Исследование роли фуриноподобных протеиназ и металлопротеиназы МТ1-ММР в патологических процессах

Список литературы

1. Fuller R.S., Brake A .J., Thorner J. Intracellular targeting and structural conservation of a prohormone-processing endoprotease // Science. 1989, v. 246, p. 482−486.
2. Bresnahan P.A., Leduc R., Thomas L., Thorner J., Gibson H.L., Brake A.J., Barr P.J., Thomas G. Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo IIJ Cell Biol 1990, v. 111, p. 2851−2859.
3. Rockwell N.C., Krysan D.J., Komiyama Т., Fuller R.S. Precursor processing by kex2/furin proteases // Chem Rev. 2002, v. 102, p. 4525−4548.
4. Thomas G. Furin at the cutting edge: from protein traffic to embryogenesis and disease // Nat Rev Mol Cell Biol. 2002, v. 3, p. 753−766.
5. Nakayama K. Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins // Biochem J. 1997, v. 327, p. 625−635.
6. Brinton M.A. The molecular biology of West Nile Virus: a new invader of the western hemisphere // Annu Rev Microbiol. 2002, v. 56, p. 371−402.
7. Stadler К., Allison S.L., Schalich J., Heinz F.X. Proteolytic activation of tick-borne encephalitis virus by furin // J Virol. 1997, v. 71, p. 8475−8481.
8. Devriese P.P. On the discovery of Clostridium botulinum // J Hist Neurosci. 1999, v. 8, p. 43−50.
9. Aktories K., Barth H. Clostridium botulinum C2 toxin—new insights into the cellular up-take of the actin-ADP-ribosylating toxin // Int J Med Microbiol. 2004, v. 293, p. 557−564.
10. Montecucco C., Papini E. Cell penetration of bacterial protein toxins // Trends Microbiol. 1995, v. 3, p. 165−167.
11. Turton K., Chaddock J.A., Acharya K.R. Botulinum and tetanus neurotoxins: structure, function and therapeutic utility // Trends Biochem Sci. 2002, v. 27, p. 552−558.
12. Finkelstein R.A., Boesman M., Neoh S.H., LaRue M.K., Delaney R. Dissociation and recombination of the subunits of the cholera enterotoxin (choleragen) // J Immunol. 1974, v. 113, p. 145−150.
13. Gill D.M., Pappenheimer A.M., Brown R., Kurnick J.T. Studies on the mode of action of diphtheria toxin. VII. Toxin-stimulated hydrolysis of nicotinamide adenine dinucleotide in mammalian cell extracts // J Exp Med. 1969, v. 129, p. 1−21.
14. Collier R.J., Kandel J. Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymicallyactive and inactive fragments IIJ Biol Chem. 1971, v. 246, p. 14 961 503.
15. Smith H. Discovery of the anthrax toxin: the beginning of studies of virulence determinants regulated in vivo // Int J Med Microbiol. 2002, v. 291, p. 411−417.
16. Aktories K., Barmann M., Ohishi I., Tsuyama S., Jakobs K.H., Habermann E. Botulinum C2 toxin ADP-ribosylates actin // Nature. 1986, v. 322, p. 390−392.
17. Baseman J.B., Pappenheimer A.M., Gill D.M., Harper A.A. Action of diphtheria toxin in the guinea pig IIJ Exp Med. 1970, v. 132, p. 11 381 152.
18. Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor // Biochem J. 2000, v. 352, p. 739−745.
19. Stanley J.L., Smith H. Purification of factor I and recognition of a third factor of the anthrax toxin IIJ Gen Microbiol. 1961, v. 26, p. 4963.
20. Guidi-Rontani C. The alveolar macrophage: the Trojan horse of Bacillus anthracis // Trends Microbiol. 2002, v. 10, p. 405−409.
21. Green B.D., Battisti L., Koehler T.M., Thorne C.B., Ivins B.E. Demonstration of a capsule plasmid in Bacillus anthracis II Infect Immun. 1985, v. 49, p. 291−297.
22. Pezard C., Berche P., Mock M. Contribution of individual toxin components to virulence of Bacillus anthracis // Infect Immun. 1991, v. 59, p. 3472−3477.
23. Smith H., Keppie J. Observations on experimental anthrax- demonstration of a specific lethal factor produced in vivo by Bacillus anthracis И Nature. 1954, v. 173, p. 869−870.
24. Mourez M. Anthrax toxins // Rev Physiol Biochem Pharmacol. 2004, v. 152, p. 135−164.
25. Bradley K.A., Mogridge J., Mourez M., Collier R.J., Young J.A. Identification of the cellular receptor for anthrax toxin // Nature. 2001, v. 414, p. 225−229.
26. Scobie H.M., Rainey G.J., Bradley K.A., Young J.A. Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor И Proc Natl AcadSci USA. 2003, v. 100, p. 5170−5174.
27. Santelli E., Bankston L.A., Leppla S.H., Liddington R.C. Crystal structure of a complex between anthrax toxin and its host cell receptor II Nature. 2004, v. 430, p. 905−908.
28. Gordon V.M., Klimpel K.R., Arora N., Henderson M.A., Leppla S.H. Proteolytic activation of bacterial toxins by eukaryotic cells isperformed by furin and by additional cellular proteases // Infect lmmun. 1995, v. 63, p. 82−87.
29. Milne J.C., Furlong D., Hanna P.C., Wall J.S., Collier R.J. Anthrax protective antigen forms oligomers during intoxication of mammalian cells IIJ Biol Chem. 1994, v. 269, p. 20 607−20 612.
30. Beauregard K.E., Collier R.J., Swanson J.A. Proteolytic activation of receptor-bound anthrax protective antigen on macrophages promotes its internalization // Cell Microbiol. 2000, v. 2, p. 251−258.
31. Lacy D.B., Mourez M., Fouassier A., Collier R.J. Mapping the anthrax protective antigen binding site on the lethal and edema factors И J Biol Chem. 2002, v. 277, p. 3006−3010.
32. Arora N., Leppla S.H. Residues 1−254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides // J Biol Chem. 1993, v. 268, p. 3334−3341.
33. Wesche J., Elliott J.L., Falnes P.O., Olsnes S., Collier R.J. Characterization of membrane translocation by anthrax protective antigen 11 Biochemistry. 1998, v. 37, p. 15 737−15 746.
34. Mogridge J., Cunningham K., Collier R.J. Stoichiometry of anthrax toxin complexes // Biochemistry. 2002, v. 41, p. 1079−1082.
35. Lacy D.B., Lin H.C., Melnyk R.A., Schueler-Furman O., Reither L., Cunningham K., Baker D., Collier R.J. A model of anthrax toxin lethal factor bound to protective antigen // Proc Natl Acad Sci USA.2005, v. 102, p. 16 409−16 414.
36. Melnyk R.A., Hewitt K.M., Lacy D.B., Lin H.C., Gessner C.R., Li S., Woods V.L., Collier R.J. Structural determinants for the binding of anthrax lethal factor to oligomeric protective antigen IIJ Biol Chem.2006, v. 281, p. 1630−1635.
37. Abrami L., Liu S., Cosson P., Leppla S.H., van der Goot F.G. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process IIJ Cell Biol. 2003, v. 160, p. 321−328.
38. Liu S., Leppla S.H. Cell surface tumor endothelium marker 8 cytoplasmic tail-independent anthrax toxin binding, proteolytic processing, oligomer formation, and internalization IIJ Biol Chem. 2003, v. 278, p. 5227−5234.
39. Blaustein R.O., Koehler T.M., Collier R.J., Finkelstein A. Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers // Proc Natl Acad Sci USA. 1989, v. 86, p. 2209−2213.
40. Miller С.J., Elliott J.L., Collier RJ. Anthrax protective antigen: prepore-to-pore conversion И Biochemistry. 1999, v. 38, p. 1 043 210 441.
41. Benson E.L., Huynh P.D., Finkelstein A., Collier R.J. Identification of residues lining the anthrax protective antigen channel // Biochemistry. 1998, v. 37, p. 3941−3948.
42. Krantz B.A., Trivedi A.D., Cunningham K., Christensen K.A., Collier R.J. Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin // JMol Biol. 2004, v. 344, p. 739−756.
43. Zhang S., Udho E., Wu Z., Collier R.J., Finkelstein A. Protein translocation through anthrax toxin channels formed in planar lipid bilayers // Biophys J. 2004, v. 87, p. 3842−3849.
44. Krantz B.A., Finkelstein A., Collier R.J. Protein Translocation through the Anthrax Toxin Transmembrane Pore is Driven by a Proton Gradient IIJ Mol Biol. 2006, v. 355, p. 968−979.
45. Leppla S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells // Proc Natl Acad Sci USA. 1982, v. 79, p. 3162−3166.
46. Klimpel K.R., Arora N., Leppla S.H. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity // Mol Microbiol. 1994, v. 13, p. 1093−1100.
47. Kochi S.K., Schiavo G., Mock M., Montecucco C. Zinc content of the Bacillus anthracis lethal factor // FEMS Microbiol Lett. 1994, v. 124, p. 343−348.
48. Pellizzari R., Guidi-Rontani C., Vitale G., Mock M., Montecucco C. Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/lFNgamma-induced release of NO and TNFalpha // FEBS Lett. 1999, v. 462, p. 199−204.
49. Chopra A.P., Boone S.A., Liang X., Duesbery N.S. Anthrax lethal factor proteolysis and inactivation of МАРК kinase /IJ Biol Chem. 2003, v. 278, p. 9402−9406.
50. Zucker S., Pei D., Cao J., Lopez-Otin C. Membrane type-matrix metalloproteinases (MT-MMP) // Curr Top Dev Biol. 2003, v. 54, p. 1−74.
51. Itoh Y., Seiki M. MT1-MMP: a potent modifier of pericellular microenvironment IIJ Cell Physiol. 2006, v. 206, p. 1−8.
52. Hotary K.B., Allen E.D., Brooks P.C., Datta N.S., Long M.W., Weiss S.J. Membrane type I matrix metalloproteinase usurps tumor growth control imposed by the three-dimensional extracellular matrix // Cell. 2003, v. 114, p. 33−45.
53. Seiki M. Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion // Cancer Lett. 2003, v. 194, p. 1−11.
54. Shiomi Т., Okada Y. MT1-MMP and MMP-7 in invasion and metastasis of human cancers // Cancer Metastasis Rev. 2003, v. 22, p. 145−152.
55. Zucker S., Vacirca J. Role of matrix metalloproteinases (MMPs) in colorectal cancer // Cancer Metastasis Rev. 2004, v. 23, p. 101−117.
56. Soulie P., Carrozzino F., Pepper M.S., Strongin A.Y., Poupon M.F., Montesano R. Membrane-type-1 matrix metalloproteinase confers tumorigenicity on nonmalignant epithelial cells // Oncogene. 2005, v. 24, p. 1689−1697.
57. Holmbeck K., Bianco P., Yamada S., Birkedal-Hansen H. MT1-MMP: a tethered collagenase // J Cell Physiol. 2004, v. 200, p. 11−19.
58. Hornebeck W., Emonard H., Monboisse J.C., Bellon G. Matrix-directed regulation of pericellular proteolysis and tumor progression // Semin Cancer Biol. 2002, v. 12, p. 231−241.
59. Kajita M., Itoh Y., Chiba Т., Mori H., Okada A., Kinoh H., Seiki M. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration IIJ Cell Biol. 2001, v. 153, p. 893−904.
60. Deryugina E.I., Ratnikov B.I., Strongin A.Y. Prinomastat, a hydroxamate inhibitor of matrix metalloproteinases, has a complex effect on migration of breast carcinoma cells // Int J Cancer. 2003, v. 104, p. 533−541.
61. Hernandez-Barrantes S., Bernardo M., Toth M., Fridman R. Regulation of membrane type-matrix metalloproteinases // Semin Cancer Biol 2002, v. 12, p. 131−138.
62. Itoh Y., Seiki M. MT1-MMP: an enzyme with multidimensional regulation // Trends Biochem Sci. 2004, v. 29, p. 285−289.
63. Osenkowski P., Toth M., Fridman R. Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP) // J Cell Physiol 2004, v. 200, p. 2−10.
64. Wang X., Ma D., Keski-Oja J., Pei D. Co-recycling of MT1-MMP and MT3-MMP through the trans-Golgi network. Identification of DKV582 as a recycling signal /IJ Biol Chem. 2004, v. 279, p. 93 319 336.
65. Uekita Т., Itoh Y., Yana I., Ohno H., Seiki M. Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity // J Cell Biol. 2001, v. 155, p. 1345−1356.
66. Jiang A., Lehti K., Wang X., Weiss S.J., Keski-Oja J., Pei D. Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis // Proc Natl Acad Sci USA. 2001, v. 98, p. 13 693−13 698.
67. Doxsey S., McCollum D., Theurkauf W. Centrosomes in Cellular Regulation И Annu Rev Cell Dev Biol. 2005, v 21., p. 411−434.
68. Doxsey S., Zimmerman W., Mikule K. Centrosome control of the cell cycle // Trends Cell Biol. 2005, v. 15, p. 303−311.
69. Nigg E.A. Centrosome aberrations: cause or consequence of cancer progression? II Nat Rev Cancer. 2002, v. 2, p. 815−825.
70. Fukasawa К. Centrosome amplification, chromosome instability and cancer development // Cancer Lett. 2005, v. 230, p. 6−19.
71. Pihan G.A., Purohit A., Wallace J., Malhotra R., Liotta L., Doxsey S.J. Centrosome defects can account for cellular and genetic changes that characterize prostate cancer progression // Cancer Res. 2001, v. 61, p. 2212−2219.
72. Pihan G., Doxsey S.J. Mutations and aneuploidy: co-conspirators in cancer? // Cancer Cell. 2003, v. 4, p. 89−94.
73. Giet R., Petretti C., Prigent C. Aurora kinases, aneuploidy and cancer, a coincidence or a real link? // Trends Cell Biol. 2005, v. 15, p. 241 250.
74. Duensing S. A tentative classification of centrosome abnormalities in cancer // Cell Biol Int. 2005, v. 29, p. 352−359.
75. Duensing A., Duensing S. Guilt by association? p53 and the development of aneuploidy in cancer // Biochem Biophys Res Commun. 2005, v. 331, p. 694−700.
76. Park S., Leppla S.H. Optimized production and purification of Bacillus anthracis lethal factor // Protein Expr Purif. 2000, v. 18, p. 293−302.
77. Doxsey S.J., Stein P., Evans L., Calarco P.D., Kirschner M. Pericentrin, a highly conserved centrosome protein involved in microtubule organization // Cell. 1994, v. 76, p. 639−650.
78. Deryugina E.I., Soroceanu L., Strongin A.Y. Up-regulation of vascular endothelial growth factor by membrane-type 1 matrix metalloproteinase stimulates human glioma xenograft growth and angiogenesis// Cancer Res. 2002, v. 62, p. 580−588.
79. Rozanov D.V., Golubkov V.S., Strongin A.Y. Membrane type-1 matrix metalloproteinase (MT1-MMP) protects malignant cells from tumoricidal activity of re-engineered anthrax lethal toxin // Int J Biochem Cell Biol. 2005, v. 37, p. 142−154.
80. Ramirez D.M., Leppla S.H., Schneerson R., Shiloach J. Production, recovery and immunogenicity of the protective antigen from a recombinant strain of Bacillus anthracis // JInd Microbiol Biotechnol. 2002, v. 28, p. 232−238.
81. Ratnikov В., Deryugina E., Leng J., Marchenko G., Dembrow D., Strongin A. Determination of matrix metalloproteinase activity using biotinylated gelatin II Anal Biochem. 2000, v. 286, p. 149−155.
82. Fugere M., Limperis P.C., Beaulieu-Audy V., Gagnon F., Lavigne P., Klarskov K., Leduc R., Day R. Inhibitory potency and specificity ofsubtilase-like pro-protein convertase (SPC) prodomains // J Biol Chem. 2002, v. 277, p. 7648−7656.
83. Pannifer A.D., Wong T.Y., Schwarzenbacher R., Renatus M., Petosa C., Bienkowska J., Lacy D.B., Collier R.J., Park S., Leppla S.H., Hanna P., Liddington R.C. Crystal structure of the anthrax lethal factor I I Nature. 2001, v. 414, p. 229−233.
84. Petosa C., Collier R.J., Klimpel K.R., Leppla S.H., Liddington R.C. Crystal structure of the anthrax toxin protective antigen // Nature. 1997, v. 385, p. 833−838.
85. Bieth J.G. Theoretical and practical aspects of proteinase inhibition kinetics II Methods Enzymol. 1995, v. 248, p. 59−84.
86. Deryugina E.I., Bourdon M.A., Reisfeld R.A., Strongin A. Remodeling of collagen matrix by human tumor cells requiresactivation and cell surface association of matrix metalloproteinase-2 // Cancer Res. 1998, v. 58, p. 3743−3750.
87. Stawowy P., Fleck E. Proprotein convertases furin and PC5: targeting atherosclerosis and restenosis at multiple levels // J Mol Med. 2005, v. 83, p. 865−875.
88. Mousa S.A., Shakibaei M., Sitte N., Schafer M., Stein C. Subcellular pathways of beta-endorphin synthesis, processing, and release from immunocytes in inflammatory pain // Endocrinology. 2004, v. 145, p. 1331−1341.
89. Klimpel K.R., Molloy S.S., Thomas G., Leppla S.H. Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin // Proc Natl Acad Sci USA. 1992, v. 89, p. 10 277−10 281.
90. Komiyama Т., Swanson J.A., Fuller R.S. Protection from anthrax toxin-mediated killing of macrophages by the combined effects of furin inhibitors and chloroquine // Antimicrob Agents Chemother. 2005, v. 49, p. 3875−3882.
91. Liu S., Schubert R.L., Bugge Т.Н., Leppla S.H. Anthrax toxin: structures, functions and tumour targeting // Expert Opin Biol Ther. 2003, v. 3, p. 843−853.
92. Banks D.J., Barnajian M., Maldonado-Arocho F.J., Sanchez A.M., Bradley K.A. Anthrax toxin receptor 2 mediates Bacillus anthracis killing of macrophages following spore challenge // Cell Microbiol. 2005, v. 7, p. 1173−1185.
93. Popov S.G., Villasmil R., Bernardi J., Grene E., Cardwell J., Popova Т., Wu A., Alibek D., Bailey C., Alibek K. Effect of Bacillus anthracis lethal toxin on human peripheral blood mononuclear cells // FEBSLett. 2002, v. 527, p. 211−215.
94. YusofR., Clum S" Wetzel M., Murthy H.M., Padmanabhan R. Purified NS2B/NS3 serine protease of dengue virus type 2 exhibits cofactor NS2B dependence for cleavage of substrates with dibasic amino acids in vitro И J Biol Chem. 2000, v. 275, p. 9963−9969.
95. Henrich S., Cameron A., Bourenkov G.P., Kiefersauer R., Huber R., Lindberg I., Bode W., Than M.E. The crystal structure of the proprotein processing proteinase furin explains its stringent specificity // Nat Struct Biol. 2003, v. 10, p. 520−526.
96. Yamshchikov V.F., Trent D.W., Compans R.W. Upregulation of signalase processing and induction of prM-E secretion by theflavivirus NS2B-NS3 protease: roles of protease components // J Virol 1997, v. 71, p. 4364−4371.
97. Elshuber S., Allison S.L., Heinz F.X., Mandl C.W. Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus // J Gen Virol 2003, v. 84, p. 183−191.
98. Yamshchikov V.F., Compans R.W. Processing of the intracellular form of the west Nile virus capsid protein by the viral NS2B-NS3 protease: an in vitro study // J Virol 1994, v. 68, p. 5765−5771.
99. Boyd S.E., Pike R.N., Rudy G.B., Whisstock J.C., Garcia de la Banda M. PoPS: a computational tool for modeling and predicting protease specificity // JBioinform Comput Biol 2005, v. 3, p. 551−585.
100. Chernoff G.F. Shiverer: an autosomal recessive mutant mouse with myelin deficiency // JHered. 1981, v. 72, p. 128.
101. Lutton J.D., Winston R., Rodman T.C. Multiple sclerosis: etiological mechanisms and future directions // Exp Biol Med (Maywood). 2004, v. 229, p. 12−20.
102. Pedraza L. Nuclear transport of myelin basic protein // JNeurosci Res. 1997, v. 50, p. 258−264.
103. Seiwa C., Kojima-Aikawa K., Matsumoto I., Asou H. CNS myelinogenesis in vitro: myelin basic protein deficient shiverer oligodendrocytes // J Neurosci Res. 2002, v. 69, p. 305−317.
104. Kacprzak M.M., Peinado J.R., Than M.E., Appel J., Henrich S., Lipkind G., Houghten R.A., Bode W., Lindberg I. Inhibition of furin by polyarginine-containing peptides: nanomolar inhibition by nona-D-arginine H J Biol Chem. 2004, v. 279, p. 36 788−36 794.
105. Cameron A., Appel J., Houghten R.A., Lindberg I. Polyarginines are potent furin inhibitors И J Biol Chem. 2000, v. 275, p. 36 741−36 749.
106. Jean F., Stella K., Thomas L., Liu G., Xiang Y., Reason A.J., Thomas G. alpha 1-Antitrypsin Portland, a bioengineered serpin highly selective for furin: application as an antipathogenic agent // Proc Natl AcadSci USA. 1998, v. 95, p. 7293−7298.
107. Moayeri M., Leppla S.H. The roles of anthrax toxin in pathogenesis // Curr Opin Microbiol. 2004, v. 7, p. 19−24.
108. Bardwell A.J., Abdollahi M., Bardwell L. Anthrax lethal factor-cleavage products of МАРК (mitogen-activated protein kinase) kinases exhibit reduced binding to their cognate MAPKs // Biochem J. 2004, v. 378, p. 569−577.
109. Park J.M., Greten F.R., Li Z.W., Karin M. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition // Science.2002, v. 297, p. 2048−2051.
110. Gordon V.M., Rehemtulla A., Leppla S.H. A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen // Infect Immun. 1997, v. 65, p. 3370−3375.
111. Collier R.J., Young J.A. Anthrax toxin // Annu Rev Cell Dev Biol.2003, v. 19, p. 45−70.
112. Chambers T.J., Nestorowicz A., Amberg S.M., Rice C.M. Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication // J Virol. 1993, v. 67, p. 6797−6807.
113. Falgout В., Miller R.H., Lai C.J. Deletion analysis of dengue virus type 4 nonstructural protein NS2B: identification of a domain required for NS2B-NS3 protease activity IIJ Virol. 1993, v. 67, p. 2034−2042.
114. Jan L.R., Yang C.S., Trent D.W., Falgout В., Lai C.J. Processing of Japanese encephalitis virus non-structural proteins: NS2B-NS3 complex and heterologous proteases // J Gen Virol. 1995, v. 76, p. 573−580.
115. Lobigs M. Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3 // Proc Natl Acad Sci USA. 1993, v. 90, p. 6218−6222.
116. Droll D.A., Krishna Murthy H.M., Chambers T.J. Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletionanalysis define regions important for protease complex formation and function// Virology. 2000, v. 275, p. 335−347.
117. Falgout В., Pethel M., Zhang Y.M., Lai C.J. Both nonstructural proteins NS2B and NS3 are required for the proteolytic processing of dengue virus nonstructural proteins // J Virol. 1991, v. 65, p. 24 672 475.
118. Preugschat F., Yao C.W., Strauss J.H. In vitro processing of dengue virus type 2 nonstructural proteins NS2A, NS2B, and NS3 // J Virol. 1990, v. 64, p. 4364−4374.
119. Bauvois B. Transmembrane proteases in cell growth and invasion: new contributors to angiogenesis? // Oncogene. 2004, v. 23, p. 317 329.
120. Holmbeck K., Bianco P., Chrysovergis K., Yamada S., Birkedal-Hansen H. MTl-MMP-dependent, apoptotic remodeling of unmineralized cartilage: a critical process in skeletal growth // J Cell Biol 2003, v. 163, p. 661−671.
121. Le Roy C., Wrana J.L. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling // Nat Rev Mol Cell Biol 2005, v. 6, p. 112−126.
122. Nabi I.R., Le P.U. Caveolae/raft-dependent endocytosis // J Cell Biol. 2003, v. 161, p. 673−677.
123. Remacle A., Murphy G., Roghi C. Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface П J Cell Sci. 2003, v. 116, p. 3905−3916.
124. Remacle A.G., Rozanov D.V., Baciu P.C., Chekanov A.V., Golubkov V.S., Strongin A.Y. The transmembrane domain is essential for the microtubular trafficking of membrane type-1 matrix metalloproteinase (MT1-MMP) // J Cell Sci. 2005, v. 118, p. 49 754 984.
125. Zimmerman W.C., Sillibourne J., Rosa J., Doxsey S.J. Mitosis-specific anchoring of gamma tubulin complexes by pericentrin controls spindle organization and mitotic entry // Mol Biol Cell. 2004, v. 15, p. 3642−3657.