Hier finden Sie die Publikationen von Prof. Dr. Harald Kolmar


Generation of Semi-Synthetic Shark IgNAR Single-Domain Antibody Libraries.
Grzeschik J, Könning D, Hinz SC, Krah S, Schröter C, Empting M, Kolmar H, Zielonka S.
Methods Mol Biol. 2018;1701:147-167. doi: 10.1007/978-1-4939-7447-4_8.
A novel one-step approach for the construction of yeast surface display Fab antibody libraries.
Rosowski S, Becker S, Toleikis L, Valldorf B, Grzeschik J, Demir D, Willenbücher I, Gaa R, Kolmar H, Zielonka S, Krah S.
Microb Cell Fact. 2018 Jan 9;17(1):3. doi: 10.1186/s12934-017-0853-z.
Beyond antibody engineering: directed evolution of alternative binding scaffolds and enzymes using yeast surface display.
Könning D, Kolmar H.
Microb Cell Fact. 2018 Feb 26;17(1):32. doi: 10.1186/s12934-018-0881-3. Review.
Shark attack: Haiantikörper für Biomedizin und Biotechnologie.
D Könning, J Grzeschik, SC Hinz, S Krah, M Empting, H Kolmar, S. Zielonka
BIOspektrum, March 2018, Volume 24, Issue 2, pp 142–145
Covalent Attachment of Enzymes to Paper Fibers for Paper-Based Analytical Devices.
Böhm A, Trosien S, Avrutina O, Kolmar H, Biesalski M.
Front. Chem. | doi: 10.3389/fchem.2018.00214
Isolation of pH-Sensitive Antibody Fragments by Fluorescence-Activated Cell Sorting and Yeast Surface Display. Schröter C, Krah S, Beck J, Könning D, Grzeschik J, Valldorf B, Zielonka S, Kolmar H. Methods Mol Biol. 2018;1685:311-331. doi: 10.1007/978-1-4939-7366-8_19.
Generation of potent anti-HER1/2 immunotoxins by protein ligation using split inteins. Pirzer T, Becher KS, Rieker M, Meckel T, Mootz HD, Kolmar H. ACS Chem Biol. 2018 Jun 19. doi: 10.1021/acschembio.8b00222. [Epub ahead of print] PMID: 29920062
Directed Evolution of a Bond-Forming Enzyme: Ultrahigh-Throughput Screening of Microbial Transglutaminase Using Yeast Surface Display.
Deweid L, Neureiter L, Englert S, Schneider H, Deweid J, Yanakieva D, Sturm J, Bitsch S, Christmann A, Avrutina O, Fuchsbauer HL, Kolmar H.
Chemistry. 2018 Jul 26. doi: 10.1002/chem.201803485. [Epub ahead of print] PMID: 30047596


Engineering Bispecific Antibodies with Defined Chain Pairing.
Krah S, Sellmann C, Rhiel L, Schröter C, Dickgießer S, Beck J, Zielonka S, Toleikis L, Hock B, Kolmar H, Becker S.
N Biotechnol. 2017 Jan 27. pii: S1871-6784(16)32478-5. doi: 10.1016/j.nbt.2016.12.010. [Epub ahead of print]
Generation of human bispecific common light chain antibodies by combining animal immunization and yeast display.
Krah S, Schröter C, Eller C, Rhiel L, Rasche N, Beck J, Sellmann C, Günther R, Toleikis L, Hock B, Kolmar H, Becker S.
Protein Eng Des Sel. 2017 Jan 5. doi: 10.1093/protein/gzw077.
A simplified procedure for antibody engineering by yeast surface display: Coupling display levels and target binding by ribosomal skipping.
Grzeschik J, Hinz SC, Könning D, Pirzer T, Becker S, Zielonka S, Kolmar H.
Biotechnol J. 2017 Feb;12(2). doi: 10.1002/biot.201600454.
Highlight issue: protein design.
Sterner R, Höcker B, Kolmar H.
Biol Chem. 2017 Jan 1;398(1):1-2. doi: 10.1515/hsz-2016-0322. No abstract available.
Camelid and shark single domain antibodies: structural features and therapeutic potential.
Könning D, Zielonka S, Grzeschik J, Empting M, Valldorf B, Krah S, Schröter C, Sellmann C, Hock B, Kolmar H.
Curr Opin Struct Biol. 2017 Aug;45:10-16. doi: 10.1016/ Epub 2016 Nov 16. Review.
Spontaneous Isopeptide Bond Formation as a Powerful Tool for Engineering Site-Specific Antibody-Drug Conjugates.
Siegmund V, Piater B, Zakeri B, Eichhorn T, Fischer F, Deutsch C, Becker S, Toleikis L, Hock B, Betz UA, Kolmar H.
Sci Rep. 2016 Dec 16;6:39291. doi: 10.1038/srep39291.
Semi-synthetic vNAR libraries screened against therapeutic antibodies primarily deliver anti-idiotypic binders.
Könning D, Rhiel L, Empting M, Grzeschik J, Sellmann C, Schröter C, Zielonka S, Dickgießer S, Pirzer T, Yanakieva D, Becker S, Kolmar H.
Sci Rep. 2017 Aug 29;7(1):9676. doi: 10.1038/s41598-017-10513-9.


An Apoptosis-Inducing Peptidic Heptad That Efficiently Clusters Death Receptor 5
Valldorf B, Fittler H, Deweid L, Ebenig A, Dickgiesser S, Sellmann C, Becker J, Zielonka S, Empting M, Avrutina O, Kolmar H.
Angew Chem Int Ed Engl. 2016 Mar 15
Spontaneous Isopeptide Bond Formation as a Powerful Tool for Engineering Site-Specific Antibody-Drug Conjugates
Siegmund V, Piater B, Zakeri B, Eichhorn T, Fischer F, Deutsch C, Becker S, Toleikis L, Hock B, Betz UA, Kolmar H.
Sci Rep. 2016 Dec 16;6:39291. doi: 10.1038/srep39291.
Camelid and shark single domain antibodies: structural features and therapeutic potential.
Könning D, Zielonka S, Grzeschik J, Empting M, Valldorf B, Krah S, Schröter C, Sellmann C, Hock B, Kolmar H.
Curr Opin Struct Biol. 2016 Nov 16;45:10-16. doi: 10.1016/ Review.
Nanoscale Biodegradable Organic-Inorganic Hybrids for Efficient Cell Penetration and Drug Delivery.
Hörner S, Knauer S, Uth C, Jöst M, Schmidts V, Frauendorf H, Thiele CM, Avrutina O, Kolmar H.
Angew Chem Int Ed Engl. 2016 Nov 14;55(47):14842-14846. doi: 10.1002/anie.201606065.
Balancing Selectivity and Efficacy of Bispecific Epidermal Growth Factor Receptor (EGFR) × c-MET Antibodies and Antibody-Drug Conjugates.
Sellmann C, Doerner A, Knuehl C, Rasche N, Sood V, Krah S, Rhiel L, Messemer A, Wesolowski J, Schuette M, Becker S, Toleikis L, Kolmar H, Hock B.
J Biol Chem. 2016 Nov 25;291(48):25106-25119.
Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase.
Fiebig D, Schmelz S, Zindel S, Ehret V, Beck J, Ebenig A, Ehret M, Fröls S, Pfeifer F, Kolmar H, Fuchsbauer HL, Scrima A.
J Biol Chem. 2016 Sep 23;291(39):20417-26. doi: 10.1074/jbc.M116.731109.
PROLink-Single Step Circularization and Purification Procedure for the Generation of an Improved Variant of Human Growth Hormone.
Rasche N, Tonillo J, Rieker M, Becker S, Dorr B, Ter-Ovanesyan D, Betz UA, Hock B, Kolmar H.
Bioconjug Chem. 2016 May 18;27(5):1341-7. doi: 10.1021/acs.bioconjchem.6b00137.
Coupled reactions on bioparticles: Stereoselective reduction with cofactor regeneration on PhaC inclusion bodies
Spieler V, Valldorf B, Maaß F, Kleinschek A, Hüttenhain SH, Kolmar H.
Biotechnol J. 2016 Feb 22
Single-domain antibodies for biomedical applications.
Krah S, Schröter C, Zielonka S, Empting M, Valldorf B, Kolmar H.
Immunopharmacol Immunotoxicol. 2016;38(1):21-8. doi: 10.3109/08923973.2015.1102934. Review.
Isolation of a pH-Sensitive IgNAR Variable Domain from a Yeast-Displayed, Histidine-Doped Master Library
Doreen Könning, Stefan Zielonka, Carolin Sellmann, Christian Schröter, Julius Grzeschik, Stefan Becker, Harald Kolmar
Mar Biotechnol (NY). 2016 Feb 2


Aptamers Binding to c-Met Inhibiting Tumor Cell Migration
Birgit Piater, Achim Doerner, Ralf Guenther, Harald Kolmar, Bjoern Hock
PLoS One. 2015 Dec 11
Single-domain antibodies for biomedical applications.
Krah S, Schröter C, Zielonka S, Empting M, Valldorf B, Kolmar H.
Immunopharmacol Immunotoxicol. 2015 Nov 9:1-8.
Engineering a constrained peptidic scaffold towards potent and selective furin inhibitors.
Fittler H, Depp A, Avrutina O, Dahms SO, Than ME, Empting M, Kolmar H.
Chembiochem. 2015 Oct 1. doi: 10.1002/cbic.201500447.
Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site-Specific Conjugation
Siegmund V, Schmelz S, Dickgiesser S, Beck J, Ebenig A, Fittler H, Frauendorf H, Piater B, Betz UA, Avrutina O, Scrima A, Fuchsbauer HL, Kolmar H
Angew Chem Int Ed Engl. 2015 Sep 14.
Self-Assembled Hybrid Aptamer-Fc Conjugates for Targeted Delivery: A Modular Chemoenzymatic Approach
Stephan Dickgiesser, Nicolas Rasche, DaichiNasu, Stephen Middel, Sebastian Hörner, Olga Avrutina, Ulf Diederichsen, Harald Kolmar
ACS Chem Biol. 2015 Jul 14
Combination of inverse electron-demand Diels-Alder reaction with highly efficient oxime ligation expands the toolbox of site-selective peptide conjugations
Sebastian Hörner, Christina Uth, Olga Avrutina, Holm Frauendorf, Manfred Wiessler, Harald Kolmar
Chemical Communications, 06/2015; DOI: 10.1039/C5CC03434E
The Shark Strikes Twice: Hypervariable Loop 2 of Shark IgNAR Antibody Variable Domains and Its Potential to Function as an Autonomous Paratope
Stefan Zielonka, Martin Empting, Doreen Könning, Julius Grzeschik, Simon Krah, Stefan Becker, Stephan Dickgiesser, Harald Kolmar
Mar Biotechnol (NY). 2015 May 24
Cystine-knot peptides targeting cancer-relevant human cytotoxic T lymphocyte-associated antigen 4 (CTLA-4)
Franziska Maaß, Joycelyn Wüstehube-Lausch, Stephan Dickgießer, Bernhard Valldorf, Michael Reinwarth, Hans-Ulrich Schmoldt, Matin Daneschdar, Olga Avrutina, Ugur Sahin, Harald Kolmar
J Pept Sci. 2015 May 10. doi: 10.1002/psc.2782.
At-line mid infrared spectroscopy for monitoring downstream processing unit operations
Florian Capito, Romas Skudas, Harald Kolmar,
A generic approach to engineer antibody pH-switches using combinatorial histidine scanning libraries and yeast display.
Christian Schröter, Ralf Günther, Laura Rhiel, Stefan Becker, Lars Toleikis, Achim Doerner, Janine Becker, Andreas Schönemann, Daichi Nasu, Berend Neuteboom, Harald Kolmar, Björn Hock,
MAbs. 2015 Jan 2;7(1):138-51,
Structural insights and biomedical potential of IgNAR scaffolds from sharks.
Stefan Zielonka, Martin Empting, Julius Grzeschik, Doreen Könning, Caroline J Barelle, Harald Kolmar,
MAbs. 2015 Jan 2;7(1):15-25,
Bacterial Secretion Systems for Use in Biotechnology: Autotransporter-Based Cell Surface Display and Ultrahigh-Throughput Screening of Large Protein Libraries.
Jaeger KE, Kolmar H.
Springer Berlin Heidelberg 2015,, Buchkapitel


REAL-Select: Full-Length Antibody Display and Library Screening by Surface Capture on Yeast Cells
Laura Rhiel, Simon Krah, Ralf Günther, Stefan Becker, Harald Kolmar, Björn Hock,
PLoS ONE 01/2014; 9(12)
Fragmentation follows structure: top-down mass spectrometry elucidates the topology of engineered cystine-knot miniproteins.
Reinwarth M, Avrutina O, Fabritz S, Kolmar H.
PLoS One. 2014 ;9(10):e108626,
Effective PHIP Labeling of Bioactive Peptides Boosts the Intensity of the NMR Signal.
Sauer G, Nasu D, Tietze D, Gutmann T, Englert S, Avrutina O, Kolmar H, Buntkowsky G.
Angew Chem Int Ed Engl. 2014 ;53(47):12941-5,
A Chemoenzymatic Approach to Protein Immobilization onto Crystalline Cellulose Nanoscaffolds.
Uth C, Zielonka S, Hörner S, Rasche N, Plog A, Orelma H, Avrutina O, Zhang K, Kolmar H
Angew Chem Int Ed Engl. 2014;53(46):12618-23,
Shark Attack: High affinity binding proteins derived from shark vNAR domains by stepwise in vitro affinity maturation.
Zielonka S, Weber N, Becker S, Doerner A, Christmann A, Christmann C, Uth C, Fritz J, Schäfer E, Steinmann B, Empting M, Ockelmann P, Lierz M, Kolmar H.
J Biotechnol. 2014 pii: S0168-1656(14)00204-1,
Potent inhibitors of human matriptase-1 based on the scaffold of sunflower trypsin inhibitor.
Fittler H, Avrutina O, Empting M, Kolmar H.
J Pept Sci. 2014;20(6):415-20,
Feasibility of polyelectrolyte-driven Fab fragment separation.
Capito F, Kolmar H, Edelmann B, Skudas R.
Biotechnol J. 2014;9(5):698-701,
A general strategy for antibody library screening via conversion of transient target binding into permanent reporter deposition.
Maass A, Heiseler T, Maass F, Fritz J, Hofmeyer T, Glotzbach B, Becker S, Kolmar H,
Protein Engineering Design & Selection (2014) 27(2):41-47,
Azobenzene switch with a long-lived cis-state to photocontrol the enzyme activity of a histone deacetylase-like amidohydrolase.
Korbus M, Balasubramanian G, Muller-Plathe F, Kolmar H, Meyer-Almes FJ,
Biological chemistry (2014) 395(4):401-412.,
Protein production in yarrowia lipolytica via fusion to the secreted lipase lip2p.
Hofmeyer T, Bulani SI, Grzeschik J, Krah S, Glotzbach B, Uth C, Avrutina O, Brecht M, Goringer HU, van Zyl P, Kolmar H, Molecular biotechnology (2014) 56(1):79-90.
Therapeutic antibody engineering by high efficiency cell screening.
Doerner A, Rhiel L, Zielonka S, Kolmar H,
FEBS letters (2014) 588(2):278-287.
Required polymer lengths per precipitated protein molecule in protein-polymer interaction.
Capito F, Kolmar H, Stanislawski B, Skudas R,
J Polym Res (2014) 21(2).
Feasibility of polyelectrolyte-driven fab fragment separation.
Capito F, Kolmar H, Edelmann B, Skudas R,
Biotechnology journal (2014) 9(5):698-701.


Oxidative folding of peptides with cystine-knot architectures: Kinetic studies and optimization of folding conditions.
Reinwarth M, Glotzbach B, Tomaszowski M, Fabritz S, Avrutina O, Kolmar H:
Chembiochem : a European journal of chemical biology (2013) 14(1):137-146
Phip-label: Parahydrogen-induced polarization in propargylglycine-containing synthetic oligopeptides.
Korner M, Sauer G, Heil A, Nasu D, Empting M, Tietze D, Voigt S, Weidler H, Gutmann T, Avrutina O, Kolmar H et al,
Chemical communications (2013) 49(71):7839-7841.
Cube-octameric silsesquioxane-mediated cargo peptide delivery into living cancer cells.
Hörner S, Fabritz S, Herce HD, Avrutina O, Dietz C, Stark RW, Cardoso MC, Kolmar H,
Organic & biomolecular chemistry (2013) 11(14):2258-2265
Arranged sevenfold: Structural insights into the c-terminal oligomerization domain of human c4b-binding protein.
Hofmeyer T, Schmelz S, Degiacomi MT, Dal Peraro M, Daneschdar M, Scrima A, van den Heuvel J, Heinz DW, Kolmar H,
Journal of molecular biology (2013) 425(8):1302-1317
Structural characterization of spinacia oleracea trypsin inhibitor iii (soti-iii).
Glotzbach B, Schmelz S, Reinwarth M, Christmann A, Heinz DW, Kolmar H,
Acta Crystallogr D (2013) 69(114-120
Combinatorial optimization of cystine-knot peptides towards high-affinity inhibitors of human matriptase-1.
Glotzbach B, Reinwarth M, Weber N, Fabritz S, Tomaszowski M, Fittler H, Christmann A, Avrutina O, Kolmar H,
PloS one (2013) 8(10)
Performance evaluation of thick film open tubular silica capillary by reversed phase liquid chromatography.
Forster S, Kolmar H, Altmaier S,
Journal of Chromatography A (2013) 1283(110-115
Preparation and kinetic performance assessment of thick film 10-20 mu m open tubular silica capillaries in normal phase high pressure liquid chromatography.
Forster S, Kolmar H, Altmaier S,
Journal of Chromatography A (2013) 1315(127-134
Combinatorial tuning of peptidic drug candidates: High-affinity matriptase inhibitors through incremental structure-guided optimization.
Fittler H, Avrutina O, Glotzbach B, Empting M, Kolmar H,
Organic & biomolecular chemistry (2013) 11(11):1848-1857
Bioconjugation on cube-octameric silsesquioxanes.
Fabritz S, Horner S, Avrutina O, Kolmar H,
Organic & biomolecular chemistry (2013) 11(14):2224-2236
Matrix effects during monitoring of antibody and host cell proteins using attenuated total reflection spectroscopy.
Capito F, Skudas R, Stanislawski B, Kolmar H,
Biotechnology progress (2013) 29(1):265-274
Polyelectrolyte-protein interaction at low ionic strength: Required chain flexibility depending on protein average charge.
Capito F, Skudas R, Stanislawski B, Kolmar H,
Colloid Polym Sci (2013) 291(7):1759-1769
Customization of copolymers to optimize selectivity and yield in polymer-driven antibody purification processes.
Capito F, Skudas R, Stanislawski B, Kolmar H,
Biotechnology progress (2013) 29(6):1484-1493
Host cell protein quantification by fourier transform mid infrared spectroscopy (ft-mir).
Capito F, Skudas R, Kolmar H, Stanislawski B, (2013) 110(1):252-259,
Biotechnology and bioengineering
Mid-infrared spectroscopy-based antibody aggregate quantification in cell culture fluids.
Capito F, Skudas R, Kolmar H, Hunzinger C,
Biotechnology journal (2013) 8(8):912-U948
Feasibility study of semi-selective protein precipitation with salt-tolerant copolymers for industrial purification of therapeutic antibodies.
Capito F, Bauer J, Rapp A, Schroter C, Kolmar H, Stanislawski B,
Biotechnology and bioengineering (2013) 110(11):2915-2927


Braces for the peptide backbone: Insights into structure-activity relationships of protease inhibitor mimics with locked amide conformations
Tischler M, Nasu D, Empting M, Schmelz S, Heinz DW, Rottmann P, Kolmar H, Buntkowsky G, Tietze D, Avrutina O,
Angew Chem Int Edit (2012) 51(15):3708-3712
Chemical synthesis, backbone cyclization and oxidative folding of cystine-knot peptides – promising scaffolds for applications in drug design.
Reinwarth M, Nasu D, Kolmar H, Avrutina O,
Molecules (2012) 17(11):12533-12552
A sensitive method for rapid detection of alkyl halides and dehalogenase activity using a multistep enzyme assay.
Fabritz S, Maaß F, Avrutina O, Heiseler T, Steinmann B, Kolmar H.
AMB Express. 2012 Sep 24;2(1):51. doi: 10.1186/2191-0855-2-51
Synthesis and characterization of new generation open tubular silica capillaries for liquid chromatography.
Forster S, Kolmar H, Altmaier S,
Journal of Chromatography A (2012) 1265(88-94
From pico to nano: Biofunctionalization of cube-octameric silsesquioxanes by peptides and miniproteins. Organic & biomolecular chemistry
Fabritz S, Hörner S, Könning D, Empting M, Reinwarth M, Dietz C, Glotzbach B, Frauendorf H, Kolmar H, Avrutina O,
Organic & biomolecular chemistry(2012) 10(31):6287-6293
Between two worlds: A comparative study on in vitro and in silico inhibition of trypsin and matriptase by redox-stable sfti-1 variants at near physiological pH
Avrutina O, Fittler H, Glotzbach B, Kolmar H, Empting M,
Organic & biomolecular chemistry (2012) 10(38):7753-7762,


Autotransporters with gdsl passenger domains: Molecular physiology and biotechnological applications.
Wilhelm S, Rosenau F, Kolmar H, Jaeger KE,
Chembiochem : a European journal of chemical biology (2011) 12(10):1476-1485
Decorating microbes: Surface display of proteins on escherichia coli.
van Bloois E, Winter RT, Kolmar H, Fraaije MW,
Trends in biotechnology (2011) 29(2):79-86
DNA libraries for the construction of phage libraries: Statistical and structural requirements and synthetic methods.
Lindner T, Kolmar H, Haberkorn U, Mier W,
Molecules (2011) 16(2):1625-1641
Natural and engineered cystine knot miniproteins for diagnostic and therapeutic applications.
Kolmar H,
Current pharmaceutical design (2011) 17(38):4329-4336
„Triazole bridge“: Disulfide-bond replacement by ruthenium-catalyzed formation of 1,5-disubstituted 1,2,3-triazoles.
Empting M, Avrutina O, Meusinger R, Fabritz S, Reinwarth M, Biesalski M, Voigt S, Buntkowsky G, Kolmar H,
Angew Chem Int Edit (2011) 50(22):5207-5211
Bi-specific aptamers mediating tumor cell lysis.
Boltz A, Piater B, Toleikis L, Guenther R, Kolmar H, Hock B,
Journal of Biological Chemistry (2011) 286(24):21896-21905


In vivo enzyme immobilization by inclusion body display.
Steinmann B, Christmann A, Heiseler T, Fritz J, Kolmar H,
Applied and environmental microbiology (2010) 76(16):5563-5569
Engineered cystine knot miniproteins as potent inhibitors of human mast cell tryptase beta.
Sommerhoff CP, Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Diederichsen U, Kolmar H,
Journal of molecular biology (2010) 395(1):167-175
Engineered cystine-knot miniproteins for diagnostic applications.
Kolmar H,
Expert review of molecular diagnostics (2010) 10(3):361-368
Towards click bioconjugations on cube-octameric silsesquioxane scaffolds.
Fabritz S, Heyl D, Bagutski V, Empting M, Rikowski E, Frauendorf H, Balog I, Fessner WD, Schneider JJ, Avrutina O, Kolmar H
Organic & biomolecular chemistry (2010) 8(9):2212-2218
Sunflower trypsin inhibitor 1 derivatives as molecular scaffolds for the development of novel peptidic radiopharmaceuticals.
Boy RG, Mier W, Nothelfer EM, Altmann A, Eisenhut M, Kolmar H, Tomaszowski M, Kramer S, Haberkorn U,
Molecular Imaging and Biology (2010) 12(4):377-385


Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins.
Kolmar H,
Curr Opin Pharmacol (2009) 9(5):608-614
Application of copper(i) catalyzed azide-alkyne [3+2] cycloaddition to the synthesis of template-assembled multivalent peptide conjugates.
Avrutina O, Empting M, Fabritz S, Daneschdar M, Frauendorf H, Diederichsen U, Kolmar H,
Organic & biomolecular chemistry (2009) 7(20):4177-4185


Characterisation of the barrier caused by luminally secreted gastro-intestinal proteolytic enzymes for two novel cystine-knot microproteins.
Werle M, Kolmar H, Albrecht R, Bernkop-Schnurch A,
Amino Acids (2008) 35(1):195-200
Alternative binding proteins get mature: Rivalling antibodies.
Kolmar H, Skerra A,
Febs J (2008) 275(11):2667-2667
Alternative binding proteins: Biological activity and therapeutic potential of cystine-knot miniproteins.
Kolmar H,
Febs J (2008) 275(11):2684-2690
Knottin cyclization: Impact on structure and dynamics.
Heitz A, Avrutina O, Le-Nguyen D, Diederichsen U, Hernandez JF, Gracy J, Kolmar H, Chiche L,
Bmc Struct Biol (2008)
Single-cell high-throughput screening to identify enantioselective hydrolytic enzymes.
Becker S, Hobenreich H, Vogel A, Knorr J, Wilhelm S, Rosenau F, Jaeger KE, Reetz MT, Kolmar H,
Angew Chem Int Edit (2008) 47(27):5085-5088
Head-to-tail cyclized cystine-knot peptides by a combined recombinant and chemical route of synthesis.
Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Wentzel A, Frauendorf H, Sommerhoff CP, Diederichsen U, Kolmar H:, Chembiochem : a European journal of chemical biology (2008) 9(1):33-37


Functional cell-surface display of a lipase-specific chaperone.
Wilhelm S, Rosenau F, Becker S, Buest S, Hausmann S, Kolmar H, Jaeger KE,
Chembiochem : a European journal of chemical biology (2007) 8(1):55-60
Functional genomics of pseudomonas aeruginosa to identify habitat-specific determinants of pathogenicity.
Wiehlmann L, Munder A, Adams T, Juhas M, Kolmar H, Salunkhe P, Tummler B,
Int J Med Microbiol (2007) 297(7-8):615-623
Relation between scaffold size and membrane bound enzyme caused degradation of two novel cystine knot microproteins.
Werle M, Kolmar H, Bernkop-Schnurch A,
Lett Drug Des Discov (2007) 4(1):33-36
Evaluation and improvement of the properties of the novel cystine-knot microprotein mcoeeti for oral administration.
Werle M, Kafedjiiski K, Kolmar H, Bernkop-Schnurch A,
Int J Pharmaceut (2007) 332(1-2):72-79
Grafting of thrombopoietin-mimetic peptides into cystine knot miniproteins yields high-affinity thrombopoietin antagonists and agonists.
Krause S, Schmoldt HU, Wentzel A, Ballmaier M, Friedrich K, Kolmar H,
Febs J (2007) 274(1):86-95
Crystal structure of the electron transfer complex rubredoxin-rubredoxin reductase of pseudomonas aeruginosa.
Hagelueken G, Wiehlmann L, Adams TM, Kolmar H, Heinz DW, Tummler B, Schubert WD,
P Natl Acad Sci USA (2007) 104(30):12276-12281
Ultrahigh-throughput screening to identify e-coli cells expressing functionally active enzymes on their surface.
Becker S, Michalczyk A, Wilhelm S, Jaeger KE, Kolmar H,
Chembiochem : a European journal of chemical biology (2007) 8(8):943-949


The potential of cystine-knot microproteins as novel pharmacophoric scaffolds in oral peptide drug delivery.
Werle M, Schmitz T, Huang HL, Wentzel A, Kolmar H, Bernkop-Schnurch A,
J Drug Target (2006) 14(3):137-146
Inhibition of platelet aggregation by grafting rgd and kgd sequences on the structural scaffold of small disulfide-rich proteins.
Reiss S, Sieber M, Oberle V, Wentzel A, Spangenberg P, Claus R, Kolmar H, Losche W,
Platelets (2006) 17(3):153-157
Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein mcoeeti.
Niemann HH, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW,
Journal of molecular biology (2006) 356(1):1-8
The crystal structure of sdsa1, an alkylsulfatase from pseudomonas aeruginosa, defines a third class of sulfatases
Hagelueken G, Adams TM, Wiehlmann L, Widow U, Kolmar H, Tummler B, Heinz DW, Schubert WD,
(vol 103, pg 7631, 2006). P Natl Acad Sci USA (2006) 103(28):10824-10824


A fusion protein system for the recombinant production of short disulfide bond rich cystine knot peptides using barnase as a purification handle.
Schmoldt HU, Wentzel A, Becker S, Kolmar H,
Protein Expres Purif (2005) 39(1):82-89
Structure of ecballium elaterium trypsin inhibitor ii (eeti-ii): A rigid molecular scaffold.
Kratzner R, Debreczeni JE, Pape T, Schneider TR, Wentzel A, Kolmar H, Sheldrick GM, Uson I,
Acta Crystallogr D (2005) 61(1255-1262
A generic system for the escherichia coli cell-surface display of lipolytic enzymes.
Becker S, Theile S, Heppeler N, Michalczyk A, Wentzel A, Wilhelm S, Jaeger KE, Kolmar H,
FEBS letters (2005) 579(5):1177-1182
Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor mcoti-ii.
Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Le Nguyen D, Sommerhoff CP, Diederichsen U, Kolmar H,
Biological chemistry (2005) 386(12):1301-1306
Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation.
Adams TM, Wentzel A, Kolmar H,
J Bacteriol (2005) 187(2):522-533


Bacteria displaying interleukin-4 mutants stimulate mammalian cells and reflect the biological activities of variant soluble cytokines.
Krause S, Wurdemann D, Wentzel A, Christmann A, Fehr H, Kolmar H, Friedrich K:
Chembiochem : a European journal of chemical biology (2004) 5(6):804-810
Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts.
Becker S, Schmoldt HU, Adams TM, Wilhelm S, Kolmar H,
Curr Opin Biotech (2004) 15(4):323-329
Fmoc-assisted synthesis of a 29-residue cystine-knot trypsin inhibitor containing a guaninyl amino acid at the p1-position.
Avrutina O, Schmoldt HU, Kolmar H, Diederichsen U,
Eur J Org Chem (2004) 23):4931-4935


Display of passenger proteins on the surface of escherichia coli k-12 by the enterohemorrhagic e-coli intimin eaea.
Wentzel A, Christmann A, Adams T, Kolmar H,
J Bacteriol (2001) 183(24):7273-7284
Epitope mapping and affinity purification of monospecific antibodies by escherichia coli cell surface display of gene-derived random peptide libraries.
Christmann A, Wentzel A, Meyer C, Meyers G, Kolmar H,
J Immunol Methods (2001) 257(1-2):163-173


Sequence requirements of the gpng beta-turn of the ecballium elaterium trypsin inhibitor ii explored by combinatorial library screening.
Wentzel A, Christmann A, Kratzner R, Kolmar H,
Journal of Biological Chemistry (1999) 274(30):21037-21043
Toxr co-operative interactions are not modulated by environmental conditions or periplasmic domain conformation.
Dziejman M, Kolmar H, Fritz HJ, Mekalanos JJ,
Mol Microbiol (1999) 31(1):305-317
The cystine knot of a squash-type protease inhibitor as a structural scaffold for escherichia coli cell surface display of conformationally constrained peptides.
Christmann A, Walter K, Wentzel A, Kratzner R, Kolmar H,
Protein Eng (1999) 12(9):797-806
The cystine-knot motif as a structural scaffold for the presentation of a constrained peptide library.
Kratzner R, Kolmar H,
Protein Eng (1997) 10(85-85
Dimerisation of the glycophorin a transmembrane segment in membranes probed with the toxr transcription activator.
Langosch D, Brosig B, Kolmar H, Fritz HJ,
Journal of molecular biology (1996) 263(4):525-530
The degp and degq periplasmic endoproteases of escherichia coli: Specificity for cleavage sites and substrate conformation.
Kolmar H, Waller PRH, Sauer RT,
J Bacteriol (1996) 178(20):5925-5929
Contribution of the intramolecular disulfide bridge to the folding stability of rei(v), the variable domain of a human immunoglobulin kappa light chain.
Frisch C, Kolmar H, Schmidt A, Kleemann G, Reinhardt A, Pohl E, Uson I, Schneider TR, Fritz HJ,
Fold Des (1996) 1(6):431-440
Membrane insertion of the bacterial signal-transduction protein toxr and requirements of transcription activation studied by modular replacement of different protein substructures.
Kolmar H, Hennecke F, Gotze K, Janzer B, Vogt B, Mayer F, Fritz HJ,
Embo J (1995) 14(16):3895-3904
Immunoglobulin mutant library genetically screened for folding stability exploiting bacterial signal-transduction.
Kolmar H, Frisch C, Gotze K, Fritz HJ,
Journal of molecular biology (1995) 251(4):471-476
A genetic screen for protein-protein interaction within the periplasmic space of escherichia-coli.
Kolmar H, Hennecke F, Frisch C, Brundl K, Fritz HJ,
J Cell Biochem (1994) 169-169
Dimerization of bence-jones proteins – linking the rate of transcription from an escherichia-coli promoter to the association constant of rei(v).
Kolmar H, Frisch C, Kleemann G, Gotze K, Stevens FJ, Fritz HJ,
Biol Chem H-S (1994) 375(1):61-70
Establishing a screen for antibody hapten interaction based on escherichia-coli genetics.
Hennecke F, Kolmar H, Brundl K, Fritz HJ,
J Cell Biochem (1994) 214-214
Immunoglobulin folding stability genetically screened in escherichia-coli and construction of a disulfide-free variable domain.
Fritz HJ, Brundl K, Frisch C, Kolmar H,
J Cell Biochem (1994) 213-213
A soluble immunoglobulin variable domain without a disulfide bridge – construction, accumulation in the cytoplasm of escherichia-coli, purification and physicochemical characterization.
Frisch C, Kolmar H, Fritz HJ,
Biol Chem H-S (1994) 375(5):353-356
General mutagenesis gene-expression procedure for the construction of variant immunoglobulin domains in escherichia-coli – production of the bence-jones protein rei(v) via fusion to beta-lactamase.
Kolmar H, Ferrando E, Hennecke F, Wippler J, Fritz HJ,
Journal of molecular biology (1992) 228(2):359-365
Dependence of conformational stability of an immunoglobulin variable domain on cdr sequence.
Kolmar H, Brundl K, Fritz HJ,
Biol Chem H-S (1991) 372(9):695-695
The vsr gene-product of escherichia-coli k-12 is a strand-specific and sequence-specific DNA mismatch endonuclease.
Hennecke F, Kolmar H, Brundl K, Fritz HJ,
Nature (1991) 353(6346):776-778
New developments in the gapped duplex DNA approach to oligonucleotide-directed mutation construction.
Kramer W, Friedrich K, Kolmar H, Pschorr J, Teufel M, Fritz HJ,
Biol Chem H-S (1989) 370(8):770-771
Phasduction – a simplified protocol for oligonucleotide-directed mutagenesis by the gapped duplex DNA method.
Friedrich K, Kolmar H, Fritz HJ,
Nucleic Acids Res (1989) 17(14):5862-5862
DNA mismatch repair and its application in genetic-engineering.
Kolmar H, Zell R, Fritz HJ,
Biol Chem H-S (1987) 368(9):1130-1130

Book Contributions

Expression of two synthetic genes in Escherichia coli and in Staphylococcus carnosus.
Friedrich, K., Kolmar, H., Pschorr, J., Wippler, J., Fritz, H.-J. (1990).
In: Protein Engineering. Ikehara, M., Oshima, T., Titani, K. (Eds.) Japan Scientific Societies Press, Tokyo, pp. 111-119.
Oligonucleotide-directed mutagenesis with single-stranded cloning vectors.
Kolmar, H., Fritz, H.-J. (1995).
In: DNA Cloning 1: A practical approach. D. Glover, B. D. Hames (Eds.). IRL Press, Oxford, pp. 193-224.
Enzyme Engineering by bacterial cell surface display.
Adams, T., Kolmar, H. (2002)
In: Enzyme functionality: Design, Engineering and Screening. A: Svendson (Ed.). Marcel Dekker, Inc., New York.
DegP Protease.
Kolmar, H(2004).
In: Handbook of Proteolytic Enzymes. 2nd Edition. A.J. Barrett, N. D. Rawlings, F. Woessner (Eds.). Academic Press, New York.
FACS Screening of Combinatorial Peptide and Protein Libraries Displayed on the Surface of Escherichia coli Cells.
Adams, T., Schmoldt, H.-U., Kolmar, H. (2004)
In: Evolutionary Methods in Biotechnology. S: Brakman, A Schwienhorst (Eds.) Wiley-VCH, Weinheim.
Schmoldt, H.-U., Daneschdar, M., Kolmar, H., Blind, M. (2008)
In: Methods in Molecular Biology, Nucleic acid and peptide aptamers”. Humana press. Accepted.
Bacterial Secretion Systems for Use in Biotechnology: Autotransporter-Based Cell Surface Display and Ultrahigh-Throughput Screening of Large Protein Libraries.
Karl-erich Jaeger and Harald Kolmar
In:Hydrocarbon and Lipid Microbiology Protocols. Springer.