If you have news that you would like distributed via HUPO's website, newsletter, or social media channels, please email office(at)hupo.org.
The hallmark update paper each year is the HPP Metrics publication, is now online, lead by Dr Gil Omenn and the leaders of neXTprot, the Peptide Atlas, the HPP, C-HPP and B/D-HPP:
“The 2023 Report on the Human Proteome from the HUPO Proteome Project”, by Gilbert S. Omenn,* Lydie Lane, Christopher M. Overall, Cecilia Lindskog, Charles Pineau, Nicolle H. Packer, Ileana M. Cristea, Susan T. Weintraub, Sandra Orchard, Michael H. A. Roehrl, Edouard Nice, Tiannan Guo, Jennifer E. Van Eyk, Siqi Liu, Nuno Bandeira, Ruedi Aebersold, Robert L. Moritz, and Eric W. Deutsch. ABSTRACT: Since 2010, the Human Proteome Project (HPP), the flagship initiative of the Human Proteome Organization (HUPO), has pursued two goals: (1) to credibly identify the protein parts list and (2) to make proteomics an integral part of multiomics studies of human health and disease. The HPP relies on international collaboration, data sharing, standardized reanalysis of MS data sets by PeptideAtlas and MassIVE-KB using HPP Guidelines for quality assurance, integration and curation of MS and non-MS protein data by neXtProt, plus extensive use of antibody profiling carried out by the Human Protein Atlas. According to the neXtProt release 2023-04-protein expression has now been credibly detected (PE1) for 18,397 of the 19,778 neXtProt predicted proteins coded in the human genome (93%). Of these PE1 proteins, 17,453 were detected with mass spectrometry (MS) in accordance with HPP Guidelines and 944 by a variety of non-MS methods. The number of neXtProt PE2, PE3, and PE4 missing proteins now stands at 1381. Achieving the unambiguous identification of 93% of predicted proteins encoded from across all chromosomes represents remarkable experimental progress on the Human Proteome parts list. Meanwhile, there are several categories of predicted proteins that have proved resistant to detection regardless of protein-based methods used. Additionally there are some PE1−4 proteins that probably should be reclassified to PE5, specifically 21 LINC entries and ∼30 HERV entries; these are being addressed in the present year. Applying proteomics in a wide array of biological and clinical studies ensures integration with other omics platforms as reported by the Biology and Disease-driven HPP teams and the antibody and pathology resource pillars. Current progress has positioned the HPP to transition to its Grand Challenge Project focused on determining the primary function(s) of every protein itself and in networks and pathways within the context of human health and disease.
The HUPO Early Career Researcher (ECR) Committee is delighted to welcome Pathmanaban Ramasamy. Keep reading to know more about him!
Pathmanaban Ramasamy (Paddy) is a junior post-doc in the CompOmics group at Ghent University in Belgium. During his joint Ph.D. program between Ghent University and Vrije Universiteit Brussel, he leveraged his expertise in structural bioinformatics and proteomics informatics to unravel the role of local amino acid interactions in protein folding, fold stability, and the location of post-translational modifications (PTMs). He endeavors to unravel the "where, how, and why" of protein PTMs through a comprehensive large-scale investigation that spans these modifications within sequence, structure, and biophysical contexts.
He has been extremely active in bringing the MS proteomics and structure communities together at the European scale, investing heavily in an ELIXIR Europe-funded cross-over study between the three key communities: the 3D-BioInfo (protein structure), Intrinsically Disordered Proteins, and MS Proteomics communities. Paddy is enthusiastic about becoming a member of the HUPO-ECR and looks forward to actively contributing to the support of young proteomics researchers through his involvement with HUPO-ECR and YPIC.
Prof. Hong Wang Institute Of Hematology & Blood Diseases Hospital, Chinese Academy of Medical Sciences & Peking Union Medical College, China
The PSI meeting 2024 will take place from March 18-20th 2024 at the Kyoto University, Japan.
View event details here.
The meeting is sponsored by: JPOST (JST-NBDC) and JPDM (JSPS).
Organizers: Yasushi Ishihama & Shujiro Okuda.
Program: The provisional agenda will be posted soon.
Registration: Registration for attending the meeting is now open.
The January HUPOST is now available.....check out the latest HUPO 2024 news, ETC Webinars, ECR Manuscript Competition, upcoming events & much more...
The HUPO Early Career Researcher (ECR) Initiative is delighted to welcome Nick Riley and Mahshid Moballegh Nasery.
Nick Riley is an assistant professor of chemistry at the University of Washington. With a background in mass spectrometry instrumentation, proteomics, and glycobiology from his graduatework with Prof. Josh Coon at University of Wisconsin-Madison and his postdoctoral work with Prof. Carolyn Bertozzi at Stanford University, he now leads a research program focused on innovative bioanalytical and chemical biology technologies to investigate essential principles of glycocode regulation and dysregulation. Nick has been involved with HUPO and US HUPO for a number of years and is excited to join the HUPO ECR committee to support the vibrant and supportive communities that help early career scientists build their scientific careers in proteomics research.
Mahshid Moballegh Nasery pursued a diverse academic journey, beginning with a Bachelor's in Chemistry and delving closer into biology with a Master's in Medical Toxicology, where her focus on cancer led to publications in articles and a chapter book. Her passion for proteomics started to grow as she attended her proteomics course and attended an ECR day meeting! Currently engaged in research at the University of Debrecen, under the supervision of Dr. Eva Csosz. Her recent membership in YPIC (Young Proteomics Investigators Club) reflects her eagerness to expand her network and engage actively with fellow proteomics scientists. She aims to deepen her involvement in various activities, leveraging her multi-disciplinary background, to contribute meaningfully to the scientific community. Driven by a thirst for knowledge and a desire to make impactful contributions, Mahshid is passionate about exploring within the vibrant realm of proteomics and biochemistry.
What is your current position and affiliation? I am a project group leader (a position somewhat between postdoc and group leader) at the Max Planck Institute of Biochemistry within the group of Matthias Mann. How would you like your work to contribute to the field of proteomics? I currently focus on clinical mass spectrometry-based proteomics and nearly any project I am working on involves patient samples or is a direct collaboration with clinicians. I would like to continue employing this powerful method to uncover biological mechanisms and better understand diseases, which ultimately will benefit patients with better treatments. In the best case scenario, this leads for example to the discovery of novel biomarkers or therapeutic targets, but also a better functional understanding without the identification of distinct single biomarkers is a step in the right direction. Biomarker discovery is often done with large patient cohorts and I hope to contribute to the field by enabling such studies from a technical perspective and providing the community with unique datasets. In parallel to this work, I would like to transform proteomics from a method for biomarker discovery by retrospective analysis to a tool for pro- and diagnostics in the future.
What have you found in the HUPO community/congress?I had the chance to attend the HUPO world congresses two times so far. I found it to be a perfect intersection of different interest groups forming a thriving community between biological expertise and technical solutions. How was your experience/what did it mean to present your work at HUPO?Having been invited to the ECR manuscript competition to HUPO in Busan to present my work meant a lot to me. Sharing the excitement about new findings is definitely a driver of motivation for me to work as a scientist and being given the opportunity to do so in such a venue has been a major pleasure. I received a plethora of positive feedback from this wonderful community, which is truly motivating.
REGISTER HERE
WEBINAR DESCRIPTION: RPPA is a high-throughput protein array technology that simultaneously measures hundreds or thousands of samples on glass slides with high precision and reliability, using specific antibodies. RPPA and mass spectrometry-based protein profiling are complementary technologies for protein profiling. In attending this webinar, attendees will learn about RPPA's high-throughput capabilities and laser-captured microdissection technology. They will understand how these technologies precisely measure protein expression, modifications, and phosphorylation in tumor cells.
RPPA Technology Overview: Understand the high-throughput nature of RPPA for simultaneous analysis of numerous samples with minimal amounts. And explore how RPPA measures protein levels and modifications, offering a detailed molecular profile of tumor cells. Clinical Applications: Learn how RPPA and LCM aid in accurate diagnosis and prognosis, particularly in cancer, influencing clinical decision-making. Understand RPPA's role in predicting responses to targeted therapies, shaping the future of personalized medicine.
CLINICAL APPLICATIONS:Learn how RPPA and LCM aid in accurate diagnosis and prognosis, particularly in cancer, influencing clinical decision-making. Understand RPPA's role in predicting responses to targeted therapies, shaping the future of personalized medicine.
SPEAKER BIO: Dr. Rosa Isela Gallagher obtained her Ph.D. in Cell and Molecular Biology from GMU in 2019. She has accumulated more than 15 years of expertise in Reverse Phase Protein Array (RPPA) and Laser Capture Microdissection (LCM) technologies and is currently a Senior Research Scientist in the Center for Applied Proteomics and Molecular Medicine, led by Drs. Lance Liotta and Emanuel Petricoin III, the inventors of both technologies. RPPA is a high-throughput, antibody-based protein array technology capable of conducting assays on small amount of materials on thousands of samples simultaneously. This platform measures protein expression levels and modifications, including phosphorylation. Dr. Gallagher’s current research focuses on the molecular profiling of tumor cells utilizing LCM and RPPA to investigate unique signaling pathway profiles and new disease mechanisms to guide diagnosis, prognosis, and targeted therapeutics.
The December HUPOST is now available.....check out the ETC webinars, HPP Chair & Co-chair nominations, C-HPP updates, upcoming events & a farewell message from HUPOST editor Ben Garcia...
DATE: Wednesday, February 21, 2024 TIME: 7am PST / 10am EST / 4pm CET LOCATION: Zoom (link to follow upon registration) SPEAKER: Oliver Raether
WEBINAR DESCRIPTION:
Trapped ion mobility spectrometry (TIMS) is a powerful analytical technique that separates and characterizes gas-phase ions based on their mobility in a buffer gas. TIMS has been widely applied in various fields, such as proteomics, metabolomics, lipidomics, and pharmaceutical research. It offers sensitivity, speed, and resolution for complex and challenging samples.
LEARNING OBJECTIVES:
In the first part of this webinar, you will learn about the history of the TIMS research and development, including the chronological launch of the different timsTOF instruments and SW capabilities by Bruker. You’ll learn about the differences and similarities of the timsTOF instruments, the possible upgrade paths and software options.
In the webinar, you will also learn about the different data-independent acquisition (DIA) mass spectrometry methods currently used in proteomics and how new approaches benefit from the additional ion mobility dimension and new acquisition modes.
Finally, in the third part of this webinar, you will learn about some of the future approaches that are currently under development for the TIMS technique, such as TIMS gas phase fractionation and filtering. This is a novel setup that uses two or three TIMS analyzers in a row to separate and isolate different regions of the m/z vs 1/K0 space. This can increase the selectivity and sensitivity of the TIMS technique, and improve applications and workflows especially for heterogeneous proteomics samples. You will see how these methods work, and what are the advantages and challenges of implementing it.
SPEAKER BIO: Oliver Raether is Research and Development Manager at Bruker Daltonics in Bremen. He received his M.Sc. in engineering from the Hamburg University of Technology (1995). Over the past nearly three decades he and his colleagues have developed orthogonal time of flight mass spectrometers including since 2010 the timsTOF product line. He has produced 14 peer reviewed journal articles and is inventor/co-inventor of 71 patents in the field of mass spectrometry and, more recently, ion mobility spectrometry (h-index 13). His awards include the HUPO Science and Technology Award for contributions on Trapped Ion Mobility Mass Spectrometry Instrumentation (2020).