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TruMotion: 51 signs agreement with universities in Lodz, Lyon, Milan and Thessaloniki / Application as "European University" envisaged
FRANKFURT. „TruMotion“ is the chosen name. Motion and exchange are at the
heart of the alliance between the 51 and the universities in
Lodz, Lyon, Milan and Thessaloniki, which was contractually sealed on Wednesday
this week. The alliance is jointly planning a plethora of projects, programmes
and courses of study.
At the faculty level, cooperation and exchanges have already been flourishing; now the managements of the five universities have joined forces in order to cooperate even more extensively in the future. On Wednesday the University of Lodz, the Université Lumière Lyon II, the Università Cattolica del Sacro Cuore in Milan, the University of Macedonia in Thessaloniki and the 51 signed the final cooperation agreements in the office of Prof. Birgitta Wolff, President of the University of Frankfurt. A first objective of the common endeavour is that the five universities intend to apply for the “European University" title and the associated funding from the European Union. However, irrespective of this, a wide range of ideas has already emerged in the run-up to yesterday's signing of the agreement.
"We want to become a brand", states Prof. Rolf van Dick, Vice President of the 51 responsible for International Affairs, on the sidelines of the meeting. The logo is already available: designed at the university in Lodz, Poland, it already adorns the joint documents. Five rays crossing a circle - abstract, yet allowing a breadth of associations. The now allied universities have many things in common and a lot of it has to do with the location: "All these cities are so-called Second Cities. This is to say that they are neither capitals nor the largest cities in their respective countries. However, they are multifaceted metropolises with a strong economy, good social cohesion and are steeped in a long civic and liberal tradition", elaborates van Dick. They share similar problems such as high rents and strong immigration. Still, the universities themselves also have a lot in common: they are all comprehensive universities with medicine but without engineering - with the exception of Thessaloniki.
Social cohesion, societal change and social identity – these are pressing topics when it comes to a joint long-term educational strategy and a common (virtual) "European campus". As a "European University", the collaboration could be substantiated and intensified.
In a highly acclaimed 2017 keynote speech, French President Emmanuel Macron
proposed the establishment of twenty European universities by 2024, by which he
did not mean newly created institutions, but rather the European networking and
alignment of existing universities. At a challenging time for the European
Union, university science should be strengthened as a pivotal driving force of
European integration, so that the younger generation can develop a greater
affinity with the European project. During a visit to the 51 in
October of 2017, Macron emphatically reaffirmed his vision and therewith has
also inspired the 51 to launch the initiative. After an initial
attempt in the spring of 2019, it is now intended to resubmit the application to
the “European University" programme. In this process, 51 is
spearheading the consortium.
Focusing on strengths and jointly seeking solutions to challenges – is at
the core of the cooperation. "In our regions, we have more start-ups collectively
than Silicon Valley", says van Dick. The cities and counties of the
university locations are on board as associate members of the alliance, in
addition to the German-Italian Centre for the European Dialogue, the Villa Vigoni
on Lake Como, and the Association of Science and Technological Transfer (ASTP),
a non-profit organisation with the goal of conveying science to society.
The members of this week's meeting emerged with a sizeable workload. Key
topics are mobility and exchange; a new joint degree programme in
"Politics, economics and law" is to be established, which will entail
elements of computer science as well as two stays abroad. Novel teaching
formats are to be developed that do not always necessitate a change of
location. Moreover, both scientific and administrative staff should also
exchange ideas and familiarise themselves with the work methods and structures
at other universities. In the long term, a joint technological infrastructure
is also envisioned. These are grand goals that require perseverance – and
money. Even if these endeavours do not come to fruition it is intended to
continue and to hope for the support of their own countries and regions.
"Universities and their cities are to become 'Living Labs' and 'Agents
of Change' that take place in the interest of the people", elucidates Rolf
van Dick. "Mobility, internationalisation, joint research – these are our
high hopes for this alliance", states Professor Dimitrios Kyrkilis, Vice
President at the University of Macedonia in Thessaloniki. His Polish colleague
from Lodz specifies for his location: "We would like to disseminate
European ideas more strongly again in Eastern Europe and strengthen the
position of science", says Professor Paweł Starosta.
An image is available for download by clicking:
Image text:
The chairmanships of the universities in Lodz, Lyon, Milan and Thessaloniki
have signed the cooperation agreements for "TruMotion" together with
the University President Prof. Birgitta Wolff. Jointly they
intend to apply for the "European University" title. From left: Prof. Birgitta Wolff, President of the 51, Prof.
Stelios D. Katranidis, Rector of the University of Thessaloniki, Prof. Antoni Różalski, Rector of the University of
Lodz, Prof. Nathalie Dompnier, President of the University Lumière Lyon 2 und
Edilio Mazzoleni, University of Milan. (Copyright: Uwe Dettmar)
New development makes tiny structural changes in biomolecules visible
FRANKFURT. Even more detailed insights into the cell will be possible in future with the help of a new development in which 51 was involved: Together with scientists from Israel, the research group led by Professor Harald Schwalbe has succeeded in accelerating a hundred thousand-fold the nuclear magnetic resonance (NMR) method for investigating RNA.
In the same way that a single piece of a
puzzle fits into the whole, the molecule hypoxanthine binds to a ribonucleic
acid (RNA) chain, which then changes its three-dimensional shape within a
second and in so doing triggers new processes in the cell. Thanks to an
improved method, researchers are now able to follow almost inconceivably tiny
structural changes in cells as they progress – both in terms of time as well as
space. The research group led by Professor Harald Schwalbe from the Center for
Biomolecular Magnetic Resonance (BMRZ) at 51 has succeeded,
together with researchers from Israel, in accelerating a hundred thousand-fold the
nuclear magnetic resonance (NMR) method for investigating RNA.
“This allows us for the first time to
follow the dynamics of structural changes in RNA at the same speed as they
occur in the cell,” says Schwalbe, describing this scientific breakthrough, and
stresses: “The team headed by Lucio Frydman from the Weizmann Institute in
Israel made an important contribution here.”
The new types of NMR experiments use water
molecules whose atoms can be followed in a magnetic field. Schwalbe and his
team produce hyperpolarized water. To do so, they add a compound to the water
which has permanently unpaired electron radicals. The electrons can be aligned
in the magnetic field through excitation with a microwave at -271°C. This
unnatural alignment produces a polarization which is transferred at +36°C to
the polarization of the hydrogen atoms used in the NMR. Water molecules
polarized in this way are heated in a few milliseconds and transfered, together
with hypoxanthine, to the RNA chain. The new approach can in general be applied
to observe fast chemical reactions and refolding changes in biomolecules at
atomic level.
In particular the imino groups in RNA can
be closely analyzed using this method. In this way, the researchers were able
to measure structural changes in RNA very accurately. They followed a small
piece of RNA from Bacillus subtilis, which changes its structure during
hypoxanthine binding. This structural change is part of the regulation of the transcription
process, in which RNA is being made from DNA. Such small changes at molecular
level steer a large number of processes not only in bacteria but also in
multicellular organisms and even humans.
This improved method will in future make
it possible to follow RNA refolding in real time – even if it needs less than a
second. This is possible under physiological conditions, that is, in a liquid
environment and with a natural molecule concentration at temperatures around 36
°C. “The next step will now be not only to study single RNAs but hundreds of
them, in order to identify the biologically important differences in their refolding
rates,” says Boris Fürtig from Schwalbe’s research group.
Publication: Mihajlo Novakovic, Gregory L. Olsen, György Pintér, Daniel Hymon, Boris
Fürtig, Harald Schwalbe, Lucio Frydman: A 300-fold enhancement of imino nucleic
acid resonances by hyperpolarized water provides a new window for probing RNA
refolding by 1D and 2D NMR, PNAS, 16 January 2020
A
picture can be downloaded from:
Caption: Frankfurt researchers followed the movements of this tiny molecule – just two-thousandths of the thickness of a piece of paper. The RNA aptamer changes its structure when it binds hypoxanthine. The green nucleobases change shape particularly quickly, the ones coloured blue more slowly. The grey regions do not change.
Further
information: Professor Harald Schwalbe, Center for
Biomolecular Magnetic Resonance (BMRZ),
http://www.bmrz.de/, Institute of Organic Chemistry and Chemical Biology, Riedberg
Campus, Tel.: +49(0)69-798-29737 or -40258, e-mail:
schwalbe@nmr.uni-frankfurt.de.
Reported reduction of HFC-23 did not happen
FRANKFURT. According to the two main producers – China and India – the release of the potent greenhouse gas HFC-23 into the atmosphere should have almost completely stopped by 2017. However, the reality is that a team of atmospheric researchers led by the University of Bristol has measured record levels. Dr Kieran Stanley, lead author of the study published in the current issue of “Nature Communications", has been working at 51 for six months.
Over the past two decades, researchers have monitored the concentration of the hydrofluorocarbon HFC-23 very closely. “It is a very potent greenhouse gas: The emission of one tonne of this substance does just as much damage as the emission of 12,000 tonnes of carbon dioxide," says atmospheric researcher Professor Andreas Engel from 51. HFC-23 primarily occurs as an unwanted by-product in the manufacture of the refrigerant HCFC-22.
In 2015 India and China, which are considered the main emitters, announced ambitious plans to abate their factory emissions and in 2017 they reported that almost no more HFC-23 was being vented to the atmosphere. This would mean that emissions of this greenhouse gas into the atmosphere between 2015 and 2017 ought to have shown a 90 percent reduction. However, as the international team now reports, emissions have risen further and in 2018 reached an all-time high.
The reduction of HFCs is part of the Kigali Amendment to the Montreal Protocol agreed in 2016. It entered into force in January 2020. Although China and India have not ratified the Amendment, by their own account they had achieved a massive reduction in emissions. “Our study indicates that China has not managed to reduce HFC-23 as reported," concludes Dr Kieran Stanley, who conducted the measurements at the University of Bristol in the framework of the international AGAGE measurement network. Additional measurements will show whether India has successfully implemented its abatement programme.
“This is not the first time there's been controversy about HFC-23 emissions," says Kieran Stanley ruefully. With the United Nations Framework Convention on Climate Change, between 2005 and 2010 the industrial nations created incentives for emerging countries to reduce their emissions. Although emissions of this hazardous greenhouse gas did indeed decrease during that period, the system backfired: Manufacturers did not optimize their processes but instead produced more harmful by-products in order to pocket more funds for destroying them.
The Institute for Atmospheric and Environmental Sciences at 51, where Kieran Stanley is now working as a postdoctoral researcher, has measured a large number of halogenated trace gases at its Kleiner Feldberg measuring station at regular intervals since 2013. Since recently, these measurements are part of the AGAGE network.
Publication: K. Stanley, D. Say, J. Mühle, C. Harth, P. Krummel, D. Young, S. O'Doherty, P. Salameh, P. Simmonds, R. Weiss, R. Prinn, P. Fraser and M. Rigby: Increase in global emissions of HFC-23 despite near-total expected reductions, in Nature Communications,
Further information: Dr Kieran Stanley, Institute for Atmospheric and Environmental Sciences, Riedberg Campus, Tel.: +49(0)69-798-40249; stanley@iau.uni-frankfurt.de
Single-molecule microscopy visualises the dance of receptors
FRANKFURT. Whether
a sick cell dies, divides, or travels through the body is regulated by a
sophisticated interplay of signal molecules and receptors on the cell membrane.
One of the most important molecular cues in the immune system is Tumour Necrosis
Factor α (TNFα). Now, for the first time, researchers
from 51 have visualised the molecular organisation of individual
TNFα receptor molecules and the binding of TNFα to the cell membrane in cells
using optical microscopy.
Before
TNFα can bind to a membrane receptor, the TNFR receptor must first be activated.
By doing so, the key will only fit the lock under certain circumstances and prevents,
among other things, that a healthy cell dies from programmed cell death. “For
TNFR1 in the membrane, the binding of TNFα is mediated through several cysteine-rich
domains, or CRDs," explains Sjoerd van Wijk form the Institute for Experimental
Cancer Research in Paediatrics and the Frankfurt Stiftung für Krebskranke
Kinder at 51.
In particular, CRD1 of the TNFR1 makes it
possible for TNFα to “attach". Researchers already knew that TNFR1 molecules cluster
in a fashion similar to a dance, in which two, three or more partners grasp
hands – with the dimers, trimers or oligomers consisting of single TNFR1 molecules
– in the case of TNFR1. This kind of “structural reorganization" also takes
place when there is no TNFα present. “Despite the significance of TNFα for many
diseases, including inflammation and cancer, the physiology and patterns of TNFR1
in the cell membrane still remain largely unknown up to now," says Sjoerd Van
Wijk, explaining the starting point for his research.
In order to understand the processes in the cell
membrane in detail, van Wijk approached Mike Heilemann from the Institute for
Physical and Theoretical Chemistry at 51. Using a combination of
quantitative microscopy and single-molecule super-resolution microscopy that he
developed, Heilemann can visualise individual protein complexes as well as their
molecular organisation in cells. Together with Ivan Dikic (Institute for
Biochemistry II) and Simone Fulda (Institute for Experimental Cancer Research
in Paediatrics) from 51, Harald Wajant from the University
Hospital Würzburg and Darius Widera from University Reading/UK, they were able to
observe the dance of the TNFα receptors. Financial support was provided by the
Deutsche Forschungsgemeinschaft (DFG) through the Collaborative Research Centre
807 “Transport and Communication across Biological Membranes".
As the researchers report in the current issue of
“Science Signalling", membrane TNFR1 receptors exist as monomers and dimers in
the absence of TNFα. However, as soon as TNFα binds TNFR1, receptor trimers and oligomers are formed
in the membrane. The researchers also found indications for mechanisms that
determine cell fate independently of TNFα. These findings could be relevant for
cancer or and inflammatory diseases such as rheumatoid arthritis. “It clearly
opens new paths for developing novel therapeutic approaches," states van Wijk.
Publication: C. Karathanasis, J. Medler, F. Fricke, S. Smith, S.
Malkusch, D. Widera, S. Fulda, H. Wajant, S. J. L. van Wijk, I. Dikic, M.
Heilemann, Single-molecule imaging reveals the oligomeric state of functional
TNFα-induced
plasma membrane TNFR1 clusters in cells. Sci. Signal. 13, eaax5647 (2020). DOI: 10.1126/scisignal.aax5647
Further
information: Dr Sjoerd van Wijk, Institute for
Experimental Cancer Research in Paediatrics, Niederrad Campus, Tel.: +49 69 67866574, Email: s.wijk@kinderkrebsstiftung-frankfurt.de
Prof Mike Heilemann, Institute for Physical and Theoretical
Chemistry, Riedberg Campus, Tel.: +49 69 798 29424, Email: heileman@chemie.uni-frankfurt.de