@misc{BaumannArndtMueller2013,
  author    = {Baumann, Tobias and Arndt, Katja Maren and M{\"u}ller, Kristian M.},
  title     = {Directional cloning of DNA fragments using deoxyinosine-containing oligonucleotides and endonuclease V},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {983},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-43108},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-431085},
  pages     = {13},
  year      = {2013},
  abstract  = {Background: DNA fragments carrying internal recognition sites for the restriction endonucleases intended for cloning into a target plasmid pose a challenge for conventional cloning. Results: A method for directional insertion of DNA fragments into plasmid vectors has been developed. The target sequence is amplified from a template DNA sample by PCR using two oligonucleotides each containing a single deoxyinosine base at the third position from the 5' end. Treatment of such PCR products with endonuclease V generates 3' protruding ends suitable for ligation with vector fragments created by conventional restriction endonuclease reactions. Conclusions: The developed approach generates terminal cohesive ends without the use of Type II restriction endonucleases, and is thus independent from the DNA sequence. Due to PCR amplification, minimal amounts of template DNA are required. Using the robust Taq enzyme or a proofreading Pfu DNA polymerase mutant, the method is applicable to a broad range of insert sequences. Appropriate primer design enables direct incorporation of terminal DNA sequence modifications such as tag addition, insertions, deletions and mutations into the cloning strategy. Further, the restriction sites of the target plasmid can be either retained or removed.},
  language  = {en}
}
@article{FeinerTeschnerTeschneretal.2019,
  author    = {Feiner, Rebecca Christine and Teschner, Julian and Teschner, Kathrin E. and Radukic, Marco T. and Baumann, Tobias and Hagen, Sven and Hannappel, Yvonne and Biere, Niklas and Anselmetti, Dario and Arndt, Katja Maren and M{\"u}ller, Kristian Mark},
  title     = {rAAV Engineering for Capsid-Protein Enzyme Insertions and Mosaicism Reveals Resilience to Mutational, Structural and Thermal Perturbations},
  series = {International journal of molecular sciences},
  volume    = {20},
  journal   = {International journal of molecular sciences},
  number    = {22},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1422-0067},
  doi       = {10.3390/ijms20225702},
  pages     = {19},
  year      = {2019},
  abstract  = {Recombinant adeno-associated viruses (rAAV) provide outstanding options for customization and superior capabilities for gene therapy. To access their full potential, facile genetic manipulation is pivotal, including capsid loop modifications. Therefore, we assessed capsid tolerance to modifications of the structural VP proteins in terms of stability and plasticity. Flexible glycine-serine linkers of increasing sizes were, at the genetic level, introduced into the 587 loop region of the VP proteins of serotype 2, the best studied AAV representative. Analyses of biological function and thermal stability with respect to genome release of viral particles revealed structural plasticity. In addition, insertion of the 29 kDa enzyme beta-lactamase into the loop region was tested with a complete or a mosaic modification setting. For the mosaic approach, investigation of VP2 trans expression revealed that a Kozak sequence was required to prevent leaky scanning. Surprisingly, even the full capsid modification with beta-lactamase allowed for the assembly of capsids with a concomitant increase in size. Enzyme activity assays revealed lactamase functionality for both rAAV variants, which demonstrates the structural robustness of this platform technology.},
  language  = {en}
}
@article{BaumannArndtMueller2013,
  author    = {Baumann, Tobias and Arndt, Katja Maren and M{\"u}ller, Kristian M.},
  title     = {Directional cloning of DNA fragments using deoxyinosine-containing oligonucleotides and endonuclease V},
  series = {BMC biotechnology},
  volume    = {13},
  journal   = {BMC biotechnology},
  number    = {10},
  publisher = {BioMed Central},
  address   = {London},
  issn      = {1472-6750},
  doi       = {10.1186/1472-6750-13-81},
  pages     = {11},
  year      = {2013},
  abstract  = {Background: DNA fragments carrying internal recognition sites for the restriction endonucleases intended for cloning into a target plasmid pose a challenge for conventional cloning. Results: A method for directional insertion of DNA fragments into plasmid vectors has been developed. The target sequence is amplified from a template DNA sample by PCR using two oligonucleotides each containing a single deoxyinosine base at the third position from the 5' end. Treatment of such PCR products with endonuclease V generates 3' protruding ends suitable for ligation with vector fragments created by conventional restriction endonuclease reactions. Conclusions: The developed approach generates terminal cohesive ends without the use of Type II restriction endonucleases, and is thus independent from the DNA sequence. Due to PCR amplification, minimal amounts of template DNA are required. Using the robust Taq enzyme or a proofreading Pfu DNA polymerase mutant, the method is applicable to a broad range of insert sequences. Appropriate primer design enables direct incorporation of terminal DNA sequence modifications such as tag addition, insertions, deletions and mutations into the cloning strategy. Further, the restriction sites of the target plasmid can be either retained or removed.},
  language  = {en}
}
@article{JedrusikBodeStudenckaSmolkaetal.2013,
  author    = {Jedrusik-Bode, Monika and Studencka, Maja and Smolka, Christian and Baumann, Tobias and Schmidt, Henning and Kampf, Jan and Paap, Franziska and Martin, Sophie and Tazi, Jamal and M{\"u}ller, Kristian M. and Kr{\"u}ger, Marcus and Braun, Thomas and Bober, Eva},
  title     = {The sirtuin SIRT6 regulates stress granule formation in C. elegans and mammals},
  series = {Journal of cell science},
  volume    = {126},
  journal   = {Journal of cell science},
  number    = {22},
  publisher = {Company of Biologists Limited},
  address   = {Cambridge},
  issn      = {0021-9533},
  doi       = {10.1242/jcs.130708},
  pages     = {5166 -- +},
  year      = {2013},
  abstract  = {SIRT6 is a NAD(+)-dependent deacetylase that modulates chromatin structure and safeguards genomic stability. Until now, SIRT6 has been assigned to the nucleus and only nuclear targets of SIRT6 are known. Here, we demonstrate that in response to stress, C. elegans SIR-2.4 and its mammalian orthologue SIRT6 localize to cytoplasmic stress granules, interact with various stress granule components and induce their assembly. Loss of SIRT6 or inhibition of its catalytic activity in mouse embryonic fibroblasts impairs stress granule formation and delays disassembly during recovery, whereas deficiency of SIR-2.4 diminishes maintenance of P granules and decreases survival of C. elegans under stress conditions. Our findings uncover a novel, evolutionary conserved function of SIRT6 in the maintenance of stress granules in response to stress.},
  language  = {en}
}
@phdthesis{Baumann2013,
  author    = {Baumann, Tobias},
  title     = {Stability and Interconnected protein properties studied with TEM ß-lactamase},
  address   = {Potsdam},
  pages     = {155 S.},
  year      = {2013},
  language  = {en}
}
@article{HagenBaumannWagneretal.2014,
  author    = {Hagen, Sven and Baumann, Tobias and Wagner, Hanna J. and Morath, Volker and Kaufmann, Beate and Fischer, Adrian and Bergmann, Stefan and Schindler, Patrick and Arndt, Katja Maren and Mueller, Kristian M.},
  title     = {Modular adeno-associated virus (rAAV) vectors used for cellular virus-directed enzyme prodrug therapy},
  series = {Scientific reports},
  volume    = {4},
  journal   = {Scientific reports},
  publisher = {Nature Publ. Group},
  address   = {London},
  issn      = {2045-2322},
  doi       = {10.1038/srep03759},
  pages     = {11},
  year      = {2014},
  abstract  = {The pre-clinical and clinical development of viral vehicles for gene transfer increased in recent years, and a recombinant adeno-associated virus (rAAV) drug took center stage upon approval in the European Union. However, lack of standardization, inefficient purification methods and complicated retargeting limit general usability. We address these obstacles by fusing rAAV-2 capsids with two modular targeting molecules (DARPin or Affibody) specific for a cancer cell-surface marker (EGFR) while simultaneously including an affinity tag (His-tag) in a surface-exposed loop. Equipping these particles with genes coding for prodrug converting enzymes (thymidine kinase or cytosine deaminase) we demonstrate tumor marker specific transduction and prodrug-dependent apoptosis of cancer cells. Coding terminal and loop modifications in one gene enabled specific and scalable purification. Our genetic parts for viral production adhere to a standardized cloning strategy facilitating rapid prototyping of virus directed enzyme prodrug therapy (VDEPT).},
  language  = {en}
}
@article{KuekenshoenerHagemannWohlwendetal.2014,
  author    = {Kuekenshoener, Tim and Hagemann, Urs B. and Wohlwend, Daniel and Raeuber, Christina and Baumann, Tobias and Keller, Sandro and Einsle, Oliver and Mueller, Kristian M. and Arndt, Katja Maren},
  title     = {Analysis of Selected and Designed Chimeric D- and L-alpha-Helix Assemblies},
  series = {Biomacromolecules : an interdisciplinary journal focused at the interface of polymer science and the biological sciences},
  volume    = {15},
  journal   = {Biomacromolecules : an interdisciplinary journal focused at the interface of polymer science and the biological sciences},
  number    = {9},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1525-7797},
  doi       = {10.1021/bm5006883},
  pages     = {3296 -- 3305},
  year      = {2014},
  abstract  = {D-Peptides have been attributed pharmacological advantages over regular L-peptides, yet design rules are largely unknown. Based on a designed coiled coil-like D/L heterotetramer, named L-Base/D-Acid, we generated a library offering alternative residues for interaction with the D-peptide. Phage display selection yielded one predominant peptide, named HelixA, that differed at 13 positions from the scaffold helix. In addition to the observed D-/L-heterotetramers, ratio-dependent intermediate states were detected by isothermal titration calorimetry. Importantly, the formation of the selected HelixA/D-Acid bundle passes through fewer intermediate states than L-Base/D-Acid. Back mutation of HelixA core residues to L-Base (HelixLL) revealed that the residues at e/g-positions are responsible for the different intermediates. Furthermore, a Val-core variant (PeptideVV) was completely devoid of binding D-Acid, whereas an Ile-core helix (HelixII) interacted with D-Acid in a significantly more specific complex than L-Base.},
  language  = {en}
}
@book{ZhangPlauthEberhardtetal.2020,
  author    = {Zhang, Shuhao and Plauth, Max and Eberhardt, Felix and Polze, Andreas and Lehmann, Jens and Sejdiu, Gezim and Jabeen, Hajira and Servadei, Lorenzo and M{\"o}stl, Christian and B{\"a}r, Florian and Netzeband, Andr{\´e} and Schmidt, Rainer and Knigge, Marlene and Hecht, Sonja and Prifti, Loina and Krcmar, Helmut and Sapegin, Andrey and Jaeger, David and Cheng, Feng and Meinel, Christoph and Friedrich, Tobias and Rothenberger, Ralf and Sutton, Andrew M. and Sidorova, Julia A. and Lundberg, Lars and Rosander, Oliver and Sk{\"o}ld, Lars and Di Varano, Igor and van der Walt, Est{\´e}e and Eloff, Jan H. P. and Fabian, Benjamin and Baumann, Annika and Ermakova, Tatiana and Kelkel, Stefan and Choudhary, Yash and Cooray, Thilini and Rodr{\´i}guez, Jorge and Medina-P{\´e}rez, Miguel Angel and Trejo, Luis A. and Barrera-Animas, Ari Yair and Monroy-Borja, Ra{\´u}l and L{\´o}pez-Cuevas, Armando and Ram{\´i}rez-M{\´a}rquez, Jos{\´e} Emmanuel and Grohmann, Maria and Niederleithinger, Ernst and Podapati, Sasidhar and Schmidt, Christopher and Huegle, Johannes and de Oliveira, Roberto C. L. and Soares, F{\´a}bio Mendes and van Hoorn, Andr{\´e} and Neumer, Tamas and Willnecker, Felix and Wilhelm, Mathias and Kuster, Bernhard},
  title     = {HPI Future SOC Lab - Proceedings 2017},
  number    = {130},
  editor    = {Meinel, Christoph and Polze, Andreas and Beins, Karsten and Strotmann, Rolf and Seibold, Ulrich and R{\"o}dszus, Kurt and M{\"u}ller, J{\"u}rgen},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  isbn      = {978-3-86956-475-3},
  issn      = {1613-5652},
  doi       = {10.25932/publishup-43310},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-433100},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {ix, 235},
  year      = {2020},
  abstract  = {The "HPI Future SOC Lab" is a cooperation of the Hasso Plattner Institute (HPI) and industry partners. Its mission is to enable and promote exchange and interaction between the research community and the industry partners. The HPI Future SOC Lab provides researchers with free of charge access to a complete infrastructure of state of the art hard and software. This infrastructure includes components, which might be too expensive for an ordinary research environment, such as servers with up to 64 cores and 2 TB main memory. The offerings address researchers particularly from but not limited to the areas of computer science and business information systems. Main areas of research include cloud computing, parallelization, and In-Memory technologies. This technical report presents results of research projects executed in 2017. Selected projects have presented their results on April 25th and November 15th 2017 at the Future SOC Lab Day events.},
  language  = {en}
}
@book{RanaMohapatraSidorovaetal.2022,
  author    = {Rana, Kaushik and Mohapatra, Durga Prasad and Sidorova, Julia and Lundberg, Lars and Sk{\"o}ld, Lars and Lopes Grim, Lu{\´i}s Fernando and Sampaio Gradvohl, Andr{\´e} Leon and Cremerius, Jonas and Siegert, Simon and Weltzien, Anton von and Baldi, Annika and Klessascheck, Finn and Kalancha, Svitlana and Lichtenstein, Tom and Shaabani, Nuhad and Meinel, Christoph and Friedrich, Tobias and Lenzner, Pascal and Schumann, David and Wiese, Ingmar and Sarna, Nicole and Wiese, Lena and Tashkandi, Araek Sami and van der Walt, Est{\´e}e and Eloff, Jan H. P. and Schmidt, Christopher and H{\"u}gle, Johannes and Horschig, Siegfried and Uflacker, Matthias and Najafi, Pejman and Sapegin, Andrey and Cheng, Feng and Stojanovic, Dragan and Stojnev Ilić, Aleksandra and Djordjevic, Igor and Stojanovic, Natalija and Predic, Bratislav and Gonz{\´a}lez-Jim{\´e}nez, Mario and de Lara, Juan and Mischkewitz, Sven and Kainz, Bernhard and van Hoorn, Andr{\´e} and Ferme, Vincenzo and Schulz, Henning and Knigge, Marlene and Hecht, Sonja and Prifti, Loina and Krcmar, Helmut and Fabian, Benjamin and Ermakova, Tatiana and Kelkel, Stefan and Baumann, Annika and Morgenstern, Laura and Plauth, Max and Eberhard, Felix and Wolff, Felix and Polze, Andreas and Cech, Tim and Danz, Noel and Noack, Nele Sina and Pirl, Lukas and Beilharz, Jossekin Jakob and De Oliveira, Roberto C. L. and Soares, F{\´a}bio Mendes and Juiz, Carlos and Bermejo, Belen and M{\"u}hle, Alexander and Gr{\"u}ner, Andreas and Saxena, Vageesh and Gayvoronskaya, Tatiana and Weyand, Christopher and Krause, Mirko and Frank, Markus and Bischoff, Sebastian and Behrens, Freya and R{\"u}ckin, Julius and Ziegler, Adrian and Vogel, Thomas and Tran, Chinh and Moser, Irene and Grunske, Lars and Sz{\´a}rnyas, G{\´a}bor and Marton, J{\´o}zsef and Maginecz, J{\´a}nos and Varr{\´o}, D{\´a}niel and Antal, J{\´a}nos Benjamin},
  title     = {HPI Future SOC Lab - Proceedings 2018},
  number    = {151},
  editor    = {Meinel, Christoph and Polze, Andreas and Beins, Karsten and Strotmann, Rolf and Seibold, Ulrich and R{\"o}dszus, Kurt and M{\"u}ller, J{\"u}rgen},
  publisher = {Universit{\"a}tsverlag Potsdam},
  address   = {Potsdam},
  isbn      = {978-3-86956-547-7},
  issn      = {1613-5652},
  doi       = {10.25932/publishup-56371},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-563712},
  publisher      = {Universit{\"a}t Potsdam},
  pages     = {x, 277},
  year      = {2022},
  abstract  = {The "HPI Future SOC Lab" is a cooperation of the Hasso Plattner Institute (HPI) and industry partners. Its mission is to enable and promote exchange and interaction between the research community and the industry partners. The HPI Future SOC Lab provides researchers with free of charge access to a complete infrastructure of state of the art hard and software. This infrastructure includes components, which might be too expensive for an ordinary research environment, such as servers with up to 64 cores and 2 TB main memory. The offerings address researchers particularly from but not limited to the areas of computer science and business information systems. Main areas of research include cloud computing, parallelization, and In-Memory technologies. This technical report presents results of research projects executed in 2018. Selected projects have presented their results on April 17th and November 14th 2017 at the Future SOC Lab Day events.},
  language  = {en}
}