VENUE CHANGE! The NovAliX Conference will now take place at HILTON STRASBOURG - More info here.
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Read the Testimonials of the 2015 Conference attendees now!
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Accommodation - important notice
During the same week of June a session of the European Parliament will take place in Strasbourg, we therefore recommend you to book your accommodation well in advance!
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Keynote Lectures
X-ray Crystallography: an Ever-Reemerging Technology (KN02)
| Dr Gerard BRICOGNE (GLOBAL PHASING LTD., Cambridge, United Kingdom) Read more
Gerard Bricogne is the founder and director of Global Phasing Ltd., a small non-profit research group specialised in methods and software for macromolecular X-ray crystallography, supported mostly by a Consortium of pharmaceutical companies who make extensive use of its software. He started his PhD work in 1972 at the MRC Laboratory of Molecular Biology, under the supervision of David Blow, at a time when there were only 12 structures in the PDB, and has dedicated his whole research career to the field of mathematical and computational methods. He applied his PhD work on non-crystallographic symmetry to the solution of the first two virus crystal structures, then became interested in the role of probability theory in the direct solution of the phase problem. This led him to introduce Bayesian statistical methods into the areas of experimental phasing and structure refinement, implemented respectively in the SHARP and BUSTER programs from his group. His other interests have been in the improvement of processing methods for diffraction data, through an EEC Workshop held in 1986-89 whose influence is still felt today, and more recently in improving the design and conduct of diffraction experiments themselves. His contributions to the advancement of crystallographic methods were recognised by the award of the Aminoff Prize of the Royal Swedish Academy of Sciences in 2009. Close window
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The Discovery of ABL001, an Allosteric Inhibitor of BCR-ABL (KN01)
| Dr Sandra JACOB (NOVARTIS INSTITUTES FOR BIOMEDICAL RESEARCH, Basel, Switzerland) Read more
Sandra Jacob is executive director and head of Structural Biophysics in the Novartis Institutes for BioMedical Research in Basel, Switzerland. Her group works mainly in lead discovery and optimization using X-ray, NMR and other biophysical methods to find and characterize interactions of ligands with proteins and RNA. Sandra is recognized for her expertise in kinase inhibition and her work has resulted in the discovery of Tasigna, a drug for the treatment of Chronic Myelogenous Leukemia. She is a driver of novel approaches for target modulation, the most recent examples being non-ATP site inhibitors of kinases. She studied Chemistry at the University of Melbourne in Australia and followed this up with a Ph.D. using protein crystallography at the St. Vincent’s Institute of Medical research in Melbourne. She joined Ciba Geigy, now Novartis, after studies including lipocalins at Uppsala University in Sweden and focusing on membrane proteins at the University of Basel. Close window
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Session 1: Emerging Technologies
A 5-Year Retrospective on Non-Covalent Mass Spectrometry Applied to Drug Discovery (OC01)
| Dr Mathias ANTOINE (INSTITUT DE RECHERCHES SERVIER, Croissy-sur-Seine, France) Read more
Mathias Antoine is Research Scientist at the Servier Research Institute (Croissy sur Seine, France) where he is responsible for Biophysics, Mass Spectrometry and Enzymology within the Protein Chemistry and Molecular Interactions department.
His research interests include the application of biophysical, kinetic and mass spectrometry methods to decipher the molecular mechanism of action of protein ligands and enzyme modulators, to understand the enzymology of selected targets and to characterize mAbs and Antibody-Drug Conjugates.
Molecular enzymologist by training, he obtained his PhD from the University of Nancy before moving to the University of Nebraska-Lincoln for a postdoc. He returned to France and joined Servier initially as a postdoctoral fellow to apply stopped-flow methods to the study of binding kinetics before taking a permanent position as a Protein Science scientist, setting-up a protein mass spectrometry platform. He continued as a Structural Biology team leader, helping to establish in-house protein crystallography capabilities. Before taking his current position, he was in charge of the Mass Spectrometry, Mechanistic Enzymology and Kinetics team.
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Maldi Mass Spectrometry: From Imaging to Ultra-High-Throughput-Screening (Maldi-Uhts) (OC02)
| Dr Jens FUCHSER (BRUKER DALTONICS, Bremen, Germany) Read more
Jens Fuchser’s passion for analytical chemistry started at the University of Göttingen, Germany, where he studied chemistry and received a PhD in Natural Compound Analysis in 1995. Having finished his thesis he moved to Durham, UK for a Post-doc position. In 1997 Jens moved to Potsdam where he was heading the MS facility of AnalytiCon Discovery. Since more than 15 years Jens works for Bruker Daltonics in Bremen, with emphasize on mass spectrometry for small molecule MALDI Imaging and Drug Discovery. Close window
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Mass Spectrometry and its Role in Drug Discovery (PL01)
| Prof. Carol ROBINSON (UNIVERSITY OF OXFORD, Oxford, United Kingdom) Read more
Carol Robinson is a Royal Society Research Professor and Doctor Lee’s Professor of Chemistry Elect at the University of Oxford. She is recognised for pioneering the use of mass spectrometry for her research into the 3D structure of proteins. Her most recent work is concerned with examining how small molecules, specifically lipids, impact on the structure and function of membrane assemblies.
Carol’s graduate education was completed whilst working full-time in her post at Pfizer. She was subsequently admitted to the University of Cambridge where she completed her PhD in two years. Following an eight-year career break to begin raising her three children, she returned to research taking up professorial posts at the both the University of Oxford and later the University of Cambridge. She returned to Oxford in 2009 to take up the Chair of Dr. Lee’s Professor of Chemistry.
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Exploring GPCR and Membrane Protein Dynamics with Solution NMR and X-ray Free-Electron Lasers (PL02)
| Prof. Gebhard F.X. SCHERTLER (PAUL SCHERRER INSTITUTE, Villigen, Switzerland) Read more
Prof. Gebhard F.X. Schertler
Head of Biology and Chemistry and Member of the Directorial Board of PSI
Professor for Structural Biology D-BIOL ETH Zurich
Paul Scherrer Institut (PSI)
OFLC 109
CH-5232 Villigen PSI
Core competencies: investigating the structure and function of G protein-coupled receptors (GPCRs) and other membrane proteins (ion channels, transporters)
• First structures of a ligand binding GPCR (adrenergic receptors)
• Micro and nanocrystallography; serial crystallography (millisecond SMX and femtosecond SFX)
• Prior to coming to the Paul Scherrer Institut in 2009: group leader at the MRC Laboratory of Molecular Biology (Cambridge, UK)
• 18 years of pharma industry relations at MRC, including own projects
• One of the scientific founders of Heptares and remained on the scientific advisory board until 2014
• Responsible for biological applications on the Swiss Free Electron Laser (SwissFEL)
• Full Professor for Structural Biology at the ETH in Zürich, Switzerland
• Average Citations per publication of over 100, 10 highly cited papers (200-1000 citations)
• Member of the directorial board of PSI
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Session 2: Biophysics for Challenging Targets
New Strategy for Challenging Targets: Time Resolved Molecular Interaction Analysis on Living Cells Using LigandTracer (PL03)
| Dr Karl ANDERSSON (RIDGEVIEW INSTRUMENTS AB, Vänge, Sweden) Read more
Karl Andersson is CEO at Ridgeview Instruments AB, as associate professor at Uppsala University. He has a 20 year history in the molecular interaction industry, mainly on the scientific and engineering side. During 10 years at Biacore R&D, Karl were among other things leading a team developing high-throughput automated data evaluation procedures (as implemented in Biacore® 4000). Next, Karl invented LigandTracer® technology and founded Ridgeview Instruments AB to pioneer time-resolved interaction analysis on living cells using one of his own inventions, this in close collaboration with Uppsala University. With about 25 patents and 45 published papers, most related to interaction analysis, Karl has made an impact on this industry and aim at continuing in a similar manner. Close window
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Thermodynamics of the Ribosome Translation Machinery (OC04)
| Dr Eric ENNIFAR (CNRS, Strasbourg, France) Read more
Eric Ennifar received a Master degree in Biological Crystallography and NMR from University of Strasbourg, France. He obtained a Ph.D. in Structural Biology in 2001 from the University of Strasbourg where he solved X-ray structures of the HIV-1 genomic RNA Dimerization Initiation Site, and of the ribosomal S15/mRNA complex in the laboratory of Philippe Dumas. He then moved to the European Molecular Biology Laboratory in Heidelberg (Germany) for a postdoctoral fellowship in the group of Dietrich Suck working on X-ray crystallography of DNA recombinases and resolvases. In 2003, he joined the CNRS unit “Architecture et Réactivité de l’ARN” in Strasbourg, headed by Prof. Eric Westhof. He is now CNRS Research Director, group leader of the team “Structure and Dynamics of Biomolecular Machines”. His current research is focused on the ribosome translational machinery, the HIV-1 Reverse Transcription complex and structure-based drug design of HIV-1 RNA ligands using structural and biophysical approaches. He was awarded the CNRS 2014 bronze medal.
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Combining Binding Thermodynamics and Kinetic Binding Mechanisms to Assess The Selectivity of Inhibitors of Histone Deacetylase-Like Amidohydrolases (OC03)
| Mr Christian MEYNERS (UNIVERSITY OF APPLIED SCIENCES DARMSTADT, Darmstadt, Germany) Read more
* Currently a second year Ph.D. student in the research group of Prof. Meyer-Almes at the University of Applied Sciences Darmstadt, working on the influence of thermodynamic and kinetic parameters on the selectivity of ligand binding by members of the histone deacetylase family.
* M.Sc. in Biosystems engineering from the University of Applied Sciences Darmstadt
* B.Sc. in Biotechnology from the University of Applied Sciences Darmstadt
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Probing the Structure and Dynamics of Proteins with Single-Molecule Spectroscopy (PL04)
| Prof. Ben SCHULER (UNIVERSITY OF ZURICH, Zurich, Switzerland) Read more
Ben Schuler is Professor of Molecular Biophysics. He joined the department as Assistant Professor in 2004 and was promoted to Full Professor in 2009.
He investigates the structure, dynamics, folding and misfolding of proteins with a close combination of biochemical and spectroscopic methods, in particular single molecule fluorescence.
Ben Schuler studied Chemistry and Biochemistry at the University of Regensburg, Germany, and at the University of Kent, UK. He received his PhD in Physical Biochemistry from the University of Regensburg in 1998 and did his postdoctoral research in the Laboratory of Chemical Physics at the National Institutes of Health in Bethesda, USA. Ben Schuler then headed an independent research group at the University of Potsdam in Germany supported by the Emmy Noether Program of the Deutsche Forschungsgemeinschaft Close window
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Session 3: Special Focus on Cryo-EM
Cullin-Ring Ubiquitin E3 Ligase Regulation by the Cop9 Signalosome (OC05)
| Dr Simone CAVADINI (FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH, Basel, Switzerland) Read more
Simone Cavadini is project leader in Nicolas Thomä's laboratory at the Friedrich Miescher Institute for Biomedical Research (FMI) in Basel, Switzerland. He uses cryo-EM in combination with other biophysical methods to elucidate structure and function of large protein complexes involved in DNA repair. Most recently he has sought to understand how protein degradation under the control of cullin-RING ubiquitin E3 ligases (CRLs), notable for their roles in DNA repair, is regulated by the COP9 signalosome (CSN).
He studied chemistry at the Swiss Federal Institute of Technology in Lausanne (EPFL). He received his PhD (EPFL, 2009) for developing new NMR techniques to probe the structure and dynamics of biomolecules under the supervision of Geoffrey Bodenhausen. He then moved for a short period to the Institut Biochimique SA (IBSA) in Lugano, Switzerland, where he worked as a mass spectrometry scientist, helping establish their mass spectrometry facility. In 2011 he joined the Thomä laboratory (FMI) for post-doctoral studies on the CRL-CSN complexes before becoming a project leader at the FMI in 2014
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High-Resolution Electron Cryo-Microscopy of Membrane Protein Complexes (PL05)
| Prof. Werner KÜHLBRANDT (MAX PLANCK INSTITUTE OF BIOPHYSICS, Frankfurt am Main, Germany) Read more
Werner Kühlbrandt studied chemistry and crystallography at the Free University Berlin, and biochemistry and biophysics at King’s College London. He did his PhD with Nigel Unwin at the MRC Laboratory of Molecular Biology in Cambridge, UK, investigating the structure of two-dimensional ribosome crystals by electron microscopy. As a postdoc, he turned to structural studies of membrane proteins, first at the ETH Zürich, and then at Imperial College London, to determine the high-resolution structure of the plant light-harvesting complex, LHC-II. After a short stay at UC Berkeley, CA, he became a group leader at EMBL Heidelberg in 1988. Since 1997 he is a director at the Max Planck Institute of Biophysics in Frankfurt, Germany, where his department of Structural Biology investigates the structure and mechanisms of membrane proteins by X-ray and electron crystallography, single-particle cryoEM, electron tomography and functional studies. Close window
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Visualizing Dynamic Macromolecular Complexes at High Resolution by Cryo-EM (PL06)
| Prof. Holger STARK (MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY, Göttingen, Germany) Read more
Current Title and Position:
Prof. Dr. Holger Stark, Director of the department “Structural Dynamics” at the Max-Planck-Institute for biophysical Chemistry in Goettingen, Germany
Research Field:
Structure determination of large macromolecular complexes by cryo-EM with a focus on complexes involved in translation, splicing and cell cycle regulation.
Education and former professional experience:
Studies in Biochemistry at the Free University in Berlin. PhD thesis in 1997 about the 3D structure determination of the 70S ribosome by cryo-EM. Postdoc at the Imperial College in London. Group leader position in cryo-EM in Marburg (1998). From 2000-2007 research group leader at the MPI for biophysical Chemistry in Goettingen, Germany. Since 2007 full professor at the Goettingen University and since 2015 Director of the Max-Planck-Institute of biophysical Chemistry.
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EM in Industry: Expectations and Perspectives (PL07)
| Dr Denis ZEYER (NOVALIX, Illkirch, France) Read more
Denis earned his M.Sc. in biological crystallography and NMR at the Louis Pasteur University (Strasbourg, France). His Ph.D. in protein X-ray crystallography (with Dr. Jean-Paul Renaud and Dr. Dino Moras at the Institute of Genetics and Molecular and Cellular Biology, Strasbourg, France, in collaboration with BMS) led to the publication of pioneering structures in the PPAR family of nuclear receptors.
In 2003 Denis built the structural biology group and launched the research services business of AliX. In that capacity he has been instrumental in building a sound client base including major pharmaceutical companies; establishing a reputation for scientific excellence and reliability; and in technical improvements though internal and external innovations. Denis was appointed CEO of AliX in 2008 and has been CEO of NovAliX since its inception.
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Session 4: Computational Biophysics
Structural Stability of Protein-Ligand Complexes: Applications in Virtual Screening (PL08)
| Prof. Xavier BARRIL (BARCELONA UNIVERSITY, Barcelona, Spain) Read more
Xavier Barril is an ICREA Research Professor at Barcelona University’s School of Pharmacy and co-founder of Minoryx Therapeutics. His research focuses on the discovery of bioactive molecules exploiting unusual mechanisms of action. In parallel, his group develops new computational tools to tackle such tough targets and strives to improve the molecular understanding of pharmacological and biological events. Previously he worked at Vernalis (Cambridge, UK), where he was involved in a range of projects, mainly in the oncology area. He has co-authored more than 60 scientific publications, including research papers, reviews and book chapters. With a strong focus on translational research, Prof. Barril is co-author of 8 patents and co-founder of Minoryx Therapeutics, a company dedicated to the development of new treatments for rare diseases. Close window
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Uncoupling the Structure-Activity Relationships of Beta-2 Adrenergic Receptor Ligands from Membrane Binding (OC07)
| Dr Callum DICKSON (NOVARTIS INSTITUTES FOR BIOMEDICAL RESEARCH, Cambridge, United States) Read more
I studied Chemical Physics at the University of Edinburgh, during which time I spent a year working in the Pfizer computer-aided drug design group as a trainee (Sandwich UK site, now closed). I then completed a PhD in computational chemistry at Imperial College London, working on the molecular dynamics simulation of lipid membranes and drug-membrane interactions.
I am now a postdoc in the CADD group at Novartis (Cambridge MA, USA site) working on molecular dynamics simulations of membrane proteins and small molecule membrane permeation. I have been a postdoc at Novartis for almost two years.
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Diverse Applications of Free Energy Calculations in Drug Discovery (OC06)
| Dr David RINALDO (SCHRÖDINGER, Mannheim, Germany) Read more
David Rinaldo received a "Diplôme d'Ingénieur" from the "Ecole Nationale Supérieure de Chimie de Montpellier" (France) in 1999. He then started his graduate studies at the "Université Joseph Fourier" in Grenoble (France) under the supervision of Martin Field where he was modelling metalloproteins using QM and MD simulations techniques. He obtained his PhD in 2003 and moved to Colombia University for postdoctoral studies under the supervision of Pr Richard Friesner. There he applied QM/MM techniques to the study of metalloproteins and he developed DFT functional corrections for transition metals. In 2007 he joined Schrodinger where he is currently Senior Applications Scientist. He is supporting Schrodinger's customers in all aspects of CADD. Close window
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Computational Exploration of Protein Dynamics for Ligand Design (PL09)
| Prof. Rebecca WADE (HEIDELBERG INSTITUTE FOR THEORETICAL STUDIES AND HEIDELBERG UNIVERSITY, Heidelberg, Germany) Read more
Rebecca Wade is Scientific Director at Heidelberg Institute for Theoretical Studies (HITS) where she leads the Molecular and Cellular Modeling group. She also holds a Professorship in “Computational Structural Biology” at the Center for Molecular Biology (ZMBH), Heidelberg University, Germany.
Her research is focused on the development and application of computer-aided methods to model and simulate biomolecular interactions. She is an author of over 200 scientific publications, as well as software programs and web servers that are used world-wide.
Rebecca Wade studied at Oxford University and received her doctorate in molecular biophysics in 1988. She was a group leader at the European Molecular Biology Laboratory (EMBL) in Heidelberg before moving to HITS in 2001.
URL: www.h-its.org/mcm.
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Session 5: Cellular Biophysics
Insulin Degrading Enzyme: Drug Target Engagement in Hela Cells by Cellular Thermal Shift Assay (OC08)
| Dr Adrien HERLEDAN (INSTITUT PASTEUR DE LILLE, Lille, France) Read more
Adrien HERLÉDAN completed a master degree in Molecular and Cellular Biology in 2004 in Montpellier and worked 4 years in the protein array domain at the University of Nantes.
He works actually in the research unity U1177 "Drugs and Molecules for Living Systems". The Lab's work is to design and study compounds that modulate selected molecular targets in a desired way to treat infectious and metabolic diseases. He’s engineer in biochemistry on a screening platform for 5 years and his mission spans the whole medicinal chemistry support process: compound library management, assay development, screening to hit generation and the hit-to-lead process.
He conducted a screening campaign in TSA (Thermal Shift Assay) in collaboration with a biopharmaceutical company and developed actually Cellular TSA (CETSA) approaches.
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The Life and Death of Cells: Cellular Bioenergetics for Better Phenotype Based Drug Discovery (PL10)
| Dr Magnus JANSSON (SYMCEL SVERIGE AB, Spanga, Sweden) Read more
Magnus Jansson is the Chief Scientific Officer Symcel Sverige AB. He holds a PhD in biochemistry and protein engineering from The Royal Institute of Technology in Stockholm. He has 25 years of experience from the biotechnology and pharmaceutical development industry working on bio-molecular biophysics and preclinical drug discovery. Magnus has extensive experience from different laboratory disciplines such as gene cloning, recombinant protein production, target discovery research, bioinformatics, assay development, protein structure determination and biophysical characterization. Dr. Jansson joined Symcel in 2009 and is responsible for technology and applications development. Dr. Jansson has a long standing interest in developing and implementing novel technologies to advance biological research. Close window
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Imaging of G-protein Coupled Receptors while Quantifying their Ligand-binding Free Energy Landscape to Mutiple Ligands (PL11)
| Prof. Daniel MÜLLER (ETH ZÜRICH, Basel, Switzerland) Read more
Daniel Müller holds the Chair of Biophysics at the Department of Biosystems Science and Engineering at the ETH Zürich. The Department is located in Basel where Müller co-directs the Swiss National Competence Center of Research (NCCR) Molecular Systems Engineering (www.nccr-mse.ch). The motivation of the NCCR, which encompasses 28 research groups, is to engineer molecular factories for biotechnological applications and to control cells, tissues and organs. Müller develops bionanotechnological tools and assays to quantify the physical and chemical interactions that define the structure and function relationship of membrane proteins. Beginning from the understanding of these molecular principles he further develops tools to image and observe how receptors form dynamic assemblies in cellular membranes and how this assembly can regulate their functional state. On the cellular and tissue level Müller characterizes how cells control these assemblies depending on their state and vice versa. Finally he applies the tools and know-how to control basic cellular processes such as folding, signaling, transport, mitosis and adhesion. Close window
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Session 6: Biophysics for Biotherapeutics
The Neonatal Fc Receptor (FcRn) Binds Independently to Both Sites of the IgG Homodimer with Identical Affinities (PL12)
| Dr Yasmina ABDICHE (RINAT-PFIZER, San Francisco, United States) Read more
Yasmina Abdiche is a Research Fellow at Rinat, part of Pfizer’s Oncology Research Unit, in South San Francisco, California, which she joined in 2004. She leads the Bioanalytical group, which uses various biosensor technologies and automation to support multiple research projects. After graduating from Oxford University in the UK with a PhD in Biological Chemistry and a Master’s degree in Chemistry, Yasmina completed post-doctoral research in Dr David Myszka’s laboratory at the University of Utah in Salt Lake City, where she optimized biosensor methods for characterizing small molecule interactions and helped to establish carbonic anhydrase as a benchmark model system. Yasmina is co-inventor of TEV-48125 (formerly RN307), an anti-CGRP antibody which demonstrated POC in PhIIb clinical trials for migraine, and co-inventor of RN316 (bococizumab), a PCSK9 inhibitor currently in PhIII clinical trials for hypercholesteremia. Close window
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Analysis of Bispecific Interactions with the Switchsense Biosensor (OC09)
| Dr Ulrich RANT (DYNAMIC BIOSENSORS GMBH, Martinsried/Planegg, Germany) Read more
Dr. Ulrich Rant received his PhD in biophysics (summa cum laude) from the Technical University Munich, Germany, in 2005. After a PostDoc at TU Munich and a research stay at the Fujitsu Laboratories Ltd., Japan, he became a group leader at TU Munich in 2007. Uli was awarded a Carl-von-Linde Jr. Research Fellowship by the TUM Institute of Advanced Studies and selected a principal investigator in the Nanosystems Initiative Munich Cluster, both supported through Germany’s Excellence Initiative. Also, he was awarded a GO-Bio grant for the creation of a biotech venture by Germany’s ministry of science (2011 and 2013) and received the Robert-Sauer Award by the Bavarian Academy of Sciences (2012). Uli authored more than 70 papers and patents in the fields of biomolecular analysis and nanotechnology.
Uli is a co-founder and CEO of Dynamic Biosensors GmbH, a Munich based biotech company, which commercializes a novel chip platform for protein detection and analysis (switchSENSE). Close window
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Combinatorial SEC, AUC and TEM Approach for the Characterization of mAb Dimers (PL13)
| Dr Arne RUFER (F. HOFFMANN-LA ROCHE LTD., Basel, Switzerland) Read more
Dr. Arne Rufer is a Principal Scientist in the Chemical Biology department at F. Hoffmann-La Roche in Basel. His main role is to employ biophysical methods, such as analytical ultracentrifugation, fluorescence spectroscopy and light scattering, for the characterization of protein-protein and protein-small molecule complexes as well as biologics. Previously, he was a postdoctoral fellow at the Max Planck Institute for Medical Research in Heidelberg. Dr. Arne Rufer studied biology and biochemistry at the University of Cologne and the University of New Hampshire. He received his PhD from University of Cologne on a project jointly run with F. Hoffmann-La Roche in the field of X-ray crystallography for structure based drug design. Close window
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Kinetic Excursion Analysis (Kinexa) of Avidity Enhancement of a Multi-Valent Adnectin Binding to Clustered Receptors on Cho Cells (OC10)
| Dr Lumelle SCHNEEWEIS (BRISTOL-MYERS SQUIBB, Princeton, NJ, United States) Read more
Lumelle Schneeweis is a Senior Investigator at Bristol-Myers Squibb where she provides biophysical leadership and analysis for biologics discovery programs. She holds a Ph.D. in Biochemistry & Molecular Biophysics from the University of Pennsylvania. She has 16 years of experience studying the binding affinity and oligomeric state of proteins ranging from fusion proteins and antibodies to single domain biologics, PEG-conjugates, and multisubunit enzymes. Her work focuses on complementary methods for measuring binding affinity and kinetics to support drug discovery. Close window
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