@article{BrechunZhenJaikaranetal.2019,
  author    = {Brechun, Katherine E. and Zhen, Danlin and Jaikaran, Anna and Borisenko, Vitali and Kumauchi, Masato and Hoff, Wouter D. and Arndt, Katja Maren and Woolley, Andrew G},
  title     = {Detection of Incorporation of p-Coumaric Acid into Photoactive Yellow Protein Variants in Vivo},
  series = {Biochemistry},
  volume    = {58},
  journal   = {Biochemistry},
  number    = {23},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0006-2960},
  doi       = {10.1021/acs.biochem.9b00279},
  pages     = {2682 -- 2694},
  year      = {2019},
  abstract  = {We report the design and characterization of photoactive yellow protein (PYP)-blue fluorescent protein (mTagBFP) fusion constructs that permit the direct assay of reconstitution and function of the PYP domain. These constructs allow for in vivo testing of co-expression systems for enzymatic production of the p-coumaric acid-based PYP chromophore, via the action of tyrosine ammonia lyase and p-coumaroyl-CoA ligase (pCL or 4CL). We find that different 4CL enzymes can function to reconstitute PYP, including 4CL from Arabidopsis thaliana that can produce similar to 100\% holo-PYP protein under optimal conditions. mTagBFP fusion constructs additionally enable rapid analysis of effects of mutations on PYP photocycles. We use this mTagBFP fusion strategy to demonstrate in vivo reconstitution of several PYP-based optogenetic tools in Escherichia coli via a biosynthesized chromophore, an important step for the use of these optogenetic tools in vivo in diverse hosts.},
  language  = {en}
}
@misc{BrechunWoolleyArndt2017,
  author    = {Brechun, Katherine E. and Woolley, Andrew and Arndt, Katja Maren},
  title     = {A Bacterial Bandpass Assay for Protein-Protein Interactions},
  series = {Protein science : a publication of the Protein Society},
  volume    = {26},
  journal   = {Protein science : a publication of the Protein Society},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {0961-8368},
  pages     = {198 -- 198},
  year      = {2017},
  language  = {en}
}
@article{BrechunArndtWoolley2017,
  author    = {Brechun, Katherine E. and Arndt, Katja Maren and Woolley, G. Andrew},
  title     = {Strategies for the photo-control of endogenous protein activity},
  series = {Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers},
  volume    = {45},
  journal   = {Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers},
  publisher = {Elsevier},
  address   = {London},
  issn      = {0959-440X},
  doi       = {10.1016/j.sbi.2016.11.014},
  pages     = {53 -- 58},
  year      = {2017},
  language  = {en}
}
@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{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}
}
@misc{AzumaKuekenshoenerMaetal.2014,
  author    = {Azuma, Yusuke and K{\"u}kensh{\"o}ner, Tim and Ma, Guangyong and Yasunaga, Jun-ichiro and Imanishi, Miki and Tanaka, Gen and Nakase, Ikuhiko and Maruno, Takahiro and Kobayashi, Yuji and Arndt, Katja Maren and Matsuoka, Masao and Futaki, Shiroh},
  title     = {Controlling leucine-zipper partner recognition in cells through modification of a-g interactions},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-98758},
  pages     = {4},
  year      = {2014},
  abstract  = {By focusing on the a-g interactions, successful design and selection were accomplished to obtain a leucine-zipper segment that discriminates the appropriate partner over another that provides very similar patterns of electrostatic interactions.},
  language  = {en}
}
@article{AzumaKuekenshoenerMaetal.2014,
  author    = {Azuma, Yusuke and Kuekenshoener, Tim and Ma, Guangyong and Yasunaga, Jun-ichiro and Imanishi, Miki and Tanaka, Gen and Nakase, Ikuhiko and Maruno, Takahiro and Kobayashi, Yuji and Arndt, Katja Maren and Matsuoka, Masao and Futaki, Shiroh},
  title     = {Controlling leucine-zipper partner recognition in cells through modification of a-g interactions},
  series = {Chemical communications},
  volume    = {50},
  journal   = {Chemical communications},
  number    = {48},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1359-7345},
  doi       = {10.1039/c4cc00555d},
  pages     = {6364 -- 6367},
  year      = {2014},
  abstract  = {By focusing on the a-g interactions, successful design and selection were accomplished to obtain a leucine-zipper segment that discriminates the appropriate partner over another that provides very similar patterns of electrostatic interactions.},
  language  = {en}
}
@book{Arndt2010,
  author    = {Arndt, Katja Maren},
  title     = {Proteine zur Krebstherapie - Zielen, Steuern, Hemmen : Antrittsvorlesung 2010-12-08},
  publisher = {Univ.-Bibl.},
  address   = {Potsdam},
  year      = {2010},
  abstract  = {Biotechnologie, Biologie, Protein Engineering, Therapeutische Peptide, Protein Design, Selektionssysteme / biotechnology, biology, protein enginieering, therapeutic peptides, protein design, selection systems},
  language  = {de}
}