complex specific: used to measure the concentration of the drug bound to the target.Each binding mode has a different utility across the design and development of various assay formats, depending on the therapeutic in question. Independent of its binding mode, the anti-ID reagents' quality is essential for successful assay development, requiring high specificity, sensitivity and reproducibility, all of which are factors that can be limited when using antibodies.Owing to the difficulties described above, alternative binding reagents are increasingly being explored that could supplement, or in some cases supersede, antibodies in PK assays. There are a range of potential engineered 'antibody alternative' binders currently available in various formats, including nanoCLAMPs [6], anticalins [7], affibodies [8] and Affimer® binders [9]. Affimer protein scaffolds are particularly well suited for commercial anti-ID applications.Introducing Affimer technologyAffimer proteins are based on a scaffold of naturally occurring proteins called cystatins. They are engineered to stably display two variable loops, which gives rise to a potential diversity of 422 unique binding surfaces. At 14 kDa, they are just 1/10th the size of the average antibody. The structural simplicity of Affimer molecules is key to their advantages. Expressed as a single domain, they have no disulfide bridges or post-translational modifications – this simplifies their production, minimizing the risk of structural variation and resultant loss of assay consistency, a major issue seen with antibodies used as anti-ID reagents.In contrast to anti-ID antibodies, which typically take 6–9 months to be developed, Affimer reagents can be developed in a short timeframe of 12–14 weeks. This process can be completed without the need for the additional affinity maturation often required for antibody binders – a lengthy, iterative series of steps that can introduce instabilities into the protein structure [10]. Extensive standardization to ensure consistency between lots is often necessary when using antibodies in PK assays. However, due to the simple process required to produce Affimer binders, recombinant protein variability is significantly minimized between lots, resulting in a high level of reproducibility and lot-to-lot consistency.Demonstrating Affimer utilityThe utility of Affimer reagents for PK assays has been demonstrated by identifying specific binders to the existing therapeutic monoclonal antibody Trastuzumab, in a short timeframe. The roughly 3-month development process involves using gene libraries to encode variable loops, with Affimer proteins binding specifically to the target therapeutic antibody being rapidly selected by phage display experiments. Cloning the successful binding phage outputs into an expression vector generates a reliable supply of the desired Affimer binder. The properties of the Affimer binder can be examined by using it as a capture reagent in an IgG-detection sandwich enzyme-linked immunosorbent assay, validating its specific binding to the biotherapeutic over a clinically relevant concentration range.Using this rapid discovery and development process, Affimer binders for a number of different therapeutic antibodies including rituximab, adalimumab, eculizumab, nivolumab, ipilimumab and pembrolizumab have been identified, and have been shown to accurately and precisely quantify the target antibody within a bioanalytical assay environment, yielding highly reproducible calibration curves [11].Standard anti-ID antibodies or fragments can lack specificity due to some level of cross-reactivity to background human IgGs present at high concentration in serum, resulting in inaccurate analysis. Specificity of reagents for target biotherapeutic antibodies is essential to their performance within patient samples. Upon incubation with the target therapeutic antibody, Affimer reagents have been shown to maintain specificity to their target antibodies in the presence of matrix, and to exhibit minimal interaction with other antibody therapeutics [5], illustrating the highly specific nature of the binders. This is valuable in assessing PKs during clinical trials and in determining optimal dosing windows for patients, because the accuracy of drug measurement is retained despite variation in human antibody levels across different blood samples.Different matrices will always give rise to slightly different background results, but minimizing the effect of matrix differences can drastically simplify PK assay setup, and may help move away from the need to run bridging assays. Using a generic secondary reagent, it was possible to measure the Affimer reagent capture of a therapeutic monoclonal antibody, with minimal matrix interference at different serum concentrations [5,11]. However, when using commercially available antigen-binding fragments as capture reagents, significant matrix effect is observed, leading to reduced dynamic range in serum [5,11]. While Affimer reagents exhibit reduced matrix interference, any issues in different sera can easily be mitigated using readily available assay optimization tools such as protein-free blockers [11].In addition to flexibility in the choice of detection reagents, Affimer binder assay performance can also be modulated using defined surface options to tweak dynamic range or increase sensitivity, when all other assay conditions are fixed. This modulation is easily achieved by titrating nonbinding scaffold proteins into the assay-coating mixture to spread surface distribution of functional binding sites. Sensitivity can be further driven by making multidomain Affimer and bi-paratopic capture surfaces [11].The supply of anti-ID reagents must be both stable and secure in order to meet quality-control requirements for critical reagents and minimize batch variation. As monoclonal antibodies are incredibly time-consuming to produce and are at high risk of batch-to-batch variability, it is necessary to maintain banks of hybridomas or cell lines for quick recovery for consistent production. This also poses a risk in case of disaster causing cell banks to be lost. Owing to the simplicity of the Affimer reagent production process, it is much cheaper and quicker to reliably remake Affimer gene constructs should these be lost. It is also possible to store Affimer reagents stably for long time periods when dried on plate surfaces, even at room temperature. This has been demonstrated using Affimer anti-ID binders for adalimumab, rituximab and trastuzumab, which showed no significant loss of assay performance after 3 months at 25°C [11].ConclusionThe efficacy and reliability of drug development and diagnostics, of which outputs from PK assays are an essential part, is dependent on the quality of each individual process involved. It is, therefore, vital that researchers challenge and investigate these steps, and the reagents used. Certain limitations posed by the use of traditional antibody molecules may be overcome by high-quality alternatives, such as Affimer binders. These alternatives offer flexibility and specificity to ensure consistent and stable processes within both drug development and diagnostics, helping to speed the development of new biologic medicines, and to define more targeted dosing windows for patients.Financial & competing interests disclosureMatt Johnson is Chief Technology Officer at Avacta Life Sciences, developer of Affimer® technology. Affimer proteins have applications across diagnostics, drug/biomarker discovery, biotech research and development, and therapeutics. The author has no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.No writing assistance was utilized in the production of this manuscript.Papers of special note have been highlighted as: • of interest; •• of considerable interestReferences1. Tuntland T, Ethell B, Kosaka T et al. Implementation of pharmacokinetic and pharmacodynamic strategies in early research phases of drug discovery and development at Novartis Institute of Biomedical Research. Front. Pharmacol. 5, 174 (2014). • Outlining the importance of pharmacokinetic (PK) assays throughout the drug discovery and development process.Medline, Google Scholar2. Lee C, Park C, Hsiao C. Abstract 4659. Point of care PK quantitation device for pharmacokinetic guided dosing of paclitaxel as a companion diagnostic device. Poster presented at: American Association for Cancer Research Annual Meeting 2014. CA, USA, 5–9 April 2014. • Demonstrating an application of PK assays in point-of-care companion diagnostics.Crossref, Google Scholar3. Paul KF, McLeod J. Restructuring proteomics: the rise of next-generation affinity reagents. Drug Discov. World Winter issue, 17–22 (2014).Google Scholar4. Baker M. Reproducibility crisis: blame it on the antibodies. Nature 521(7552), 274–276 (2015). • Outlining some of the features of antibodies that can lead to reproducibility issues, and the implications this has for the 'reproducibility crisis'.Crossref, Medline, CAS, Google Scholar5. Nuttall J, Nicholl A, Ford R et al. Poster POS028. Affimer® anti-idiotypic binders: high-performing critical reagents for diverse clinical needs. Poster presented at: 4th European Bioanalysis Forum Young Scientist Symposium. Bologna, Italy, 21 March 2019.Google Scholar6. Suderman R, Rice D, Gibson S, Strick E, Chao D. Development of polyol-responsive antibody mimetics for single-step protein purification. Protein Expr. Purif. 134, 114–124 (2017).Crossref, Medline, CAS, Google Scholar7. Skerra A. Alternative binding proteins: anticalins – harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities. FEBS J. 275(11), 2677–2683 (2008).Crossref, Medline, CAS, Google Scholar8. Surat P. Affibody Molecule Discovery and Uses (2018). https://www.news-medical.net/life-sciences/Affibody-Molecule-Discovery-and-Uses.aspxGoogle Scholar9. Tiede C, Bedford R, Heseltine S et al. Affimer proteins are versatile and renewable affinity reagents. eLife 6, e24903 (2017). •• Outlining a discovery process for Affimer reagents, and demonstrating their potential as alternative affinity reagents to antibodies.Medline, Google Scholar10. Julian MC, Li L, Garde S, Wilen R, Tessier PM. Efficient affinity maturation of antibody variable domains requires co-selection of compensatory mutations to maintain thermodynamic stability. Sci. Rep. 7, 45259 (2017). • Describing the lengthy process of affinity maturation often required to develop monoclonal antibody affinity reagents.Google Scholar11. Johnson M. Improving PK and drug monitoring assays with the Afiimer® Platform. Presented at: 12th European Bioanalysis Forum Open Symposium, Barcelona, Spain, 21 November 2019. •• Describing a series of experiments that demonstrate the utility of Affimer anti-ID reagents in PK assays, through development and optimization of Affimer binders for a number of therapeutic antibodies.Google ScholarFiguresReferencesRelatedDetailsCited ByIntact Protein Mass Spectrometry for Therapeutic Protein Quantitation, Pharmacokinetics, and Biotransformation in Preclinical and Clinical Studies: An Industry Perspective1 September 2020 | Journal of the American Society for Mass Spectrometry, Vol. 32, No. 8Recent Advances in the Scaffold Engineering of Protein BindersCurrent Pharmaceutical Biotechnology, Vol. 22, No. 7The importance of quality critical reagents for the entire developmental lifecycle of a biopharmaceutical: a pharmacokinetic case studyAndrew P Mayer & Kristy J Fraley26 March 2021 | Bioanalysis, Vol. 13, No. 10 Vol. 12, No. 3 Follow us on social media for the latest updates Metrics History Received 2 December 2019 Accepted 2 December 2019 Published online 24 January 2020 Published in print February 2020 Information© 2020 Newlands PressKeywordsaffimerantibodyassay developmentbinding reagentsbiotherapeutics drug developmentELISApharmacokinetic assaystherapeuticsFinancial & competing interests disclosureMatt Johnson is Chief Technology Officer at Avacta Life Sciences, developer of Affimer® technology. Affimer proteins have applications across diagnostics, drug/biomarker discovery, biotech research and development, and therapeutics. The author has no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.No writing assistance was utilized in the production of this manuscript.PDF download

There is an exponential growth in the number of cyber-attack incidents resulting in significant financial loss and national security concerns. Secure cyberspace has been designated as one of the National Academy of Engineering (NAE) Grand Challenges in engineering. Broadly, the security threats are targeted on software programs, operating system and network with the intention to launch confidentiality, integrity and availability violations. Existing undergraduate and graduate-level cybersecurity education curriculum rely primarily on didactic teaching methods with little focus on student centered, inquiry-based teaching, known to improve student learning. With growing number of security incidents taking place, it is utmost important to prepare a workforce equipped with knowledge of the threat space and existing state-of-the-art solution. Such comprehensive understanding is only possible by a dedicated hands-on course on cybersecurity where students can learn the key concepts by editing the hardware, software and OS, and, network policies. Unfortunately, such extensive and deep flexibilities are not provided in current cybersecurity curriculum. In this paper, we introduce a hands-on and modular self-learning Cybersecurity Training (CST) Kit to advance cybersecurity education. Students can promptly apply newly acquired knowledge on the CST Kit as part of the learning process. This Kit accompanies Do-It-Yourself (DIY) training modules that is used to model and investigate cybersecurity issues and their prevention to all levels of the cybersecurity workforce, including undergraduate and graduate students and K-12 science and technology teachers. The Kit also covers various aspects of cybersecurity issues including, hardware, software, operating system and network security. A coursework is developed on hardware security for Senior undergraduate and graduate students. A preliminary survey conducted among students who were introduced to the modular board to implement hardware security threats such as, side-channel attack shows an 120% improvement in their understanding after the CST Kit based activities. The components of the CST Kit are also used in a 4-day summer workshop for K-12 teachers. Teachers took pre- and post- concept inventories to assess their learning of content throughout the workshop and the results indicated improvement of 58%. These assessments focused on vulnerabilities and specific types of attacks, system security, data transmission and encryption, permutations and combinatorics, and binary numbers.