{"id":16,"date":"2025-09-30T13:57:49","date_gmt":"2025-09-30T11:57:49","guid":{"rendered":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/?page_id=16"},"modified":"2025-10-14T15:03:40","modified_gmt":"2025-10-14T13:03:40","slug":"service","status":"publish","type":"page","link":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/service\/","title":{"rendered":"Publications"},"content":{"rendered":"\n<p class=\"has-text-align-left\">Heiringhoff RS, Greve JN, <strong>Zahn M<\/strong>, Manstein DJ <strong>(2025)<\/strong>. Structure of the Human Non-Muscle Myosin 2A Motor Domain: Insights into Isoform-Specific Mechanochemistry. <em><strong>J Biol Chem.<\/strong><\/em>  <a href=\"https:\/\/doi.org\/10.1016\/j.jbc.2025.110691\">https:\/\/doi.org\/10.1016\/j.jbc.2025.110691<\/a><\/p>\n\n\n\n<p>Dexter GN, Grigg JC, <strong>Zahn M<\/strong>, Wheatley EJ, Lian J, Mohn WW, Eltis LD <strong>(2025)<\/strong>. Characterization of a two-component kinase that initiates the bacterial catabolism of hydroxyphenylethanones. <em><strong>J Biol Chem.<\/strong><\/em>, 301(6), 110210. <a href=\"https:\/\/doi.org\/10.1016\/j.jbc.2025.110210\">https:\/\/doi.org\/10.1016\/j.jbc.2025.110210<\/a><\/p>\n\n\n\n<p>Kuatsjah E, Schwartz A, <strong>Zahn M<\/strong>, Tornesakis K, Kellermyer ZA, Ingraham MA, Woodworth SP, Ramirez KJ, Cox PA, Pickford AR, Salvach\u00faa D (<strong>2024<\/strong>). Biochemical and structural characterization of enzymes in the 4-hydroxybenzoate catabolic pathway of lignin-degrading white-rot fungi. <em><strong>Cell Rep.<\/strong><\/em>, 43(12):115002. <a href=\"https:\/\/doi.org\/10.1016\/j.celrep.2024.115002\">https:\/\/doi.org\/10.1016\/j.celrep.2024.115002<\/a><\/p>\n\n\n\n<p>Clark M, Tornesakis K, K\u00f6nig G, <strong>Zahn M<\/strong>, Lichtenstein BR, Pickford AR, Cox PA. <strong>(2024)<\/strong>. Understanding the Catalytic Efficiency of Two Polyester Degrading Enzymes: An Experimental and Theoretical Investigation. <em><strong>ACS Omega<\/strong><\/em>, 9(44):44724\u201344733. <a href=\"https:\/\/doi.org\/10.1021\/acsomega.4c06528\">https:\/\/doi.org\/10.1021\/acsomega.4c06528<\/a><\/p>\n\n\n\n<p>Reinke PYA, Heiringhoff RS, Reindl T, Baker K, Taft MH, Meents A, Mulvihill DP, Davies OR, Fedorov R, <strong>Zahn M<\/strong>, Manstein DJ (<strong>2024<\/strong>). Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin ortholog TpmCdc8. <em><strong>J Biol Chem.<\/strong><\/em>, 300(12), 107925. <a href=\"https:\/\/doi.org\/10.1016\/j.jbc.2024.107925\">https:\/\/doi.org\/10.1016\/j.jbc.2024.107925<\/a><\/p>\n\n\n\n<p>Avilan L, Lichtenstein BR, Koenig G, <strong>Zahn M<\/strong>, Allen MD, Oliveira L, Clark M, Bemmer V, Graham R, Austin HP, Dominick, G., Johnson, CW, Beckham GT, McGeehan JE, Pickford AR (<strong>2023<\/strong>). Concentration-dependent inhibition of mesophilic PETases on poly(ethylene terephthalate) can be eliminated by enzyme engineering. <strong>ChemSusChem.<\/strong>, 16(8). <a href=\"https:\/\/doi.org\/10.1002\/cssc.202202277\">https:\/\/doi.org\/10.1002\/cssc.202202277<\/a><\/p>\n\n\n\n<p>McNaught KJ, Kuatsjah E, Zahn M, Prates \u00c9T, Shao H, Bentley GJ, Pickford AR, Gruber JN, Hestmark KV, Jacobson DA, Poirier BC, Ling C, San Marchi M, Michener WE, Nicora CD, Sanders JN, Szostkiewicz CJ, Veli\u010dkovi\u0107 D, Zhou M, Munoz N, Kim YM, Magnuson JK, Burnum-Johnson KE, Houk KN, McGeehan JE, Johnson CW, Beckham GT (<strong>2023<\/strong>). Initiation of fatty acid biosynthesis in Pseudomonas putida KT2440. <em><strong>Metab. Eng.<\/strong><\/em>, 76:193-203. <a href=\"https:\/\/doi.org\/10.1016\/j.ymben.2023.02.006\">https:\/\/doi.org\/10.1016\/j.ymben.2023.02.006<\/a><\/p>\n\n\n\n<p>Kuatsjah E, <strong>Zahn M<\/strong>, Chen X, Kato R, Hinchen DJ, Konev MO, Katahira R, Orr C, Wagner A, Zou Y, Haugen SJ, Ramirez KJ, Michener JK, Pickford AR, Kamimura N, Masai E, Houk KN, McGeehan JE, Beckham GT (<strong>2023<\/strong>). Biochemical and structural characterization of a sphingomonad diarylpropane lyase for cofactorless deformylation. <em><strong>PNAS<\/strong><\/em>, 120(4). <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1073\/pnas.2212246120\" target=\"_blank\">https:\/\/doi.org\/10.1073\/pnas.2212246120<\/a> <\/p>\n\n\n\n<p> Erickson E, Gado JE, Avil\u00e1n L, Bratti F, Brizendine RK, Cox PA, Gill R, Graham R, Kim DJ, K\u00f6nig G, Michener WE, Poudel S, Ramirez KJ, Shakespeare TJ, <strong>Zahn M<\/strong>, Boyd ES, Payne CM, DuBois JL, Pickford AR, Beckham GT, McGeehan JE. (<strong>2022<\/strong>). Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity. <em><strong>Nat Commun. <\/strong><\/em>13(1):7850. <a href=\"https:\/\/doi.org\/10.1038\/s41467-022-35237-x\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1038\/s41467-022-35237-x<\/a><\/p>\n\n\n\n<p>Bleem A, Kuatsjah E, Presley GN, Hinchen DJ, <strong>Zahn M<\/strong>, Garcia DC, Michener WE, Koenig G, Tornesakis K, Allemann MN, Giannone RJ, McGeehan J, Beckham GT <span class=\"amp\">&amp;<\/span> Michener JK (<strong>2022<\/strong>). Discovery, characterization, and metabolic engineering of Rieske non-heme iron monooxygenases for guaiacol O-demethylation. <em><strong>Chem Catalysis<\/strong><\/em>. <a href=\"https:\/\/doi.org\/10.1016\/j.checat.2022.04.019\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1016\/j.checat.2022.04.019<\/a><\/p>\n\n\n\n<p>Navas LE, <strong>Zahn M<\/strong>, Bajwa H, Grigg JC, Wolf ME, Chan A, Murphy MEP, McGeehan JE, Eltis LD (<strong>2022<\/strong>). Characterization of a phylogenetically distinct extradiol dioxygenase involved in the bacterial catabolism of lignin-derived aromatic compounds. <em><strong>J Biol Chem.<\/strong>, <\/em>298(5):101871. <a href=\"https:\/\/doi.org\/10.1016\/j.jbc.2022.101871\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1016\/j.jbc.2022.101871<\/a><\/p>\n\n\n\n<p>Kincannon WM*, <strong>Zahn M*<\/strong>, Clare R, Romberg A, Larson J, Lusty-Beech J, Bothner B, Beckham GT, McGeehan JE, DuBois JL (<strong>2022<\/strong>). Biochemical and structural characterization of an aromatic ring-hydroxylating dioxygenase for terephthalic acid catabolism. <em><strong>PNAS<\/strong><\/em>. 119(13). (*Authors share first authorship) <a href=\"https:\/\/doi.org\/10.1073\/pnas.2121426119\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1073\/pnas.2121426119<\/a><\/p>\n\n\n\n<p><strong>Zahn M<\/strong>, K\u00f6nig G, Pham HVC, Seroka B, Lazny R, Yang G, Ouerfelli O, Lotowski Z <span class=\"amp\">&amp;<\/span> Rohwerder T (<strong>2022<\/strong>). Mechanistic details of the actinobacterial lyase-catalyzed degradation reaction of 2-hydroxyisobutyryl-CoA. <em><strong>J Biol Chem.<\/strong><\/em>, 298 (1).<a href=\"https:\/\/doi.org\/10.1016\/j.jbc.2021.101522\" target=\"_blank\" rel=\"noreferrer noopener\"> https:\/\/doi.org\/10.1016\/j.jbc.2021.101522<\/a><\/p>\n\n\n\n<p>Erickson E, Shakespeare TJ, Bratti F, Buss B, Graham R, Hawkins M, Koenig G, Michener WE, Miscall J, Ramirez K, Rorrer NA, <strong>Zahn M<\/strong>, Pickford A, McGeehan JE <span class=\"amp\">&amp;<\/span> Beckham GT (<strong>2022<\/strong>). Comparative performance of PETase as a function of reaction conditions, substrate properties, and product accumulation. <em><strong>ChemSusChem,<\/strong><\/em> 15 (1). <a href=\"https:\/\/doi.org\/10.1002\/cssc.202102517\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1002\/cssc.202102517<\/a><\/p>\n\n\n\n<p>Kuatsjah E, Johnson CW, Salvach\u00faa D, Werner A, <strong>Zahn M<\/strong>, Szostkiewicz CJ, Singer CA, Dominick G, Okekeogbu I, Haugen SJ, Woodworth SP, Ramirez KJ, Giannone RJ, Hettich RL, McGeehan JE <span class=\"amp\">&amp;<\/span> Beckham GT (<strong>2022<\/strong>). Debottlenecking 4-hydroxybenzoate hydroxylation in <em>Pseudomonas putida<\/em> KT2440 improves muconate productivity from <em>p<\/em>-coumarate. <em><strong>Metab Eng.<\/strong><\/em>, 70:31-42. <a href=\"https:\/\/doi.org\/10.1016\/j.ymben.2021.12.010\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1016\/j.ymben.2021.12.010<\/a><\/p>\n\n\n\n<p>Ryan MD, Parkes AL, Corbett D, Dickie AP, Southey M, Andersen OA, Stein DB, Barbeau OR, Sanzone A, Thommes P, Barker J, Cain R, Compper C, Dejob M, Dorali A, Etheridge D, Evans S, Faulkner A, Gadouleau E, Gorman T, Haase D, Holbrow-wilshaw M, Krulle T, Li X, Lumley C, Mertins B, Napier S, Odedra R, Papadopoulos K, Roumpelakis V, Spear K, Trimby E, Williams J, <strong>Zahn M<\/strong>, Keefe AD, Zhang Y, Soutter H T, Centrella PA, Clark MA, Cuozzo JW, Dumelin CE, Deng B, Hunt A, Sigel EA, Troast DM <span class=\"amp\">&amp;<\/span> Dejonge BL (<strong>2021<\/strong>). Discovery of novel UDP-N-Acetylglucosamine Acyltransferase (LpxA) inhibitors with activity against <em>Pseudomonas aeruginosa<\/em>. <em><strong>J Med Chem.<\/strong><\/em>, 64(19):14377-14425. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/acs.jmedchem.1c00888\" target=\"_blank\">https:\/\/doi.org\/10.1021\/acs.jmedchem.1c00888<\/a><\/p>\n\n\n\n<p>Gray DA, White JB, Oluwole AO, Rath P, Glenwright AJ, Mazur A, <strong>Zahn M<\/strong>, Basl\u00e9 A, Morland C, Evans SL, Cartmell A, Robinson CV, Hiller S, Ranson NA, Bolam DN, van den Berg B (<strong>2021<\/strong>). Insights into SusCD-mediated glycan import by a prominent gut symbiont. <em><strong>Nat Commun.<\/strong><\/em>, 12(1):44. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1038\/s41467-020-20285-y\" target=\"_blank\">https:\/\/doi.org\/10.1038\/s41467-020-20285-y<\/a><\/p>\n\n\n\n<p>Luther A, Urfer M, <strong>Zahn M<\/strong>, M\u00fcller M, Wang SY, Mondal M, Vitale A, Hartmann JB, Sharpe T, Monte FL, Kocherla H, Cline E, Pessi G, Rath P, Modaresi SM, Chiquet P, Stiegeler S, Verbree C, Remus T, Schmitt M, Kolopp C, Westwood MA, Desjonqu\u00e8res N, Brabet E, Hell S, LePoupon K, Vermeulen A, Jaisson R, Rithi\u00e9 V, Upert G, Lederer A, Zbinden P, Wach A, Moehle K, Zerbe K, Loche, HH, Bernardini F, Dale GE, Eberl L, Wollscheid B, Hiller S, Robinson JA, Obrecht D (<strong>2019<\/strong>). Chimeric peptidomimetic antibiotics against Gram-negative bacteria. <em><strong>Nature<\/strong><\/em>, 576(7787):452-458. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1038\/s41586-019-1665-6\" target=\"_blank\">https:\/\/doi.org\/10.1038\/s41586-019-1665-6<\/a><\/p>\n\n\n\n<p><strong>Zahn M<\/strong>, Kurteva-Yaneva N, Schuster J, Krug U, Georgi T, M\u00fcller RH, Rohwerder T, Str\u00e4ter N (<strong>2019<\/strong>). Structures of 2-Hydroxyisobutyric Acid-CoA Ligase Reveal Determinants of Substrate Specificity and Describe a Multi-Conformational Catalytic Cycle. <em><strong>J Mol Biol<\/strong><\/em>, 431(15):2747-2761. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.jmb.2019.05.027\" target=\"_blank\">https:\/\/doi.org\/10.1016\/j.jmb.2019.05.027<\/a><\/p>\n\n\n\n<p>Kaur H*, Hartmann J-B*, Jakob RP*, <strong>Zahn M<\/strong>*, Zimmermann I, Maier T, Seeger MA, Hiller S (<strong>2019<\/strong>). Identification of conformation-selective nanobodies against the membrane protein insertase BamA by an integrated structural biology approach. <em><strong>J Biomol NMR<\/strong><\/em>, 73(6-7):375-384. (*Authors share first authorship) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1007\/s10858-019-00250-8\" target=\"_blank\">https:\/\/doi.org\/10.1007\/s10858-019-00250-8<\/a><\/p>\n\n\n\n<p>Bhamidimarri SP, <strong>Zahn M<\/strong>, Prajapati JD, Schleberger C, S\u00f6derholm S, Hoover J, West J, Kleinekath\u00f6fer U, Bumann D, Winterhalter M, van den Berg B (<strong>2019<\/strong>). A Multidisciplinary Approach toward Identification of Antibiotic Scaffolds for Acinetobacter baumannii. <em><strong>Structure<\/strong><\/em>. 27(2): 268-280. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.str.2018.10.021\" target=\"_blank\">https:\/\/doi.org\/10.1016\/j.str.2018.10.021<\/a><\/p>\n\n\n\n<p>Abell\u00f3n-Ruiz J, <strong>Zahn M<\/strong>, Basl\u00e9 A, van den Berg B (<strong>2018<\/strong>). Crystal structure of the Acinetobacter baumannii outer membrane protein Omp33. <em><strong>Acta Cryst.<\/strong><\/em><strong>D74<\/strong>, 852-860. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1107\/s205979831800904x\" target=\"_blank\">https:\/\/doi.org\/10.1107\/s205979831800904x<\/a><\/p>\n\n\n\n<p>Hartmann J-B*, <strong>Zahn M<\/strong>*, Burmann IM, Bibow S, Hiller S (<strong>2018<\/strong>). Sequence-specific solution NMR assignments of the \u03b2-barrel insertase BamA to monitor its conformational ensemble at the atomic level. <em><strong>J Am Chem Soc.<\/strong><\/em>, 140(36):11252-11260. (*Both authors share first authorship) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/jacs.8b03220\" target=\"_blank\">https:\/\/doi.org\/10.1021\/jacs.8b03220<\/a><\/p>\n\n\n\n<p>Acosta S, Ferrara L, Pathania M, Masi M, Wang J, Bodrenko I, <strong>Zahn M<\/strong>, Winterhalter M, Stavenger RA, Pages JM, Naismith JH, van den Berg B, Page M, Ceccarelli M <strong>(2018)<\/strong>. Getting drugs into Gram-negative bacteria: Rational rules for permeation through general porins. <em><strong>ACS Infect Dis.<\/strong>, <\/em>4 (10):1487-1498. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/acsinfecdis.8b00108\" target=\"_blank\">https:\/\/doi.org\/10.1021\/acsinfecdis.8b00108<\/a><\/p>\n\n\n\n<p>Aunkham A*, <strong>Zahn M<\/strong>*, Kesireddy A, Pothula KR, Schulte A, Basl\u00e9 A, Kleinekath\u00f6fer U, Suginta W, van den Berg B (<strong>2018<\/strong>). Structural basis for chitin acquisition by marine Vibrio species. <em><strong>Nat Commun.<\/strong><\/em>, 9 (1):220. (*Both authors share first authorship) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1038\/s41467-017-02523-y\" target=\"_blank\">https:\/\/doi.org\/10.1038\/s41467-017-02523-y<\/a><\/p>\n\n\n\n<p><strong>Zahn M<\/strong>, Bhamidimarri SP, Basl\u00e9 A, Winterhalter M, van den Berg B (<strong>2016<\/strong>). Structural Insights into Outer Membrane permeability of Acinetobacter baumannii. <em><strong>Structure<\/strong><\/em>, 24 (2), 221-31. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.str.2015.12.009\" target=\"_blank\">https:\/\/doi.org\/10.1016\/j.str.2015.12.009<\/a><\/p>\n\n\n\n<p><strong>Zahn M<\/strong>, D&#8217;Agostino T, Eren E, Basl\u00e9 A, Ceccarelli M, van den Berg B (<strong>2015<\/strong>). Small-Molecule Transport by CarO, an Abundant Eight-Stranded \u03b2-Barrel Outer Membrane Protein from Acinetobacter baumannii. <em><strong>J. Mol. Biol.<\/strong><\/em>, 427 (14), 2329-39. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.jmb.2015.03.016\" target=\"_blank\">https:\/\/doi.org\/10.1016\/j.jmb.2015.03.016<\/a><\/p>\n\n\n\n<p>Kurteva-Yaneva N*, <strong>Zahn M*<\/strong>, Weichler MT, Starke R, Harms H, M\u00fcller RH, Str\u00e4ter N, Rohwerder T (<strong>2015<\/strong>). Structural Basis of the Stereospecificity of Bacterial B12-dependent 2-Hydroxyisobutyryl-CoA Mutase. <em><strong>J. Biol. Chem.<\/strong><\/em>, 290 (15), 9727-37. (*Both authors share first authorship) <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1074\/jbc.m115.645689\" target=\"_blank\">https:\/\/doi.org\/10.1074\/jbc.m115.645689<\/a><\/p>\n\n\n\n<p>Schwan G, Barbar Asskar G, H\u00f6fgen N, Kubicova L, Funke U, Egerland U, <strong>Zahn M<\/strong>, Nieber K, Scheunemann M, Str\u00e4ter N, Brust P, Briel D (<strong>2014<\/strong>). Fluorine-containing 6,7-dialkoxybiaryl-based inhibitors for phosphodiesterase\u200510\u2009A: synthesis and in vitro evaluation of inhibitory potency, selectivity, and metabolism. <em><strong>ChemMedChem.<\/strong><\/em>, 9, 1476-1487. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1002\/cmdc.201300522\" target=\"_blank\">https:\/\/doi.org\/10.1002\/cmdc.201300522<\/a><\/p>\n\n\n\n<p><strong>Zahn<\/strong> <strong>M<\/strong>, Kieslich B, Berthold N, Knappe D, Hoffmann R, Strater N (<strong>2014<\/strong>). Structural identification of DnaK binding sites within bovine and sheep bactenecin Bac7. <em><strong>Protein Pept Lett.<\/strong><\/em>,21, 407-412. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.2174\/09298665113206660111\" target=\"_blank\">https:\/\/doi.org\/10.2174\/09298665113206660111<\/a><\/p>\n\n\n\n<p><strong>Zahn M<\/strong>, Berthold N, Kieslich B, Knappe D, Hoffmann R, Str\u00e4ter N (<strong>2013<\/strong>). Structural studies on the forward and reverse binding modes of proline rich antimicrobial peptides to the chaperone DnaK. <em><strong>J. Mol. Biol.<\/strong><\/em>,425, 2463-2479. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1016\/j.jmb.2013.03.041\" target=\"_blank\">https:\/\/doi.org\/10.1016\/j.jmb.2013.03.041 <\/a><\/p>\n\n\n\n<p>Simeonov P, <strong>Zahn M<\/strong>, Str\u00e4ter N <span class=\"amp\">&amp;<\/span> Zuchner T (<strong>2012<\/strong>). Crystal structure of a supercharged variant of the human enteropeptidase light chain. <em><strong>Proteins<\/strong><\/em><strong>, <\/strong>80, 1907-1910. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1002\/prot.24084\" target=\"_blank\">https:\/\/doi.org\/10.1002\/prot.24084<\/a><\/p>\n\n\n\n<p>Czihal P, Knappe D, Fritsche S, <strong>Zahn M<\/strong>, Berthold N, Piantavigna S, M\u00fcller U, Van Dorpe S, Herth N, Binas A, Kohler G, De Spiegeleer B, Martin LL, Nolte O, Str\u00e4ter N, Alber G <span class=\"amp\">&amp;<\/span> Hoffmann R (<strong>2012<\/strong>). Api88 is a novel antibacterial designer peptide to treat systemic infections with multidrug-resistant gram-negative pathogens. <em><strong>ACS Chem. Biol.<\/strong><\/em>,7, 1281-1291. <a rel=\"noreferrer noopener\" href=\"https:\/\/doi.org\/10.1021\/cb300063v\" target=\"_blank\">https:\/\/doi.org\/10.1021\/cb300063v<\/a><\/p>\n\n\n\n<p>Knappe D, <strong>Zahn M<\/strong>, Sauer U, Schiffer G, Str\u00e4ter N <span class=\"amp\">&amp;<\/span> Hoffmann R (<strong>2011<\/strong>). Rational design of oncocin derivatives with superior protease stabilities and antibacterial activities based on the high-resolution structure of the oncocin-DnaK complex. <em><strong>Chembiochem.<\/strong><\/em>, 12, 874-876. <a href=\"https:\/\/doi.org\/10.1002\/cbic.201000792\" target=\"_blank\" rel=\"noreferrer noopener\">https:\/\/doi.org\/10.1002\/cbic.201000792<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p>Heiringhoff RS, Greve JN, Zahn M, Manstein DJ (2025). Structure of the Human Non-Muscle Myosin 2A Motor Domain: Insights into Isoform-Specific Mechanochemistry. J Biol Chem. https:\/\/doi.org\/10.1016\/j.jbc.2025.110691 Dexter GN, Grigg JC, Zahn M, Wheatley EJ, Lian J, Mohn WW, Eltis LD (2025). Characterization of a two-component kinase that initiates the bacterial catabolism of hydroxyphenylethanones. J Biol [&hellip;]<\/p>\n","protected":false},"author":6234,"featured_media":0,"parent":0,"menu_order":3,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/pages\/16"}],"collection":[{"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/users\/6234"}],"replies":[{"embeddable":true,"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/comments?post=16"}],"version-history":[{"count":10,"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/pages\/16\/revisions"}],"predecessor-version":[{"id":179,"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/pages\/16\/revisions\/179"}],"wp:attachment":[{"href":"https:\/\/blogs.urz.uni-halle.de\/proteinproductionfacility\/wp-json\/wp\/v2\/media?parent=16"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}