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RESEARCH - H. D. Mootz - General publication list




  • Jedlitzke, B., Yilmaz, Z., Dörner, W., Mootz, H. D.
    Photobodies: Light-activatable single-domain antibody fragments.
    Angew. Chem Int. Ed., 2020, epub 2019 Nov 22, doi: 10.1002/anie.201912286.

2019 - 2010



  • Bhagawati, M., Terhorst, T. M. E., Füsser, F., Hoffmann, S., Pasch, T., Pietrokovski, S., Mootz, H. D.
    A mesophilic cysteine-less split intein for protein trans-splicing applications under oxidizing conditions.
    Proc. Natl. Acad. Sci. U S A, 2019, 116, 22164-22172, doi: 10.1073/pnas.1909825116.

  • Kötter, A., Mootz, H. D., Heuer, A.
    Standard binding free energy of a SIM-SUMO complex.
    J. Chem. Theory Comput., 2019, 15, 6403-6410, doi: 10.1021/acs.jctc.9b00428.

  • Reille-Seroussi, M., Mayer, S. V., Dörner, W., Lang, K., Mootz, H. D.
    Expanding the genetic code with a lysine derivate bearing an enzymatically removable phenylacetyl group.
    Chem. Comm. (Camb), 2019, 55, 4793-4796, doi: 10.1039/c9cc00475k.

  • Degen, A., Mayerthaler, F., Mootz, H. D., Di Ventura, B.
    Context-dependent activity of A domains in the tyrocidine synthetase.
    Sci. Reports, 2019, 9, 5119, doi: 10.1038/s41598-019-41492-8.

  • Böcker, J. K., Dörner, W., Mootz. H. D.
    Light-control of the ultra-fast Gp41-1 split intein with preserved stability of a genetically encoded photo-caged amino acid in bacterial cells.
    Chem. Comm. (Camb), 2019, 55, 1287-1290, doi: 10.1039/c8cc09204d.

  • Böcker, J. K., Dörner, W., Mootz, H. D.
    Rational design of an improved photo-activatable intein for the production of head-to-tail cyclized peptides
    Biol. Chem., 2019, 400, 417-427, doi: 10.1515/hsz-2018-0367.

  • Palei, S., Becher, K. S., Nienberg, C., Jose, J., Mootz, H. D.
    Bacterial cell surface display of semisynthetic cyclic peptides
    ChemBioChem., 2019, 20, 72-77, doi: 10.1002/cbic.201800552.

  • Friedel, K., Popp, M., Matern, J. C. J., Gazdag, E. M., Thiel, I. V., Volkmann, G., Blankenfeldt, W., Mootz, H. D.
    A functional interplay between intein and extein sequence in protein splicing compensates for the essential block B histidine
    Chem. Sci., 2019, 10, 239-251, doi: 10.1039/C8SC01074A.

  • Di Ventura, B., Mootz, H. D.
    Switchable inteins for conditional protein splicing
    Biol. Chem., 2019, 400, 467-475, doi: 10.1515/hsz-2018-0309.



  • Hagmann, V., Sommer, S., Fabian, P., Bierlmeier, J., van Treel, N., Mootz, H. D., Schwarzer, D., Azevedo, J. E., Dodt, G.
    Chemically monoubiquitinated PEX5 binds to the peroxisomal docking and export complex.
    Sci. Reports, 2018, 8, 16014. DOI:10.1038/s41598-018-34200-5.

  • Grill, D., Matos, A. L. L., de Vries, W. C., Kudruk, S., Heflik, M., Dörner, W., Mootz, H. D., Ravoo, B. J., Galla, H.-J., Gerke, V.
    Bridging of membrane surfaces by annexin A2
    Sci. Reports, 2018, 8, 14662. doi: 10.1038/s41598-018-33044-3.

  • Matern, J. C. J., Friedel, K., Binschik, J., Becher, K.-S., Yilmaz, Z., Mootz, H. D.
    Altered coordination of individual catalytic steps in different and evolved inteins reveals kinetic plasticity of the protein splicing pathway
    J. Am. Chem. Soc., 2018, 140, 11267-11275. doi: 10.1021/jacs.8b04794.

  • Pirzer, T., Becher, K.-S., Rieker, M., Meckel, T., Mootz, H. D., Kolmar, H.
    Generation of potent anti-HER1/2 immunotoxins by protein ligation using split inteins
    ACS Chem. Biol., 2018, 13, 2058-2066. doi: 10.1021/acschembio.8b00222.

  • Kost, L. J., Mootz, H. D.
    A FRET sensor to monitor bivalent SUMO-SIM interactions in SUMO chain binding
    ChemBioChem, 2018, 19, 177-184. dx.doi.org/10.1002/cbic.201700507



  • Moll, J. M., Wehmöller, M., Frank, N. C., Homey, L., Baran, P., Garbers, C., Lamertz, L., Axelrod, J. H., Galun, E., Mootz, H. D., Scheller, J.
    Split2 protein-ligation generates active IL-6-type Hyper-cytokines from inactive precursors
    ACS Synth. Biol., 2017, 6, 2260-2272. DOI: 10.1021/acssynbio.7b00208

  • Alfermann, J., Sun, X., Mayerthaler, F., Morrell, T. E., Dehling, E., Volkmann, G., Komatsuzaki, T., Yang, H., Mootz, H. D.
    FRET monitoring of a nonribosomal peptide synthetase.
    Nat. Chem. Biol., 2017, 13, 1009-1015. DOI:10.1038/nchembio.2435.

  • Falkenberg, K. D., Jakobs, A., Matern, J. C., Dörner, W., Uttarkar, S., Trentmann, A., Steinmann, S., Coulibaly, A., Schomburg, C., Mootz, H. D., Schmidt, T. J., Klempnauer, K.-H.
    Withaferin A, a natural compound with anti-tumor activity, is a potent inhibitor of transcription factor C/EBPβ
    Biochim. Biophys. Acta, 2017, 1864, 1349-1358, DOI: 10.1016/j.bbamcr.2017.05.003

  • Bachmann, A.-L., Mootz, H. D.
    N-terminal chemical protein labeling using the naturally split GOS-TerL intein.
    J. Pep. Sci, 2017, 23, 624-630. DOI: 10.1002/psc.2996.

  • Taupitz, K. F., Dörner, W., Mootz, H. D.
    Covalent capturing of transient SUMO-SIM interactions using unnatural amino acid mutagenesis and photocrosslinking.
    Chem. Eur. J., 2017, 23, 5878-5982 DOI: 10.1002/chem.201605619.
    Selected as "hot" paper by the editors.

  • Neugebauer, M., Böcker, J. K., Matern, J. C. J., Pietrokovski, S., Mootz, H. D.
    Development of a screening system for inteins active in protein splicing based on intein insertion into the LacZα-peptide.
    Biol. Chem., 2017, 398, 57-67. DOI: 10.1515/hsz-2016-0229.

  • Palei, S., Mootz, H. D.
    Preparation of semisynthetic peptide macrocycles using split inteins.
    Methods Mol. Biol., 2017, 1495, 77-92. DOI: 10.1007/978-1-4939-6451-2_6

  • Mootz, H. D. (issue editor)
    Split inteins: Methods and Protocols, Springer, Humana press.
    Methods Mol. Biol., 2017, ISBN 978-1-4939-6449-9.



  • Dehling*, E., Volkmann*, G., Matern, J. C. J., Dörner, W., Alfermann, J., Diecker, J., Mootz, H. D.
    Mapping of the communication-mediating interface in nonribosomal peptide synthetases using a genetically encoded photocrosslinker supports an upside-down helix-hand motif.
    J. Mol. Biol., 2016, 428, 4345-4360. DOI:10.1016/j.jmb.2016.09.007.

  • Nienberg, C., Retterath, A., Becher, K. S., Saenger, T., Mootz, H. D., Jose, J.
    Site-specific labeling of protein kinase CK2: Combining surface display and click chemistry for drug discovery applications.
    Pharmaceuticals, 2016, 9, 36. doi: 10.3390/ph9030036.

  • Palei, S., Mootz, H. D.
    Cyclic peptides made by linking synthetic and genetically encoded fragments.
    ChemBioChem, 2016, 17, 378-382. DOI: 10.1002/cbic.201500673.



  • Fischle, W., Mootz, H. D., Schwarzer, D.
    Synthetic histone code.
    Curr. Opin. Chem. Biol., 2015, 28, 131-140. DOI: 10.1016/j.cbpa.2015.07.005.

  • Bachmann, A.-L., Mootz, H. D.
    An unprecedented combination of serine and cysteine nucleophiles in a split intein with an atypical split site.
    J. Biol. Chem., 2015, 290, 28792-28804. DOI: 10.1074/jbc.M115.677237.

  • Fischle, W., Schwarzer, D., Mootz, H. D.
    Chromatin chemistry goes cellular.
    Nat. Chem., 2015, 7, 371-373. DOI: 10.1038/nchem.2249.

  • Sommer, S.,# Ritterhof, T.,# Melchior, F., Mootz, H. D.
    A stable chemical SUMO1-Ubc9 conjugate specifically binds as a thioester mimic to the RanBP2 E3-ligase complex.
    ChemBioChem, 2015, 16, 1183-1189. DOI: 10.1002/cbic.201500011
    # contributed equally

  • Böcker, J. K., Friedel, K., Matern, J. C. Bachmann, A.-L., Mootz, H. D.
    Generation of a genetically encoded, photoactivatable intein for the controlled production of cyclic peptides.
    Angew. Chem. Int. Ed., 2015, 54, 2116-2120. DOI: 10.1002/anie.201409848
    Angew. Chem., 2015, 127, 2144-2148. DOI: 10.1002/ange.201409848

  • Bachmann, A.-L., Matern, J., Schütz, V., Mootz, H. D.
    Chemical-tag labeling of proteins using fully recombinant split inteins.
    Methods Mol. Biol., 2015, 1266, 145-159. DOI:10.1007/978-1-4939-2272_10

  • Matern, J., Bachmann, A.-L., Thiel, I. V., Volkmann, G., Wasmuth, A., Binschik, J., Mootz, H. D.
    Ligation of synthetic peptides to proteins using semisynthetic protein trans-splicing.
    Methods Mol. Biol., 2015, 1266, 129-143. DOI: 10.1007/978-1-4939-2272-7_9



  • Sun, X., Li, H., Alfermann, J., Mootz, H. D., Yang, H.
    Kinetics Profiling of Gramicidin S Synthetase A, a Member of Nonribosomal Peptide Synthetases.
    Biochemistry, 2014, 53, 7983-7989. DOI: 10.1021/bi501156m

  • Schütz, V., Mootz, H. D.
    Click-tag and amine-tag: New chemical tag approaches for efficient protein labeling in vitro and on live cells using the naturally split Npu DnaE intein.
    Angew. Chem. Int. Ed., 2014, 53, 4113-4117,
    Angew. Chem., 2014, 126, 4197-4201.

  • Thiel, I. V., Volkmann, G., Pietrokovski, S., Mootz, H. D.
    An atypical naturally split intein engineered for highly efficient protein labeling.
    Angew. Chem. Int. Ed., 2014, 53, 1306-1310,
    Angew. Chem., 2014, 126, 1330-1334.

  • van Treel, N. D., Mootz, H. D.
    SUMOylated RanGAP1 prepared by click chemistry.
    J. Pept. Sci., 2014, 20, 121-127.



  • Zettler, J., Eppmann, S., Busche, A., Dikovskaya, D., Dötsch, V., Mootz, H. D., Sonntag, T.
    SPLICEFINDER - A fast and easy screening method for active protein trans-splicing positions.
    PLOS ONE, 2013, 8, e7292.

  • Kawai, S., Cooper, D., Landes, C. F., Mootz, H. D., Yang, H., Komatsuzaki, T.
    Numerical construction of estimators for single-molecule fluorescence measurements.
    J. Phys. Chem. B, 2013, 117, 8061-8074.

  • Dresselhaus, T. Weikart, N. D. Mootz, H. D., Waller, M. P.
    Naturally and synthetically linked Lys48 diubiquitin: A QM/MM study.
    RSC Adv., 2013, 3, 16122-16129.

  • Wasmuth, A., Ludwig, C., Mootz, H. D.
    Structure-activity studies on the upstream splice junction of a semisynthetic intein.
    Bioorg. Med. Chem., 2013, 21, 3495-3503.

  • Sommer, S., Weikart, N. D., Linne, U., Mootz, H. D.
    Covalent inhibition of SUMO and ubiquitin-specific cysteine proteases by an in situ thiol-alkyne addition.
    Bioorg. Med. Chem., 2013, 21, 2511-2517.
    This article was featured on the cover of the journal issue. It was highlighted in an Editors' choice article in Science (2013, 339, 1498) and in a Highlight article in Angew. Chem. Int. Ed., (2013, doi: 10.1002/anie.201303544).

  • Binschik, J., Mootz, H. D.
    Chemical bypass of intein-catalyzed N-S-acyl shift in protein splicing.
    Angew. Chem. Int. Ed., 2013, 52, 4260-4264,
    Angew. Chem., 2013, 125, 4354-4358.

  • Volkmann, G., Mootz, H. D.
    Recent progress in intein research: from mechanism to directed evolution and applications.
    Cell. Mol. Life Sci., 2013, 70, 1185-1206.



  • Carvajal-Vallejos, P., Pallissé, R., Mootz, H. D., Schmidt, S. R.
    Unprecedented rates and efficiencies revealed for new natural split inteins from metagenomic sources.
    J. Biol. Chem., 2012, 287, 28686-28696.

  • Schwarzer, D., Ludwig, C., Thiel, I. V., Mootz, H. D.
    Probing intein-catalyzed thioester formation by unnatural amino acid substitutions in the active site.
    Biochemistry, 2012, 51, 233-242.

  • Weikart, N. D., Sommer, S., Mootz, H. D.
    Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding.
    Chem. Commun., 2012, 48, 296-298.



  • Appleby-Tagoe, J. H., Thiel, I. V., Wang, Y., Wang, Y., Mootz, H. D., Liu, X.-Q.
    Highly efficient and more general cis- and trans-splicing inteins through sequential directed evolution.
    J. Biol. Chem., 2011, 286, 34440-34447.

  • Sommer, S., Weikart, N. D., Brockmeyer, A., Janning, P., Mootz, H. D.
    Expanded click conjugation of recombinant proteins with ubiquitin-like modifiers reveals altered substrate preference of SUMO2-modified Ubc9.
    Angew. Chem. Int. Ed., 2011, 50, 9888-9892.

  • Sonntag, T., Mootz, H. D.
    An intein-cassette integration approach used for the generation of a split TEV protease activated by conditional protein splicing.
    Mol. BioSys., 2011, 6, 2031-2039.

  • Binschik, J., Zettler, J., Mootz, H. D.
    Photocontrol of protein activity mediated by the cleavage reaction of a split intein.
    Angew. Chem. Int. Ed., 2011, 50, 3249-3252;
    Angew. Chem., 2011, 123, 3307-3310.
    Selected as a hot paper by Angew. Chem..

  • Dhar, T., Mootz, H. D.
    Modification of transmembrane and GPI-anchored proteins on living cells by efficient protein trans-splicing using the Npu DnaE intein.
    Chem. Commun., 2011, 47, 3063-3065.
    Featured on the inside cover of Chem. Commun..

  • Dhar, T., Kurpiers, T., Mootz, H. D.
    Extending the scope of site-specific cysteine bioconjugation by appending a prelabeled cysteine tag to proteins using protein trans-splicing.
    Methods Mol. Biol.,, 2011,  751, 131-142.



  • Garbe, D., Thiel, I. V., Mootz, H. D.
    Protein trans-splicing on an M13 bacteriophage: Towards directed evolution of a semisynthetic intein by phage display.
    J. Pept. Sci. 2010, 16, 575-581.

  • Weikart, N. D., Mootz, H. D.
    Generation of site-specific and enzymatically stable conjugates of recombinant proteins with ubiquitin-like modifiers by the Cu(I)-catalyzed azide-alkyne cycloaddition.
    ChemBioChem 2010, 11, 774-777.

  • Zettler, J., Mootz, H. D.
    Conformational changes in the cross-talk between adenylation and peptidyl-carrier protein domains of nonribosomal peptide synthetases.
    FEBS J. 2010,  277, 1159-1171.

2009 - 2000



  • Mootz, H. D.
    Split inteins as versatile tools for protein semisynthesis.
    ChemBioChem 2009, 10, 2579-2589.

  • Ludwig, C., Schwarzer, D., Zettler, J., Garbe, D., Janning, P., Czeslik, C., Mootz, H. D.
    Semisynthesis of proteins using split inteins
    Methods in Enzymol. 2009, 462, 77-96.

  • Brenzel, S., Cebi, M., Reiß, P., Koert, U., Mootz, H. D.
    Expanding the scope of protein trans-splicing to fragment ligation of an integral membrane protein: Towards modulating porin-based ion channels by chemical modification.
    ChemBioChem 2009, 10, 983-986.

  • Zettler, J., Schütz, V., Mootz, H. D.
    The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction.
    FEBS Lett. 2009, 583, 909-914.

  • Kurpiers, T., Mootz, H. D.
    Bioorthogonal ligation in the spotlight.
    Angew. Chem. Int. Ed. 2009, 48, 1729-1731; Angew. Chem. 2009, 121, 1757-1760.

  • Mootz, H. D.
    Using split inteins to prepare semi-synthetic proteins and to study the mechanism of protein trans-splicing, in Chemical Biology: “Learning through Case Studies”
    Eds.Waldmann & Janning, pp. 159-174, WILEY-VCH (2009).



  • Kurpiers, T., and Mootz, H. D.
    Site-specific chemical modification of proteins with a pre-labelled cysteine tag using the artificially split Mxe GyrA intein.
    ChemBioChem 2008, 9, 2317-2325.

  • Ludwig, C., Schwarzer, D., Mootz H. D.
    Interaction studies and alanine scanning analysis of a semi-synthetic split intein reveal thiazoline ring formation from an intermediate of the protein splicing reaction.
    J. Biol. Chem. 2008, 283, 25264-25272.

  • Rosenfeldt, G., Muñoz-Viana, R., Mootz, H. D., von Arnim, A. G., Batschauer, A.
    Chemically induced and light-independent cryptochrome photoreceptor activation.
    Molecular Plant 2008, 1, 4-14.



  • Kurpiers, T., and Mootz, H. D.
    Regioselective cysteine bioconjugation by appending a modified cysteine tag to a protein using protein splicing in trans.
    Angew. Chem. Int. Ed.2007, 46, 5234-5237; Angew. Chem. 2007, 119, 5327-5330.

  • Mootz, H. D.
    Protein-Spleißen durch Inteine: Eine Fundgrube für proteinchemische Anwendungen
    Biospektrum 2007, 02, 165-167.

  • Schwarzer, D., and Mootz, H. D.
    Semisynthese von Proteinen.
    Nachrichten aus der Chemie 2007, 55, 276-279.



  • Ludwig, T., Pfeiff, M., Linne, U., and Mootz, H. D.
    Ligation of a synthetic peptide to the N-terminus of a recombinant protein using semi-synthetic protein trans-splicing.
    Angew. Chem. Int. Ed. 2006, 45, 5218-522; Angew. Chem. 2006, 118, 5343-5347.

  • Roelfes, G., Mootz, H. D.
    Probing the molecular basis of protein function through chemistry – Conference Report.
    ChemBioChem 2006, 7, 545-549.

  • Brenzel, S., Kurpiers, T., and Mootz, H. D.
    Engineering artificially split inteins for applications in protein chemistry: Biochemical characterization of the split Ssp DnaB intein and comparison to the split Sce VMA intein.
    Biochemistry 2006, 45, 1571-1578.



  • Brenzel, S., Ludwig, C., Mootz, H. D.
    Switchable Inteins: new tools to control protein function by using regulated protein splicing.
    Proceedings of the 19th Symposium of the American Peptide Society “Understanding biology using peptides”, Sylvie E. Blondelle (Editor), p. 754-758 (2005).

  • Brenzel, S., and Mootz, H. D.
    Design of an intein that can be inhibited with a  small molecule ligand.
    J. Am. Chem. Soc. 2005, 127, 4176-4177.



  • Mootz, H. D., Blum, E., and Muir, T. W.
    Activation of an autoinhibited protein kinase using conditional protein splicing.
    Angew. Chem. Int. Ed. 2004, 43, 5189-5192; Angew. Chem. 2004, 116, 5301-5304.

  • Gruenewald, S., Mootz, H. D., Stehmeier, P., and Stachelhaus, T.
    In vivo production of artificial nonribosomal peptide products in the heterologous host Escherichia coli.
    Applied and Environmental Microbiology 2004, 70, 3282-3291.



  • Linne, U., Stein, D. B., Mootz, H. D., and Marahiel, M. A.
    Systematic and quantitative analysis of protein-protein recognition between nonribosomal peptide synthetases investigated in the tyrocidine biosynthetic template.
    Biochemistry 2003, 42, 5114-5124.

  • Mootz, H. D., Blum, E. S., Tyszkiewicz, A. B., and Muir, T.W.
    Conditional protein splicing: A new tool to control protein structure and function in vitro and in vivo.
    J. Am. Chem. Soc. 2003, 125, 10561-10569. This work was discussed in a News Focus article in Science, issue June 13, 2003.



  • Mootz, H. D., and Muir, T. W.
    Protein splicing triggered by a small molecule.
    J. Am. Chem. Soc. 2002, 124, 9044-9045. A news article featuring this paper appeared in Chemical & Engineering News, issue July 22, 2002.

  • Schwarzer, D., Mootz, H. D., Linne, U., and Marahiel, M. A.
    Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases.
    Proc. Natl. Acad. Sci. USA. 2002, 99, 14083-14088.

  • Mootz, H. D., Kessler, N., Linne, U., Eppelmann, K., Schwarzer, D., and Marahiel, M. A.
    Decreasing the ring size of a cyclic nonribosomal peptide antibiotic by in-frame module deletion in the biosynthetic genes.
    J. Am. Chem. Soc. 2002, 124, 10980-10981.

  • Mootz, H. D., Schörgendorfer, K., and Marahiel, M. A.
    Functional characterization of 4’-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae lys5.
    FEMS Microbiol. Lett. 2002, 213, 51-57.

  • Mootz, H. D., Schwarzer, D., and Marahiel, M. A.
    Ways of assembling complex natural products on modular peptide synthetases.
    ChemBioChem 2002, 3, 490-504.

  • Stachelhaus, T., Mootz, H. D., and Marahiel, M. A.
    Nonribosomal assembly of peptide antibiotics on modular protein templates.
    In “Bacillus subtilis and its closest relatives: from genes to cells”, pp. 415-437; Editors A.L. Sonenshein, J.A. Hoch and R. Losick, American Society for Microbiology, Washington, D.C. (2002).



  • Mootz, H. D., and Marahiel, M. A.
    In Encyclopedia of Molecular Medicine,  Editor T.E. Creighton, John Wiley & Sons, New York (2001).

  • Schwarzer, D., Mootz, H. D., and Marahiel, M. A.
    Exploring the impact of different thioesterase domains for the design of hybrid peptide synthetases.
    Chem. Biol. 2001, 8, 997-1010.

  • Mootz, H. D., Finking, R., and Marahiel, M. A.
    4’-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis.
    J. Biol. Chem. 2001, 276, 37289-37298.

  • Döring, V., Mootz, H. D., Nangle, L. A., Hendrickson, T. L., de Crécy-Lagard, V., Schimmel, P., and Marlière, P.
    Enlarging the amino acid set of Escherichia coli by infiltration of the valine coding pathway.
    Science 2001, 292, 501-504.



  • Trauger, J. W., Kohli, R. M., Mootz, H. D., Marahiel, M. A. and Walsh, C. T.
    Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase.
    Nature 2000, 407, 215-218.

  • Mootz, H. D., Schwarzer, D., and Marahiel, M. A.
    Construction of hybrid peptide synthetases by module and domain fusions.
    Proc. Natl. Acad. Sci. USA. 2000,  97, 5848-5853.

1999 - 1997



  • Mootz, H. D., and Marahiel, M. A.
    Design and application of multimodular peptide synthetases.
    Curr. Opin. Biotech. 1999, 10, 341-348

  • Stachelhaus, T., Mootz, H. D., and Marahiel, M. A.
    The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases.
    Chem. Biol. 1999, 6, 493-505.

  • Mootz, H. D., and Marahiel, M. A.
    In Encyclopedia of Molecular Biology, pp. 2706-2708, Editor T.E. Creighton, John Wiley & Sons, New York (1999).



  • Stachelhaus, T., Mootz, H. D., Bergendahl, V., and Marahiel, M. A.
    Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain.
    J. Biol. Chem. 1998, 273, 22773-22781.



  • Mootz, H. D., and Marahiel, M. A.
    Biosynthetic systems for nonribosomal peptide antibiotic assembly.
    Curr. Opin. Chem. Biol. 1997, 1, 543-551.

  • Marahiel, M. A., Stachelhaus, T., and Mootz, H. D.
    Modular peptide synthetases involved in non-ribosomal peptide biosynthesis.
    Chem. Rev. 1997, 97, 2651-2673.

  • Mootz, H. D., and Marahiel, M. A.
    The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains.
    J. Bacteriol. 1997, 179, 6843-6850.

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