Projects

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Description	[methodology]

We strive to gain quantitative insight into biomolecular dynamics, in order to understand the molecular basis of protein function and also malfunction leading to disease. Ultimately, we aim to understand and alter such nanoscale processes in a controlled way.
We engineer synthetic cellular memory platforms that enable the reconstruction of cellular histories and can be applied as living diagnostics.	A fundamental challenge in biology is to understand how cells function and integrate complex molecular information to perform different behaviors. For example, the differentiation of a stem cell into two daughter cells with distinct identities or the transformation of a normal cell into a cancer cell. This challenge has motivated the creation of numerous technologies facilitating detailed intracellular observations at the level of DNA, RNA, protein, and metabolites. Despite the power of these approaches, they generally require destructive methods and therefore observations are limited to a few snapshots in time or select asynchronous cellular processes. One provocative solution to this is to introduce DNA writing and molecular recording platforms within cells that enable the encoding, storage, and retrieval of molecular information. Towards the goal of continuously recording molecular events within cells, my laboratory is developing and applying Record-seq, a ‘transcriptional recording’ platform that employs CRISPR spacer acquisition from RNA to capture and convert intracellular RNAs into DNA, permanently storing transcriptional information in the DNA of living cells. The newly acquired sequences serve as transcriptional records, which are retrievable via deep sequencing and can be leverage to reconstruct cellular histories. This technology provides an entirely new mode of interrogating dynamic biological and physiological processes and opens up numerous avenues for future work in engineering cellular systems.


	We develop and deploy methods in computational protein design for applications in synthetic biology and cellular engineering. Recent advances in machine learning and AI have greatly augmented our abilities to understand, engineer and design biomolecules, in particular proteins. These tools can now be used to gain structural insights (e.g. AlphaFold), and to design new proteins from scratch. Molecular characteristics such as self-assembly or epitope binding can be defined, and proteins new-to-nature generated for these exact purposes. We are designing and experimentally implementing protein systems for complex cellular engineering. We aim to interface with cellular pathways using compact circuits composed of de novo designed proteins capable of rapid computations directly at the protein level. For implementing this new form of cellular programming, we generate synthetic interactomes and deploy these for in situ classification and reporting of cell states.

Our research focuses on the deployment of multiple immobilized molecular catalysts on a flow microreactor platform to convert elementary starting materials over telescoped reactions into chemically and structurally complex products. The interactions of different agents in multiple compartments on a solid-state platform result in a molecular factory.	A combination of multiple catalyst permutations and applied reaction conditions enables screening of diverse parameter spaces for the conversion of suitable starting materials. This approach aims at not only synthesizing one catalysis product from one starting material, but multiple products from the same starting material and whole compound libraries. This bio-inspired approach resembles the biosynthetic processes that are taking place in a biological cell, in which multiple metabolites are often produced from a single molecule. Our research comprises the design and synthesis of complementary catalysts, linkers and starting materials for heterogeneous catalysis with molecular catalyst monolayers, as well as the immobilization of these catalysts in flow microreactors and conducting synthetic operation on these platforms. This project is in close collaboration with the Mayor group and IBM Research - Zurich in Rüschlikon. The silicon-based flow microreactors are being fabricated by microfabrication techniques, are scalable in the number of compartments, and allow various reaction control features such as nanoscale electrode arrays, catalyst-supporting surfaces, externally controllable micro-heaters and nanophotonic sensing sites to be implemented and to be used as reaction feedback controls.
The chemical and physical processes enabling the transformation of matter in living systems is regulated by complex feedback loops. Such tightly cross-regulated processes enable highly complex reaction cascades as well as transport and exchange mechanisms that have not yet been achieved in synthetic systems. The project „Nanopores as Solid-State Approach to Interlinked Reaction Compartments" strives to simulate isolated feedback mechanisms to investigate the underlying regulation mechanisms in detail and to identify the parameters governing the system.	To fabricate such interlinked reaction compartments, we aim at fabricating nanopore devices based on a solid-state approach using top-down fabrication techniques. Self-assembled monolayers (SAMs) of functional molecular building blocks are physically separated but remain addressable by electrical, optical or electrochemical means. The SAMs are highly oriented which enables correlations between chemical structure and electronic as well as ionic transport properties in single-molecular junctions to be studied. Preliminary studies will allow us to mimic a biological response and to investigate isolated feedback mechanisms in detail. Additionally, from a materials point of view, the resulting oligomers may be interesting. Their physical properties are length-dependent and, thanks to a feedback mechanism, their length-distribution may become tunable by specific parameters dictated by the system, leading to a new size-control approach with wide potential applications in material science. Modular systems can easily be expanded with additional functionalities. For example redox-dependent chromophores that will facilitate the investigation of the systems dynamics as it can be investigated by optical microscopy. The project is not only geared towards investigating feedback mechanisms across vesicle membranes but also towards integrating vesicles as molecular factories. With such vesicles, molecular devices enabling photo-induced charge separation across the vesicle membrane will be studied. In a later stage of the project, we envisage electrochemical interconnecting of different functionalized vesicles to build up gradients of chemical potentials.
Molecular systems derive their functional breadth from the interplay of multiple elements. The successful cooperation of these elements is often limited to narrow windows of operation, which are often difficult to identify.	We are optimizing complex in vitro systems so they can successfully operate in these windows. For this, we develop cell free systems that allow the synthesis of multiple catalysts and other protein-based elements, and compartmentalize the synthesis in nanoliter or picoliter-sized droplets. This helps us to investigate thousands of system compositions per minute. We use this to develop design rules for multi-membered systems and prepare such droplets for analysis in a classical way (i.e., by fluorescence) and by label-free methods, such as mass-spectrometry. This way we can optimize system function for a variety of objectives, ranging from enzyme evolution to the engineering of smart systems for metabolic diseases.
Building autonomous synthetic organelles and cells with a defined function using a repertoire of functional modules (toolkit) and containing inside a minimal metabolism for survival, represents the ultimate goal of this project group.	Such complex processors will open a wide variety of possibilities ranging from environmental to medical applications. One of the most important challenges will be to provide a large repertoire of engineered and modular biomolecular-transport and -energy conversion systems for assembly of nanoreactors with diverse functionalities in lipid bilayers and block copolymers. Initially, modules will include light-driven proton pumps and proton-driven solute transporters in the membrane, and metabolizing enzymes inside the container. Next, more complex powering systems will be explored such as combinations of light-driven proton pumps with sodium/proton antiporters with the objective: to energise sodium-driven solute transporters. This will significantly increase the repertoire and specificity of translocating modules. The availability of numerous, highly specialized membrane proteins in milligram amounts offers the unique opportunity to use them as building blocks and toolkit to assemble molecular factories in the form of nanoreactors and functional surfaces using bottom-up approaches. This project group has a strong expertise and knowledge in biochemistry, function and structure of membrane proteins. Furthermore, the group already possesses a significant number of recombinant transport proteins for different solutes such as peptides, sugars, amino acids and antibiotics that can be used as modules for engineering and assembly of nanoreactors.
This project shows true interdisciplinary, transversal research: Clinical tests are conducted with light sensitive, molecular systems in partnership with the Friedrich-Miescher Institute of our industry-partner, Novartis. Should the tests be successful, this project could enable blind people to see in black and white again and, eventually, regain their full color vision.	Retinitis pigmentosa (RP) refers to a diverse group of progressive, hereditary diseases of the retina that lead to incurable blindness and affects 2 million people worldwide. Artificial photoreceptors constructed by gene delivery of light-activated channels or pumps (functional molecular modules) to surviving cell types in the remaining retinal circuit have shown to restore photosensitivity in animal models of RP at the level of the retina and cortex as well as behaviourally. Simply said, in a degenerated macula the first step is missing: there are no more rods and cones that can detect light and subsequently convert light into neural signal. The visual nerves however are intact. In tests with apes and dogs the genetically delivered molecular factories dock successfully with the visual nerve of the eye and are activated by light, producing certain impulses that enables blind animals to see again.
	Molecular Systems Engineering (MSE) incarnates a novel approach to clinical innovation that considerably expands the toolbox of molecular sciences and healthcare both theoretically and technically. The prospects of this emerging field to bring about scientific and clinical innovation crucially depend on proactively addressing potential ethical and regulatory bottlenecks. Such issues include three major domains, that is: issues associated with society’s appraisal of the novel bio-technological characteristics of engineered molecular systems; the ethical and legal aspects linked to the clinical translation of MSE into healthcare applications; and the development of appropriate regulatory standards for the assessment of MSE applications by regulatory agencies. To address those issues, this project brings new empirical research and analytical competences on ethics and regulatory issues of MSE technologies. Thanks to considerable experience and reputation in the field of bioethics and health policy, the ETH Zürich’s Health Ethics and Policy lab led by the PIs Effy Vayena, and Alessandro Blasimme will ensure dedicated research on all of the above issues. Normative and empirical research on the ethics of MSE will result in specific ethical guidelines to guide the long-term development of the field in the future. As far as regulatory aspects are concerned, relevant national and international stakeholders – including regulators – will be engaged and a regulatory roadmap for MSE will be developed.
This project uses state-of-the-art molecular and genomic editing platforms to engineer immune cells for applications in biotechnology and cellular immunotherapy.	Our ongoing projects are focused on applying molecular and genome editing tools to engineer various types of immune cells. The precise genomic exchange of highly similar immunogenomic genes has not been demonstrated before using genome-editing tools, thus a series of aims and milestones to advance this goal have been established. For example, in one of aims we are engineering mammalian cellular factories for protein production. In another aim we are using precise genome editing to improve cellular therapeutics for transplantation and cancer. We will combine our efforts with the network of NCCR researchers to push the boundaries of immunological systems engineering. Scientific Highlights Plug-and-(dis)play mammalian cells. We have used precise genome editing to develop a platform for rapid generation of stable cell lines capable of surface expression and secretion of recombinant proteins. The simplicity of our plug-and-(dis)play platform is highlighted by the fact that it only requires a single transfection and screening step to generate stable cells. We envision these cell lines can be applied for generating recombinant protein reagents and therapeutics. Reprogramming MHC-specificity immune cells. We have established a proof-of-concept for MHC-allelic replacement, which could be used in the future for improving the donor-host matching, which is a major challenge in allogeneic cellular transplantations in cancer. We used genome editing methods to precisely exchange the MHC region of immune cells, which were then subsequently verified for functions immune activity. Our methods can be applied for the engineering of other immunogenomic regions, which would have value in cellular immunotherapy.
In this project we aim to use visible light to drive electrons across a membrane and to accumulate charges in such a way that NAD⁺ (nicotinamide adenosine dinucleotide) can be converted to NADH. The latter can then fuel enzymatic cascade reactions which ultimately lead to value-added products that are synthesized in the closed compartment of a molecular factory. The use of vesicles made from block copolymer membranes that make up the closed compartment offers the advantage that the enzymatic chemistry can be performed in a protected environment and that oxidation and reduction products resulting from photochemistry can be spatially separated from one another.	The photophysical and photochemical aspects of this project are addressed by the Wenger group while the enzyme chemistry is taken care of by the Ward group. Vesicles built from block copolymers will be made in collaboration with the groups of Meier and Palivan. In the first phase of the project, strategies for photodriven electron accumulation are explored in suitable model compounds. For example, covalently linked Ru(bpy)₃²⁺ (bpy = 2,2’-bipyridine) – naphthalene diimide (NDI) systems are investigated with a view to reducing NDI to NDI^- and finally NDI^2- in the course of photoirradiation of the Ru(bpy)₃²⁺ photosensitizer in presence of sacrificial or non-sacrificial electron donors. Once the challenge of achieving efficient electron accumulation has been tackled, it will be possible to perform light-driven two-electron reduction of suitable small molecule catalysts which are able to reduce NAD⁺ to NADH. In parallel, the Wenger group explores the possibility of obtaining other fuels by means of photochemistry, for example formate from CO₂. Formate can act as an electron source for various enzymatic reactions hence this molecule can potentially be used to initiate enzyme cascades. Close interaction between the Wenger and Ward groups is key for this purpose. Furthermore, strategies for the oriented incorporation of molecular wires into block copolymer membranes are explored jointly between the Palivan and Wenger groups. In order to obtain net electron transfer from the outside to the inside of the molecular factories made from vesicles, it will be essential to orient donor-bridge-acceptor systems properly in the membrane. Possible long-term perspectives include the incorporation of proton pumps into the vesicles in order to transport protons across the membranes, in addition to electrons. This avenue will be explored jointly with the group of Fotiadis. An addition possible avenue is the use of artificial metalloenzymes in the enzyme cascades that rely on engineered anion-π catalysis, as implemented jointly be the groups of Matile and Ward.
In the design of biological systems (synthetic biology), the aims range from detailed model-based design of novel systems to general concepts for the rational and – potentially automatic – design of large-scale circuits.	Robust systems designed to enable the use of engineered molecular systems in biotechnological and medical applications are of particular interest. This project will address various aspects of methods and model development for Molecular Systems Engineering to enable rational (model-based) design of molecular systems and component features such as kinetic parameters in iterations with experimental (analysis) approaches. For the rational design of synthetic molecular systems, mathematical models of different types have been developed. While a growing number of computational design tools implements such formal approaches, major challenges remain, for example, in terms of systematic model development and in the rational design of informative experiments for systems characterization. In the area of model-based analysis and design of genetic circuits, the development of computational models and design methods will enable rational design of parts and circuits. Another focus on the design of engineered metabolic networks will support molecular engineering of complex biosynthetic and energy-producing systems by integration from molecular modules to factories.
Strategies to integrate and exploit artificial metalloenzymes within mammalian cells for biomedical applications.	With synthetic biology applications in mind, attempts to exploit organometallic catalysts within a cellular environment have been met with limited success. Thanks to their know-how in organometallic- and bioinorganic chemistry with an emphasis on catalysis, this group has pioneered the field of artificial metalloenzymes (ArMs) based on the non-covalent incorporation of a catalytically competent organometallic cofactor within a host protein. The resulting hybrid catalysts display features which are reminiscent of both homogeneous- and enzymatic catalysts. With biomedical applications in mind, the main challenge to be addressed within the NCCR Molecular Systems Engineering is the integration of ArMs within mammalian cells. The ultimate goal of this effort is to complement natural enzymes for the on-site production or uncaging of drugs and for diagnosis purposes. The bio-orthogonality of some of the ArMs developed within the group allows to complement the natural reaction repertoire. To integrate artificial metalloenzymes within mammalian cells, the following strategies will be investigated: i) encapsulation within polymerosomes or ii) incorporation of cell-penetrating disulfides on ArMs. Alternatively host proteins overexpressed on the cell surface of diseased cells will be exploited to accumulate organometallic cofactors which can uncage drugs and accumulate drugs where needed.
This project programs nanoscopic reaction compartments, nanoreactors, vesicles, nanocontainers, organelles and cells with functional molecular modules that can be of biological, bioengineered or synthetic origin.	A wide variety of functional molecular modules that assemble into a toolbox are and will be established within the NCCR Molecular Systems Engineering. Molecular modules from this toolbox will be used to functionally program molecular factories. AFM-based nanotechnological methods to manipulate single cells, organelles and proteins at (sub-)nanometre resolution will be further developed and applied to program for example, nanoreactors, organelles or cells with functional modules such as proteins that have been functionally engineered. The nanomechanical approach to functionally reprogram targets using molecular modules is worldwide unique and enables detergent free, stoichiometric insertion of molecular modules into targets. Subsequently, a method will be developed to program molecular factories by the nanomechanical extraction and for the insertion of functional molecular modules.
Benefitting from synergies and the unique expertise of various projects within the NCCR Molecular Systems Engineering, the focus will be on the design of cellular diagnosis and therapeutic production factories that detect and correct physiological disorders.	In modern medicine, diagnosis of disorders kick-off therapeutic interventions and early-stage discovery of pathologies significantly improves therapeutic success. However, most disorders will only be diagnosed when discomfort urges a patient to seek medical advice. In these cases treatment may be too late. Tumour markers, immune response proteins and pathology-associated metabolites are monitored for diagnosis and therapy management by quantitative analysis of blood samples or biopsies. This requires medical intervention that is typically initiated when the patient has symptoms and is seeking medical advice. However, preventive medical check-ups for the prognosis of physiological disorders are not receiving enough attention. Synthetic gene circuits that constantly monitor physiological processes, detect a pathological situation and produce diagnostic output or coordinate therapeutic interventions could change our health-care system from the standard symptom-treatment scheme to a symptom-free preventive care strategy. Scientific Highlight Mind-Controlled Gene Expression (read the publication in full here): The Fussenegger-Group has designed a synthetic mind-controlled gene switch that enables human brain activities and mental states to wirelessly program transgene expression in cells. This device harnesses the electric energy of a person’s brainwaves thanks to an electro-encephalogram to trigger a light-emitting diode, which remotely activates light-inducible genes (optogenetic switch) in a small implant placed in mice. This technolgy, which was selected by the Scientist as one of 2014’s “Big-Advance” in Science, may provide cell-based treatments that respond to specific mental states.
The focus of our research is the development of microfluidic methods for applications in the life sciences.	In this project, we pursue three aims: i) The creation of small biochemical reactors (“artificial cells”) and ii) networks in the sense of molecular factories, and iii) the development of high-throughput, label-free screening methods with improved analytical readout. In all approaches, we use droplet microfluidics as the basic technology for the creation of controlled nL-volumes. Our system can be employed for a wide range of applications and adapted to many assays, which are developed by other groups in the NCCR.

Publications

S. Tarvirdipour, S. N. Abdollahi, J. Koser, M. Bina, C. A. Schoenenberger, C. G. Palivan “Enhanced antimicrobial protection through surface immobilization of antibiotic-loaded peptide multicompartment micelles“ J. Mater. Chem. B 2025. [DOI]

M. S. Muthwill, M. Kraus, M. Bina, M. Malekovic, I. A. Dinu, C. G. Palivan “Solid-Supported Polymer Membranes: How Different Deposition Methods Influence Their Inner Morphology and Properties“ Langmuir 2025. [DOI]

Z. Lin, P. Guha Ray, J. Huang, P. Buchmann, M. Fussenegger “Electromagnetic wireless remote control of mammalian transgene expression“ Nat. Nanotechnol. 2025. [DOI]

K. S. Csizi, A. E. Frackowiak, R. D. Lovchik, E. Lortscher, E. Lörtscher “Opportunities of scalable and electrostatically optimized electrodes for electric field- and current-driven microfluidic applications“ Biomicrofluidics 2025. [DOI]

J. J. Han, M. Fussenegger “Designing supramolecular catalytic systems for mammalian synthetic metabolism“ Nat. Rev. Mater. 2025. [DOI]

J. Fernandez de Santaella, N. G. Koch, L. Widmer, M. Nash “Amber Codon Mutational Scanning and Bioorthogonal PEGylation for Epitope Mapping of Antibody Binding Sites on Human Arginase-1“ ACS Chem. Biol. 2025. [DOI]

Y. Q. Xie, M. Fussenegger “Plasmid-based electroporation for efficient genetic engineering in immortalized T lymphocytes“ Metab. Eng. 2025. [DOI]

J. Figueiredo da Silva, A. Roshanasan, M. Bus, D. Fotiadis, A. W. Knoll, J. H. van Esch, H. Wolf “Control of a Gel-Forming Chemical Reaction Network Using Light-Triggered Proton Pumps“ Langmuir 2025. [DOI]

R. Strutt, P. Juskova, S. F. Berlanda, S. D. Kramer, P. Dittrich “Engineering a Biohybrid System to Link Antibiotic Efficacy to Membrane Depth in Bacterial Infections“ Small 2025. [DOI]

J. Huang, S. Xue, A. P. Teixeira, M. Fussenegger “A mediator-free sonogenetic switch for therapeutic protein expression in mammalian cells“ Nucleic Acids Res. 2025. [DOI]

L. Heuberger, A. Balestri, S. Tarvirdipour, L. E. Kapinos, R. Y. H. Lim, E. Loertscher, C. A. Schoenenberger, C. G. Palivan, E. Lörtscher “Polymeric Giant Unilamellar Vesicles Support Longevity of Native Nuclei in Protocells“ Small Sci. 2025. [DOI]

Y. Lu, M. Knezevic, A. Prescimone, B. Goldfuss, K. Tiefenbacher “Site-selective C(sp3)–H oxidation of alkyl substrates devoid of functional handles“ Chem 2025. [DOI]

M. Mumme, A. Wixmerten, A. Ivkovic, G. M. Peretti, T. Yilmaz, S. Reppenhagen, O. Pullig, S. Miot, K. Izadpanah, M. Jakob, L. Mangiavini, C. Sosio, F. Vuletic, O. Bieri, S. Biguzzi, B. Gahl, G. Lehoczky, R. Vukojevic, S. Hausner, A. Gryadunova, M. Haug, A. Barbero, I. Martin “Clinical relevance of engineered cartilage maturation in a randomized multicenter trial for articular cartilage repair“ Sci. Transl. Med. 2025. [DOI]

I. Casas-Rodrigo, T. Vornholt, K. Castiglione, T. M. Roberts, M. Jeschek, T. R. Ward, S. Panke “Permeabilisation of the Outer Membrane of for Enhanced Transport of Complex Molecules“ Microb. Biotechnol. 2025. [DOI]

J. Huang, A. P. Teixeira, T. Gao, S. Xue, M. Xie, M. Fussenegger “Aspirin-responsive gene switch regulating therapeutic protein expression“ Nat. Commun. 2025. [DOI]

M. Breitfeld, C. L. Dietsche, M. A. Saucedo-Espinosa, S. F. Berlanda, P. Dittrich “Ultrafast Formation of Microdroplet Arrays with Chemical Gradients for Label-Free Determination of Enzymatic Reaction Kinetics“ Small 2025. [DOI]

M. Mahameed, S. Xue, B. Danuser, G. C. Hamri, M. Xie, M. Fussenegger “Nitroglycerin-responsive gene switch for the on-demand production of therapeutic proteins“ Nat. Biomed. Eng. 2025. [DOI]

P. Khateri, T. Koottungal, D. Wong, R. W. Strauss, L. Janeschitz-Kriegl, M. Pfau, L. Schmetterer, H. P. N. Scholl “Looking outside the box with a pathology aware AI approach for analyzing OCT retinal images in Stargardt disease“ Sci. Rep. 2025. [DOI]

N. Ayoub, N. Djabeur, D. Harder, J. M. Jeckelmann, Z. Ucurum, S. Hirschi, D. Fotiadis “Actinorhodopsin: an efficient and robust light-driven proton pump for bionanotechnological applications“ Sci. Rep. 2025. [DOI]

A. Muller, J. Sullivan, W. Schwarzer, M. Wang, C. Park-Windhol, P. W. Hasler, L. Janeschitz-Kriegl, M. Duman, B. Klingler, J. Matsell, S. M. Hostettler, P. Galliker, Y. Hou, P. Balmer, T. Virag, L. A. Barrera, L. Young, Q. Xu, D. P. Magda, F. Kilin, A. Khadka, P. H. Moreau, L. Fellmann, T. Azoulay, M. Quinodoz, D. Karademir, J. Leppert, A. Fratzl, G. Kosche, R. Sharma, J. Montford, M. Cattaneo, M. Croyal, T. Cronin, S. Picelli, A. Grison, C. S. Cowan, A. Kusnyerik, P. Anders, M. Renner, Z. Z. Nagy, A. Szabo, K. Bharti, C. Rivolta, H. P. N. Scholl, D. Bryson, G. Ciaramella, B. Roska, B. Gyorgy “High-efficiency base editing in the retina in primates and human tissues“ Nat. Med. 2025. [DOI]

A. Marchand, S. Buckley, A. Schneuing, M. Pacesa, M. Elia, P. Gainza, E. Elizarova, R. M. Neeser, P. W. Lee, L. Reymond, Y. Miao, L. Scheller, S. Georgeon, J. Schmidt, P. Schwaller, S. J. Maerkl, M. Bronstein, B. Correia “Targeting protein–ligand neosurfaces with a generalizable deep learning tool“ Nature 2025. [DOI]

A. P. Teixeira, N. Franko, M. Fussenegger “Engineering Gene and Protein Switches for Regulation of Lineage-Specifying Transcription Factors“ Biotechnol. Bioeng. 2025. [DOI]

P. Guha Ray, R. Rajasekaran, B. Pratihar, S. De, S. Dhara, M. Fussenegger “Skin-Integrated Electrogenetic Regulation of Vasculature for Accelerated Wound Healing“ Adv. Sci. 2025. [DOI]

J. Pulparayil Mathew, C. Seno, M. Jaiswal, C. Simms, N. Reichholf, D. Van den Eynden, T. N. Parac‐Vogt, J. De Roo “The Central Role of Oxo Clusters in Zirconium-Based Esterification Catalysis“ Small Sci. 2025. [DOI]

L. Fiorini, J. Koster, G. Piccini, B. Goldfuss, A. Prescimone, F. Fabris, K. Tiefenbacher, A. Scarso “Unusual Reaction of Isocyanides with Aromatic Aldehydes Catalyzed by a Supramolecular Capsule“ Chem. Eur. J. 2024. [DOI]

D. Lotter, A. Huber, J. Wellauer, O. Wenger, C. Sparr “Photoinduced Energy Transfer via an Atropisomeric Molecular Bridge“ Helv. Chim. Acta 2024. [DOI]

S. Ghosh, S. Schmid “The potential of fluorogenicity for single molecule FRET and DyeCycling“ QRB Discovery 2024. [DOI]

A. Mei, K. P. Letscher, S. Reddy “Engineering next-generation chimeric antigen receptor-T cells: recent breakthroughs and remaining challenges in design and screening of novel chimeric antigen receptor variants“ Curr. Opin. Biotechnol. 2024. [DOI]

I. Morita, A. Faraone, E. Salvisberg, K. L. Zhang, R. P. Jakob, T. Maier, T. R. Ward “Directed Evolution of an Artificial Hydroxylase Based on a Thermostable Human Carbonic Anhydrase Protein“ ACS Catal. 2024. [DOI]

O. Belli, K. Karava, R. Farouni, R. Platt “Multimodal scanning of genetic variants with base and prime editing“ Nat. Biotechnol. 2024. [DOI]

G. Renno, D. Chen, Q. X. Zhang, R. M. Gomila, A. Frontera, N. Sakai, T. R. Ward, S. Matile “Pnictogen-Bonding Enzymes“ Angew. Chem. Int. Ed. 2024. [DOI]

L. Heuberger, M. Korpidou, A. Guinart, D. Doellerer, D. M. Lopez, C. A. Schoenenberger, D. Milinkovic, E. Lörtscher, B. L. Feringa, C. G. Palivan “Photoreceptor-Like Signal Transduction Between Polymer-Based Protocells“ Adv. Mater. 2024. [DOI]

M. Mukherjee, V. Waser, E. F. Morris, N. V. Igareta, A. H. Follmer, R. P. Jakob, D. Üzümcü, T. Maier, T. R. Ward “Artificial Peroxidase Based on the Biotin–Streptavidin Technology that Rivals the Efficiency of Natural Peroxidases“ ACS Catal. 2024. [DOI]

S. Saidjalolov, F. Coelho, J. Bouffard, M. Cognet, J. Moreno, N. Rose, N. Sakai, S. Matile “Thiol-Mediated Uptake (TMU, TIMEUP)“ Chimia 2024. [DOI]

G. M. P. Giordano Attianese, S. Shui, E. Cribioli, M. Triboulet, L. Scheller, M. Hafezi, P. Reichenbach, P. Gainza, S. Georgeon, B. Correia, M. Irving “Dual ON/OFF-switch chimeric antigen receptor controlled by two clinically approved drugs“ Proc. Natl. Acad. Sci. U.S.A. 2024. [DOI]

S. Saidjalolov, X. X. Chen, J. Moreno, M. Cognet, L. Wong-Dilworth, F. Bottanelli, N. Sakai, S. Matile “Asparagusic Golgi Trackers“ JACS Au 2024. [DOI]

M. Bina, J. P. Coats, M. Skowicki, M. Malekovic, V. Mihali, C. G. Palivan “Hybrid Planar Copolymer Membranes with Dual Functionality against Bacteria Growth“ Langmuir 2024. [DOI]

G. Persiani, D. Sokolova, R. Ivanov, S. Merget, T. Maintok, D. Häussinger, K. Tiefenbacher “Catalyzing the Enantioselective Tail-to-Head Terpene Cyclization Inside Optically Active Hexameric Resorcin[4]arene Capsules: A Surprising Odd-Even Effect of the Catalyst“ Eur. J. Org. Chem. 2024. [DOI]

S. F. Berlanda, M. Breitfeld, P. Dittrich “MALDI Mass Spectrometry on High-Density Droplet Arrays: Matrix Deposition, Selective Removal, and Recrystallization“ ACS Meas. Sci. Au 2024. [DOI]

D. Pretot, M. Della Volpe Waizel, K. Kaminska, P. Valmaggia, G. Placidi, B. Falsini, F. N. Fries, N. Szentmary, C. Rivolta, H. P. N. Scholl, G. Calzetti “Retinal oxygen metabolic function in choroideremia and retinitis pigmentosa“ Graefes Arch. Clin. Exp. Ophthalmol. 2024. [DOI]

A. Jozeliunaite, S. Y. Guo, N. Sakai, S. Matile “Electric-Field Catalysis on Carbon Nanotubes in Electromicrofluidic Reactors: Monoterpene Cyclizations“ Angew. Chem. Int. Ed. 2024. [DOI]

D. Chen, X. Zhang, A. A. Vorobieva, R. Tachibana, A. Stein, R. P. Jakob, Z. Zou, D. A. Graf, A. Li, T. Maier, B. Correia, T. R. Ward “An evolved artificial radical cyclase enables the construction of bicyclic terpenoid scaffolds via an H-atom transfer pathway“ Nat. Chem. 2024. [DOI]

P. Abe, A. Lavalley, I. Morassut, A. J. Santinha, S. Roig-Puiggros, A. Javed, E. Klingler, N. Baumann, J. Prados, R. Platt, D. Jabaudon “Molecular programs guiding arealization of descending cortical pathways“ Nature 2024. [DOI]

Q. X. Zhang, G. Renno, J. J. Nué-Martinez, C. Besnard, R. M. Gomila, A. Frontera, N. Sakai, S. Matile “Pnictogen-Bonding Catalysis Compared with Ion Transport in Lipid Bilayer Membranes: Entering the Goldilocks Inverted Region“ CCS Chem. 2024. [DOI]

E. Kapetanovic, C. R. Weber, M. Bruand, D. Poschl, J. Kucharczyk, E. Hirth, C. Dietsche, R. Khan, B. Wagner, O. Belli, R. Vazquez-Lombardi, R. Castellanos-Rueda, R. B. Di Roberto, K. Kalinka, L. Raess, K. Ly, S. Rai, P. Dittrich, R. Platt, E. Oricchio, S. Reddy “Engineered allogeneic T cells decoupling T-cell-receptor and CD3 signalling enhance the antitumour activity of bispecific antibodies“ Nat. Biomed. Eng. 2024. [DOI]

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D. Monserrat Lopez, V. Grimaudo, G. Prone, A. Flisch, A. Riedo, R. Zboray, T. Lüthi, M. Mayor, M. Fussenegger, P. Broekmann, P. Wurz, E. Lörtscher “Automated, 3-D and Sub-Micron Accurate Ablation-Volume Determination by Inverse Molding and X-Ray Computed Tomography“ Adv. Sci. 2022. [DOI]

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M. Mansouri, M. Fussenegger “Electrogenetics: Bridging synthetic biology and electronics to remotely control the behavior of mammalian designer cells“ Current Opinion in Chemical Biology 2022. [DOI]

A. Bharioke, M. Munz, A. Brignall, G. Kosche, M. F. Eizinger, N. Ledergerber, D. Hillier, B. Gross-Scherf, K. Conzelmann, E. Macé, B. Roska “General anesthesia globally synchronizes activity selectively in layer 5 cortical pyramidal neurons“ Neuron 2022. [DOI]

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H. Wang, M. Xie, G. Rizzi, X. Li, K. Tan, M. Fussenegger “Identification of Sclareol As a Natural Neuroprotective Cav1.3-Antagonist Using Synthetic Parkinson-Mimetic Gene Circuits and Computer-Aided Drug Discovery“ Adv. Sci. 2022. [DOI]

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A. P. Teixeira, P. Stücheli, D. Ausländer, P. Schönenberger, S. Hürlemann, M. Fussenegger “CelloSelect – A synthetic cellobiose metabolic pathway for selection of stable transgenic CHO cell lines“ Metab. Eng. 2022. [DOI]

Z. He, A. Maynard, A. Jain, T. Gerber, R. Petri, H. Lin, M. Santel, K. Ly, J. Dupré, L. Sidow, F. Sanchis Calleja, S. M. J. Jansen, S. Riesenberg, J. G. Camp, B. Treutlein “Lineage recording in human cerebral organoids“ Nat. Methods 2022. [DOI]

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G. Gunkel-Grabole, C. G. Palivan, W. Meier “Nanostructured Surfaces through Immobilization of Self-Assembled Polymer Architectures Using Thiol–Ene Chemistry“ Macromol. Mater. Eng. 2017, 302:1600363. [DOI]

M. Garni, S. Thamboo, C. Schoenenberger, C. G. Palivan “Biopores/membrane proteins in synthetic polymer membranes“ Biochim. Biophys. Acta, Biomembr. 2017, 1859:619-38. [DOI]

Y. M. Klein, A. Lanzilotto, A. Prescimone, K. W. Krämer, S. Decurtins, S. Liu, E. C. Constable, C. E. Housecroft “Coordination behaviour of 1-(3,2':6',3''-terpyridin-4'-yl)ferrocene: structure and magnetic and electrochemical properties of a tetracopper dimetallomacrocycle“ Polyhedron 2017, 129:71-76. [DOI]

I. Craciun, G. Gunkel-Grabole, A. Belluati, C. G. Palivan, W. Meier “Expanding the potential of MRI contrast agents through multifunctional polymeric nanocarriers“ Nanomedicine 2017, 12:811-17. [DOI]

D. Alsteens, H. E. Gaub, R. Newton, M. Pfreundschuh, C. Gerber, D. J. Müller “Atomic force microscopy-based characterization and design of biointerfaces“ Nat. Rev. Mater. 2017, 2(5):17008. [DOI]

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M. Skaisgirski, X. Guo, O. Wenger “Electron Accumulation on Naphthalene Diimide Photosensitized by [Ru(2,2′-Bipyridine)3]2+“ Inorg. Chem. 2017, 56:2432-39. [DOI]

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P. Baumann, M. Spulber, O. Fischer, A. Car, W. Meier “Investigation of Horseradish Peroxidase Kinetics in an “Organelle-Like” Environment“ Small 2017, 13:1603943. [DOI] [More Information]

P. Morelli, S. Matile “Sidechain Engineering in Cell-Penetrating Poly(disulfide)s“ Helv. Chim. Acta 2017, 100. [DOI]

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Q. Zhang, L. Catti, V. R. I. Kaila, K. Tiefenbacher “To catalyze or not to catalyze: elucidation of the subtle differences between the hexameric capsules of pyrogallolarene and resorcinarene“ Chem. Sci. 2017. [DOI]

M. Bharadwaj, N. Strohmeyer, G. P. Colo, J. Helenius, N. Beerenwinkel, H. B. Schiller, R. Fässler, D. J. Müller “αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin“ Nat. Commun. 2017. [DOI]

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A. Pannwitz, A. Prescimone, O. Wenger “Ruthenium(II)–Pyridylimidazole Complexes as Photoreductants and PCET Reagents“ Eur. J. Inorg. Chem. 2017, 2017:609-15. [DOI]

L. A. Büldt, X. Guo, R. Vogel, A. Prescimone, O. Wenger “A Tris (diisocyanide) chromium (0) Complex Is a Luminescent Analog of Fe (2, 2′-Bipyridine) 32+“ J. Am. Chem. Soc. 2017, 139:985-92. [DOI]

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M. Jeschek, M. O. Bahls, V. Schneider, P. Marlière, T. R. Ward, S. Panke “Biotin-independent Strains of Escherichia coli for Enhanced Streptavidin Production“ Metab. Eng. 2017, 40:33-40. [DOI]

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N. Chuard, K. Fujisawa, P. Morelli, J. Saarbach, N. Winssinger, P. Metrangolo, G. Resnati, N. Sakai, S. Matile “Activation of Cell-Penetrating Peptides with Ionpair−π Interactions and Fluorophiles“ J. Am. Chem. Soc. 2016, 138:11264-71. [DOI]

L. A. Büldt, X. Guo, A. Prescimone, O. Wenger “A Molybdenum (0) Isocyanide Analogue of Ru (2, 2′‐Bipyridine) 32+: A Strong Reductant for Photoredox Catalysis“ Angew. Chem. Int. Ed. 2016, 55:11247-50. [DOI]

M. Jeschek, R. Reuter, T. Heinisch, C. Trindler, J. Klehr, S. Panke, T. R. Ward “Directed evolution of artificial metalloenzymes for in vivo metathesis“ Nature 2016, doi:10.1038/nature19114. [DOI] [More Information]

M. Pogson, C. Parola, W. J. Kelton, P. Heuberger, S. Reddy “Immunogenomic engineering of a plug-and-(dis)play hybridoma platform“ Nat. Commun. 2016, 7:12535. [DOI]

M. Hestericová, M. R. Correro, M. Lenz, P. F. Corvini, P. Shahgaldian, T. R. Ward “Immobilization of an artificial imine reductase within silica nanoparticles improves its performance“ Chem. Commun. 2016, 52:9462-65. [DOI]

S. J. Sigg, F. Santini, A. Najer, P. U. Richard, W. P. Meier, C. G. Palivan “Nanoparticle-based highly sensitive MRI contrast agents with enhanced relaxivity in reductive milieu“ Chem. Commun. 2016, 52:9937-40. [DOI]

Z. P. Guven, B. Ustbas, K. M. Harkness, H. Coskun, C. P. Joshi, T. M. D. Besong, F. Stellacci, O. M. Bakr, O. Akbulut “Synthesis and characterization of mixed ligand chiral nanoclusters“ Dalton Trans. 2016, 45:11297-300. [DOI]

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S. G. Keller, A. Pannwitz, F. Schwizer, J. Klehr, O. Wenger, T. R. Ward “Light-driven electron injection from a biotinylated triarylamine donor to [Ru (diimine) 3] 2+-labeled streptavidin“ Org. Biomol. Chem. 2016, 14:7197-201. [DOI]

D. Harder, S. Hirschi, Z. Ucurum, R. Goers, W. Meier, D. J. Müller, D. Fotiadis “Engineering a Chemical Switch into the Light-driven Proton Pump Proteorhodopsin by Cysteine Mutagenesis and Thiol Modification“ Angew. Chem. Int. Ed. 2016, 55:8846. [DOI]

A. Najer, D. Wu, M. G. Nussbaumer, G. Schwertz, A. Schwab, M. C. Witschel, A. Schäfer, F. Diederich, M. Rottmann, C. G. Palivan, H. Beck, W. Meier “An amphiphilic graft copolymer-based nanoparticle platform for reduction-responsive anticancer and antimalarial drug delivery“ Nanoscale 2016:DOI: 10.1039/C6NR04290B. [DOI]

Y. Okamoto, T. R. Ward, O. Wenger “From Photodriven Charge Accumulation to Fueling Enzyme Cascades in Molecular Factories“ Chimia 2016, 6:395. [DOI]

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P. Rottmann, T. R. Ward, S. Panke “Compartmentalization – A Prerequisite for Maintaining and Changing an Identity“ Chimia 2016, 6:428

C. Housecroft, C. G. Palivan, K. Gademann, W. Meier, M. Calame, V. Mikhalevich, X. Zhang, E. Piel, M. Szponarski, A. Wiesler, A. Lanzilotto, E. C. Constable, A. Fanget, R. Stoop “‘Active surfaces’ as Possible Functional Systems in Detection and Chemical (Bio) Reactivity“ Chimia 2016, 6:402. [DOI]

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M. Garni, T. Einfalt, M. Lomora, A. Car, W. Meier, C. G. Palivan “Artificial Organelles: Reactions inside Protein–Polymer Supramolecular Assemblies“ Chimia 2016, 6:424. [DOI]

S. Vujica, C. Zelmer, R. Panatala, R. Y. H. Lim “Nucleocytoplasmic Transport: A Paradigm for Molecular Logistics in Artificial Systems“ Chimia 2016, 6:413. [DOI]

A. Deplazes Zemp “Artificial Cell Research as a Field that Connects Chemical, Biological and Philosophical Questions“ Chimia 2016, 6:443. [DOI]

R. Heidari, B. Elger, R. Stutzki “On the Brink of Shifting Paradigms, Molecular Systems Engineering Ethics Needs to Take a Proactive Approach“ Chimia 2016, 6:449. [DOI]

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R. Boggavarapu, S. Hirschi, D. Harder, M. Meury, Z. Ucurum, M. J. Bergeron, D. Fotiadis “Purification of Human and Mammalian Membrane Proteins Expressed in Xenopus laevis Frog Oocytes for Structural Studies“ Heterologous Expression of Membrane Proteins 2016, 1432:223-42. [DOI]

J. Foolen, J. Shiu, M. Mitsi, Y. Zhang, C. S. Chen, V. Vogel “Full-Length Fibronectin Drives Fibroblast Accumulation at the Surface of Collagen Microtissues during Cell-Induced Tissue Morphogenesis“ PLoS One 2016, 11:e0160369. [DOI]

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P. Morelli, X. Martin-Benlloch, R. Tessier, J. Waser, N. Sakai, S. Matile “Ethynyl benziodoxolones: functional terminators for cell-penetrating poly(disulfide)s“ Polym. Chem. 2016, 7:3465-70. [DOI]

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M. Wipf, R. L. Stoop, G. Navarra, S. Rabbani, B. Ernst, K. Bedner, C. Schönenberger, M. Calame “Label-Free FimH Protein Interaction Analysis Using Silicon Nanoribbon BioFETs“ ACS Sens. 2016:DOI: 10.1021/acssensors.6b00089. [DOI]

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R. L. Stoop, M. Wipf, S. Müller, K. Bedner, I. A. Wright, C. J. Martin, E. C. Constable, A. Fanget, C. Schönenberger, M. Calame “Implementing Silicon Nanoribbon Field-Effect Transistors as Arrays for Multiple Ion Detection“ Biosensors 2016, 6:21. [DOI]

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Y. Okamoto, V. Köhler, C. E. Paul, F. Hollmann, T. R. Ward “Efficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme“ ACS Catal. 2016, 6:3553. [DOI]

M. Xie, V. Haellman, M. Fussenegger, V. Hällman “Synthetic biology-application-oriented cell engineering.“ Curr. Opin. Biotechnol. 2016, 40:139. [DOI]

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Y. Okamoto, V. Köhler, T. R. Ward “An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades“ J. Am. Chem. Soc. 2016, 138:5781. [DOI]

S. Lascano, K. Zhang, R. Wehlauch, K. Gademann, N. Sakaiab, S. Matile “The third orthogonal dynamic covalent bond“ Chem. Sci. 2016, 7:4720. [DOI]

P. Saxena, B. C. Heng, P. Bai, M. Folcher, H. Zulewski, M. Fussenegger “A programmable synthetic lineage-control network that differentiates human IPSCs into glucose-sensitive insulin-secreting beta-like cells“ Nat. Commun. 2016, 7:DOI:10.1038/ncomms11247. [DOI] [More Information]

P. Bai, H. Ye, M. Xie, P. Saxena, H. Zulewski, G. Charpin-El Hamri, V. Djonov, M. Fussenegger “A synthetic biology-based device prevents liver injury in mice“ J. Hepatol. 2016, 65:84. [DOI]

M. Akamatsu, S. Matile “Expanded Chiral Surfaces for Asymmetric Anion–π Catalysis“ Synlett 2016, 27:1041-46. [DOI]

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L. Ge, S. Villinger, S. Mari, K. Giller, C. Griesinger, S. Becker, D. J. Müller, M. Zweckstetter “Molecular Plasticity of the Human Voltage-Dependent Anion Channel Embedded Into a Membrane“ Structure 2016, 24:585-94. [DOI]

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S. J. Sigg, V. Postupalenko, J. T. Duskey, C. G. Palivan, W. Meier “Stimuli-Responsive Codelivery of Oligonucleotides and Drugs by Self-Assembled Peptide Nanoparticles“ Biomacromolecules 2016, 17:935-45. [DOI]

D. Auslaender, D. W. Fuchs, S. Huerlemann, M. Fussenegger “Engineering a ribozyme cleavage-induced split fluorescent aptamer complementation assay“ Nucleic Acids Res. 2016, 44:e94. [DOI]

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F. N. Miros, Y. Zhao, G. Sargsyan, M. Pupier, C. Besnard, C. Beuchat, J. Mareda, N. Sakai, S. Matile “Enolate Stabilization by Anion–π Interactions: Deuterium Exchange in Malonate Dilactones on π-Acidic Surfaces“ Chem. Eur. J. 2016, 22:2648-57. [DOI]

M. A. Burkhardt, J. Waser, V. Milleret, I. Gerber, M. Y. Emmert, J. Foolen, S. P. Hoerstrup, F. Schlottig, V. Vogel “Synergistic interactions of blood-borne immune cells, fibroblasts and extracellular matrix drive repair in an in vitro peri-implant wound healing model“ Sci. Rep. 2016, 6:21071. [DOI]

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T. Szikra, S. Trenholm, A. Drinnenberg, J. Jüttner, Z. Raics, K. Farrow, M. Biel, G. Awatramani, D. A. Clark, J. A. Sahel, R. Azeredo da Silveira, B. Roska “Rods in daylight act as relay cells for cone-driven horizontal cell–mediated surround inhibition“ Nat. Neurosci. 2014, 17:1728. [DOI]

K. Fujisawa, C. Beuchat, M. Humbert-Droz, A. Wilson, T. A. Wesolowski, J. Mareda, N. Sakai, S. Matile “Anion-π and cation-π interactions on the same surface“ Angew. Chem. Int. Ed. 2014, 53:11266-9. [DOI]

D. Steuerwald, S. M. Fruh, R. Griss, R. D. Lovchik, V. Vogel “Nanoshuttles propelled by motor proteins sequentially assemble molecular cargo in a microfluidic device“ Lab Chip 2014, 14:3729-38. [DOI]

F. N. Miros, G. Huang, Y. Zhao, N. Sakai, S. Matile “Coumarin synthesis on π-acidic surfaces“ Supramol. Chem. 2014, 27:303-09. [DOI]

K. Yonehara, B. Roska “Neuroscience: retinal projectome reveals organizing principles of the visual system“ Curr. Biol. 2014, 24:R833-5. [DOI]

H. Hayashi, A. Sobczuk, A. Bolag, N. Sakai, S. Matile “Antiparallel three-component gradients in double-channel surface architectures“ Chem. Sci. 2014, 5:4610-14. [DOI]

D. Wu, M. Spulber, F. Itel, M. Chami, T. Pfohl, C. G. Palivan, W. Meier “Effect of Molecular Parameters on the Architecture and Membrane Properties of 3D Assemblies of Amphiphilic Copolymers“ Macromolecules 2014, 47:5060-69. [DOI]

T. Cronin, L. H. Vandenberghe, P. Hantz, J. Juttner, A. Reimann, A. E. Kacsó, R. M. Huckfeldt, V. Busskamp, H. Kohler, P. S. Lagali, B. Roska, J. Bennett “Efficient transduction and optogenetic stimulation of retinal bipolar cells by a synthetic adeno-associated virus capsid and promoter“ EMBO Mol. Med. 2014, 6:1175. [DOI]

P. Baumann, M. Spulber, I. A. Dinu, C. G. Palivan “Cellular Trojan Horse Based Polymer Nanoreactors with Light-sensitive Activity“ J. Phys. Chem. B 2014, 118:9361. [DOI]

A. S. Chuong, M. L. Miri, V. Busskamp, G. A. C. Matthews, L. C. Acker, A. T. Sørensen, A. Young, N. C. Klapoetke, M. A. Henninger, S. B. Kodandaramaiah, M. Ogawa, S. B. Ramanlal, R. C. Bandler, B. D. Allen, C. R. Forest, B. Y. Chow, X. Han, Y. Lin, K. M. The, B. Roska, J. A. Cardin, E. S. Boyden “Noninvasive optical inhibition with a red-shifted microbial rhodopsin “ Nat. Neurosci. 2014, 17:1123. [DOI]

V. Busskamp, J. Krol, D. Nelidova, J. Daum, T. Szikra, B. Tsuda, J. Jüttner, K. Farrow, B. Gross Scherf, C. P. Patino Alvarez, C. Genoud, V. Sothilingam, N. Tanimoto, M. Stadler, M. Seeliger, M. Stoffel, W. Filipowicz, B. Roska “miRNAs 182 and 183 Are Necessary to Maintain Adult Cone Photoreceptor Outer Segments and Visual Function“ Neuron 2014, 83:586. [DOI]

R. A. Kellogg, R. Gomez-Sjoberg, A. A. Leyrat, S. Tay “High-throughput microfluidic single-cell analysis pipeline for studies of signaling dynamics“ Nat. Protoc. 2014, 9:1713-26. [DOI]

K. D. Schleicher, S. L. Dettmer, L. E. Kapinos, S. Pagliara, U. F. Keyser, S. Jeney, R. Y. H. Lim “Selective transport control on molecular velcro made from intrinsically disordered proteins“ Nat. Nanotechnol. 2014, 9:525. [DOI]

A. V. Jentzsch, S. Matile “Anion transport with halogen bonds“ Halogen Bonding I 2014:205-39. [DOI]

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Project management	Persons involved	[grouplink]
Murielle Delley	N.N.	Delley group @UniBas
Sonja Schmid	N.N.	Schmid group @UniBas
Randall Platt	N.N.	Platt group @D-BSSE
Florian Seebeck	N.N.	Seebeck group @UniBas
Bruno Correia	N.N.	Correia group @EPFL
Basile Wicky	N.N.	Wicky group @D-BSSE
Jonathan De Roo	N.N.	De Roo group @UniBas
Christof Sparr	N.N.	Sparr group @UniBas
Marcel Mayor	N.N.	Mayor group @UniBas
Sven Panke	N.N.	Panke group @D-BSSE
Dimitrios Fotiadis	N.N.	Fotiadis group @UniBe
Botond Roska	N.N.	Roska group @IOB
Effy Vayena	N.N.	Vayena group @ETHZ
Sai Reddy	N.N.	Reddy group @D-BSSE
Oliver Wenger	N.N.	Wenger group @UniBas
Jörg Stelling	N.N.	Stelling group @D-BSSE
Thomas R. Ward	N.N.	Ward group @UniBas
Daniel J. Müller	N.N.	Müller group @D-BSSE
Martin Fussenegger	N.N.	Fussenegger group @D-BSSE
Petra Dittrich	N.N.	Dittrich group @D-BSSE

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Scientific Highlights

Scientific Highlight

Publications