NewS

AI Tools in Grant Writing Applications, Research Articles, CVs, etc.

Chairs: Emily Hashimoto-Roth (University of Toronto, Canada) and Ruth Huttenhain (Stanford University, USA)

Speakers:

• Dr. Laura Elo (University of Turku, Finland)
• Dr. Min-Sik Kim (Daegu Gyeongbuk Institute of Science & Technology, South Korea)
• Dr. Jack Washington (Molecular Omics, United Kingdom)

The session "AI tools in grant writing applications, research articles, CVs, etc." focused on the integration of new artificial intelligence (AI) technologies into various aspects of scientific document production and publication.

Attendees shared the utility of AI tools such as ChatGPT to enhance their daily work efficiency, mentioning that these tools are quite useful for brainstorming and idea generation. In particular, using ChatGPT as a writing aid was recognized as a valuable tool to overcome writer's block or "blank-page-o-phobia”. It was also discussed how AI tools can also be very useful for editing and proofreading, especially when English is not the writer’s first language. The potential use of AI by journals for proofreading to identify formatting and writing errors was also discussed, indicating the evolving role of AI in scientific publishing.

Participants also questioned mentors regarding best practices for AI tools in research. IN short it was mentioned that AI can be leveraged to polish visualization, troubleshoot software code, and even interpret results, but such tools should be used with caution. Despite the benefits of using ChatGPT prompts for writing, the need for critical review and manual editing to ensure the final written output meets scientific standards was emphasized. Ethical concerns, including the risk of data leaks when using AI tools for proofreading and the need for transparency of AI contributions was mentioned. Overall, the session shed light on the growing role of AI in proteomics research and the broader scientific publishing landscape. It offered an exploration on AI’s potential to enhance efficiency, address ethical concerns, and possibly reshape the way scientific research is published and shared in the future.

Promoting Your Science

Chairs: Daniel Garama (Hudson Institute of Medical Research, Australia) and Mathieu Lavallée-Adam (University of Ottawa, Canada)

Speakers:

• Dr. Alexey Nesvizhskii (University of Michigan, USA)
• Dr. Hyun Woo Park (Yonsei University, South Korea)
• Dr. Stephen Pennington (University College Dublin, Ireland)
• Paula Burton (Mass Dynamics, Australia)

This session explored the many aspects of promoting your science as well as how scientific outreach can help in advancing one’s career.

It was clearly highlighted during the session that one key aspect of promoting your science involves, identifying target audiences. In addition to attending specialized conferences, participants discussed alternative methods for identifying the right audience for their research. Strategies included utilizing social media, publishing in widely read journals, and engaging with interdisciplinary communities. The session touched on the topic of maintaining a professional online presence. While recognizing the value sharing elements of one’s personal life, participants advised caution about posting some personal photos online, emphasizing the usefulness of a separate professional profile to maintain a credible image.

Attendees also discussed the role of institutional support in self-promotion. Many shared how universities, institutes, and companies can provide resources, such as funding, mentorship, and networking opportunities, to aid in career advancement and science promotion. Interestingly, participants considered some of the challenges related with dealing with opposition. Speakers shared their experiences on how they find the courage and confidence to address opposition to their ideas and results. The importance of constructive feedback, resilience, and persistence was highlighted. Finally, the panelists emphasized the importance of diversity and inclusion efforts in academia and research.

Geographical Differences for Academic Job Applications

Chairs: Andreas Hober (AstraZeneca, Sweden) and Lívia Rosa-Fernandes (Macquarie University Centre for Motor Neuron Disease Research, Australia)

Speakers:

• Dr. Nicki Packer (Macquarie University, Australia)
• Dr. Uwe Völker (University Greifswald, Germany)
• Dr. Yu-Ju Chen (Academia Sinica, Taiwan)
• Dr. Birgit Schilling (Buck Institute, USA)

During this session, attendees learned about the added value of conducting research abroad. In particular the benefits of exposure to different scientific cultures and networking opportunities were highlighted. Still, it was acknowledged that working abroad is not a universal requirement for a successful career. International relocation can have profound effects on personal aspects, such as partnerships and family. For example, some participants were curious regarding the challenges faced by expecting or new parents in finding jobs. The conversation emphasized the importance of supportive and flexible work environments to accommodate family responsibilities.

Attendees discussed the current job demand in the proteomics field, recognizing its rapid growth with increasing opportunities in academia, industry, and healthcare. Tips were shared for students aspiring to secure positions, including reaching out to potential mentors and the importance of making a good impression during a job interview by attaining  to a professional etiquette. For graduate students interested in finding postdoctoral positions, panelists shared how most postdocs typically find their positions, highlighting networking, collaborations, and mentor recommendations as effective strategies. The timing of grant applications for postdoctoral researchers and beyond was a significant topic. Advice emphasized starting early, cultivating strong grant-writing skills, and being strategic.

In addition, participants acknowledged diverse career paths within proteomics research outside of the traditional academic route. These paths encompassed roles in scientific communication, project management, bioinformatics, and more. Some attendees expressed their interest in transitioning to industry and panelists debated the optimal timing for transitioning from academia to industry. It was agreed that this decision should be based on individual career goals and the alignment of research interests with industry demands.

The main goal of the new HUPO single-cell proteomics (SCP) initiative is to provide guidance and create a comparative overview of novel mass spectrometry (MS)-based low-input and single-cell technologies. After the first reports of SCP with large cells (i.e., oocytes) the field has quickly moved to ever more comprehensive analysis of single mammalian cells or even subcellular components.^1–3 A variety of workflows have since demonstrated valuable insights into cellular identities and their function, driven entirely by the proteome and their post-translational modifications.^4–6 However, deep proteome profiling of single mammalian cells or small subpopulations remains an analytical challenge for most non-specialized laboratories.

The growing interest in the SCP workflows and its application to biological questions has driven the initiation of this international SCP initiative. Our team is comprised of a diverse group of early, middle and advanced level scientists with growing expertise in diverse workflows and instrumentation. We aim to provide a comparative overview of current SCP approaches for the community to ease the implementation in more laboratories and integration to novel biological projects. Considering the ongoing trend away from bulk analysis towards resolving cellular heterogeneity, we believe that such unifying efforts will drive the understanding of complex tissue hierarchies and orchestrated spatiotemporal interactions.

To this end, our first goal is to perform a multi-laboratory study, processing the same batch of cells across different platforms and establish the first of such direct comparisons. We will leverage the knowledge of our SCP initiative members, who have pioneered various parts of the SCP workflows, including sample collection and preparation, chromatographic separation, acquisition strategies and analysis approaches.^2,3,7–9 We consider utilization of one cell batch especially important for these comparisons, as cell handling and the cell cycle heavily influence cell size and proteome composition.^5,10 Our portfolio of SCP workflows will include isobaric multiplexing (i.e. TMT) with one chemical label for multiple cells (i.e. carrier - SCoPE) to facilitate sufficient peptide signal even with less sensitive MS instrumentation.² Following tremendous improvements in instrument sensitivity and implementation of ion-mobility separation also label-free SCP workflows have been successfully demonstrated.^5,11 Those are typically paired with data independent acquisition (DIA), which massively reduces precursor stochasticity in comparison to data dependent acquisition.¹² Most standard TMT-based workflows rely on small isolation windows to reduce precursor co-isolation to relatively quantify a single precursor through their reporter ions.¹³ Scanning speeds of current instrumentation therefore restrict isobaric labeling workflows to DDA, which suffer from detrimental amounts of missing data across large sample cohorts.¹² The alternative label-free SCP approaches, however, are notoriously low in throughput as only once cell at a time is being analyzed in comparison to the isobaric labelling strategies (i.e. TMTpro = 18 samples or HyperSCP = 28).^14,15 As most applications for SCP require the analysis of hundreds or even thousands of cells, most recently a combination of non-isobaric chemical labeling with DIA allowing for relative quantification between up to three samples at the MS1 level was introduced.^16,17 This reduces missingness across a large number of samples while still increasing throughput through multiplexing.

As an alternative to chemical multiplexing, many groups aim to increase measurement throughput by optimizing chromatographic separation. Due to their low input, SCP samples do not require such extensive separation, allowing for the effective gradient length to be reduced in comparison to bulk.^5,18–22 Short gradients and most efficient inject-to-inject times has been implemented with the disposable trap columns of the Evosep One. Those are regularly used for SCP workflows, due to the combination of in-line clean up the sample and simultaneous separation of peptides, while the previous sample is still acquired on the MS.^5,23,24 SCP initiative team members also most recently demonstrated significantly reduced separation times employing non-commercial alternatives to increase chromatographic throughput.^18,21,22 Additionally, to the various acquisition and peptide separation efforts, the SCP community has proposed smart strategy to streamline sample preparation for reduced peptide losses and improved reproducibility.^{2,7,8,11,20,25–27} Our comparative analysis will therefore include both plate-based sample preparation at higher volumes (i.e. 1-3uL) and dedicated chip or slide based approaches with low nanoliter volumes within dedicated instruments such as the cellenONE and Tecan Uno.^{3,7,20,27–29}

The entire proteomics community, but especially researchers focusing on improvements in SCP, are heavily dependent on instrumentation sensitivity and throughput advances. The introduction of the Thermo Fisher Scientific Astral combining the Orbitrap and a novel asymmetric track lossless analyzer with optimized ion transfer and flight track design was readily awaited.^30–32 The combination of 200 Hz scanning speed in the Astral analyzer with the unprecedented resolution of the Orbitrap demonstrates great potential for profiling single cells.³² This now complements SCP studies regularly performed on earlier generation Orbitrap instruments, most recently linear ion trap analyzers and the highly sensitive time-of-flight instruments with trapped ion-mobility separation for operation at 100% duty cycle.^3,5,33,34 The latter has been updated this year to the Bruker Daltonics timsTOF Ultra with a more efficient ion source, allowing more ions to enter the instrument and thereby again boosting sensitivity, as well as improving dynamic range.^10,35 The combination of instrument vendors striving to improve sensitivity and throughput paired with the introduction of alternative acquisition strategies and outside the box thinking is pushing the field forward every day. Our SCP initiative therefore aims to support further development, provide a comparative overview of many techniques for multidisciplinary scientists and guide study design to make SCP more readily available for the scientific community.

Contributed by Dr. Budnik Bogdan, chair of the B/D-HPP single-cell initiative

References:

1.         Lombard‐Banek, C., Moody, S.A., and Nemes, P. (2016). Single-Cell Mass Spectrometry for Discovery Proteomics: Quantifying Translational Cell Heterogeneity in the 16-Cell Frog (Xenopus) Embryo. Angewandte Chemie International Edition 55, 2454–2458. 10.1002/anie.201510411.

2.         Budnik, B., Levy, E., Harmange, G., and Slavov, N. (2018). SCoPE-MS: mass spectrometry of single mammalian cells quantifies proteome heterogeneity during cell differentiation. Genome Biology 19. 10.1186/s13059-018-1547-5.

3.         Zhu, Y., Clair, G., Chrisler, W.B., Shen, Y., Zhao, R., Shukla, A.K., Moore, R.J., Misra, R.S., Pryhuber, G.S., Smith, R.D., et al. (2018). Proteomic Analysis of Single Mammalian Cells Enabled by Microfluidic Nanodroplet Sample Preparation and Ultrasensitive NanoLC-MS. Angewandte Chemie International Edition 57, 12370–12374. 10.1002/anie.201802843.

4.         Specht, H., Emmott, E., Petelski, A.A., Huffman, R.G., Perlman, D.H., Serra, M., Kharchenko, P., Koller, A., and Slavov, N. (2021). Single-cell proteomic and transcriptomic analysis of macrophage heterogeneity using SCoPE2. Genome Biology 22, 50. 10.1186/s13059-021-02267-5.

5.         Brunner, A.-D., Thielert, M., Vasilopoulou, C., Ammar, C., Coscia, F., Mund, A., Hoerning, O.B., Bache, N., Apalategui, A., Lubeck, M., et al. (2022). Ultra-high sensitivity mass spectrometry quantifies single-cell proteome changes upon perturbation. Molecular Systems Biology 18, e10798. 10.15252/msb.202110798.

6.         Zhu, Y., Scheibinger, M., Ellwanger, D.C., Krey, J.F., Choi, D., Kelly, R.T., Heller, S., and Barr-Gillespie, P.G. (2019). Single-cell proteomics reveals changes in expression during hair-cell development. eLife 8, e50777. 10.7554/eLife.50777.

7.         Ctortecka, C., Hartlmayr, D., Seth, A., Mendjan, S., Tourniaire, G., and Mechtler, K. (2022). An automated workflow for multiplexed single-cell proteomics sample preparation at unprecedented sensitivity. 2021.04.14.439828. 10.1101/2021.04.14.439828.

8.         Schoof, E.M., Furtwängler, B., Üresin, N., Rapin, N., Savickas, S., Gentil, C., Lechman, E., Keller, U. auf dem, Dick, J.E., and Porse, B.T. (2021). Quantitative single-cell proteomics as a tool to characterize cellular hierarchies. Nat Commun 12, 3341. 10.1038/s41467-021-23667-y.

9.         Végvári, Á., Rodriguez, J.E., and Zubarev, R.A. (2022). Single-Cell Chemical Proteomics (SCCP) Interrogates the Timing and Heterogeneity of Cancer Cell Commitment to Death. Anal. Chem. 94, 9261–9269. 10.1021/acs.analchem.2c00413.

10.       Evosep (2023). AN-021A - Pushing-the-boundaries-for-robust-and-high-throughput-single-cell-proteomics.pdf. https://www.evosep.com/wp-content/uploads/2022/12/AN-021A-Pushing-the-boundaries-for-robust-and-high-throughput-single-cell-proteomics.pdf.

11.       Zhu, Y., Piehowski, P.D., Zhao, R., Chen, J., Shen, Y., Moore, R.J., Shukla, A.K., Petyuk, V.A., Campbell-Thompson, M., Mathews, C.E., et al. (2018). Nanodroplet processing platform for deep and quantitative proteome profiling of 10–100 mammalian cells. Nature Communications 9, 882. 10.1038/s41467-018-03367-w.

12.       Muntel, J., Kirkpatrick, J., Bruderer, R., Huang, T., Vitek, O., Ori, A., and Reiter, L. (2019). Comparison of Protein Quantification in a Complex Background by DIA and TMT Workflows with Fixed Instrument Time. J. Proteome Res. 18, 1340–1351. 10.1021/acs.jproteome.8b00898.

13.       Savitski, M.M., Mathieson, T., Zinn, N., Sweetman, G., Doce, C., Becher, I., Pachl, F., Kuster, B., and Bantscheff, M. (2013). Measuring and Managing Ratio Compression for Accurate iTRAQ/TMT Quantification. Journal of Proteome Research 12, 3586–3598. 10.1021/pr400098r.

14.       Liang, Y., Truong, T., Saxton, A.J., Boekweg, H., Payne, S.H., Van Ry, P.M., and Kelly, R.T. (2023). HyperSCP: Combining Isotopic and Isobaric Labeling for Higher Throughput Single-Cell Proteomics. Anal. Chem. 95, 8020–8027. 10.1021/acs.analchem.3c00906.

15.       Li, J., Cai, Z., Bomgarden, R.D., Pike, I., Kuhn, K., Rogers, J.C., Roberts, T.M., Gygi, S.P., and Paulo, J.A. (2021). TMTpro-18plex: The Expanded and Complete Set of TMTpro Reagents for Sample Multiplexing. J Proteome Res 20, 2964–2972. 10.1021/acs.jproteome.1c00168.

16.       Derks, J., Leduc, A., Wallmann, G., Huffman, R.G., Willetts, M., Khan, S., Specht, H., Ralser, M., Demichev, V., and Slavov, N. (2022). Increasing the throughput of sensitive proteomics by plexDIA. Nat Biotechnol, 1–10. 10.1038/s41587-022-01389-w.

17.       Thielert, M., Itang, E.C., Ammar, C., Rosenberger, F.A., Bludau, I., Schweizer, L., Nordmann, T.M., Skowronek, P., Wahle, M., Zeng, W.-F., et al. (2023). Robust dimethyl-based multiplex-DIA doubles single-cell proteome depth via a reference channel. Molecular Systems Biology n/a, e11503. 10.15252/msb.202211503.

18.       Zheng, R., Matzinger, M., Mayer, R., Valenta, A., Sun, X., and Mechtler, K. (2023). A high-sensitivity low-nanoflow LC-MS configuration for high-throughput sample-limited proteomics. 2023.04.27.538542. 10.1101/2023.04.27.538542.

19.       Xiang, P., Zhu, Y., Yang, Y., Zhao, Z., Williams, S.M., Moore, R.J., Kelly, R.T., Smith, R.D., and Liu, S. (2020). Picoflow Liquid Chromatography–Mass Spectrometry for Ultrasensitive Bottom-Up Proteomics Using 2-μm-i.d. Open Tubular Columns. Anal. Chem. 92, 4711–4715. 10.1021/acs.analchem.9b05639.

20.       Matzinger, M., Müller, E., Dürnberger, G., Pichler, P., and Mechtler, K. (2022). Robust and easy-to-use one pot workflow for label free single cell proteomics. 2022.10.03.510693. 10.1101/2022.10.03.510693.

21.       Kreimer, S., Binek, A., Chazarin, B., Cho, J.H., Haghani, A., Hutton, A., Marbán, E., Mastali, M., Meyer, J.G., Mesquita, T., et al. (2023). High-Throughput Single-Cell Proteomic Analysis of Organ-Derived Heterogeneous Cell Populations by Nanoflow Dual-Trap Single-Column Liquid Chromatography. Anal. Chem. 95, 9145–9150. 10.1021/acs.analchem.3c00213.

22.       Webber, K.G.I., Truong, T., Johnston, S.M., Zapata, S.E., Liang, Y., Davis, J.M., Buttars, A.D., Smith, F.B., Jones, H.E., Mahoney, A.C., et al. (2022). Label-Free Profiling of up to 200 Single-Cell Proteomes per Day Using a Dual-Column Nanoflow Liquid Chromatography Platform. Anal. Chem. 10.1021/acs.analchem.2c00646.

23.       Bache, N., Geyer, P.E., Bekker-Jensen, D.B., Hoerning, O., Falkenby, L., Treit, P.V., Doll, S., Paron, I., Müller, J.B., Meier, F., et al. (2018). A Novel LC System Embeds Analytes in Pre-formed Gradients for Rapid, Ultra-robust Proteomics. Molecular & Cellular Proteomics 17, 2284–2296. 10.1074/mcp.TIR118.000853.

24.       Ye, Z., Sabatier, P., Martin-Gonzalez, J., Eguchi, A., Bekker-Jensen, D.B., Bache, N., and Olsen, J.V. (2023). One-Tip enables comprehensive proteome coverage in minimal cells and single zygotes. 2023.08.10.552756. 10.1101/2023.08.10.552756.

25.       Johnson, K.R., Gao, Y., Greguš, M., and Ivanov, A.R. (2022). On-capillary Cell Lysis Enables Top-down Proteomic Analysis of Single Mammalian Cells by CE-MS/MS. Anal. Chem. 10.1021/acs.analchem.2c03045.

26.       Johnston, S.M., Webber, K.G.I., Xie, X., Truong, T., Nydegger, A., Lin, H.-J.L., Nwosu, A., Zhu, Y., and Kelly, R.T. (2023). Rapid, One-Step Sample Processing for Label-Free Single-Cell Proteomics. J. Am. Soc. Mass Spectrom. 34, 1701–1707. 10.1021/jasms.3c00159.

27.       Sanchez-Avila, X., Truong, T., Xie, X., Webber, K.G.I., Johnston, S.M., Lin, H.-J.L., Axtell, N.B., Puig-Sanvicens, V., and Kelly, R.T. (2023). Easy and Accessible Workflow for Label-Free Single-Cell Proteomics. J. Am. Soc. Mass Spectrom. 10.1021/jasms.3c00240.

28.       Leduc, A., Huffman, R.G., Cantlon, J., Khan, S., and Slavov, N. (2022). Exploring functional protein covariation across single cells using nPOP. Genome Biology 23, 261. 10.1186/s13059-022-02817-5.

29.       Dou, M., Clair, G., Tsai, C.-F., Xu, K., Chrisler, W.B., Sontag, R.L., Zhao, R., Moore, R.J., Liu, T., Pasa-Tolic, L., et al. (2019). High-Throughput Single Cell Proteomics Enabled by Multiplex Isobaric Labeling in a Nanodroplet Sample Preparation Platform. Anal. Chem. 91, 13119–13127. 10.1021/acs.analchem.9b03349.

30.       Stewart, H., Grinfeld, D., Giannakopulos, A., Petzoldt, J., Shanley, T., Garland, M., Denisov, E., Peterson, A., Damoc, E., Zeller, M., et al. (2023). Parallelized Acquisition of Orbitrap and Astral Analyzers Enables High-Throughput Quantitative Analysis. 2023.06.02.543408. 10.1101/2023.06.02.543408.

31.       Heil, L.R., Damoc, E., Arrey, T.N., Pashkova, A., Denisov, E., Petzoldt, J., Peterson, A., Hsu, C., Searle, B.C., Shulman, N., et al. (2023). Evaluating the performance of the Astral mass analyzer for quantitative proteomics using data independent acquisition. 2023.06.03.543570. 10.1101/2023.06.03.543570.

32.       Petrosius, V., Aragon-Fernandez, P., Arrey, T.N., Üresin, N., Furtwängler, B., Stewart, H., Denisov, E., Petzoldt, J., Peterson, A.C., Hock, C., et al. (2023). Evaluating the capabilities of the Astral mass analyzer for single-cell proteomics. 2023.06.06.543943. 10.1101/2023.06.06.543943.

33.       Phlairaharn, T., Ye, Z., Krismer, E., Pedersen, A.-K., Pietzner, M., Olsen, J.V., Schoof, E.M., and Searle, B.C. (2023). Optimizing Linear Ion-Trap Data-Independent Acquisition toward Single-Cell Proteomics. Anal. Chem. 10.1021/acs.analchem.3c00842.

34.       Phlairaharn, T., Grégoire, S., Woltereck, L.R., Petrosius, V., Furtwängler, B., Searle, B.C., and Schoof, E.M. (2022). High Sensitivity Limited Material Proteomics Empowered by Data-Independent Acquisition on Linear Ion Traps. J. Proteome Res. 21, 2815–2826. 10.1021/acs.jproteome.2c00376.

35.       Bruker Daltonik (2023). 1901442-timstof-ultra-ebook-rev2.pdf. https://www.bruker.com/en/products-and-solutions/mass-spectrometry/timstof.html.

The September HUPOST is now available featuring important congress information, 2023 HUPO Awardees, ECR activities and competition finalists and much more!

Thank you to all who joined and participated in the HUPO ECR Panel Discussion on Translating Science from Benchtop to Biotech on August 9, 2023.

This panel is part of a seminar series organized by the HUPO Early Career Researcher Committee and The Young Proteomics Investigators Club (YPIC). These panels offer a space to foster professional development by engaging with the community. This time, two delightful panelists provided their time and expertise: Ruedi Aebersold (Co-founder of Biognosys) and Jarrod Sandow (Director and Senior Scientist at IonOpticks).

They commented on important considerations about scientific entrepreneurship such as intellectual property. Attendees learned about the resources often available within institutes or at incubators to refine a business plan . All in all this panel session highlighted the interesting opportunities of commercializing science, which can take the shape of a product, a service or developing proteomics technology. Thank you to our panelists and everyone that participated and made this such a great event.

Stay tuned for upcoming panel sessions!

The August HUPOST is now available featuring important congress information, next ECR webinar, ECR competition finalists, HUPO member notices, C-HPP workshop and more!

The HUPO ECR Committee is delighted to showcase the finalists of the 9th annual edition of the Manuscript Competition - take a look at their short bios below:

Dr. Johannes Bruno Müller-Reif
Max Planck Institute Of Biochemistry, Germany

Dr. Johannes Bruno Müller-Reif is a project leader and head of the Pediatric Proteomics Group at the Max Planck Institute of Biochemistry (MPIB). During his doctorate with Prof. Matthias Mann he focused on extending proteomics across the tree of life. Following his PhD, he joined the proteomics start-up OmicEra, where he significantly contributed to high-throughput proteomics methods for biomarker discovery and clinical research. Concurrently, Dr. Müller-Reif maintained a relationship with MPIB as a guest scientist, and his growing expertise led him to establish a research group with focus on the intersection of mass spectrometry-based proteomics and pediatrics. Dr. Müller-Reif’s research is multifaceted. A cornerstone of his work involves applying mass spectrometry-based proteomics to large patient cohorts to enhance biomarker discovery. In this capacity, he co-leads the MOMI cohort’s plasma proteomics efforts to address adverse pregnancy outcomes, supported by the Bill and Melinda Gates Foundation. He also focuses on the utilization of proteomics for investigating rare pediatric diseases. Furthermore, Dr. Müller-Reif pioneers the use of proteomics in specialized applications such as platelet biology and studying organisms inaccessible through conventional methods. This innovative approach not only exemplifies the practical versatility of proteomics but also ties back to his doctoral research on the proteome landscape of the kingdoms of life.

Dr. Pavel Sinitcyn
Morgridge Institute For Research,  United States

Pavel Sinitcyn is a distinguished Morgridge Interdisciplinary Postdoctoral Fellow at UW-Madison, conducting cutting edge research in the Joshua Coon lab. With a strong background in developing software solutions for proteomics data processing, Pavel has played a pivotal role in developing tools such as MaxQuant, MaxDIA, Perseus, and Deep Proteomic Sequencing Method.

Prof. Hong Wang
Institute Of Hematology & Blood Diseases Hospital, Chinese Academy Of Medical Sciences & Peking Union Medical College, China

Hong Wang got his Ph.D degree in 2017 at the University of Tennessee Health Science Center/St Jude Children’s Hospital in USA. After a continuous postdoc training and senior scientist experience at St. Jude, he joined the institute of Hematology and Blood diseases hospital, Chinese Academy of Medical Sciences & Peking Union Medical College in 2021. He is now a professor of the National Key Laboratory of Blood Science and Founding Director of the Center for Advanced Technologies.

Dr. Wang has developed multiple cutting-edge Mass Spectrometry-based proteomics technologies enabling ultradeep whole proteomic profiling with sub-microgram materials. He also developed advanced bioinformatics pipelines for multi-omics integration. He has published several high impact research articles on prestigious journals as corresponding/first authors in the last five years, e.g. Immunity, Cancer Cell, Nature Communications, PNAS, Genome Biology and Molecular Neurodegeneration. His research interests including: 1, to develop high-throughput single-cell and single-cell type proteomics technologies;   2, to use advanced multi-omics integrative strategies to dissect the blood ecosystems in systematic diseases.

HUPO Early Career Researcher (ECR) Online Panel Webinar

DATE:  Wednesday, August 9, 2023
TIME:  9 am CEST (Central European Summer Time)
LOCATION:  Zoom
SPEAKERS:  Reudi Abersold (Co-founder of Biognosys) and Jarrod Sandow (Director and Senior Scientist at IonOpticks)

Want to learn about turning science into a business? Join us for the coming online panel discussion taking place on August 9 at 9 am CEST. This panel is part of a seminar series organized by the HUPO Early Career Researcher Committee and The Young Proteomics Investigators Club (YPIC). These seminars offer a space to foster professional development by engaging with the community. During this one-hour panel, we will hear on thoughts and views from experienced researchers on their involvement and trajectory in the establishment of successful biotechs! 

REGISTER HERE

DATE: Thursday, July 20, 2023
TIME: 11 am - 1330 pm EDT
LOCATION: Zoom

Exciting B/D-HPP webinar on aging and disease coming up. Join us and listen to diverse topics in aging and disease proteomics including cancer, Alzheimer’s disease, geroscience, and others.

PLEASE NOTE: All times listed below are Eastern Daylight Time (EDT).

1100 am EDT - ROGER REDDELL - Progress Towards Utilisation of Tissue Proteomics in the Cancer Clinic

1130 am EDT - RENA ROBINSON - High-throughput Proteomics Applications in Aging & Alzheimer’s Disease

1200 pm EDT - MAGGIE LAM - Post-transcriptional Regulation of Aging and Diseases

1230 pm EDT - BIRGIT SCHILLING - TBA

1300 pm EDT - NATHAN BASISTY - Leveraging Proteomics for Translational Geroscience

1330 pm EDT - Closing Remarks

REGISTER HERE