Lysozym (German Wikipedia)

Analysis of information sources in references of the Wikipedia article "Lysozym" in German language version.

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ajcn.org

  • Bo Lönnerdal: Nutritional and physiologic significance of human milk proteins. In: The American journal of clinical nutrition. Band 77, Nr. 6, Juni 2003, S. 1537S–1543S, PMID 12812151 (ajcn.org).

deutsche-apotheker-zeitung.de

doi.org

  • Pierre Jollès, Jacqueline Jollès: What’s new in lysozyme research? Always a model system, today as yesterday. In: Molecular and Cellular Biochemistry. Band 63, Nr. 2, September 1984, S. 165–189, doi:10.1007/BF00285225, PMID 6387440.
  • P. Laschtschenko: Über die keimtötende und entwicklungshemmende Wirkung von Hühnereiweiß. In: Zeitschrift für Hygiene und Infektionskrankheiten. Band 64, Nr. 1, Dezember 1909, S. 419–427, doi:10.1007/BF02216170.
  • A. Fleming: On a Remarkable Bacteriolytic Element Found in Tissues and Secretions. In: Proceedings of the Royal Society B: Biological Sciences. Band 93, Nr. 653, 1. Mai 1922, S. 306–317, doi:10.1098/rspb.1922.0023.
  • C. C. F. Blake, D. F. Koenig, G. A. Mair, A. C. T. North, D. C. Phillips, V. R. Sarma: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution. In: Nature. Band 206, Nr. 4986, 22. Mai 1965, S. 757–761, doi:10.1038/206757a0, PMID 5891407.
  • Louise N. Johnson, David C. Phillips: Structure of Some Crystalline Lysozyme-Inhibitor Complexes Determined by X-Ray Analysis At 6 Å Resolution. In: Nature. Band 206, Nr. 4986, 22. Mai 1965, S. 761–763, doi:10.1038/206761a0, PMID 5840126.
  • C. C. F. Blake, G. A. Mair, A. C. T. North, D. C. Phillips, V. R. Sarma: On the Conformation of the Hen Egg-White Lysozyme Molecule. In: Proceedings of the Royal Society B: Biological Sciences. Band 167, 1009, A Discussion on the Structure and Function of Lysozyme, 18. April 1967, S. 365–377, doi:10.1098/rspb.1967.0034.
  • C. C. F. Blake, G. A. Mair, A. C. T. North, D. C. Phillips, V. R. Sarma: Crystallographic Studies of the Activity of Hen Egg-White Lysozyme. In: Proceedings of the Royal Society B: Biological Sciences. Band 167, 1009, A Discussion on the Structure and Function of Lysozyme, 18. April 1967, S. 378–388, doi:10.1098/rspb.1967.0034.
  • David J. Vocadlo, Gideon J. Davies, Roger Laine, Stephen G. Withers: Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. In: Nature. Band 412, Nr. 6849, 23. August 2001, S. 835–838, doi:10.1038/35090602, PMID 11518970.
  • Gideon Davies, Bernard Henrissat: Structures and mechanisms of glycosyl hydrolases. In: Structure. Band 3, Nr. 9, September 1995, S. 853–859, doi:10.1016/S0969-2126(01)00220-9.
  • Bernard Henrissat, Gideon Davies: Structural and sequence-based classification of glycoside hydrolases. In: Current Opinion in Structural Biology. Band 7, Nr. 5, Oktober 1997, S. 637–644, doi:10.1016/S0959-440X(97)80072-3, PMID 9345621.
  • Lien Callewaert, Maarten Walmagh, Chris W. Michiels, Rob Lavigne: Food applications of bacterial cell wall hydrolases. In: Current Opinion in Biotechnology. Band 22, Nr. 2, April 2011, S. 164–171, doi:10.1016/j.copbio.2010.10.012, PMID 21093250.
  • Lien Callewaert, Chris W. Michiels: Lysozymes in the animal kingdom. In: Journal of Biosciences. Band 35, Nr. 1, März 2010, S. 127–160, doi:10.1007/s12038-010-0015-5, PMID 20413917.
  • I. Müller, N. Subert, H. Otto, R. Herbst, H. Rühling, M. Maniak, M. Leippe: A Dictyostelium Mutant with Reduced Lysozyme Levels Compensates by Increased Phagocytic Activity. In: Journal of Biological Chemistry. Band 280, Nr. 11, 11. Januar 2005, S. 10435–10443, doi:10.1074/jbc.M411445200, PMID 15640146.
  • N. L. Thakur, S. Perovi -Ottstadt, R. Batel, M. Korzhev, B. Diehl-Seifert, I. M. Mueller, W. E. G. Mueller: Innate immune defense of the sponge Suberites domuncula against gram-positive bacteria: induction of lysozyme and AdaPTin. In: Marine Biology. Band 146, Nr. 2, Januar 2005, S. 271–282, doi:10.1007/s00227-004-1438-z.
  • David M Irwin, Jason M Biegel, Caro-Beth Stewart: Evolution of the mammalian lysozyme gene family. In: BMC Evolutionary Biology. Band 11, Nr. 1, 2011, S. 166, doi:10.1186/1471-2148-11-166, PMID 21676251, PMC 3141428 (freier Volltext).
  • P. Huang, W. S. Li, J. Xie, X. M. Yang, D. K. Jiang, S. Jiang, L. Yu: Characterization and expression of HLysG2, a basic goose-type lysozyme from the human eye and testis. In: Molecular immunology. Band 48, Nr. 4, Januar 2011, S. 524–531, doi:10.1016/j.molimm.2010.10.008, PMID 21093056.
  • R. Kuroki, L. Weaver, B. Matthews: A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme. In: Science. Band 262, Nr. 5142, 24. Dezember 1993, S. 2030–2033, doi:10.1126/science.8266098, PMID 8266098.
  • Walter A. Baase, Lijun Liu, Dale E. Tronrud, Brian W. Matthews: Lessons from the lysozyme of phage T4. In: Protein Science. Band 19, Nr. 4, April 2010, S. 631–641, doi:10.1002/pro.344.
  • Jane D Funkhouser, Nathan N Aronson: Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family. In: BMC Evolutionary Biology. Band 7, Nr. 1, 2007, S. 96, doi:10.1186/1471-2148-7-96, PMID 17594485, PMC 1945033 (freier Volltext).
  • N. A. Udaya Prakash, M. Jayanthi, R. Sabarinathan, P. Kangueane, Lazar Mathew, K. Sekar: Evolution, Homology Conservation, and Identification of Unique Sequence Signatures in GH19 Family Chitinases. In: Journal of Molecular Evolution. Band 70, Nr. 5, Mai 2010, S. 466–478, doi:10.1007/s00239-010-9345-z, PMID 20480157.
  • Manuela Villion, Sylvain Moineau: Bacteriophages of Lactobacillus. In: Frontiers in Bioscience, Band 14, Nr. 14, Februar 2009, S. 1661–1683; doi:10.2741/3332, PMID 19273154. Siehe insbes. Tbl. 2: Lactobacillus Siphoviridae phages auf S. 1667.
  • H. A. McKenzie, F.H. White (Jr.): Lysozyme and α-lactalbumin: structure, function and interrelationships. In: Advances in Protein Chemistry. Band 41, 1991, S. 173–315, doi:10.1016/S0065-3233(08)60198-9, PMID 2069076.
  • Yasuhiro Nonaka, Daisuke Akieda, Tomoyasu Aizawa, Nobuhisa Watanabe, Masakatsu Kamiya, Yasuhiro Kumaki, Mineyuki Mizuguchi, Takashi Kikukawa, Makoto Demura, Keiichi Kawano: X-ray crystallography and structural stability of digestive lysozyme from cow stomach. In: FEBS Journal. Band 276, Nr. 8, April 2009, S. 2192–2200, doi:10.1111/j.1742-4658.2009.06948.x, PMID 19348005.
  • M. Xu, A. Arulandu, D. K. Struck, S. Swanson, J. C. Sacchettini, R. Young: Disulfide Isomerization After Membrane Release of Its SAR Domain Activates P1 Lysozyme. In: Science. Band 307, Nr. 5706, 7. Januar 2005, S. 113–117, doi:10.1126/science.1105143, PMID 15637279.
  • A. Rau, T. Hogg, R. Marquardt, R. Hilgenfeld: A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution. In: Journal of Biological Chemistry. Band 276, Nr. 34, August 2001, S. 31994–31999, doi:10.1074/jbc.M102591200, PMID 11427528.
  • Erik J. van Asselt, Kor H. Kalk, Bauke W. Dijkstra: Crystallographic Studies of the Interactions of Lytic Transglycosylase Slt35 with Peptidoglycan. In: Biochemistry. Band 39, Nr. 8, Februar 2000, S. 1924–1934, doi:10.1021/bi992161p.
  • Maike Bublitz, Lilia Polle, Christin Holland, Dirk W. Heinz, Manfred Nimtz, Wolf-Dieter Schubert: Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes. In: Molecular Microbiology. Band 71, Nr. 6, März 2009, S. 1509–1522, doi:10.1111/j.1365-2958.2009.06619.x, PMID 19210622.
  • Severine Layec, Bernard Decaris, Nathalie Leblond-Bourget: Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation. In: Research in Microbiology. Band 159, Nr. 7-8, September 2008, S. 507–515, doi:10.1016/j.resmic.2008.06.008, PMID 18656532.
  • Edie Scheurwater, Chris W. Reid, Anthony J. Clarke: Lytic transglycosylases: Bacterial space-making autolysins. In: The International Journal of Biochemistry & Cell Biology. Band 40, Nr. 4, Januar 2008, S. 586–591, doi:10.1016/j.biocel.2007.03.018.
  • T. Goto, Y. Abe, Y. Kakuta, K. Takeshita, T. Imoto, T. Ueda: Crystal structure of Tapes japonica Lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change. In: Journal of Biological Chemistry. Band 282, Nr. 37, 10. Juli 2007, S. 27459–27467, doi:10.1074/jbc.M704555200, PMID 17631496.
  • David L. Ollis, Eong Cheah, Miroslaw Cygler, Bauke Dijkstra, Felix Frolow, Sybille M. Franken, Michal Harel, S. Jamse Remington, Israel Silman, Joseph Schrag, Joel L. Sussman, Koen H.G. Verschueren, Adrian Goldman: The α/β hydrolase fold. In: Protein Engineering, Design and Selection (PEDS). Band 5, Nr. 3, 1992, S. 197–211, doi:10.1093/protein/5.3.197, PMID 1409539.
  • Ronny Helland, Renate L. Larsen, Solrun Finstad, Peter Kyomuhendo, Atle N. Larsen: Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism. In: Cellular and Molecular Life Sciences. Band 66, Nr. 15, August 2009, S. 2585–2598, doi:10.1007/s00018-009-0063-x, PMID 19543850.
  • R. Kuroki, L. H. Weaver, B. W. Matthews: Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. In: Proceedings of the National Academy of Sciences. Band 96, Nr. 16, 3. August 1999, S. 8949–8954, doi:10.1073/pnas.96.16.8949, PMID 10430876, PMC 17713 (freier Volltext).
  • A. Fokine, K. A. Miroshnikov, M. M. Shneider, V. V. Mesyanzhinov, M. G. Rossmann: Structure of the Bacteriophage φKZ Lytic Transglycosylase gp144. In: Journal of Biological Chemistry. Band 283, Nr. 11, 14. Januar 2008, S. 7242–7250, doi:10.1074/jbc.M709398200, PMID 18160394.
  • Bin Yang, Jianwu Wang, B. o. Tang, Yufang Liu, Chengdong Guo, Penghua Yang, Tian Yu, Rong Li, Jianmin Zhao, Lei Zhang, Yunping Dai, Ning Li, Vladimir Uversky: Characterization of Bioactive Recombinant Human Lysozyme Expressed in Milk of Cloned Transgenic Cattle. In: PLoS ONE. Band 6, Nr. 3, 16. März 2011, S. e17593, doi:10.1371/journal.pone.0017593.
  • Jia Tong, HengXi Wei, XiaoFang Liu, WenPing Hu, MingJun Bi, YuanYuan Wang, QiuYan Li, Ning Li: Production of recombinant human lysozyme in the milk of transgenic pigs. In: Transgenic Research. Band 20, Nr. 2, April 2011, S. 417–419, doi:10.1007/s11248-010-9409-2.
  • M. Revenis, M. Kaliner: Lactoferrin and lysozyme deficiency in airway secretions: Association with the development of bronchopulmonary dysplasia. In: The Journal of Pediatrics. Band 121, Nr. 2, August 1992, S. 262–270, doi:10.1016/S0022-3476(05)81201-6, PMID 1640295.
  • Elli Koivunen, Carola Groenhagen-Riska, Matti Klockars, Olof Selroos: Blood Monocytes and Serum and Bone Marrow Lysozyme in Sarcoidosis. In: Acta Medica Scandinavica. Band 210, Nr. 1-6, 12. Januar 1981, S. 107–110, doi:10.1111/j.0954-6820.1981.tb09784.x.
  • Bärbel Porstmann, Kurt Jung, Helmut Schmechta, Ursula Evers, Monika Pergande, Tomas Porstmann, Hans-Joachim Kramm, Heinz Krause: Measurement of lysozyme in human body fluids: Comparison of various enzyme immunoassay techniques and their diagnostic application. In: Clinical Biochemistry. Band 22, Nr. 5, Oktober 1989, S. 349–355, doi:10.1016/S0009-9120(89)80031-1.
  • Michael H. Grieco, Mohan M. Reddy, Harish B. Kothari, Michael Lange, Elena Buimovici-Klein, Daniel William: Elevated β2-microglobulin and lysozyme levels in patients with acquired immune deficiency syndrome. In: Clinical Immunology and Immunopathology. Band 32, Nr. 2, August 1984, S. 174–184, doi:10.1016/0090-1229(84)90119-3.
  • I. Torsteinsdóttir, L. Håkansson, R. Hällgren, B. Gudbjörnsson, N.-G. Arvidson, P. Venge: Serum lysozyme: a potential marker of monocyte/macrophage activity in rheumatoid arthritis. In: Rheumatology. Band 38, Nr. 12, 1999, S. 1249–1254, doi:10.1093/rheumatology/38.12.1249.
  • Per Venge, Tony Foucard, Jörn Henriksen, Lena Håkansson, Anders Kreuger: Serum-levels of lactoferrin, lysozyme and myeloperoxidase in normal, infection-prone and leukemic children. In: Clinica Chimica Acta. Band 136, Nr. 2-3, 31. Januar 1984, S. 121–130, doi:10.1016/0009-8981(84)90283-3.
  • Johan Brouwer, Trudi van Leeuwen-Herberts, Marjo Otting-van de Ruit: Determination of lysozyme in serum, urine, cerebrospinal fluid and feces by enzyme immunoassay. In: Clinica Chimica Acta. Band 142, Nr. 1, 15. September 1984, S. 21–30, doi:10.1016/0009-8981(84)90097-4.

europa.eu

eur-lex.europa.eu

efsa.europa.eu

jbc.org

lww.com

journals.lww.com

  • P. E. Perillie, K. Khan, S. C. Finch: Serum lysozyme in pulmonary tuberculosis. In: American Journal of Medical Science. Band 265, Nr. 4, April 1973, S. 297–302, PMID 4196282 (lww.com).

nih.gov

ncbi.nlm.nih.gov

  • Pierre Jollès, Jacqueline Jollès: What’s new in lysozyme research? Always a model system, today as yesterday. In: Molecular and Cellular Biochemistry. Band 63, Nr. 2, September 1984, S. 165–189, doi:10.1007/BF00285225, PMID 6387440.
  • Robert E. Canfield: The Amino Acid Sequence of Egg White Lysozyme. In: The Journal of biological chemistry. Band 238, Nr. 8, August 1963, S. 2698–2707, PMID 14063294 (jbc.org).
  • C. C. F. Blake, D. F. Koenig, G. A. Mair, A. C. T. North, D. C. Phillips, V. R. Sarma: Structure of Hen Egg-White Lysozyme: A Three-dimensional Fourier Synthesis at 2 Å Resolution. In: Nature. Band 206, Nr. 4986, 22. Mai 1965, S. 757–761, doi:10.1038/206757a0, PMID 5891407.
  • Louise N. Johnson, David C. Phillips: Structure of Some Crystalline Lysozyme-Inhibitor Complexes Determined by X-Ray Analysis At 6 Å Resolution. In: Nature. Band 206, Nr. 4986, 22. Mai 1965, S. 761–763, doi:10.1038/206761a0, PMID 5840126.
  • David J. Vocadlo, Gideon J. Davies, Roger Laine, Stephen G. Withers: Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. In: Nature. Band 412, Nr. 6849, 23. August 2001, S. 835–838, doi:10.1038/35090602, PMID 11518970.
  • Bernard Henrissat: A classification of glycosyl hydrolases based on amino-acid sequence similarities. In: Biochemical Journal. Band 280, Nr. 2, 1. Dezember 1991, S. 309–316, PMID 1747104, PMC 1130547 (freier Volltext).
  • Bernard Henrissat, Amos Bairoch: New families in the classification of glycosyl hydrolases based on amino- acid sequence similarities. In: The Biochemical journal. Band 293, Nr. 3, 1. August 1993, S. 781–788, PMID 8352747, PMC 1134435 (freier Volltext).
  • Bernard Henrissat, Amos Bairoch: Updating the sequence-based classification of glycosyl hydrolases. In: The Biochemical journal. Band 316, Nr. 2, 1. Juni 1996, S. 695–696, PMID 8687420, PMC 1217404 (freier Volltext).
  • Bernard Henrissat, Gideon Davies: Structural and sequence-based classification of glycoside hydrolases. In: Current Opinion in Structural Biology. Band 7, Nr. 5, Oktober 1997, S. 637–644, doi:10.1016/S0959-440X(97)80072-3, PMID 9345621.
  • Lien Callewaert, Maarten Walmagh, Chris W. Michiels, Rob Lavigne: Food applications of bacterial cell wall hydrolases. In: Current Opinion in Biotechnology. Band 22, Nr. 2, April 2011, S. 164–171, doi:10.1016/j.copbio.2010.10.012, PMID 21093250.
  • Lien Callewaert, Chris W. Michiels: Lysozymes in the animal kingdom. In: Journal of Biosciences. Band 35, Nr. 1, März 2010, S. 127–160, doi:10.1007/s12038-010-0015-5, PMID 20413917.
  • I. Müller, N. Subert, H. Otto, R. Herbst, H. Rühling, M. Maniak, M. Leippe: A Dictyostelium Mutant with Reduced Lysozyme Levels Compensates by Increased Phagocytic Activity. In: Journal of Biological Chemistry. Band 280, Nr. 11, 11. Januar 2005, S. 10435–10443, doi:10.1074/jbc.M411445200, PMID 15640146.
  • J. Fastrez: Phage lysozymes. In: EXS (Lysozymes: Model Enzymes in Biochemistry and Biology). Band 75, 1996, S. 35–64, PMID 8765293.
  • J. J. Beintema und A. C. Terwisscha van Scheltinga: Plant lysozymes. In: EXS (Lysozymes: Model Enzymes in Biochemistry and Biology). Band 75, 1996, S. 75–86, PMID 8765295.
  • J.-V. Höltje: Bacterial lysozymes. In: EXS (Lysozymes: Model Enzymes in Biochemistry and Biology). Band 75, 1996, S. 65–74, PMID 8765294.
  • H. A. McKenzie: α-Lactalbumins and lysozymes. In: EXS (Lysozymes: Model Enzymes in Biochemistry and Biology). Band 75, 1996, S. 365–409, PMID 8765309.
  • David M Irwin, Jason M Biegel, Caro-Beth Stewart: Evolution of the mammalian lysozyme gene family. In: BMC Evolutionary Biology. Band 11, Nr. 1, 2011, S. 166, doi:10.1186/1471-2148-11-166, PMID 21676251, PMC 3141428 (freier Volltext).
  • NCBI; Dezember 2009
  • P. Huang, W. S. Li, J. Xie, X. M. Yang, D. K. Jiang, S. Jiang, L. Yu: Characterization and expression of HLysG2, a basic goose-type lysozyme from the human eye and testis. In: Molecular immunology. Band 48, Nr. 4, Januar 2011, S. 524–531, doi:10.1016/j.molimm.2010.10.008, PMID 21093056.
  • R. Kuroki, L. Weaver, B. Matthews: A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme. In: Science. Band 262, Nr. 5142, 24. Dezember 1993, S. 2030–2033, doi:10.1126/science.8266098, PMID 8266098.
  • J.-V. Höltje: Lytic transglycosidases. In: EXS (Lysozymes: Model Enzymes in Biochemistry and Biology). Band 75, 1996, S. 425–429, PMID 8765311.
  • Jane D Funkhouser, Nathan N Aronson: Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family. In: BMC Evolutionary Biology. Band 7, Nr. 1, 2007, S. 96, doi:10.1186/1471-2148-7-96, PMID 17594485, PMC 1945033 (freier Volltext).
  • N. A. Udaya Prakash, M. Jayanthi, R. Sabarinathan, P. Kangueane, Lazar Mathew, K. Sekar: Evolution, Homology Conservation, and Identification of Unique Sequence Signatures in GH19 Family Chitinases. In: Journal of Molecular Evolution. Band 70, Nr. 5, Mai 2010, S. 466–478, doi:10.1007/s00239-010-9345-z, PMID 20480157.
  • NCBI: Lactobacillus phage mv1 (spezies)
  • Manuela Villion, Sylvain Moineau: Bacteriophages of Lactobacillus. In: Frontiers in Bioscience, Band 14, Nr. 14, Februar 2009, S. 1661–1683; doi:10.2741/3332, PMID 19273154. Siehe insbes. Tbl. 2: Lactobacillus Siphoviridae phages auf S. 1667.
  • H. A. McKenzie, F.H. White (Jr.): Lysozyme and α-lactalbumin: structure, function and interrelationships. In: Advances in Protein Chemistry. Band 41, 1991, S. 173–315, doi:10.1016/S0065-3233(08)60198-9, PMID 2069076.
  • J. P. van de Merwe, J. Lindemans, G. J. Mol: Plasma lysozyme levels and decay of neutrophilic granulocytes in patients with Crohn’s disease. In: Hepatogastroenterology. Band 27, Nr. 2, April 1980, S. 130–134, PMID 7216126.
  • Yasuhiro Nonaka, Daisuke Akieda, Tomoyasu Aizawa, Nobuhisa Watanabe, Masakatsu Kamiya, Yasuhiro Kumaki, Mineyuki Mizuguchi, Takashi Kikukawa, Makoto Demura, Keiichi Kawano: X-ray crystallography and structural stability of digestive lysozyme from cow stomach. In: FEBS Journal. Band 276, Nr. 8, April 2009, S. 2192–2200, doi:10.1111/j.1742-4658.2009.06948.x, PMID 19348005.
  • M. Xu, A. Arulandu, D. K. Struck, S. Swanson, J. C. Sacchettini, R. Young: Disulfide Isomerization After Membrane Release of Its SAR Domain Activates P1 Lysozyme. In: Science. Band 307, Nr. 5706, 7. Januar 2005, S. 113–117, doi:10.1126/science.1105143, PMID 15637279.
  • A. Rau, T. Hogg, R. Marquardt, R. Hilgenfeld: A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 A resolution. In: Journal of Biological Chemistry. Band 276, Nr. 34, August 2001, S. 31994–31999, doi:10.1074/jbc.M102591200, PMID 11427528.
  • Maike Bublitz, Lilia Polle, Christin Holland, Dirk W. Heinz, Manfred Nimtz, Wolf-Dieter Schubert: Structural basis for autoinhibition and activation of Auto, a virulence-associated peptidoglycan hydrolase of Listeria monocytogenes. In: Molecular Microbiology. Band 71, Nr. 6, März 2009, S. 1509–1522, doi:10.1111/j.1365-2958.2009.06619.x, PMID 19210622.
  • Severine Layec, Bernard Decaris, Nathalie Leblond-Bourget: Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation. In: Research in Microbiology. Band 159, Nr. 7-8, September 2008, S. 507–515, doi:10.1016/j.resmic.2008.06.008, PMID 18656532.
  • J.-V. Höltje: Lysozyme substrates. In: EXS (Lysozymes: Model Enzymes in Biochemistry and Biology). Band 75, 1996, S. 105–110, PMID 8765297.
  • T. Goto, Y. Abe, Y. Kakuta, K. Takeshita, T. Imoto, T. Ueda: Crystal structure of Tapes japonica Lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change. In: Journal of Biological Chemistry. Band 282, Nr. 37, 10. Juli 2007, S. 27459–27467, doi:10.1074/jbc.M704555200, PMID 17631496.
  • David L. Ollis, Eong Cheah, Miroslaw Cygler, Bauke Dijkstra, Felix Frolow, Sybille M. Franken, Michal Harel, S. Jamse Remington, Israel Silman, Joseph Schrag, Joel L. Sussman, Koen H.G. Verschueren, Adrian Goldman: The α/β hydrolase fold. In: Protein Engineering, Design and Selection (PEDS). Band 5, Nr. 3, 1992, S. 197–211, doi:10.1093/protein/5.3.197, PMID 1409539.
  • Ronny Helland, Renate L. Larsen, Solrun Finstad, Peter Kyomuhendo, Atle N. Larsen: Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism. In: Cellular and Molecular Life Sciences. Band 66, Nr. 15, August 2009, S. 2585–2598, doi:10.1007/s00018-009-0063-x, PMID 19543850.
  • R. Kuroki, L. H. Weaver, B. W. Matthews: Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. In: Proceedings of the National Academy of Sciences. Band 96, Nr. 16, 3. August 1999, S. 8949–8954, doi:10.1073/pnas.96.16.8949, PMID 10430876, PMC 17713 (freier Volltext).
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