Characterization of the specificity of human neutrophil elastase for Shigella flexneri virulence factorsPetra Averhoff111.11.1.121.1.21.1.334562#3641.1.451.21.2.161.2.271.2.38427#45591.3101.41.4.1111.4.2436#36712360#8613421#16114408#39615454#1101.4.31617466#470181.5192192.12.1.1202.1.22.1.3212.1.42.22.2.12.2.2222.2.32.2.42.32.3.1232.3.22.3.32.3.4242.3.52.42.52.5.1252.5.22.5.3262.5.4272.62.6.1282.6.22.6.3292.72.7.12.7.22.7.3302.7.4312.7.52.8323323.13.1.133527#15534627#2113.1.235474#1573.2363.2.137437#19238409#2823.2.23940493#2783.2.341582#36842302#15243486#190443.2.4561#27645593#5503.2.546546#20847477#36148550#27649351#2583.2.650570#1935152530#54853582#4304544.14.1.14.1.255564.24.2.14.2.257 NE mutants 35-41 and 58A-61370#4175859NE mutants F192A, F192K and A213V60361#34161NE mutants F215Y and F215A 62395#381NE mutants 216-218 and 216-22463406#41964NE mutant N98L and N98A65528#4194.2.3665665.1575#3435.2636#630491#5645.3593#6615.4488#619464#291329#145405#288AbbreviationsReferencesCurriculum Vitae PublicationsAcknowledgementsSelbständigkeitserklärungenTable of contentsHelp References

Allaoui, A.; Sansonetti, P. J. and Parsot, C. (1992): MxiJ, a lipoprotein involved in secretion of Shigella Ipa invasins, is homologous to YscJ, a secretion factor of the Yersinia Yop proteins, J Bacteriol 174 [23], pp.7661-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1332940 Allaoui, A.; Sansonetti, P. J. and Parsot, C. (1993): MxiD, an outer membrane protein necessary for the secretion of the Shigella flexneri lpa invasins, Mol Microbiol 7 [1], pp.59-68. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8437520 Ancliff, P. J.; Gale, R. E.; Liesner, R.; Hann, I. M. and Linch, D. C. (2001): Mutations in the ELA2 gene encoding neutrophil elastase are present in most patients with sporadic severe congenital neutropenia but only in some patients with the familial form of the disease, Blood 98 [9], pp.2645-50. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11675333 Andrews, G. P.; Hromockyj, A. E.; Coker, C. and Maurelli, A. T. (1991): Two novel virulence loci, mxiA and mxiB, in Shigella flexneri 2a facilitate excretion of invasion plasmid antigens, Infect Immun 59 [6], pp.1997-2005. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2037361 Arends, M. J. and Wyllie, A. H. (1991): Apoptosis: mechanisms and roles in pathology, Int Rev Exp Pathol 32, pp.223-54. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1677933 Avila, J. L. and Convit, J. (1976): Physicochemical characteristics of the glycosaminoglycan-lysosomal enzyme interaction in vitro. A model of control of leucocytic lysosomal activity, Biochem J 160 [2], pp.129-36. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12748 Baggiolini, M.; Schnyder, J.; Bretz, U.; Dewald, B. and Ruch, W. (1979): Cellular mechanisms of proteinase release from inflammatory cells and the degradation of extracellular proteins, Ciba Found Symp [75], pp.105-21. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=399884 Bangalore, N.; Travis, J.; Onunka, V. C.; Pohl, J. and Shafer, W. M. (1990): Identification of the primary antimicrobial domains in human neutrophil cathepsin G, J Biol Chem 265 [23], pp.13584-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2116408 Barrett, A. J. and Rawlings, N. D. (1995): Families and clans of serine peptidases, Arch Biochem Biophys 318 [2], pp.247-50. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7733651 Beatty, K.; Bieth, J. and Travis, J. (1980): Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin, J Biol Chem 255 [9], pp.3931-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6989830 Belaaouaj, A.; Kim, K. S. and Shapiro, S. D. (2000): Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase, Science 289 [5482], pp.1185-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10947984 Belaaouaj, A.; McCarthy, R.; Baumann, M.; Gao, Z.; Ley, T. J.; Abraham, S. N. and Shapiro, S. D. (1998): Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis, Nat Med 4 [5], pp.615-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9585238 Berg JM, Tymoczko JL, Stryer L (2003): Biochemie, 4. Auflage. ed., Spektrum Akademischer Verlag Heidelberg- Berlin,

Heidelberg
, 3-8274-1303-6. Bernardini, M. L.; Mounier, J.; d'Hauteville, H.; Coquis-Rondon, M. and Sansonetti, P. J. (1989): Identification of icsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin, Proc Natl Acad Sci U S A 86 [10], pp.3867-71. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2542950 Biggs, J. R.; Yang, J.; Gullberg, U.; Muchardt, C.; Yaniv, M. and Kraft, A. S. (2001): The human brm protein is cleaved during apoptosis: the role of cathepsin G, Proc Natl Acad Sci U S A 98 [7], pp.3814-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11259672 Birrer, P.; McElvaney, N. G.; Rudeberg, A.; Sommer, C. W.; Liechti-Gallati, S.; Kraemer, R.; Hubbard, R. and Crystal, R. G. (1994): Protease-antiprotease imbalance in the lungs of children with cystic fibrosis, Am J Respir Crit Care Med 150 [1], pp.207-13. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7912987 Blocker, A.; Gounon, P.; Larquet, E.; Niebuhr, K.; Cabiaux, V.; Parsot, C. and Sansonetti, P. (1999): The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes, J Cell Biol 147 [3], pp.683-93. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10545510 Bode, W.; Meyer, E., Jr. and Powers, J. C. (1989): Human leukocyte and porcine pancreatic elastase: X-ray crystal structures, mechanism, substrate specificity, and mechanism-based inhibitors, Biochemistry 28 [5], pp.1951-63. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2655701 Bode, W.; Wei, A. Z.; Huber, R.; Meyer, E.; Travis, J. and Neumann, S. (1986b): X-ray crystal structure of the complex of human leukocyte elastase (PMN elastase) and the third domain of the turkey ovomucoid inhibitor, Embo J 5 [10], pp.2453-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3640709 Borregaard, N. and Cowland, J. B. (1997): Granules of the human neutrophilic polymorphonuclear leukocyte, Blood 89 [10], pp.3503-21. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9160655 Bradford, M. M. (1976): A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal Biochem 72, pp.248-54. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=942051 Brinkmann, V.; Reichard, U.; Goosmann, C.; Fauler, B.; Uhlemann, Y.; Weiss, D. S.; Weinrauch, Y. and Zychlinsky, A. (2004): Neutrophil extracellular traps kill bacteria, Science 303 [5663], pp.1532-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15001782 Brown, G. R.; McGuire, M. J. and Thiele, D. L. (1993): Dipeptidyl peptidase I is enriched in granules of in vitro- and in vivo-activated cytotoxic T lymphocytes, J Immunol 150 [11], pp.4733-42. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8496587 Bruce, M. C.; Poncz, L.; Klinger, J. D.; Stern, R. C.; Tomashefski, J. F., Jr. and Dearborn, D. G. (1985): Biochemical and pathologic evidence for proteolytic destruction of lung connective tissue in cystic fibrosis, Am Rev Respir Dis 132 [3], pp.529-35. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3898942 Burg, N. D. and Pillinger, M. H. (2001): The neutrophil: function and regulation in innate and humoral immunity, Clin Immunol 99 [1], pp.7-17. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11286537 Campbell, E. J.; Silverman, E. K. and Campbell, M. A. (1989): Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity, J Immunol 143 [9], pp.2961-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2681419 Caughey, G. H. (1994): Serine proteinases of mast cell and leukocyte granules. A league of their own, Am J Respir Crit Care Med 150 [6 Pt 2], pp.S138-42. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7952649 CDC2005Centers for Disease Control and Prevention 13.10.2005http://www.cdc.gov/ncidod/dbmd/diseaseinfo/shigellosis_g.htm Chen, Y.; Smith, M. R.; Thirumalai, K. and Zychlinsky, A. (1996): A bacterial invasin induces macrophage apoptosis by binding directly to ICE, Embo J 15 [15], pp.3853-60. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8670890 Cornelis, G. R. and Van Gijsegem, F. (2000): Assembly and function of type III secretory systems, Annu Rev Microbiol 54, pp.735-74. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11018143 Coster, T. S.; Hoge, C. W.; VanDeVerg, L. L.; Hartman, A. B.; Oaks, E. V.; Venkatesan, M. M.; Cohen, D.; Robin, G.; Fontaine-Thompson, A.; Sansonetti, P. J. and Hale, T. L. (1999): Vaccination against shigellosis with attenuated Shigella flexneri 2a strain SC602, Infect Immun 67 [7], pp.3437-43. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10377124 Delacourt, C.; Herigault, S.; Delclaux, C.; Poncin, A.; Levame, M.; Harf, A.; Saudubray, F. and Lafuma, C. (2002): Protection against acute lung injury by intravenous or intratracheal pretreatment with EPI-HNE-4, a new potent neutrophil elastase inhibitor, Am J Respir Cell Mol Biol 26 [3], pp.290-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11867337 DeLano, W.L. 2002 The PyMOL Molecular Graphics System
San Carlos, Ca, USA
DeLano Scientific http://pymol.sourceforge.net/ Devaney, J. M.; Greene, C. M.; Taggart, C. C.; Carroll, T. P.; O'Neill, S. J. and McElvaney, N. G. (2003): Neutrophil elastase up-regulates interleukin-8 via toll-like receptor 4, FEBS Lett 544 [1-3], pp.129-32. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12782302 Dinarello, C. A. (1998): Interleukin-1 beta, interleukin-18, and the interleukin-1 beta converting enzyme, Ann N Y Acad Sci 856, pp.1-11. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9917859 Dinauer, M. C.; Lekstrom-Himes, J. A. and Dale, D. C. (2000): Inherited Neutrophil Disorders: Molecular Basis and New Therapies, Hematology (Am Soc Hematol Educ Program), pp.303-318. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11701548 DuPont, H. L.; Levine, M. M.; Hornick, R. B. and Formal, S. B. (1989): Inoculum size in shigellosis and implications for expected mode of transmission, J Infect Dis 159 [6], pp.1126-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2656880 Edgar, R. C. (2004): MUSCLE: multiple sequence alignment with high accuracy and high throughput, Nucleic Acids Res 32 [5], pp.1792-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15034147 Egile, C.; Loisel, T. P.; Laurent, V.; Li, R.; Pantaloni, D.; Sansonetti, P. J. and Carlier, M. F. (1999): Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility, J Cell Biol 146 [6], pp.1319-32. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10491394 Eriksson, S. (1984): Alpha 1-antitrypsin deficiency: some personal experiences, Schweiz Med Wochenschr 114 [25], pp.893-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6379866 Faber, J. P.; Poller, W.; Olek, K.; Baumann, U.; Carlson, J.; Lindmark, B. and Eriksson, S. (1993): The molecular basis of alpha 1-antichymotrypsin deficiency in a heterozygote with liver and lung disease, J Hepatol 18 [3], pp.313-21. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8228125 Faurschou, M. and Borregaard, N. (2003): Neutrophil granules and secretory vesicles in inflammation, Microbes Infect 5 [14], pp.1317-27. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14613775 Finlay, B. B. and Falkow, S. (1988): Comparison of the invasion strategies used by Salmonella cholerae-suis, Shigella flexneri and Yersinia enterocolitica to enter cultured animal cells: endosome acidification is not required for bacterial invasion or intracellular replication, Biochimie 70 [8], pp.1089-99. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3147700 Fouret, P.; du Bois, R. M.; Bernaudin, J. F.; Takahashi, H.; Ferrans, V. J. and Crystal, R. G. (1989): Expression of the neutrophil elastase gene during human bone marrow cell differentiation, J Exp Med 169 [3], pp.833-45. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2538548 Gadek, J. E.; Klein, H. G.; Holland, P. V. and Crystal, R. G. (1981): Replacement therapy of alpha 1-antitrypsin deficiency. Reversal of protease-antiprotease imbalance within the alveolar structures of PiZ subjects, J Clin Invest 68 [5], pp.1158-65. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7028785 Glickman, J. N. and Kornfeld, S. (1993): Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts, J Cell Biol 123 [1], pp.99-108. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8408210 Goldberg, M. B.; Barzu, O.; Parsot, C. and Sansonetti, P. J. (1993): Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement, Infect Agents Dis 2 [4], pp.210-1. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8173795 Goldfarb, J. P.; Brasitus, T. A. and Cleri, D. J. (1982): Shigella enterocolitis and acute renal failure, South Med J 75 [4], pp.492-3. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7041284 Gombart, A. F. and Koeffler, H. P. (2002): Neutrophil specific granule deficiency and mutations in the gene encoding transcription factor C/EBP(epsilon), Curr Opin Hematol 9 [1], pp.36-42. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11753076 Gordon, S. (2002): Pattern recognition receptors: doubling up for the innate immune response, Cell 111 [7], pp.927-30. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12507420 Graf, L.; Craik, C. S.; Patthy, A.; Roczniak, S.; Fletterick, R. J. and Rutter, W. J. (1987): Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin, Biochemistry 26 [9], pp.2616-23. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3111531 Guex, N. and Peitsch, M.C. (1997): SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling., Electrophoresis 18, pp.2714-2723. http://www.expasy.org/spdbv/ Guichon, A.; Hersh, D.; Smith, M. R. and Zychlinsky, A. (2001): Structure-function analysis of the Shigella virulence factor IpaB, J Bacteriol 183 [4], pp.1269-76. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11157939 Gullberg, U.; Lindmark, A.; Lindgren, G.; Persson, A. M.; Nilsson, E. and Olsson, I. (1995): Carboxyl-terminal prodomain-deleted human leukocyte elastase and cathepsin G are efficiently targeted to granules and enzymatically activated in the rat basophilic/mast cell line RBL, J Biol Chem 270 [21], pp.12912-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7539007 Gullberg, U.; Lindmark, A.; Nilsson, E.; Persson, A. M. and Olsson, I. (1994): Processing of human cathepsin G after transfection to the rat basophilic/mast cell tumor line RBL, J Biol Chem 269 [40], pp.25219-25. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7929211 Hampton, M. B.; Kettle, A. J. and Winterbourn, C. C. (1998): Inside the neutrophil phagosome: oxidants, myeloperoxidase, and bacterial killing, Blood 92 [9], pp.3007-17. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9787133 Harper, J. W.; Cook, R. R.; Roberts, C. J.; McLaughlin, B. J. and Powers, J. C. (1984): Active site mapping of the serine proteases human leukocyte elastase, cathepsin G, porcine pancreatic elastase, rat mast cell proteases I and II. Bovine chymotrypsin A alpha, and Staphylococcus aureus protease V-8 using tripeptide thiobenzyl ester substrates, Biochemistry 23 [13], pp.2995-3002. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6380580 Hartley B.S., Shotton D.M. (1971): Pancreatic elastase, Boyer, P.D., Ed, The Enzymes III, pp. 323-373, Academic Press,
New York
. Hasilik, A. (1992): The early and late processing of lysosomal enzymes: proteolysis and compartmentation, Experientia 48 [2], pp.130-51. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1740186 Hayward, R. D. and Koronakis, V. (1999): Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella, Embo J 18 [18], pp.4926-34. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10487745 Hedstrom, L.; Szilagyi, L. and Rutter, W. J. (1992): Converting trypsin to chymotrypsin: the role of surface loops, Science 255 [5049], pp.1249-53. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1546324 High, N.; Mounier, J.; Prevost, M. C. and Sansonetti, P. J. (1992): IpaB of Shigella flexneri causes entry into epithelial cells and escape from the phagocytic vacuole, Embo J 11 [5], pp.1991-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1582426 Hilbi, H.; Moss, J. E.; Hersh, D.; Chen, Y.; Arondel, J.; Banerjee, S.; Flavell, R. A.; Yuan, J.; Sansonetti, P. J. and Zychlinsky, A. (1998): Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB, J Biol Chem 273 [49], pp.32895-900. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9830039 Hof, P.; Mayr, I.; Huber, R.; Korzus, E.; Potempa, J.; Travis, J.; Powers, J. C. and Bode, W. (1996): The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities, Embo J 15 [20], pp.5481-91. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8896442 Horwitz, M.; Benson, K. F.; Duan, Z.; Li, F. Q. and Person, R. E. (2004): Hereditary neutropenia: dogs explain human neutrophil elastase mutations, Trends Mol Med 10 [4], pp.163-70. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15059607 Horwitz, M.; Benson, K. F.; Person, R. E.; Aprikyan, A. G. and Dale, D. C. (1999): Mutations in ELA2, encoding neutrophil elastase, define a 21-day biological clock in cyclic haematopoiesis, Nat Genet 23 [4], pp.433-6. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10581030 Introne, W.; Boissy, R. E. and Gahl, W. A. (1999): Clinical, molecular, and cell biological aspects of Chediak-Higashi syndrome, Mol Genet Metab 68 [2], pp.283-303. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10527680 Janeway, C.A.; Travers, P.; Walport, M. and Shlomchick, M. (2001): Immunobiology 5, 3. ed., Garland Publishing,
New York
. Jarry, A.; Robaszkiewicz, M.; Brousse, N. and Potet, F. (1989): Immune cells associated with M cells in the follicle-associated epithelium of Peyer's patches in the rat. An electron- and immuno-electron-microscopic study, Cell Tissue Res 255 [2], pp.293-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2784358 Kagan, B. L.; Selsted, M. E.; Ganz, T. and Lehrer, R. I. (1990): Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes, Proc Natl Acad Sci U S A 87 [1], pp.210-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1688654 Kim, W. M. and Kang, K. (2000): Enzymatic and molecular biochemical characterizations of human neutrophil elastases and a cathepsin G-like enzyme, Mol Cells 10 [5], pp.498-504. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11101139 Kornfeld, S. and Mellman, I. (1989): The biogenesis of lysosomes, Annu Rev Cell Biol 5, pp.483-525. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2557062 Kotloff, K. L.; Winickoff, J. P.; Ivanoff, B.; Clemens, J. D.; Swerdlow, D. L.; Sansonetti, P. J.; Adak, G. K. and Levine, M. M. (1999): Global burden of Shigella infections: implications for vaccine development and implementation of control strategies, Bull World Health Organ 77 [8], pp.651-66. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10516787 Kraehenbuhl, J. P. and Neutra, M. R. (1992): Molecular and cellular basis of immune protection of mucosal surfaces, Physiol Rev 72 [4], pp.853-79. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1438580 Krem, M. M. and Di Cera, E. (2001): Molecular markers of serine protease evolution, Embo J 20 [12], pp.3036-45. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11406580 Krem, M. M.; Rose, T. and Di Cera, E. (1999): The C-terminal sequence encodes function in serine proteases, J Biol Chem 274 [40], pp.28063-6. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10497153 LaBrec, E. H., Schneider, H., MagnaniT., Formal, S.B. (1964), J Bacteriol 88, pp.1503-18. Laemmli, U. K. (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 [5259], pp.680-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=5432063 Lange, R. D. (1983): Cyclic hematopoiesis: human cyclic neutropenia, Exp Hematol 11 [6], pp.435-51. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6352296 Le Huerou, I.; Wicker, C.; Guilloteau, P.; Toullec, R. and Puigserver, A. (1990): Isolation and nucleotide sequence of cDNA clone for bovine pancreatic anionic trypsinogen. Structural identity within the trypsin family, Eur J Biochem 193 [3], pp.767-73. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1701147 Lee, W. L.; Harrison, R. E. and Grinstein, S. (2003): Phagocytosis by neutrophils, Microbes Infect 5 [14], pp.1299-306. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14613773 Lesk, A. M. and Fordham, W. D. (1996): Conservation and variability in the structures of serine proteinases of the chymotrypsin family, J Mol Biol 258 [3], pp.501-37. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8642605 Lett, M. C.; Sasakawa, C.; Okada, N.; Sakai, T.; Makino, S.; Yamada, M.; Komatsu, K. and Yoshikawa, M. (1989): virG, a plasmid-coded virulence gene of Shigella flexneri: identification of the virG protein and determination of the complete coding sequence, J Bacteriol 171 [1], pp.353-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2644195 Levinson W., Jawetz E. (2002): Medical Microbiology and Immunology, 7th. ed., Lange Medical Books/McGraw-Hill,
New York
, 0-07-121236-1. Li, F. Q. and Horwitz, M. (2001): Characterization of mutant neutrophil elastase in severe congenital neutropenia, J Biol Chem 276 [17], pp.14230-41. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11278653 Lindmark, A.; Persson, A. M. and Olsson, I. (1990): Biosynthesis and processing of cathepsin G and neutrophil elastase in the leukemic myeloid cell line U-937, Blood 76 [11], pp.2374-80. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2124153 Maiorov, V. N. and Crippen, G. M. (1994): Significance of root-mean-square deviation in comparing three-dimensional structures of globular proteins, J Mol Biol 235 [2], pp.625-34. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8289285 Makino, S.; Sasakawa, C.; Kamata, K.; Kurata, T. and Yoshikawa, M. (1986): A genetic determinant required for continuous reinfection of adjacent cells on large plasmid in S. flexneri 2a, Cell 46 [4], pp.551-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3524856 Mandic-Mulec, I.; Weiss, J. and Zychlinsky, A. (1997): Shigella flexneri is trapped in polymorphonuclear leukocyte vacuoles and efficiently killed, Infect Immun 65 [1], pp.110-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8975899 Marone, G.; Casolaro, V.; Patella, V.; Florio, G. and Triggiani, M. (1997): Molecular and cellular biology of mast cells and basophils, Int Arch Allergy Immunol 114 [3], pp.207-17. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9363900 Marossy, K.; Szabo, G. C.; Pozsgay, M. and Elodi, P. (1980): Mapping of the substrate - binding site of the human granulocyte elastase by the aid of tripeptidyl-p-nitroanilide substrates, Biochem Biophys Res Commun 96 [2], pp.762-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6932873 Maurelli, A. T.; Baudry, B.; d'Hauteville, H.; Hale, T. L. and Sansonetti, P. J. (1985): Cloning of plasmid DNA sequences involved in invasion of HeLa cells by Shigella flexneri, Infect Immun 49 [1], pp.164-71. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2989179 Maurelli, A. T. and Sansonetti, P. J. (1988): Identification of a chromosomal gene controlling temperature-regulated expression of Shigella virulence, Proc Natl Acad Sci U S A 85 [8], pp.2820-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3282241 Mayer-Scholl, A.; Averhoff, P. and Zychlinsky, A. (2004): How do neutrophils and pathogens interact?, Curr Opin Microbiol 7 [1], pp.62-6. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15036142 McGrath, M. E.; Vasquez, J. R.; Craik, C. S.; Yang, A. S.; Honig, B. and Fletterick, R. J. (1992): Perturbing the polar environment of Asp102 in trypsin: consequences of replacing conserved Ser214, Biochemistry 31 [12], pp.3059-64. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1554694 McGuire, M. J.; Lipsky, P. E. and Thiele, D. L. (1993): Generation of active myeloid and lymphoid granule serine proteases requires processing by the granule thiol protease dipeptidyl peptidase I, J Biol Chem 268 [4], pp.2458-67. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8428921 McRae, B.; Nakajima, K.; Travis, J. and Powers, J. C. (1980): Studies on reactivity of human leukocyte elastase, cathepsin G, and porcine pancreatic elastase toward peptides including sequences related to the reactive site of alpha 1-protease inhibitor (alpha 1-antitrypsin), Biochemistry 19 [17], pp.3973-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6967733 Menard, R.; Prevost, M. C.; Gounon, P.; Sansonetti, P. and Dehio, C. (1996): The secreted Ipa complex of Shigella flexneri promotes entry into mammalian cells, Proc Natl Acad Sci U S A 93 [3], pp.1254-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8577750 Menard, R.; Sansonetti, P. J. and Parsot, C. (1993): Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells, J Bacteriol 175 [18], pp.5899-906. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8376337 Menard, R.; Sansonetti, P.; Parsot, C. and Vasselon, T. (1994): Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri, Cell 79 [3], pp.515-25. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7954817 Miao, E. A.; Scherer, C. A.; Tsolis, R. M.; Kingsley, R. A.; Adams, L. G.; Baumler, A. J. and Miller, S. I. (1999): Salmonella typhimurium leucine-rich repeat proteins are targeted to the SPI1 and SPI2 type III secretion systems, Mol Microbiol 34 [4], pp.850-64. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10564523 Mims C., Playfair J., Poitt I., Wakelin D., Williams R. (1998): Medical Mirobiology, 2nd. ed., L., Crowe, Ed, Mosby International Limitied,
London
, 0 7234 2781 X. Morley, A. A.; Baikie, A. G. and Galton, D. A. (1967): Cyclic leucocytosis as evidence for retention of normal homoeostatic control in chronic granulocytic leukaemia, Lancet 2 [7530], pp.1320-3. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=4170024 Mounier, J.; Vasselon, T.; Hellio, R.; Lesourd, M. and Sansonetti, P. J. (1992): Shigella flexneri enters human colonic Caco-2 epithelial cells through the basolateral pole, Infect Immun 60 [1], pp.237-48. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1729185 Mukhopadhyay, S.; Herre, J.; Brown, G. D. and Gordon, S. (2004): The potential for Toll-like receptors to collaborate with other innate immune receptors, Immunology 112 [4], pp.521-30. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15270722 Muzio, M.; Bosisio, D.; Polentarutti, N.; D'Amico, G.; Stoppacciaro, A.; Mancinelli, R.; van't Veer, C.; Penton-Rol, G.; Ruco, L. P.; Allavena, P. and Mantovani, A. (2000): Differential expression and regulation of toll-like receptors (TLR) in human leukocytes: selective expression of TLR3 in dendritic cells, J Immunol 164 [11], pp.5998-6004. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10820283 Nakajima, K.; Powers, J. C.; Ashe, B. M. and Zimmerman, M. (1979): Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site, J Biol Chem 254 [10], pp.4027-32. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=312290 Navia, M. A.; McKeever, B. M.; Springer, J. P.; Lin, T. Y.; Williams, H. R.; Fluder, E. M.; Dorn, C. P. and Hoogsteen, K. (1989): Structure of human neutrophil elastase in complex with a peptide chloromethyl ketone inhibitor at 1.84-A resolution, Proc Natl Acad Sci U S A 86 [1], pp.7-11. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2911584 Owen, C. A.; Campbell, M. A.; Sannes, P. L.; Boukedes, S. S. and Campbell, E. J. (1995): Cell surface-bound elastase and cathepsin G on human neutrophils: a novel, non-oxidative mechanism by which neutrophils focus and preserve catalytic activity of serine proteinases, J Cell Biol 131 [3], pp.775-89. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7593196 Pallen, M. J.; Dougan, G. and Frankel, G. (1997): Coiled-coil domains in proteins secreted by type III secretion systems, Mol Microbiol 25 [2], pp.423-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9282753 Perona, J. J. and Craik, C. S. (1995): Structural basis of substrate specificity in the serine proteases, Protein Sci 4 [3], pp.337-60. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7795518 Perona, J. J. and Craik, C. S. (1997): Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold, J Biol Chem 272 [48], pp.29987-90. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9374470 Perona, J. J.; Hedstrom, L.; Rutter, W. J. and Fletterick, R. J. (1995): Structural origins of substrate discrimination in trypsin and chymotrypsin, Biochemistry 34 [5], pp.1489-99. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7849008 Phillips, T. A.; VanBogelen, R. A. and Neidhardt, F. C. (1984): lon gene product of Escherichia coli is a heat-shock protein, J Bacteriol 159 [1], pp.283-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6330035 Pjura, P. E.; Lenhoff, A. M.; Leonard, S. A. and Gittis, A. G. (2000): Protein crystallization by design: chymotrypsinogen without precipitants, J Mol Biol 300 [2], pp.235-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10873462 Powers, J. C.; Gupton, B. F.; Harley, A. D.; Nishino, N. and Whitley, R. J. (1977): Specificity of porcine pancreatic elastase, human leukocyte elastase and cathepsin G. Inhibition with peptide chloromethyl ketones, Biochim Biophys Acta 485 [1], pp.156-66. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=562189 Qadri, F.; Hossain, S. A.; Ciznar, I.; Haider, K.; Ljungh, A.; Wadstrom, T. and Sack, D. A. (1988): Congo red binding and salt aggregation as indicators of virulence in Shigella species, J Clin Microbiol 26 [7], pp.1343-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3045151 Rawlings, N. D. and Barrett, A. J. (1993): Evolutionary families of peptidases, Biochem J 290 ( Pt 1), pp.205-18. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8439290 Reeves, E. P.; Lu, H.; Jacobs, H. L.; Messina, C. G.; Bolsover, S.; Gabella, G.; Potma, E. O.; Warley, A.; Roes, J. and Segal, A. W. (2002): Killing activity of neutrophils is mediated through activation of proteases by K+ flux, Nature 416 [6878], pp.291-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11907569 Rehm, H. (2002): Der Experimentator: Proteinbiochemie/ Proteomics, 4 Edition. ed., Spektrum Akademischer Verlag,
Berlin
. Rijnboutt, S.; Aerts, H. M.; Geuze, H. J.; Tager, J. M. and Strous, G. J. (1991): Mannose 6-phosphate-independent membrane association of cathepsin D, glucocerebrosidase, and sphingolipid-activating protein in HepG2 cells, J Biol Chem 266 [8], pp.4862-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1848227 Rijnboutt, S.; Kal, A. J.; Geuze, H. J.; Aerts, H. and Strous, G. J. (1991): Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells, J Biol Chem 266 [35], pp.23586-92. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1660878 Roche-Applied-Science http://www.proteoexpert.com Roos, D.; van Bruggen, R. and Meischl, C. (2003): Oxidative killing of microbes by neutrophils, Microbes Infect 5 [14], pp.1307-15. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14613774 Roos, D. and Winterbourn, C. C. (2002): Immunology. Lethal weapons, Science 296 [5568], pp.669-71. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11976433 Roughley, P. J. (1977): The degradation of proteoglycan by leucocyte elastase, Biochem Soc Trans 5 [2], pp.443-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=902859 Roughley, P. J. and Barrett, A. J. (1977): The degradation of cartilage proteoglycans by tissue proteinases. Proteoglycan structure and its susceptibility to proteolysis, Biochem J 167 [3], pp.629-37. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=603625 Rupp, R. A.; Snider, L. and Weintraub, H. (1994): Xenopus embryos regulate the nuclear localization of XMyoD, Genes Dev 8 [11], pp.1311-23. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7926732 Salvesen, G. and Enghild, J. J. (1990): An unusual specificity in the activation of neutrophil serine proteinase zymogens, Biochemistry 29 [22], pp.5304-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2383548 Salvesen, G.; Farley, D.; Shuman, J.; Przybyla, A.; Reilly, C. and Travis, J. (1987): Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases, Biochemistry 26 [8], pp.2289-93. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3304423 Sambrano, G. R.; Huang, W.; Faruqi, T.; Mahrus, S.; Craik, C. and Coughlin, S. R. (2000): Cathepsin G activates protease-activated receptor-4 in human platelets, J Biol Chem 275 [10], pp.6819-23. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10702240 Sambrook, J. and Russell, D.W. (2001): Molecular Cloning - A Laboratory Manual, 3rd. ed., Cold Spring Harbor Laboratory Press,
Cold Spring Harbor, New York
. Sansonetti, P. J. (1992): Molecular and cellular biology of Shigella flexneri invasiveness: from cell assay systems to shigellosis, Curr Top Microbiol Immunol 180, pp.1-19. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1505204 Sansonetti, P. J.; Arondel, J.; Fontaine, A.; d'Hauteville, H. and Bernardini, M. L. (1991): OmpB (osmo-regulation) and icsA (cell-to-cell spread) mutants of Shigella flexneri: vaccine candidates and probes to study the pathogenesis of shigellosis, Vaccine 9 [6], pp.416-22. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1887672 Sansonetti, P. J.; Hale, T. L.; Dammin, G. J.; Kapfer, C.; Collins, H. H., Jr. and Formal, S. B. (1983): Alterations in the pathogenicity of Escherichia coli K-12 after transfer of plasmid and chromosomal genes from Shigella flexneri, Infect Immun 39 [3], pp.1392-402. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6341237 Sansonetti, P. J.; Kopecko, D. J. and Formal, S. B. (1982): Involvement of a plasmid in the invasive ability of Shigella flexneri, Infect Immun 35 [3], pp.852-60. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6279518 Sasakawa, C.; Kamata, K.; Sakai, T.; Makino, S.; Yamada, M.; Okada, N. and Yoshikawa, M. (1988): Virulence-associated genetic regions comprising 31 kilobases of the 230-kilobase plasmid in Shigella flexneri 2a, J Bacteriol 170 [6], pp.2480-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2836357 Schechter, I. and Berger, A. (1968): On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain, Biochem Biophys Res Commun 32 [5], pp.898-902. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=5682314 School, Medic - University of Texas and Houston Medical (1995). (http://medic.med.uth.tmc.edu/path/00001522.htm) Schuster, A.; Fahy, J. V.; Ueki, I. and Nadel, J. A. (1995): Cystic fibrosis sputum induces a secretory response from airway gland serous cells that can be prevented by neutrophil protease inhibitors, Eur Respir J 8 [1], pp.10-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7744174 Shafer, W. M.; Katzif, S.; Bowers, S.; Fallon, M.; Hubalek, M.; Reed, M. S.; Veprek, P. and Pohl, J. (2002): Tailoring an antibacterial peptide of human lysosomal cathepsin G to enhance its broad-spectrum action against antibiotic-resistant bacterial pathogens, Curr Pharm Des 8 [9], pp.695-702. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11945165 Shapiro, S. D. (2002): Neutrophil elastase: path clearer, pathogen killer, or just pathologic?, Am J Respir Cell Mol Biol 26 [3], pp.266-8. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11867332 Sinha, S.; Watorek, W.; Karr, S.; Giles, J.; Bode, W. and Travis, J. (1987): Primary structure of human neutrophil elastase, Proc Natl Acad Sci U S A 84 [8], pp.2228-32. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3550808 Soesatyo, M.; Biewenga, J.; Kraal, G. and Sminia, T. (1990): The localization of macrophage subsets and dendritic cells in the gastrointestinal tract of the mouse with special reference to the presence of high endothelial venules. An immuno- and enzyme-histochemical study, Cell Tissue Res 259 [3], pp.587-93. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2180576 Steitz, T. A. and Shulman, R. G. (1982): Crystallographic and NMR studies of the serine proteases, Annu Rev Biophys Bioeng 11, pp.419-44. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7049067 Studier, F. W. (1991): Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system, J Mol Biol 219 [1], pp.37-44. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2023259 Studier, F. W.; Rosenberg, A. H.; Dunn, J. J. and Dubendorff, J. W. (1990): Use of T7 RNA polymerase to direct expression of cloned genes, Methods Enzymol 185, pp.60-89. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2199796 Szabo, G. C.; Pozsgay, M.; Gaspar, R. and Elodi, P. (1980): Specificity of pancreatic elastase with tripeptidyl-p-nitroanilide substrates, Acta Biochim Biophys Acad Sci Hung 15 [4], pp.263-763. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6945027 Tanaka, T.; Minematsu, Y.; Reilly, C. F.; Travis, J. and Powers, J. C. (1985): Human leukocyte cathepsin G. Subsite mapping with 4-nitroanilides, chemical modification, and effect of possible cofactors, Biochemistry 24 [8], pp.2040-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=4016099 Thirumalai, K.; Kim, K. S. and Zychlinsky, A. (1997): IpaB, a Shigella flexneri invasin, colocalizes with interleukin-1 beta-converting enzyme in the cytoplasm of macrophages, Infect Immun 65 [2], pp.787-93. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9009343 Thornberry, N. A. (1994): Interleukin-1 beta converting enzyme, Methods Enzymol 244, pp.615-31. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7845238 Tkalcevic, J.; Novelli, M.; Phylactides, M.; Iredale, J. P.; Segal, A. W. and Roes, J. (2000): Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G, Immunity 12 [2], pp.201-10. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10714686 Turner, D. L. and Weintraub, H. (1994): Expression of achaete-scute homolog 3 in Xenopus embryos converts ectodermal cells to a neural fate, Genes Dev 8 [12], pp.1434-47. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7926743 Urata, H.; Karnik, S. S.; Graham, R. M. and Husain, A. (1993): Dipeptide processing activates recombinant human prochymase, J Biol Chem 268 [32], pp.24318-22. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8226981 Wassef, J. S.; Keren, D. F. and Mailloux, J. L. (1989): Role of M cells in initial antigen uptake and in ulcer formation in the rabbit intestinal loop model of shigellosis, Infect Immun 57 [3], pp.858-63. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2645214 Watorek, W.; van Halbeek, H. and Travis, J. (1993): The isoforms of human neutrophil elastase and cathepsin G differ in their carbohydrate side chain structures, Biol Chem Hoppe Seyler 374 [6], pp.385-93. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8357534 Wei, A. Z.; Mayr, I. and Bode, W. (1988): The refined 2.3 A crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor, FEBS Lett 234 [2], pp.367-73. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=3391280 Weinrauch, Y.; Drujan, D.; Shapiro, S. D.; Weiss, J. and Zychlinsky, A. (2002): Neutrophil elastase targets virulence factors of enterobacteria, Nature 417 [6884], pp.91-4. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12018205 WHO (2005). http://www.who.int/vaccine_research/diseases/shigella/en/ Wiedow, O. and Meyer-Hoffert, U. (2005): Neutrophil serine proteases: potential key regulators of cell signalling during inflammation, J Intern Med 257 [4], pp.319-28. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15788001 Wiedow, O.; Muhle, K.; Streit, V. and Kameyoshi, Y. (1996): Human eosinophils lack human leukocyte elastase, Biochim Biophys Acta 1315 [3], pp.185-7. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8611657 Zhang, X. and Studier, F. W. (1997): Mechanism of inhibition of bacteriophage T7 RNA polymerase by T7 lysozyme, J Mol Biol 269 [1], pp.10-27. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9192997 Zimmerman, M. and Ashe, B. M. (1977): Sbustrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyte, Biochim Biophys Acta 480 [1], pp.241-5. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=401649 Zychlinsky, A.; Kenny, B.; Menard, R.; Prevost, M. C.; Holland, I. B. and Sansonetti, P. J. (1994): IpaB mediates macrophage apoptosis induced by Shigella flexneri, Mol Microbiol 11 [4], pp.619-27. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8196540 Zychlinsky, A.; Prevost, M. C. and Sansonetti, P. J. (1992): Shigella flexneri induces apoptosis in infected macrophages, Nature 358 [6382], pp.167-9. http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1614548