Study focused on cancer-associated fibroblasts by researchers from Germany and USA exposes new tumor targets. [more]

Researchers from Germany and Denmark uncovered a set of proteins that are enriched in pre-symptomatic non-alcoholic fatty liver disease. [more]

Chronic excessive caloric intake leads to the deposition of fat droplets in the liver. This condition, known as fatty liver, can cause permanent damage to the organ. Researchers at the Max Planck Institute of Biochemistry (MPIB) in Martinsried have now investigated the effects of this fat overflow on liver proteins. They showed that fatty liver is associated with changes in the location and activity of numerous cellular proteins. The study, which was published in the journal Developmental Cell, shows the effect of lipid deposition on fundamental cellular processes in the liver. [more]

The diagnosis of ovarian cancer is still comparable to a death sentence. Only one in six patients survives more than 10 years after diagnosis. In a new study, an international research team from Germany, the USA, and Denmark, identified a molecular mechanism that is linked to patient long-term survival for those roughly 20% of the patients. By proteomic analysis, the protein CT45 was identified as a novel prognostic cancer cell marker. The authors further showed that the protein itself increases cancer cell death after platinum chemotherapy and activates the patient’s immune system. This work will be published in the renowned scientific journal Cell. [more]

Opioids are powerful painkillers that act on the brain, but they have a range of harmful side effects including addiction. Researchers have developed a tool that gives deeper insights into the brain’s response to opioids. Using mass spectrometry, they determined changes of proteins’ phosphorylation patterns – the molecular switches of the proteins – in five different regions of the brain and assigned them to the desired and the undesired effects of opioid treatment. Their results, which are published in the journal Science, will lead the way for the identification of novel drug targets and the design of a new class of painkillers with fewer side effects. The study was performed by researchers at the Max Planck Institute of Biochemistry (MPIB) in collaboration with researchers from the Medical University of Innsbruck, Austria, University of Innsbruck, and Temple University, USA. [more]

Atlas of the Heart - A healthy heart beats about two billion times during a lifetime – thanks to the interplay of more than 10,000 proteins. Researcher from the Max Planck Institute of Biochemistry (MPIB) and the German Heart Centre at the Technical University of Munich (TUM) have now determined which and how many individual proteins are present in each type of cell that occurs in the heart. In doing so, they compiled the first atlas of the healthy human heart, known as the cardiac proteome. The atlas will make it easier to identify differences between healthy and diseased hearts in future.   [more]

Circadian is the latin meaning for “about a day”. Circadian clocks have evolved to adapt our lives to the daily environmental changes on earth: light and warmth during the day and darkness and cold at night. Scientists at the Max-Planck-Institute of Biochemistry in Martinsried discovered with the help of the mass spectrometry, that more than 25 percent of the molecular protein switches in mouse liver cells change in a daily manner. These rhythmic switches are binding sites for phosphate molecules, that regulate the function of proteins, and thereby the daily metabolic processes in the organ. The study was published in the journal Cell Metabolism. [more]

Immunotherapy for cancer: identifying suitable target antigens by mass spectrometry. The immune system can fight specifically against cancer by tumor-specific T cells although suitable altered target structures are currently mostly unknown. A team at the the Max Planck Institute of Biochemistry and Technical University of Munich (TUM) has developed a method that allows for the first time the reliable identification of suitable antigens directly from patients` tumor cells by mass spectrometry. These structures proved to be immunogenic. This procedure therefore opens up new possibilities for individualized targeted cancer treatments. [more]

International Consortium Identifies and Validates Cellular Role of Priority Parkinson’s Disease Drug Target, LRRK2 Kinase
An international public-private consortium of researchers led by The Michael J. Fox Foundation for Parkinson’s Research has had its work published in eLife. A team comprising investigators from the Max Planck Institute of Biochemistry, the University of Dundee, GlaxoSmithKline and MSD, known as Merck & Co., Inc., in the United States and Canada, has discovered that the LRRK2 kinase regulates cellular trafficking by deactivating Rab proteins. This finding illuminates a novel route for therapeutic development and may accelerate testing of LRRK2 inhibitors as a disease-modifying therapy for Parkinson’s, the second most common neurodegenerative disease. [more]

Novel proteomic technologies that are so robust and powerful that they can be used in every biological laboratory and in every clinic are expected as results of the currently starting research consortium MSmed. The European Commission is co-funding the project with 3.7 Million Euros for four years starting Dec. 1, 2015 within the research line “Future and Emerging Technologies” under the Horizon 2020 Programme. MSmed will automate workflows in mass spectrometric analysis for proteomics research to prepare them for high-throughput clinical application. [more]

Just as in the Middle Ages when there were still many uncharted areas on Earth, researchers today are aware that there is still a great deal to learn about cells in our microcosm. But instead of sextants and compasses, researchers nowadays use modern methods such as mass spectrometry to look into the world of protein molecules. Neuroscientists are focussed particularly on resolving brain complexity with its billions of specialized cells. To understand the brain’s functions, scientists from the Max Planck Institutes of Biochemistry in Martinsried and Experimental Medicine in Göttingen have for the first time quantified the entire set of proteins ‒ the proteome ‒ in the adult mouse brain. The information about which proteins and how many of them are found in the various cell types and regions has been summarized in a protein atlas. The results of these studies have now been published in the journal Nature Neuroscience. [more]

Complex life is only possible because proteins bind to each other, forming higher-order structures and signal pathways. Scientists at the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich and at the MPI of Molecular Cell Biology and Genetics in Dresden have now drawn a detailed map of human protein interactions. Using a novel mass spectrometric quantification method, the researchers determined the strength of each interaction. “Our data revealed that most interactions are weak, but critical for the structure of the entire network,” explains Marco Hein, first author of the study. The paper has now been published in the Journal Cell. [more]

Each cell in the body comprises approximately 12,000 proteins, which act like small machines to carry out various cellular processes. Researcher of the Max-Planck-Institute (MPI) in Martinsried near Munich, Germany, developed the method ‘EasyPhos’ to identify the activity of these proteins on a global scale. Using this technology, they revealed that the binding of the hormone insulin to the cell surface affects more than 1,000 proteins. These methods, which rely on mass spectrometry, enable the identification of the regulation of each of these proteins, and simplifies the simultaneous analysis of many samples in parallel. Therefore, EasyPhos is a breakthrough in deciphering the complex processes of healthy and diseased cells. The results were published today in the prestigious research journal Nature Biotechnology. [more]

Our lungs are permanently exposed to harmful environmental factors that can damage or even destroy their cells. In a specific regenerative process these injured cells must be replaced as soon as possible. In collaboration with colleagues from the Helmholtz Zentrum München, scientists at the Max Planck Institute (MPI) of Biochemistry have now, for the first time, gained detailed insights into the dynamic remodeling of the tissue during lung repair. The results have just been published in EMBO Molecular Systems Biology. [more]

Various repair mechanisms help our cells to revert continuous damage to their DNA. If they fail, mutations accumulate in the genome that can lead to devastating diseases. DNA repair defects underlie predisposition to certain cancers, such as familial breast cancer, and promote the transformation process in other spontaneous cancers. DNA repair requires many factors, but so far there have not been comprehensive analyses of the intricate pathways involved. Using novel and highly sensitive proteomic technologies, scientists of the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich now report in the journal Science the first global analysis of the protein recruitment dynamics underlying a critical DNA repair pathway. Their results shed light on the repair mechanism and identified new proteins and drug targets that could be important in maintaining genomic stability and preventing cancer. [more]

When pathogens such as bacteria or viruses invade the human body, different immune cells must work together and coordinate their defense strategies with each other. Using newly developed proteomics technologies, scientists of the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich, Germany, have now comprehensively detected the messenger proteins secreted by immune cells during such an immune response. “Our method enables an analysis of the information exchange between cells and provides a powerful tool to understand the language of our immune system in the context of disease,” said Felix Meissner, scientist at the MPI of Biochemistry. The results of the study, which was carried out in collaboration with colleagues from the MPI for Infection Biology in Berlin, have now been published in Science. [more]

Neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's disease and amyotrophic lateral sclerosis (ALS) are characterized by toxic protein aggregates in certain regions of the brain and nerve cells. The objective of the project of F.-Ulrich Hartl, Wolfgang Baumeister, Rüdiger Klein and Matthias Mann is to elucidate just how this aggregation process is linked to cytotoxicity and cell death. For their project, the four directors of the Max Planck Institutes of Biochemistry and of Neurobiology in Martinsried near Munich, Germany, have now been awarded a Synergy Grant of the European Research Council (ERC). The four professors will use the 13.9 million euros in funding to establish closely collaborating research groups throughout the project lifetime of six years. The ERC Synergy Grant is the most highly endowed research grant of the European Union and was awarded this year for the first time [more]

The genome encodes the complete information needed by an organism, including that required for protein production. Viruses, which are up to a thousand times smaller than human cells, have considerably smaller genomes. Using a type of herpesvirus as a model system, the scientists of the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich and their collaboration partners at the University of California in San Francisco have shown that the genome of this virus contains much more information than previously assumed. The researchers identified several hundred novel proteins, many of which were surprisingly small. The results of the study have now been published in Science.

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Every second, thousands of proteins fulfil essential tasks as molecular building blocks or molecular machines in the cells of our bodies. Matthias Mann, director at the Max Planck Institute of Biochemistry (MPIB) in Martinsried, is to receive the Körber European Science Prize 2012 for his ground-breaking work on the proteome, the entirety of all proteins of a living organism. This research award comes with prize money of 750,000 Euros and will be presented on September 7, 2012, in Hamburg, Germany.
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‘Proteomics’ is the large-scale study of proteins, particularly their structures and functions. Proteomics holds the potential to answer questions that genomics left unsolved. The large EU project PROSPECTS is a collaborative research effort of leading European scientists in the Proteomics field. PROSPECTS now presents a number of breakthroughs in a series of articles comprising a "Special Issue" of the top journal of the field: Molecular & Cellular Proteomics. Coordinated by Matthias Mann, director at the Max Planck Institute of Biochemistry (MPIB) in Martinsried, the scientists lay out their contribution to the future of proteomics with a powerful and versatile set of assay systems for characterizing proteome dynamics, a new ‘third generation’ proteomics strategy that offers an indispensible tool for cell biology and molecular medicine. [more]

Every cell has a vast number of proteins at its command which are involved in practically all biological processes. Every protein undertakes specified tasks and they all need to work together harmoniously. Matthias Mann, director at the Max Planck Institute of Biochemistry in Martinsried near Munich, Germany, is to receive the Louis-Jeantet Prize for Medicine 2012 for his work on the development of mass spectrometric procedures for protein analysis. The award comes with 700,000 CHF prize money (about 540,000 Euros) and will be presented on April 19, 2012 in Geneva, Switzerland. [more]

Proteins are the molecular building blocks and machinery of cells, and are involved in practically all biological processes. Matthias Mann, Director at the Max Planck Institute of Biochemistry (MPIB) in Martinsried, is to receive the Ernst Schering Prize 2012 for his seminal work exploring the proteome – the entirety of proteins of an organism. The award comes with 50,000 Euros prize money and will be presented on September 10, 2012 in Berlin. Matthias Mann has revolutionized the methods that are used for the identification and characterization of proteins, by successfully transferring methods of the physical sciences – such as mass spectrometry – to the area of molecular biology. [more]

Proteins are the molecular building blocks and machinery of cells, and are involved in practically all biological processes. Matthias Mann, Director at the Max Planck Institute of Biochemistry (MPIB) in Martinsried, is to receive the Gottfried Wilhelm Leibniz Prize 2012 for his work on the development of mass spectrometry procedures for protein analysis. The award comes with a purse of €2.5 million and will be presented on 27 February 2012 in Berlin. [more]

Proteins are the cell’s molecular building material and machineries, and they are involved in nearly every biological process. For his development of techniques to analyze proteins with the aid of mass spectrometry, Matthias Mann, director at the Max Planck Institute of Biochemistry, will be awarded the Friedrich Wilhelm Joseph von Schelling Prize of the Bavarian Academy of Sciences and Humanities 2010. [more]

Various processes in our body are controlled by subsequent changes of proteins. Therefore, the identification of such modifications is essential for the further exploration of our organism. Now, scientists of the Max Planck Institute of Biochemistry in Martinsried, Germany, have made a crucial contribution to this: Using a new method, they have been able to identify more than 6,000 glycosylated protein sites in different tissues and have thus established an important basis for the better understanding of all life processes (Cell, May 28, 2010). [more]

Scientists develop new method to identify glycosylated proteins [more]

In order to defend ourselves from viruses, germs and parasites, the immune cells of our body are equipped with different defense systems. For the first time, scientists of the Max Planck Institute (MPI) of Biochemistry and the biotech company Bavarian Nordic GmbH in Martinsried near Munich, Germany, have now investigated the proteins of a highly specialized family of immune cells. “To our surprise, we discovered that not all the members of the dendritic cell family are able to detect pathogens such as viruses”, explains Christian A. Luber, scientist at the MPI of Biochemistry. “We could predict this behavior only on the basis of their protein equipment.” The work has now been published in Immunity. [more]

Until now, extracting as many proteins as possible from biological samples has required a combination of several methods. Scientists at the Max Planck Institute of Biochemistry have now developed a new universally employable sample preparation method that combines the advantages of the usual methods and allows an unprecedented depth of proteome coverage. [more]

Several bacterial pathogens use toxins to manipulate human host cells, ultimately disturbing cellular signal transduction. Until now, however, scientists have been able to track down only a few of the proteins that interact with bacterial toxins in infected human cells. Now, researchers of the Max Planck Institute of Biochemistry in Martinsried and the Max Delbrück Center for Molecular Medicine (MDC) Berlin-Buch in Germany have identified 39 interaction partners of these toxins, using novel technology which allowed them to screen for large numbers of proteins simultaneously (Cell Host & Microbe, Vol. 5, Issue 4, 397-403)*. [more]

The multi-tasking talent MaxQuant accomplishes over night what used to take up to half a year to complete: With this software, scientists at the Max Planck Institute of Biochemistry have developed a tool that can identify proteins faster and more accurately than any other technology. [more]

Cell signaling mechanisms often transmit information via protein modifications, most importantly the reversible attachment of phosphate, the so-called protein phosphorylation. Researchers at the Max Planck Institute of Biochemistry in Martinsried have now developed a technology to identify and quantify the specific sites in proteins that get phosphorylated in answer to certain stimuli in living cells. Under the lead of Matthias Mann, the scientists found 6,600 phosphorylation sites - 90 percent of which were unknown - in 2,244 proteins and observed their temporal dynamics. All these phosphorylation sites are now listed in the newly created Phosida database to make them available for efficient use by scientists working in different areas, among them tumour researchers: Defects in cellular signaling often occur in many types of cancer. (Cell, November 2, 2006) [more]