There’s a lot more to organising events than just the logistics. The marketing team makes sure that you find out about all of our events, you don’t miss any deadlines and that all the feedback you share with us is taken into consideration for improvement — oh yeah, and they also get to organise fun competitions!
Julie is the Marketing Team Lead. She’s great company, always has super helpful tips and a big, big smile on her face. She’s the team’s scientist and the statistics guru. Julie is always willing to lend an ear if you need it and she’ll be sure to cheer you up with some optimistic vibes.
At EMBL since: June 2014
Favourite place in Heidelberg:
“Halle 02 Im Freien” on summer evenings (Thurs – Sat). When the weather is nice, they have DJs and other live shows outside on a little sandy beach. It’s a super relaxing way to spend an evening.
First thing you do before a conference/course starts and first thing you do after a conference/course finishes:
Make sure the camera is charged before the meeting and make sure to save all the pictures afterwards!
If you weren’t a marketing statistics guru what would you be?
Something in science education — perhaps a teacher or even working in a science museum.
What is the strangest/funniest thing that has ever happened at a course/conference?
We had ordered new lanyards for the name badges so that they would not flip around as easily. The first time we used them was for a big conference with hundreds of people in the auditorium. During the first session someone tweeted that it sounded like Christmas time with all the jingling going on in the auditorium!
If you were a superhero what power would you like to have?
Some sort of healing power, or the ability to change body size depending on the situation — sometimes you just need to be a little taller (or shorter!)
Favourite recipe – Shakshuka (free style cooking)
Book – Harry Potter series (Prisoner from Azkaban if I had to choose)
You’ve just found the perfect training to help you in your research or career. You excitedly scroll through the programme looking at all the relevant topics and big names, and already envision the breakthroughs you are going to make after attending the training course or conference. You can even make the application deadline! Just one last thing – how much will it all cost? Can you or your lab even afford that? This is where we come to the rescue!
EMBL offers various types of financial assistance in cooperation with the EMBL Corporate Partnership Programme, EMBO and Boehringer Ingelheim Fonds. We support scientists wishing to attend our events by waiving their registration fee, reimbursing part of their travel and childcare costs or providing onsite childcare. In 2019, a total of 410 fellowships were granted to help train scientists from around the globe. So, prepare your conference abstract or course motivation letter well and your chances to be awarded a fellowship are pretty high.
For a more detailed overview of the types of fellowships EMBL offers, go to our website. And if it so happens that your application to receive a fellowship is unsuccessful, consider approaching your institute, as well as other organisations that can support your attendance. A list of some of these organisations is available here.
Here is what some of the past fellowship awardees have to say about their experience:
“It was an honour to receive a fellowship from such an important scientific organisation. By attending the Organoids symposium, we acquired a snapshot of the current advances in the field and also a flavour of what would be the future technologies. We realised that the next step in terms of methodology for our organoid work was the development of robust imaging and drug screening capabilities. Our Institute is located in Australia, which means the cost of attending conferences in Europe is very high. Receiving financial support to attend a scientific conference is critical, especially for early-mid career researchers with limited funding capabilities.”
“I study activity mediated translation in neurons with focus on the role of RNA binding proteins such as FMRP in regulating translation downstream of glutamate receptors such as mGluR and NMDAR.
While I was at The Complex Life of RNA symposium in 2018, held at EMBL, I was able to present my work as a poster to several researchers. One such researcher from Norway got interested in my work and offered to host me for a short term in his lab to enhance my current project. After several correspondences, I was able to design a project that could also potentially start a collaboration between my home lab in India and his lab in Norway. I applied for the EMBO-STF (Short Term Fellowship) and I was successful in securing this grant for my visit to Norway. So, I believe attending this conference was a great boost for my scientific career.”
“My research focus is on genetics of DNA repair and meiosis. As faculty of a teaching-focused liberal arts college (undergraduate only) I am reliant upon conferences to keep up-to-date with recent discoveries in my field, to develop new collaborations and to gain valuable feedback on my research. I consider these experiences pivotal to my success as a researcher, both for training our next generation of scientists (most of my students I work with go on to get PhDs) and for my ability to secure grant funding. By far the most stimulating conferences I’ve been to as a PI have been EMBL and EMBO-sponsored.”
“My research is focused on understanding the role of exosomes in the progression of glioblastoma. While working on this particular area, I found significant difficulties in getting a pure population of exosomes as it is often contaminated with other biomolecules. As a result, we were in delusion whether the data which we were getting was the effect of exosomes or other biomolecules.
Fortunately, I found this course focusing on the isolation and purification of extracellular vesicles, which was extremely important for my research work. We were trained to use cutting-edge research tools for extracellular vesicles and learned bioinformatic analysis of biomolecules that are present in exosomes. I also got an opportunity to interact with world-leading researchers and discuss my research. ”
“Financial support for scientists within my institute is vital in ensuring we are able to travel overseas to make new connections and learn more about the happenings within our respective fields. New Zealand is geographically isolated, so travel can be expensive which means all financial support is beneficial in helping us to travel beyond Australia and New Zealand and learn more.”
“The Liquid Biopsy course gave me plenty of new insights for different applications of the technique in cancer research. I learned new techniques, discussed my project with top peers and met a lot of highly motivated young professionals. I incorporated the learned applications in my research and this really improved my current project.”
“I study how changes in chromatin during ageing regulate transcription and cell survival in Drosophila photoreceptor neurons. I attended the ATAC-seq course, which helped me get a hold of a new genome-wide technique that we have not used in my lab before, and I got to apply it to my PhD thesis. Also, thanks to the course and meeting one of the course instructors, I will go back to EMBL in April to take part in the scientific visitor programme.”
Bacterial resistance towards all marketed antibiotics poses an imminent threat to global health. In order to overcome this antibiotic crisis, drugs with novel mechanisms-of-action are desperately needed. Covalent inhibitors are especially promising in this regard as they are already prevalent as antibiotics (e.g. β-lactams and fosfomycin), allow targeting protein pockets that are hard to address with non-covalent interactions alone and hold the promise to overcome some mechanisms of resistance development. Furthermore, covalent inhibitors are uniquely suited to identify new binding pockets on proteins using residue-specific proteomics and in this way to broaden the scope of targetable protein targets.
The vast majority of covalent inhibitors so far either hijack the enzymatic activity of the protein by modification of catalytic serines and tyrosines or address cysteines through their inherent outstanding nucleophilicity. Nevertheless, the number of potentially addressable proteins in the bacterial proteome is significantly limited by the requirement for these amino acids to be present in target proteins. By developing electrophilic groups that are selective for other amino acids (e.g. lysine), we strive to expand the number of exploitable interaction sites for covalent inhibitors in the bacterial proteome. Furthermore, to assess the reactivity and selectivity of covalent inhibitors and to streamline the discovery of novel antibiotic targets, we develop new methods for residue-specific activity-based protein profiling.[2,3] In this way, we are convinced, that we will be able to make important contributions to overcome the antibiotic crisis.
 R. A. Bauer, Drug Discov. Today 2015, 20, 1061–1073.
 K. M. Backus et al., Nature 2016, 534, 570.
 P. R. A. Zanon, L. Lewald, S. M. Hacker Angew. Chem. Int. Ed., doi: 10.1002/anie.201912075.
Bioorthogonal reactions, namely reactions that can take place under biocompatible conditions, are having a major impact in the development of new research tools and novel therapeutic strategies. In the latter case, the discovery of the reaction commonly referred to as “click-to-release” (CtR), which triggers the liberation of a given cargo (normally a drug or a fluorophore), has led to several applications in drug delivery. This reaction happens between a 1,2,4,5-Tetrazine (Tz) fragment and certain alkenes or alkynes and, in order to achieve drug delivery specifically at the site of action, one of the two reactant counterparts should be conjugated to a biomolecule acting as a carrier, ideally a protein.
We have synthetized the previously unreported 3-bromo-1,2,4,5-tetrazine and used its excellent reactivity to attain chemoselective protein labelling onto lysines. Due to the chemical features of the formed amino-Tz. The resulting labelled lysines can undergo fast CtR reactions with trans-cyclooctenes, thereby releasing a desired cargo under physiological conditions. To showcase the applicability of this approach, we have labelled the monoclonal antibody Trastuzumab (anti-Her2) and demonstrated the specific release of the cytotoxic drug doxorubicin upon reaction in a mammalian cell culture context, resulting in a decrease in cell viability.
Additionally, we have also used 3-bromo-1,2,4,5-tetrazine to synthetize an amino-Tz containing non-natural amino acid and used it to achieve protein labelling through its genetic incorporation by amber codon suppression in Escherichia coli. The resulting site-selectively labelled proteins can also trigger fast, high yielding CtR reactions.
To summarize, we have successfully applied a new compound, 3-bromo-1,2,4,5-tetrazine, as a reagent to achieve either chemoselective or site selective protein labelling. We have applied the bioconjugated proteins to demonstrate their potential use for targeted drug delivery in a relevant cellular model, opening new therapeutically useful methodologies.
Nuclear receptors (NRs) have been one of the primary drug targets over the last decades for their ability to regulate gene expression. The traditional approach of modulating NRs is to design small synthetic molecules that interact with the ligand-binding domain (LBD) of the NR. Ligands can thereby either enhance or inhibit gene transcription. Apart from the effects on transcription, recent research shows that minor changes in the ligand scaffold can have a significant impact on the behavior of the NR. In this research, we show how small-molecules can change both the dimerization behavior of NRs and the recruitment of allosteric modulators.
The Retinoic X Receptor α (RXRα) is known as a master regulator among NRs through its ability to heterodimerize with, and thereby modulate, other NRs. We show, using a novel NanoBIT complexation assay, that small directed changes in the RXR ligand scaffold can lead to selective formation of specific hetero- and homodimers. Using our structural data and focused compound library, a model was developed to help to understand this effect of the ligand. This information can serve as a blueprint to design small-molecules that selectively target specific NRs via RXR. This makes RXR as an exciting and versatile target for NR modulation, especially when classical modulation of the partner NR is not possible.
Recently, small-molecules have been found to bind to allosteric sites of NRs. Allosteric ligands are of interest since they do not compete with the endogenous ligand of the NR and often shown an increased selectivity towards their target. We show, using X-ray crystallography and biochemical assays, that there is communication between orthosteric and allosteric ligands in the RAR-related orphan receptor γ t (RORγt). We successfully solved eleven new ternary crystal structures of RORγt in the presence of both orthosteric and allosteric ligands. These structures mechanistically show how binding of the orthosteric ligand leads to positive cooperative binding of the allosteric ligand.
Paolo first joined EMBL in 2008 as a PostDoc to study the biogenesis of the Golgi apparatus after removal of this organelle from living cells by laser nanosurgery.
Why did you choose to become a scientist?
During my studies, I was always more interested in literature and philosophy. However, when I had to decide for a university subject, out of curiosity I opted for something different: a new biotechnology course had just been opened and I enrolled. Despite this accidental start, I now think that a scientific career has been a good fit for my critical and curious mind.
Where do you see this field heading in the future?
It is very difficult to foresee where the developments are going to bring us. A few years ago, due to the developments in fluorescence proteins and light microscopy techniques, probably not many people would have bet on a bright future for electron microscopy (EM). Now the field is more active than ever, with 3D EM and correlative light and electron microscopy being key to new discoveries in biology. In the near future, I am convinced that the goal of the EM community should be to advance our methods (from sample prep to image analysis) to a higher throughput, to finally make EM a quantitative tool.
How has training influenced your career?
Working in a facility and being highly involved in training, I experience daily how important courses are to disseminate knowledge and network with a community of experts. Furthermore my personal experience shows how attending a course can change your career, even many years afterwards. At some point during my PhD studies I realised I needed to perform some EM experiments. Therefore, I applied to the course on “Electron microscopy and stereology in cell biology”. It was a great experience, I learned a lot and, when I went back home, I could finally carry out the experiment that was missing for my thesis. In addition to this, I got to know many electron microscopists, including Yannick Schwab, who was a student of the course that year. I do not know whether the good memories of that time played a role in getting me a job when, 10 years later, I applied for a position in the EMCF at EMBL (which Yannick is now heading), but for sure it helped my confidence to start a new job.
What is your number one tip for people looking for scientific training?
Even though nowadays you can find all kind of tutorials online, I believe that attending a course in person is still key because of the networking possibilities that it gives. Getting the best experts to sit with you and think about your questions and problems is incredibly valuable. And when you go back home, you will remain part of a community that is in touch to share experience and tips.
I think this course is really unique in many aspects. First of all, hands-on practicals are not just demos by the experts, but the students also have the possibility to learn using their own samples. In addition, the almost 1:1 ratio between students and trainers gives everybody the chance to be trained individually at the level they need. It is not by chance that many leading electron microscopists of today have attended this course in the past.
Interested in this course? Apply by 24 March 2020.
In 2019 EMBL-EBI celebrated their 25th anniversary. To commemorate this milestone, a series of videos – In Focus – were filmed, including one with our very own Cath Brooksbank, Head of Training at EMBL-EBI.
In the video, Cath discusses the role of technology in bioinformatics training from past to present and through to the future.
Traditionally bioinformatics training has been face-to-face, but EMBL-EBI also have a large online training offering through our Train Online programme. Train Online can be remotely accessed around the globe, at anytime, allowing our training to reach a much larger global audience at a time that suits the user.
At EMBL-EBI we also want to breakdown the isolation faced by solo bioinformaticians in institutes, and bring them together with peers through our training offering – whether in person or online via collaborative tools such as Google Docs.
And of course there will be times where face to face will not be possible. Whether due to ill health, parental leave or visa issues we understand that sometimes people cannot physically reach our on-site training courses. For those times, we have our robot avatar to enable remote access to our events. Read more about our robot.