Category: News

The European Proteomics Association (EuPA) has awarded Albert Heck the Proteomics Pioneer Award 2014. This is the most prestigious award of the society. Heck is professor in Biomolecular Mass Spectrometry and Proteomics at Utrecht University and scientific director of the Netherlands Proteomics Centre and the European large-scale proteomics facility PRIME-XS. Heck receives the award for his many and excellent contributions to the field of proteomics.

On October 8^th the award was handed over during the Award Ceremony of the 13th HUPO Annual World Congress in Madrid, Spain. The award is linked with an amount of 5.000 Euro.

EuPA is the federation of European national proteomics societies. It has been established in 2005 to coordinate and integrate national initiatives within the proteomics field. Previous Proteomics Pioneer Awardees are Ruedi Aebersold (ETH Zurich) and Amos Bairoch (Swiss Institute of Bioinformatics).

Prof Christopher Dobson, who has been awarded the 2014 Dr. H.P. Heineken Prize for Biochemistry and Biophysics (USD 200,000), will be visiting Utrecht University on September 29. Dobson will give a lecture about his research for uncovering the manner in which proteins in the human body sometimes misfold themselves and how that process may lead to age-related diseases, including Alzheimer’s, Parkinson’s and diabetes. Before this, Dr. Celia Berkers, UU researchers and winner of the Heineken Young Scientists Award for Biochemistry and Biophysics 2014, will give a lecture.

Where  Utrecht University, Marinus Ruppertbuilding, Zaal Blauw
When   29 September 2014, 15.15-17.00 hr

Attendance is free of charge, but we kindly ask you to register here.

About Christopher Dobson
Christopher Dobson is Professor of Chemical and Structural Biology, University of Cambridge (United Kingdom). Dobson has been studying the way in which biological molecules behave for many years, both in laboratories and test tubes and in the real world of the human body. His work has helped show how molecular building blocks assemble themselves into chains, and how these chains fold into complex structures.

About Celia Berkers
Dr Celia Berkers is a research group leader at Utrecht University’s Bijvoet Center for Biomolecular Research and studies interactions between medicines and the ‘metabolome’, i.e. all the small molecules in the cell and their interactions. Her work may help us develop new drugs against various diseases. She is receiving the 2014 Young Scientists Award for Biochemistry and Biophysics for her research into the workings of the proteasome, a structure that breaks down proteins in biological cells.

Heineken Prize
Every other year, the Dr H.P. Heineken Foundation awards one of the most prestigious prizes conferred in the Netherlands: the Dr H.P. Heineken Prize for Biochemistry and Biophysics. In doing so, the Foundation draws attention to the importance of these two disciplines, including the biochemical and biophysical aspects of microbiology and the physiology of seed germination. The prize does not cover technical aspects of the physiology of seed germination. The Dr H.P. Heineken Prize for Biochemistry and Biophysics consists of a crystal trophy and USD 200,000
The Heineken Young Scientists Awards are intended to give talented young scientists and scholars extra encouragement. They are presented simultaneously with the Heineken Prizes to talented young researchers whose outstanding work sets an example for other young scientists and scholars.The Heineken Young Scientists Awards consist of a work of art and EUR 10,000.
The Heineken Prizes and the Heineken Young Scientists Awards will be presented on 2 October 2014.

Please take a moment to listen to the ‘De Kennis Van Nu’ radio interview (in Dutch) with Prof. Albert Heck, which took place on Tuesday, June 24th. The interview is amongst others about the first draft of the human protein catalogue. Just click here to tune in!

 

 

 

The first two attempts at a complete catalogue of human proteins are published in Nature by two independent teams of researchers.

Albert Heck and co-author Simone Lemeer, who worked on the project in München before she joined the Biomolecular Mass Spectrometry and Proteomics Group at Utrecht University, were interviewed by Dutch and German journalists. Read the articles on Zeit Online, Spiegel Online and De Volkskrant.

The Netherlands Organisation for Scientific Research (NWO) has awarded Simone Lemeer, assistant professor Biomolecular Mass Spectrometry and Proteomics Group at Utrecht University, a Vidi grant for her research proposal ‘Elucidation of kinase inhibitor resistance in lung cancer’. With the Vidi grant NWO gives talented researchers the opportunity to develop their own line of research and to build up their own research group. Each scientist receives a maximum amount of 800,000 euros.

Vidi is aimed at excellent researchers who have gained several years of research experience after obtaining their PhDs. The scientists belong to the best ten to twenty percent in their discipline. A Vidi grant funds their research for a period of five years. Vidi is part of the NWO Talent Scheme, which consists of the Veni, Vidi and Vici grants.

NWO selects the Vidi laureates on the basis of the quality of the researcher, the innovative character of the research, the expected scientific impact of the research proposal and the possibilities for knowledge utilisation.

 

 

 

In a recent article in the Journal of the American Chemical Society researchers from the Biomolecular Mass Spectrometry and Proteomics Group of Albert Heck at Utrecht University report on improvements made on a mass analyzer (termed Orbitrap), enabling them to analyze virus particles with unprecedented precision. This allowed them to simultaneously detect and analyze multiple co-occurring virus particles with very subtle mass differences between them.

The researchers used the instrument to determine the amount of foreign protein cargo in virus-like nanocontainers. In addition, they uncovered for the first time the composition of the Adeno-Associated Virus capsid, which is the first approved vector for gene therapy in the Western world. Their experiments revealed an assortment of different capsids with small variations in the number of different capsid proteins.

Virus particles can be considered as very stable capsules holding and protecting the viral genome. These capsules can also be utilized to deliver foreign cargo in for instance gene therapy or nanotechnology. Virus particles are largely built from proteins and are some of the largest known protein complexes. Up to several hundreds of copies of the capsid proteins assemble into a tightly packed and often highly symmetric hollow shell. Determining a detailed composition of a virus particle is challenging due to the large size of the shell, requiring special instrumentation that can detect and mass analyze these massive molecules.

The work was performed in collaboration with the groups of Mavis Agbandje-McKenna (University of Florida, USA) and Alexander Makarov (Thermo Fisher Scientific, Bremen and Utrecht University).

Read the full article:
Defining the Stoichiometry and Cargo Load of Viral and Bacterial Nanoparticles by Orbitrap Mass Spectrometry.
Snijder, J., van de Waterbeemd, M., Damoc, E., Denisov, E., Grinfeld, D., Bennett, A., Agbandje-McKenna, M., Makarov, A., Heck, A.J.R.
JACS, May 1^st 2014, DOI: 10.1021/ja502616y

The work was funded by the Netherlands Proteomics Center (NPC), Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO), Fundamenteel Onderzoek der Materie (FOM; 12PR3303) and the National Institute of Health (NIH).

The pharmacological activities of a drug can only be understood if its interactions with cellular components and its effects are comprehensively characterized. PhD student Piero Giansanti of the Biomolecular Mass Spectrometry and Proteomics Group at Utrecht University, in collaboration with research teams at the CeMM in Vienna, used mass spectrometry-based chemical proteomics and quantitative phosphoproteomics to characterize the all-inclusive action of tyrosine kinase inhibitors in cancer cells. Their work represents a multiplexed view on the promiscuous action of certain tyrosine kinase inhibitors in the treatment of epidermoid carcinoma. Their approach can contribute towards optimization of new drug molecules and management of side effects, ultimately leading to a more rational approach to skin cancer therapy.

Read the full article:
Evaluating the promiscuous nature of tyrosine kinase inhibitors assessed in epidermoid carcinoma cells by both chemical- and phosphoproteomics.
Giansanti, P., Preisinger, C., Huber, K., Gridling, M., Superti-Furga, G., Bennett, K.L., Heck, A.J.R.
ACS Chem Biol. 2014 May 7.