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One of the longest serving members of the EMBL Course and Conference team, Nicola is an an event marketer who is always looking for ways to help up-and-coming scientists get ahead in the field...and she has a tendency to break into song.
It’s safe to say that 2020 has been – and continues to be – a strange year! We have all been forced to adapt the way we live and think, and at EMBL it is no different.
Traditionally we would now be presenting a sneak peek of our 2021 training programme. However, since we have had to make a range of changes to adapt our programme to the current circumstances, we are doing things a bit differently this year! Our new poster includes the updated 2020 events (virtual of course!), as well as the planned training courses and conferences for the first half of 2021.
We hope to welcome people onsite in 2021, but have back-up plans in place should this not be possible! Our EMBO | EMBL Symposia series continues, and we continue to offer a range of EMBL Conferences, EMBO Workshops, and Courses – both established and new. Ever wondered what all these different event types are? Here’s an explanation!
Our online training offerings are more popular than ever, so you also have the option to learn at your own pace with our train online and webinars to make sure you stay up-to-date with the latest scientific techniques!
The complete 2021 EMBL Course and Conference Programme will be published in November – if all goes to plan!
Virtual meetings are rapidly gaining popularity, due largely to the necessity of continuing knowledge exchange during the social isolation brought on by the Corona pandemic.
Even before the pandemic, EMBL´s Course and Conference Office was already exploring options to improve our services and the event experience on-site, including the option of digital poster presentations.
Our software provider iPosterSessions comes with easy to use WYSIWYG templates. Users can display high-resolution images, videos & animations, and the content can be updated at any time right throughout the conference – allowing poster presenters to present their research digitally and dynamically.
If you are presenting a digital poster at an upcoming (virtual!) meeting, here are eight tips to help you on your way:
Download the official template from the software provider
Most digital software providers have an official template that you can download – use it! This will reduce the risk of glitches, resolution problems and sizing issues in the final product, and you know from the outset what you have to work with.
Check out the tutorials
No two digital poster tools are the same, so take the time to browse through the online tips and tutorials to make sure you are comfortable with the software before starting. It will save you a lot of frustration in the long run!
Make your design eye-catching – it should stand out from the crowd
This is the same principle as creating a printed scientific poster – there are so many of them, so make sure yours stands out! It should be eye-catching and visually appealing. Include clear data representations, and make sure the text is to the point. It should grab attention but not explain every little thing about your results – that’s your job during the discussion.
Use media – images, sounds, video. Check that they work and display properly
Graphics and media can express details more quickly and memorably than paragraphs of text, so have a think about how you can present your work in this way and put some time into it. Be sure to check that the media files work with the software, and test every file to make sure they display or play properly.
Link to external resources
Digital posters differ from printed posters in that you can generally link to other pages online – so if there is a great external paper or online source you want to link to in order to explain your point in more detail, do it! Your audience will be grateful to have further reading handed to them on a plate if they want to find out more after the poster session.
Check your work
This should really be a no-brainer. Check your work is complete, correct and final before publishing your poster! Silly mistakes only show that you haven’t put as much time and effort into the work as you probably should have, so get someone else to go over your poster before you release it to the conference community.
Practice your presentation
Yes, it’s a digital poster presentation, and no, you won’t be talking face-to-face with your audience as you normally would, but you still need to practice your presentation beforehand and know exactly what you want to say and how you want to say it. It may feel strange online, so try presenting the poster online with a colleague or your boss (e.g. with Skype, Zoom, Google Hangouts) and get them to give you feedback and pointers.
Stick to the publishing deadline
There are deadlines for a reason, so please stick to them! You don’t want to risk your poster being excluded from the poster presentation because of tardiness. Give yourself plenty of time in case of any issues that may arise with uploading or compatibility (this shouldn’t be an issue if you followed the template and guidelines, but sometimes computers have a mind of their own!).
By guest bloggers and EMBL AV experts Christopher Höhmann and Jan Abda
Virtual events are on the rise, largely due to the necessity to adapt to the physical distancing enforcements and travel restrictions brought on by the COVID-19 pandemic.
EMBL is continuing to offer advanced training for the scientific community as safely as we can, with many events pivoting to virtual. With speakers spread all over the world with different internet connection speeds, technical support and varying levels of experience with virtual presenting, the EMBL Audiovisual team have put together a guide on how to make sure your presentation is smooth and you come across as professionally as possible for your digital lecture.
Choose your location wisely
Make sure you choose a location without a window in the background, as this will result in a high contrast, causing you to appear dark and hard to see. Make sure the background isn’t too busy, or has anything that might draw the attention away from your talk.
Pick a quiet room
When selecting the location for your presentation, make sure there is no loud background noise and that you won’t be disturbed. Who can forget Prof. Robert Kelly’s live BBC broadcast starring his adorable children as unexpected guests!
Use a headset
Ideally, use a headset in order to ensure the best possible sound. It may feel a bit strange at first, but your audience will thank you for it!
Check out a review of some of the best options here.
Use a wired connection if possible
If you have the option, connect your device directly rather than relying on a wireless internet connection. This will help avoid any possibly wireless instability or network breaks.
Avoid using the web browser
There are many different streaming software options out there. If there is a video conferencing app available for the event you are presenting at, for best results download this in advance to use for the live stream rather than relying on the less reliable web browser version.
Close other programmes
In order to save bandwidth and processing power, close all unnecessary applications on your device before your presentation starts. This will result in a smoother streaming of your talk.
Share your entire screen – carefully!
It always comes across better if you share your entire screen rather than just your keynote or PowerPoint presentation. Just be sure to keep in mind that as soon as you share your screen, everything that you can see can be seen by your audience, so be aware of what you have visible!
Troubleshooting on Macs
If you have a Mac (running Mac OS Catalina 10.15), you may have some initial problems with sharing your screen. If this is the case, try the following:
Go to System Preference → choose Security & Privacy → select the relevant app under Screen Recording and tick the box.
The (VC) app will have to be restarted in order for the changes to take effect.
Unshare before question time
When you have finished your presentation, end your screen sharing before the Q&A session starts. Your audience wants to see YOU when they are asking questions about your presentation, not the final slide of your talk.
Make it readable
Remember, people will be watching your presentation on different devices with different-sized screens. Make sure your digital presentation is clear and that the font is readable – if you can’t read it easily, neither can your audience.
Test, test, test!
At EMBL, our AV team will test the setup and conditions with you before the live event. Make sure that you carry out the test with exactly the same set-up as you plan to use on the day to eliminate the risk of any nasty surprises.
So now there’s nothing stopping you from giving a smooth and polished presentation at your next virtual conference. Take the time to get familiar with your streaming applications, practice and test the software in advance, and you shouldn’t have anything to worry about!
Jan Abda and Christopher Hoehmann are dedicated Audiovisual Technicians in the EMBL Photolab, and are responsible for ensuring the technical aspects of our onsite and virtual conferences and courses run as smoothly as possible. We would be lost without them!
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.
In 2020 the EMBL Resource Development team and industry partners of the EMBL Corporate Partnership Programme will bring together academic and industrial scientists with interests in chemical biology, chemogenomic libraries, pharmacology, medicinal chemistry and bioinformatics for the EMBL Conference: Expanding the Druggable Proteome with Chemical Biology (5-7 February 2020).
We spoke to co-organiser Gerard Drewes from GSK Cellzome about how chemical biology is helping to expand the druggable proteome.
How would you define the “druggable proteome”?
This is the fraction of our >20,000 human proteins that can be functionally modulated by a drug. Drugs can be small molecules or large molecules such as therapeutic antibodies. Estimates of how many proteins are “tractable” vary widely, I think there may be around 5,000. Only a subset of these 5,000 would be “druggable” which means that modulating them with a drug will also have a therapeutic benefit.
How are advances in chemical biology helping to expand the druggable proteome?
Small molecules are still the main modality for intracellular targets. Deep pockets, typical for enzymes, are more easily tractable than shallow pockets typical for protein-protein interactions. Chemical biology has developed tools to explore different types of pockets. I am excited in particular by the potential of DNA-encoded libraries, and small fragment approaches with covalent modes of action. Some of these compounds will just be “binders” but these can be made into target degraders as PROTACs.
How can these advances help our understanding of disease biology?
If we had more chemical probes, we could use these in a standardised, controlled way to interrogate target function in cell-based models, organoids, and in some cases animal models. Yes, we have gene editing now, but that is not the same as pharmacological modulation.
We also need in vitro models that translate better to in vivo. Our old immortalised cell lines won’t do, we are going to need more work in primary cells, organoids, etc.
What are the main challenges facing scientists in this field?
Lack of standardised probe sets. Bad probe compounds, e.g. with bad selectivity, are still used and wrong conclusions drawn.
Lack of translational in vitro models.
Why is it important to bring industry and academia together to discuss this topic?
Academia brings creativity, agility, fast progress of new ideas and concepts, thinking out of the box.
Industry sometimes lacks these but knows how to develop a compound into a drug, which requires a host of technologies not readily available to academia. Also, industry requires a new generation of drug targets with better validation, and historically targets are often discovered in academia. Once a target hypothesis exists, academics and industry should ideally collaborate to figure out how to drug it.
What will be the main highlight of this conference?