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Volumn 13, Issue 8, 2012, Pages 767-775

The role of cysteine proteinases and their inhibitors in the host-pathogen cross talk

Author keywords

Bacteria; Immune response; Protease cysteine proteinase; Proteinase inhibitor; Virus

Indexed keywords

CATHEPSIN; CYSTATIN B; CYSTEINE; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; GAMMA INTERFERON; INFLAMMASOME; INTERLEUKIN 10; LEGUMAIN; NITRIC OXIDE; PAPAIN; TOLL LIKE RECEPTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 84874827034     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312804871102     Document Type: Review
Times cited : (28)

References (140)
  • 2
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Cold Spring Harbor Symposia
    • Janeway, C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harbor Symposia. Quantitat. Biol., 1989, 54, 1-13.
    • (1989) Quantitat. Biol , vol.54 , pp. 1-13
    • Janeway, C.A.1
  • 3
    • 32944464648 scopus 로고    scopus 로고
    • Pathogen recognition and innate immunity
    • Akira, S.; Uematsu, S.; Takeuchi, O. Pathogen recognition and innate immunity. Cell, 2006, 124, 783-801.
    • (2006) Cell , vol.124 , pp. 783-801
    • Akira, S.1    Uematsu, S.2    Takeuchi, O.3
  • 4
    • 79956300649 scopus 로고    scopus 로고
    • Toll-like receptors and their crosstalk with other innate receptors in infection and immunity
    • Kawai, T.; Akira, S. Toll-like receptors and their crosstalk with other innate receptors in infection and immunity. Immunity, 2011, 34, 637-650.
    • (2011) Immunity , vol.34 , pp. 637-650
    • Kawai, T.1    Akira, S.2
  • 5
    • 3142724031 scopus 로고    scopus 로고
    • Toll-like receptor signalling
    • Akira, S.; Takeda, K. Toll-like receptor signalling. Nat. Rev. Immunol., 2004, 4, 499-511.
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 499-511
    • Akira, S.1    Takeda, K.2
  • 6
    • 35349016235 scopus 로고    scopus 로고
    • Recognition of microorganisms and activation of the immune response
    • Medzhitov, R. Recognition of microorganisms and activation of the immune response. Nature, 2007, 449, 819-826.
    • (2007) Nature , vol.449 , pp. 819-826
    • Medzhitov, R.1
  • 7
    • 48749128643 scopus 로고    scopus 로고
    • Structures of the Toll-like receptor family and its ligand complexes
    • Jin, M.S.; Lee, J.-O. Structures of the Toll-like receptor family and its ligand complexes. Immunity, 2008, 29, 182-191.
    • (2008) Immunity , vol.29 , pp. 182-191
    • Jin, M.S.1    Lee, J.-O.2
  • 8
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe, B.; Kajava, A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol., 2001, 11, 725-732.
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 9
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin, M.S.; Kim, S.E.; Heo, J.Y.; Lee, M.E.; Kim, H.M.; Paik, S.-G.; Lee, H.; Lee, J.-O. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell, 2007, 130, 1071-1082.
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, S.E.2    Heo, J.Y.3    Lee, M.E.4    Kim, H.M.5    Paik, S.-G.6    Lee, H.7    Lee, J.-O.8
  • 10
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: Update on toll-like receptors
    • Kawai, T.; Akira, S. The role of pattern-recognition receptors in innate immunity: Update on toll-like receptors.Nat. Immunol., 2010, 11, 373-384.
    • (2010) Nat. Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 11
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila toll protein signals activation of adaptive immunity
    • Medzhitov, R.; Preston-Hurlburt, P.; Janeway, C.A. A human homologue of the Drosophila toll protein signals activation of adaptive immunity. Nature, 1997, 388, 394-397.
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway, C.A.3
  • 13
    • 0036451206 scopus 로고    scopus 로고
    • TLR4 as the mammalian endotoxin sensor
    • Beutler, B. TLR4 as the mammalian endotoxin sensor. Curr. Top. Microbiol. Immunol., 2002, 270, 109-120.
    • (2002) Curr. Top. Microbiol. Immunol , vol.270 , pp. 109-120
    • Beutler, B.1
  • 15
    • 0033580949 scopus 로고    scopus 로고
    • Peptidoglycan-and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2
    • Schwandner, R.; Dziarski, R.; Wesche, H.; Rothe, M.; Kirschning, C.J. Peptidoglycan-and lipoteichoic acid-induced cell activation is mediated by Toll-like receptor 2. J. Biol. Chem., 1999, 274, 17406-17409.
    • (1999) J. Biol. Chem , vol.274 , pp. 17406-17409
    • Schwandner, R.1    Dziarski, R.2    Wesche, H.3    Rothe, M.4    Kirschning, C.J.5
  • 16
    • 0033458799 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages
    • Underhill, D.M.; Ozinsky, A.; Smith, K.D.; Aderem, A. Toll-like receptor-2 mediates mycobacteria-induced proinflammatory signaling in macrophages. Proc. Nat. Acad. Sci., 1999, 96, 14459-14463.
    • (1999) Proc. Nat. Acad. Sci , vol.96 , pp. 14459-14463
    • Underhill, D.M.1    Ozinsky, A.2    Smith, K.D.3    Aderem, A.4
  • 20
    • 74549167783 scopus 로고    scopus 로고
    • Regulation of adaptive immunity by the innate immune system
    • Iwasaki, A.; Medzhitov, R. Regulation of adaptive immunity by the innate immune system. Science, 2010, 327, 291-295.
    • (2010) Science , vol.327 , pp. 291-295
    • Iwasaki, A.1    Medzhitov, R.2
  • 21
    • 84859426282 scopus 로고    scopus 로고
    • Merops: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N.D.; Barrett, A.J.; Bateman, A. Merops: The database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res., 2012, 40, 15.
    • (2012) Nucleic Acids Res , vol.40 , pp. 15
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 22
    • 0027070658 scopus 로고
    • Cellular proteolysis: An overview
    • Barrett, A.J. Cellular proteolysis: An overview. Ann. NY. Acad. Sci., 1992, 674, 1-15.
    • (1992) Ann. NY. Acad. Sci , vol.674 , pp. 1-15
    • Barrett, A.J.1
  • 23
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings, N.D.; Barrett, A.J. Families of cysteine peptidases. Meth. Enzymol., 1994, 244, 461-486.
    • (1994) Meth. Enzymol , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barrett, A.J.2
  • 26
    • 38649111363 scopus 로고    scopus 로고
    • Cysteine cathepsins: Cellular roadmap to different functions
    • Brix, K.; Dunkhorst, A.; Mayer, K.; Jordans, S. Cysteine cathepsins: Cellular roadmap to different functions. Biochimie, 2008, 90, 194-207.
    • (2008) Biochimie , vol.90 , pp. 194-207
    • Brix, K.1    Dunkhorst, A.2    Mayer, K.3    Jordans, S.4
  • 27
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V.; Turk, B.; Turk, D. Lysosomal cysteine proteases: Facts and opportunities. EMBO J., 2001, 20, 4629 -4633.
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 28
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • Reinheckel, T.; Deussing, J.; Roth, W.; Peters, C. Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L. Biol. Chem., 2001, 382, 735-741.
    • (2001) Biol. Chem , vol.382 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 30
    • 0032522413 scopus 로고    scopus 로고
    • Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas
    • Santamaría, I.; Velasco, G.; Cazorla, M.; Fueyo, A.; Campo, E.; López-Otín, C. Cathepsin L2, a novel human cysteine proteinase produced by breast and colorectal carcinomas. Cancer Res., 1998, 58, 1624-1630.
    • (1998) Cancer Res , vol.58 , pp. 1624-1630
    • Santamaría, I.1    Velasco, G.2    Cazorla, M.3    Fueyo, A.4    Campo, E.5    López-Otín, C.6
  • 31
    • 0038687865 scopus 로고    scopus 로고
    • Human cathepsin v functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization
    • Bromme, D.; Li, Z.; Barnes, M.; Mehler, E. Human cathepsin v functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry, 1999, 38, 2377-2385.
    • (1999) Biochemistry , vol.38 , pp. 2377-2385
    • Bromme, D.1    Li, Z.2    Barnes, M.3    Mehler, E.4
  • 32
    • 1942470581 scopus 로고    scopus 로고
    • A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in s phase and processes the CDP/Cux transcription factor
    • Goulet, B.; Baruch, A.; Moon, N.S.; Poirier, M.; Sansregret, L.L.; Erickson, A.; Bogyo, M.; Nepveu, A. A cathepsin L isoform that is devoid of a signal peptide localizes to the nucleus in s phase and processes the CDP/Cux transcription factor. Mol. Cell, 2004, 14, 207-219.
    • (2004) Mol. Cell , vol.14 , pp. 207-219
    • Goulet, B.1    Baruch, A.2    Moon, N.S.3    Poirier, M.4    Sansregret, L.L.5    Erickson, A.6    Bogyo, M.7    Nepveu, A.8
  • 33
    • 0032557529 scopus 로고    scopus 로고
    • In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B
    • Mehtani, S.; Gong, Q.; Panella, J.; Subbiah, S.; Peffley, D.M.; Frankfater, A. In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. J. Biol. Chem., 1998, 273, 13236-13244.
    • (1998) J. Biol. Chem , vol.273 , pp. 13236-13244
    • Mehtani, S.1    Gong, Q.2    Panella, J.3    Subbiah, S.4    Peffley, D.M.5    Frankfater, A.6
  • 34
    • 57349176440 scopus 로고    scopus 로고
    • Nuclear cathepsin fregulates activation markers in rat hepatic stellate cells
    • Maubach, G.; Lim, M.C.C.; Zhuo, L. Nuclear cathepsin fregulates activation markers in rat hepatic stellate cells. Mol. Biol. Cell, 2008, 19, 4238-4248.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4238-4248
    • Maubach, G.1    Lim, M.C.C.2    Zhuo, L.3
  • 37
    • 52049096824 scopus 로고    scopus 로고
    • Cystatins: Biochemical and structural properties, and medical relevance
    • Turk, V.; Stoka, V.; Turk, D. Cystatins: Biochemical and structural properties, and medical relevance. Front Biosci., 2008, 13, 5406 -5420.
    • (2008) Front Biosci. , vol.13 , pp. 5406-5420
    • Turk, V.1    Stoka, V.2    Turk, D.3
  • 38
    • 33750984761 scopus 로고    scopus 로고
    • The role of cystatins in cells of the immune system
    • Kopitar-Jerala, N. The role of cystatins in cells of the immune system. FEBS Lett., 2006, 580, 6295-6301.
    • (2006) FEBS Lett , vol.580 , pp. 6295-6301
    • Kopitar-Jerala, N.1
  • 40
    • 0038835365 scopus 로고    scopus 로고
    • Thyropins mdash new structurally related proteinase inhibitors
    • Lenarcic, B.; Bevec, T. Thyropins mdash new structurally related proteinase inhibitors. Biol. Chem., 1998, 379, 105-111.
    • (1998) Biol. Chem , vol.379 , pp. 105-111
    • Lenarcic, B.1    Bevec, T.2
  • 42
    • 0029924123 scopus 로고    scopus 로고
    • Major histocompatibility complex class Ii-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L
    • Bevec, T.; Stoka, V.; Pungercic, G.; Dolenc, I.; Turk, V. Major histocompatibility complex class Ii-associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L. J. Exp. Med., 1996, 183(4), 1331-1338.
    • (1996) J. Exp. Med , vol.183 , Issue.4 , pp. 1331-1338
    • Bevec, T.1    Stoka, V.2    Pungercic, G.3    Dolenc, I.4    Turk, V.5
  • 43
    • 0031019416 scopus 로고    scopus 로고
    • A fragment of the major histocompatibility complex class Iiassociated p41 invariant chain inhibits cruzipain, the major cysteine proteinase from trypanosoma cruzi
    • Bevec, T.; Stoka, V.; Pungercic, G.; Cazzulo, J.J.; Turk, V. A fragment of the major histocompatibility complex class Iiassociated p41 invariant chain inhibits cruzipain, the major cysteine proteinase from trypanosoma cruzi. FEBS Lett., 1997, 401(2-3):259-261.
    • (1997) FEBS Lett , vol.401 , Issue.2-3 , pp. 259-261
    • Bevec, T.1    Stoka, V.2    Pungercic, G.3    Cazzulo, J.J.4    Turk, V.5
  • 44
    • 0039547996 scopus 로고    scopus 로고
    • Crystal structure of mhc class Ii-associated p41 ii fragment bound to cathepsin l reveals the structural basis for differentiation between cathepsins L and S
    • Guncar, G.; Pungercic, G.; Klemencic, I.; Turk, V.; Turk, D. Crystal structure of mhc class Ii-associated p41 ii fragment bound to cathepsin l reveals the structural basis for differentiation between cathepsins L and S. EMBO J., 1999, 18(4):793-803.
    • (1999) EMBO J , vol.18 , Issue.4 , pp. 793-803
    • Guncar, G.1    Pungercic, G.2    Klemencic, I.3    Turk, V.4    Turk, D.5
  • 46
    • 0024066065 scopus 로고
    • The 2.0 A x-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode, W.; Engh, R.; Musil, D.; Thiele, U.; Huber, R.; Karshikov, A.; Brzin, J.; Kos, J.; Turk, V. The 2.0 A x-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. Embo. J., 1988, 7, 2593-2599.
    • (1988) Embo. J , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 47
    • 0025301658 scopus 로고
    • The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction
    • Stubbs, M.T.; Laber, B.; Bode, W.; Huber, R.; Jerala, R.; Lenarcic, B.; Turk, V. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: A novel type of proteinase inhibitor interaction. Embo. J., 1990, 9, 1939-1947.
    • (1990) Embo. J , vol.9 , pp. 1939-1947
    • Stubbs, M.T.1    Laber, B.2    Bode, W.3    Huber, R.4    Jerala, R.5    Lenarcic, B.6    Turk, V.7
  • 48
    • 0022555509 scopus 로고
    • Human low-mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases
    • Salvesen, G.; Parkes, C.; Abrahamson, M.; Grubb, A.; Barrett, A.J. Human low-mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem. J., 1986, 234, 429-434.
    • (1986) Biochem. J , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 49
    • 0021676017 scopus 로고
    • Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen
    • Ohkubo, I.; Kurachi, K.; Takasawa, T.; Shiokawa, H.; Sasaki, M. Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry, 1984, 23, 5691-5697.
    • (1984) Biochemistry , vol.23 , pp. 5691-5697
    • Ohkubo, I.1    Kurachi, K.2    Takasawa, T.3    Shiokawa, H.4    Sasaki, M.5
  • 51
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpinprotease complex shows inhibition by deformation
    • Huntington, J.A.; Read, R.J.; Carrell, R.W. Structure of a serpinprotease complex shows inhibition by deformation. Nature, 2000, 407, 923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 52
    • 0037022831 scopus 로고    scopus 로고
    • The serpin SQN-5 is a dual mechanistic-class inhibitor of serine and cysteine proteinases
    • Al-Khunaizi, M. The serpin SQN-5 is a dual mechanistic-class inhibitor of serine and cysteine proteinases. Biochemistry, 2002, 41, 3189-3199.
    • (2002) Biochemistry , vol.41 , pp. 3189-3199
    • Al-Khunaizi, M.1
  • 54
    • 0028168514 scopus 로고
    • Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA
    • An example of cross-class inhibition
    • Komiyama, T.; Ray, C.A.; Pickup, D.J.; Howard, A.D.; Thornberry, N.A.; Peterson, E.P.; Salvesen, G. Inhibition of interleukin-1 beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. J. Biol. Chem., 1994, 269, 19331-19337.
    • (1994) J. Biol. Chem , vol.269 , pp. 19331-19337
    • Komiyama, T.1    Ray, C.A.2    Pickup, D.J.3    Howard, A.D.4    Thornberry, N.A.5    Peterson, E.P.6    Salvesen, G.7
  • 56
    • 28544446111 scopus 로고    scopus 로고
    • Monocyte and macrophage heterogeneity
    • Gordon, S.; Taylor, P.R. Monocyte and macrophage heterogeneity. Nature Rev. Immunol., 2005, 5, 953-964.
    • (2005) Nature Rev Immunol , vol.5 , pp. 953-964
    • Gordon, S.1    Taylor, P.R.2
  • 58
    • 79952123931 scopus 로고    scopus 로고
    • Microbial manipulation of receptor crosstalk in innate immunity
    • Hajishengallis, G.; Lambris, J.D. Microbial manipulation of receptor crosstalk in innate immunity. Nat. Rev. Immunol., 2011, 11, 187-200.
    • (2011) Nat. Rev. Immunol , vol.11 , pp. 187-200
    • Hajishengallis, G.1    Lambris, J.D.2
  • 59
    • 79953678939 scopus 로고    scopus 로고
    • Obstacles and opportunities for understanding macrophage polarization
    • Murray, P.J.; Wynn, T.A. Obstacles and opportunities for understanding macrophage polarization. J. Leukoc. Biol., 2011, 89, 557-563.
    • (2011) J. Leukoc. Biol , vol.89 , pp. 557-563
    • Murray, P.J.1    Wynn, T.A.2
  • 60
    • 0037963473 scopus 로고    scopus 로고
    • Blood monocytes consist of two principal subsets with distinct migratory properties
    • Geissmann, F.; Jung, S.; Littman, D.R. Blood monocytes consist of two principal subsets with distinct migratory properties. Immunity, 2003, 19, 71-82.
    • (2003) Immunity , vol.19 , pp. 71-82
    • Geissmann, F.1    Jung, S.2    Littman, D.R.3
  • 61
    • 0030926583 scopus 로고    scopus 로고
    • Selective suppression of interleukin-12 induction after macrophage receptor ligation
    • Sutterwala, F.S.; Noel, G.J.; Clynes, R.; Mosser, D.M. Selective suppression of interleukin-12 induction after macrophage receptor ligation. J. Exp. Med., 1997, 185, 1977-1985.
    • (1997) J. Exp. Med , vol.185 , pp. 1977-1985
    • Sutterwala, F.S.1    Noel, G.J.2    Clynes, R.3    Mosser, D.M.4
  • 62
    • 77649184739 scopus 로고    scopus 로고
    • The regulation of IL-10 production by immune cells
    • Saraiva, M.; O'Garra, A. The regulation of IL-10 production by immune cells. Nat. Rev. Immunol., 2010, 10, 170-181.
    • (2010) Nat. Rev. Immunol , vol.10 , pp. 170-181
    • Saraiva, M.1    O'Garra, A.2
  • 64
    • 0033572915 scopus 로고    scopus 로고
    • Chicken cystatin stimulates nitric oxide release from interferon-γactivated mouse peritoneal macrophages via cytokine synthesis
    • Verdot, L.; Lalmanach, G.; Vercruysse, V.; Hoebeke, J.; Gauthier, F.; Vray, B. Chicken cystatin stimulates nitric oxide release from interferon-γactivated mouse peritoneal macrophages via cytokine synthesis. Euro. J. Biochem., 1999, 266, 1111-1117.
    • (1999) Euro. J. Biochem , vol.266 , pp. 1111-1117
    • Verdot, L.1    Lalmanach, G.2    Vercruysse, V.3    Hoebeke, J.4    Gauthier, F.5    Vray, B.6
  • 66
    • 26244445000 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases in MHC class Ii antigen presentation
    • Hsing, L.C.; Rudensky, A.Y. The lysosomal cysteine proteases in MHC class Ii antigen presentation. Immunol. Rev., 2005, 207, 229-241.
    • (2005) Immunol. Rev , vol.207 , pp. 229-241
    • Hsing, L.C.1    Rudensky, A.Y.2
  • 67
    • 72949113082 scopus 로고    scopus 로고
    • Endolysosomal proteases and their inhibitors in immunity
    • Bird, P.I.; Trapani, J.A.; Villadangos, J.A. Endolysosomal proteases and their inhibitors in immunity. Nat. Rev. Immunol., 2009, 9, 871-882.
    • (2009) Nat. Rev. Immunol , vol.9 , pp. 871-882
    • Bird, P.I.1    Trapani, J.A.2    Villadangos, J.A.3
  • 69
    • 0037454948 scopus 로고    scopus 로고
    • Differential regulation of cathepsin S and cathepsin L in interferon -treated macrophages
    • Beers, C.; Honey, K.; Fink, S.; Forbush, K.; Rudensky, A. Differential regulation of cathepsin S and cathepsin L in interferon -treated macrophages. J. Exp. Med., 2003, 197, 169-179.
    • (2003) J. Exp. Med , vol.197 , pp. 169-179
    • Beers, C.1    Honey, K.2    Fink, S.3    Forbush, K.4    Rudensky, A.5
  • 70
    • 82755195248 scopus 로고    scopus 로고
    • Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms
    • Colbert, J.D.; Matthews, S.P.; Kos, J.; Watts, C. Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms. J. Biol. Chem., 2011, 286, 42082-42090.
    • (2011) J. Biol. Chem , vol.286 , pp. 42082-42090
    • Colbert, J.D.1    Matthews, S.P.2    Kos, J.3    Watts, C.4
  • 71
    • 77952951447 scopus 로고    scopus 로고
    • Increased Nucleolar Localization of Spia3g In Classically But Not Alternatively Activated Macrophages
    • Konjar S., Yin, F.; Bogyo, M.; Turk, B.; Kopitar-Jerala, N. Increased nucleolar localization of Spia3g in classically but not alternatively activated macrophages. FEBS Lett., 2010, 584, 2201-2206.
    • (2010) FEBS Lett , vol.584 , pp. 2201-2206
    • Konjar, S.1    Yin, F.2    Bogyo, M.3    Turk, B.4
  • 72
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K.; Tschopp, J. The inflammasomes. Cell, 2010, 140, 821-832.
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 73
    • 83655191553 scopus 로고    scopus 로고
    • Control of antiviral immunity by pattern recognition and the microbiome
    • 10.1111/j.1600-065X.2011.01073.x
    • Pang, I.K.; Iwasaki, A. Control of antiviral immunity by pattern recognition and the microbiome. Immunol Rev., 2012, 245(1),209-226. doi: 10.1111/j.1600-065X.2011.01073.x.
    • (2012) Immunol Rev , vol.245 , Issue.1 , pp. 209-226
    • Pang, I.K.1    Iwasaki, A.2
  • 76
    • 77953187290 scopus 로고    scopus 로고
    • Uric acid promotes an acute inflammatory response to sterile cell death in mice
    • 10.1172/JCI40124
    • Kono, H.; Chen, C.J.; Ontiveros, F.; Rock, K.L. Uric acid promotes an acute inflammatory response to sterile cell death in mice. J. Clin. Invest., 2010, 120(6), 1939-1949. doi: 10.1172/JCI40124.
    • (2010) J. Clin. Invest , vol.120 , Issue.6 , pp. 1939-1949
    • Kono, H.1    Chen, C.J.2    Ontiveros, F.3    Rock, K.L.4
  • 77
    • 79955156438 scopus 로고    scopus 로고
    • Disease-associated amyloid and misfolded protein aggregates activate the inflammasome
    • Masters, S.L.; O'Neill, L.A. Disease-associated amyloid and misfolded protein aggregates activate the inflammasome. Trends Mol. Med., 2011, 17(5), 276-282.
    • (2011) Trends Mol. Med , vol.17 , Issue.5 , pp. 276-282
    • Masters, S.L.1    O'Neill, L.A.2
  • 80
    • 77349124883 scopus 로고    scopus 로고
    • Origin and development of dendritic cells
    • Liu, K.; Nussenzweig, M.C. Origin and development of dendritic cells. Immunol. Rev., 2010, 234, 45-54.
    • (2010) Immunol. Rev , vol.234 , pp. 45-54
    • Liu, K.1    Nussenzweig, M.C.2
  • 81
    • 35549000134 scopus 로고    scopus 로고
    • Development of plasmacytoid and conventional dendritic cell subtypes from single precursor cells derived in vitro and in vivo
    • Naik, S.H. Development of plasmacytoid and conventional dendritic cell subtypes from single precursor cells derived in vitro and in vivo. Nature Immunol., 2007, 8, 1217-1226.
    • (2007) Nature Immunol , vol.8 , pp. 1217-1226
    • Naik, S.H.1
  • 83
    • 0033529891 scopus 로고    scopus 로고
    • A potent signal for growth, activation, and maturation of human dendritic cells
    • Hartmann, G.; Weiner, G.J.; Krieg, A.M. Cpg DNA: A potent signal for growth, activation, and maturation of human dendritic cells. Proc. Nat. Acad. Sci., 1999, 96, 9305-9310.
    • (1999) Proc. Nat. Acad. Sci , vol.96 , pp. 9305-9310
    • Hartmann, G.1    Weiner, G.J.2    Krieg, A.M.3    Cpg, D.N.A.4
  • 84
    • 58049209834 scopus 로고    scopus 로고
    • Inflammatory signals in dendritic cell activation and the induction of adaptive immunity
    • Joffre, O.; Nolte, M.A.; Spörri, R.; Sousa, C.R.E. Inflammatory signals in dendritic cell activation and the induction of adaptive immunity.Immunol. Rev., 2009, 227, 234-247.
    • (2009) Immunol. Rev , vol.227 , pp. 234-247
    • Joffre, O.1    Nolte, M.A.2    Spörri, R.3    Sousa, C.R.E.4
  • 85
    • 0030858138 scopus 로고    scopus 로고
    • Inflammatory stimuli induce accumulation of MHC class Ii complexes on dendritic cells
    • Cella, M.; Engering, A.; Pinet, V.; Pieters, J.; Lanzavecchia, A. Inflammatory stimuli induce accumulation of MHC class Ii complexes on dendritic cells. Nature, 1997, 388, 782-787.
    • (1997) Nature , vol.388 , pp. 782-787
    • Cella, M.1    Engering, A.2    Pinet, V.3    Pieters, J.4    Lanzavecchia, A.5
  • 86
    • 77349088003 scopus 로고    scopus 로고
    • Unraveling the functions of plasmacytoid dendritic cells during viral infections, autoimmunity, and tolerance
    • Swiecki, M.; Colonna, M. Unraveling the functions of plasmacytoid dendritic cells during viral infections, autoimmunity, and tolerance. Immunol. Rev., 2010, 234, 142-162.
    • (2010) Immunol. Rev , vol.234 , pp. 142-162
    • Swiecki, M.1    Colonna, M.2
  • 87
    • 14844340568 scopus 로고    scopus 로고
    • Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate
    • Delamarre, L.; Pack, M.; Chang, H.; Mellman, I.; Trombetta, E.S. Differential lysosomal proteolysis in antigen-presenting cells determines antigen fate. Science, 2005, 307, 1630-1634.
    • (2005) Science , vol.307 , pp. 1630-1634
    • Delamarre, L.1    Pack, M.2    Chang, H.3    Mellman, I.4    Trombetta, E.S.5
  • 88
    • 77957796763 scopus 로고    scopus 로고
    • Monocyte-derived dendritic cells exhibit increased levels of lysosomal proteolysis as compared to other human dendritic cell populations
    • McCurley, N.; Mellman, I. Monocyte-derived dendritic cells exhibit increased levels of lysosomal proteolysis as compared to other human dendritic cell populations. PLoS ONE, 2010, 5, e11949.
    • (2010) PLoS ONE , vol.e11949 , pp. 5
    • McCurley, N.1    Mellman, I.2
  • 93
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class Ii trafficking in mouse dendritic cells
    • Pierre, P.; Mellman, I. Developmental regulation of invariant chain proteolysis controls MHC class Ii trafficking in mouse dendritic cells. Cell, 1998, 93, 1135-1145.
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 94
    • 0242495719 scopus 로고    scopus 로고
    • The protease inhibitor cystatin C is differentially expressed among dendritic cell populations, but does not control antigen presentation
    • El-Sukkari, D.; Wilson, N.S.; Hakansson, K.; Steptoe, R.J.; Grubb, A.; Shortman, K.; Villadangos, J.A. The protease inhibitor cystatin C is differentially expressed among dendritic cell populations, but does not control antigen presentation. J. Immunol., 2003, 171, 5003-5011.
    • (2003) J. Immunol , vol.171 , pp. 5003-5011
    • El-Sukkari, D.1    Wilson, N.S.2    Hakansson, K.3    Steptoe, R.J.4    Grubb, A.5    Shortman, K.6    Villadangos, J.A.7
  • 96
    • 34247484007 scopus 로고    scopus 로고
    • The interaction between the ER membrane protein UNC93b and TLR3, 7, and 9 is crucial for TLR signaling
    • Brinkmann, M.M. The interaction between the ER membrane protein UNC93b and TLR3, 7, and 9 is crucial for TLR signaling. J. Cell Biol., 2007, 177, 265-275.
    • (2007) J. Cell Biol , vol.177 , pp. 265-275
    • Brinkmann, M.M.1
  • 97
    • 67449136127 scopus 로고    scopus 로고
    • Unc93b1 biases toll-like receptor responses to nucleic acid in dendritic cells toward DNA-but against RNA-sensing
    • Fukui, R. Unc93b1 biases toll-like receptor responses to nucleic acid in dendritic cells toward DNA-but against RNA-sensing. J. Exp. Med., 2009, 206, 1339-1350.
    • (2009) J. Exp. Med , vol.206 , pp. 1339-1350
    • Fukui, R.1
  • 99
    • 79955743119 scopus 로고    scopus 로고
    • Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase
    • Ewald, S.E.; Engel, A.; Lee, J.; Wang, M.; Bogyo, M.; Barton, G.M. Nucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase. J. Exp. Med., 2011, 208, 643-651.
    • (2011) J. Exp. Med , vol.208 , pp. 643-651
    • Ewald, S.E.1    Engel, A.2    Lee, J.3    Wang, M.4    Bogyo, M.5    Barton, G.M.6
  • 100
    • 57349191215 scopus 로고    scopus 로고
    • The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor
    • Ewald, S.E.; Lee, B.L.; Lau, L.; Wickliffe, K.E.; Shi, G.P.; Chapman, H.A.; Barton, G.M. The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor. Nature, 2008, 456, 658-662.
    • (2008) Nature , vol.456 , pp. 658-662
    • Ewald, S.E.1    Lee, B.L.2    Lau, L.3    Wickliffe, K.E.4    Shi, G.P.5    Chapman, H.A.6    Barton, G.M.7
  • 101
    • 56349114913 scopus 로고    scopus 로고
    • Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9
    • Park, B.; Brinkmann, M.M.; Spooner, E.; Lee, C.C.; Kim, Y.M.; Ploegh, H.L. Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9. Nat. Immunol., 2008, 9, 1407-1414.
    • (2008) Nat. Immunol , vol.9 , pp. 1407-1414
    • Park, B.1    Brinkmann, M.M.2    Spooner, E.3    Lee, C.C.4    Kim, Y.M.5    Ploegh, H.L.6
  • 102
    • 79952263266 scopus 로고    scopus 로고
    • Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus
    • Ohbayashi, T.; Irie, A.; Murakami, Y.; Nowak, M.; Potempa, J.; Nishimura, Y.; Shinohara, M.; Imamura, T. Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus. Microbiology, 2011, 157, 786-792.
    • (2011) Microbiology , vol.157 , pp. 786-792
    • Ohbayashi, T.1    Irie, A.2    Murakami, Y.3    Nowak, M.4    Potempa, J.5    Nishimura, Y.6    Shinohara, M.7    Imamura, T.8
  • 103
    • 10844268751 scopus 로고    scopus 로고
    • Chemokine-like receptor 1 expression and chemerin-directed chemotaxis distinguish plasmacytoid from myeloid dendritic cells in human blood
    • Zabel, B.A.; Silverio, A.M.; Butcher, E.C. Chemokine-like receptor 1 expression and chemerin-directed chemotaxis distinguish plasmacytoid from myeloid dendritic cells in human blood. J. Immunol., 2005, 174, 244-251.
    • (2005) J. Immunol , vol.174 , pp. 244-251
    • Zabel, B.A.1    Silverio, A.M.2    Butcher, E.C.3
  • 104
    • 27144444137 scopus 로고    scopus 로고
    • Chemerin activation by serine proteases of the coagulation, fibrinolytic, and inflammatory cascades
    • Zabel, B.A.; Allen, S.J.; Kulig, P.; Allen, J.A.; Cichy, J.; Handel, T.M.; Butcher, E.C. Chemerin activation by serine proteases of the coagulation, fibrinolytic, and inflammatory cascades. J. Biol. Chem., 2005, 280, 34661-34666.
    • (2005) J. Biol. Chem , vol.280 , pp. 34661-34666
    • Zabel, B.A.1    Allen, S.J.2    Kulig, P.3    Allen, J.A.4    Cichy, J.5    Handel, T.M.6    Butcher, E.C.7
  • 107
    • 72049098213 scopus 로고    scopus 로고
    • Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes
    • Kordis, D.; Turk, V. Phylogenomic analysis of the cystatin superfamily in eukaryotes and prokaryotes. BMC Evol. Biol., 2009, 9, 266.
    • (2009) BMC Evol. Biol , vol.9 , pp. 266
    • Kordis, D.1    Turk, V.2
  • 108
    • 0037330259 scopus 로고    scopus 로고
    • Ides and speb: Immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes
    • von Pawel-Rammingen, U.; Björck, L. Ides and speb: Immunoglobulin-degrading cysteine proteinases of Streptococcus pyogenes. Curr. Opin. Microbiol., 2003, 6, 50-55.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 50-55
    • von Pawel-Rammingen, U.1    Björck, L.2
  • 109
    • 10644276295 scopus 로고    scopus 로고
    • Enzymatic characterization of the Streptococcal endopeptidase, ides, reveals that it is a cysteine protease with strict specificity for igg cleavage due to exosite binding
    • Vincents, B.; von Pawel-Rammingen, U.; Björck, L.; Abrahamson, M. Enzymatic characterization of the Streptococcal endopeptidase, ides, reveals that it is a cysteine protease with strict specificity for igg cleavage due to exosite binding. Biochemistry, 2004, 43, 15540-15549.
    • (2004) Biochemistry , vol.43 , pp. 15540-15549
    • Vincents, B.1    von Pawel-Rammingen, U.2    Björck, L.3    Abrahamson, M.4
  • 110
    • 51649097889 scopus 로고    scopus 로고
    • The human protease inhibitor cystatin C is an activating cofactor for the Streptococcal cysteine protease ides
    • Vincents, B.; Vindebro, R.; Abrahamson, M.; von Pawel-Rammingen, U. The human protease inhibitor cystatin C is an activating cofactor for the Streptococcal cysteine protease ides. Chem. Biol., 2008, 15, 960-968.
    • (2008) Chem. Biol , vol.15 , pp. 960-968
    • Vincents, B.1    Vindebro, R.2    Abrahamson, M.3    von Pawel-Rammingen, U.4
  • 111
    • 55849086508 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum increases cathepsin L activity, thereby globally influencing neutrophil function
    • Thomas, V.; Samanta, S.; Fikrig, E. Anaplasma phagocytophilum increases cathepsin L activity, thereby globally influencing neutrophil function. Infect. Immun., 2008, 76, 4905-4912.
    • (2008) Infect. Immun , vol.76 , pp. 4905-4912
    • Thomas, V.1    Samanta, S.2    Fikrig, E.3
  • 112
    • 83655162842 scopus 로고    scopus 로고
    • The cell biology of receptor-mediated virus entry
    • Grove, J.; Marsh, M. The cell biology of receptor-mediated virus entry. J. Cell Biol., 2011, 195, 1071-1082.
    • (2011) J. Cell Biol , vol.195 , pp. 1071-1082
    • Grove, J.1    Marsh, M.2
  • 114
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I.A.; Skehel, J.J.; Wiley, D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 1981, 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 115
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusio
    • Baker, K.A.; Dutch, R.E.; Lamb, R.A.; Jardetzky, T.S. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell, 1999, 3, 309-319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 116
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the hiv envelope glycoprotein
    • Chan, D.C.; Fass, D.; Berger, J.M.; Kim, P.S. Core structure of gp41 from the hiv envelope glycoprotein. Cell, 1997, 89, 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 118
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K.; Sullivan, N.J.; Felbor, U.; Whelan, S.P.; Cunningham, J.M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science, 2005, 308, 1643-1645
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 119
    • 84863713469 scopus 로고    scopus 로고
    • Ebola and Marburg hemorrhagic fevers: Neglected tropical diseases
    • MacNeil, A.; Rollin, P.E. Ebola and Marburg hemorrhagic fevers: Neglected tropical diseases? PLoS Negl Trop Dis, 2012, 6, 26.
    • (2012) PLoS Negl Trop Dis , vol.6 , pp. 26
    • Macneil, A.1    Rollin, P.E.2
  • 120
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee, J.E.; Fusco, M.L.; Hessell, A.J.; Oswald, W.B.; Burton, D.R.; Saphire, E.O. Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature, 2008, 454, 177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5    Saphire, E.O.6
  • 121
    • 73949151882 scopus 로고    scopus 로고
    • Ebolavirus glycoprotein structure and mechanism of entry
    • Lee, J.E.; Saphire, E.O. Ebolavirus glycoprotein structure and mechanism of entry. Future Virol., 2009, 4, 621-635.
    • (2009) Future Virol , vol.4 , pp. 621-635
    • Lee, J.E.1    Saphire, E.O.2
  • 122
    • 77649174605 scopus 로고    scopus 로고
    • Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: Implications for viral entry and immunogenicity
    • Hood, C.L. Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: Implications for viral entry and immunogenicity. J. Virol., 2010, 84, 2972-2982.
    • (2010) J. Virol , vol.84 , pp. 2972-2982
    • Hood, C.L.1
  • 123
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the ebola virus glycoprotein
    • Schornberg, K.; Matsuyama, S.; Kabsch, K.; Delos, S.; Bouton, A.; White, J. Role of endosomal cathepsins in entry mediated by the ebola virus glycoprotein. J. Virol., 2006, 80, 4174-4178.
    • (2006) J. Virol , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 124
    • 72849133481 scopus 로고    scopus 로고
    • A forward genetic strategy reveals destabilizing mutations in the Ebola virus glycoprotein that alter its protease dependence during cell entry
    • Wong, A.C.; Sandesara, R.G.; Mulherkar, N.; Whelan, S.P.; Chandran, K. A forward genetic strategy reveals destabilizing mutations in the Ebola virus glycoprotein that alter its protease dependence during cell entry. J. Virol., 2010, 84, 163-175.
    • (2010) J. Virol , vol.84 , pp. 163-175
    • Wong, A.C.1    Sandesara, R.G.2    Mulherkar, N.3    Whelan, S.P.4    Chandran, K.5
  • 128
    • 79952363727 scopus 로고    scopus 로고
    • Ebola haemorrhagic fever
    • Feldmann, H.; Geisbert, T.W. Ebola haemorrhagic fever. Lancet, 2011, 377, 849-862.
    • (2011) Lancet , vol.377 , pp. 849-862
    • Feldmann, H.1    Geisbert, T.W.2
  • 130
    • 58149526807 scopus 로고    scopus 로고
    • Proteasemediated entry via the endosome of human Coronavirus 229E
    • Kawase, M.; Shirato, K.; Matsuyama, S.; Taguchi, F. Proteasemediated entry via the endosome of human Coronavirus 229E. J. Virol., 2009, 83, 712-721.
    • (2009) J. Virol , vol.83 , pp. 712-721
    • Kawase, M.1    Shirato, K.2    Matsuyama, S.3    Taguchi, F.4
  • 132
    • 65249097210 scopus 로고    scopus 로고
    • Activation of the sars coronavirus spike protein via sequential proteolytic cleavage at two distinct sites
    • Belouzard, S.; Chu, V.C.; Whittaker, G.R. Activation of the sars coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc. Natl. Acad. Sci. USA, 2009, 106, 5871-5876.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 5871-5876
    • Belouzard, S.1    Chu, V.C.2    Whittaker, G.R.3
  • 136
    • 84860234644 scopus 로고    scopus 로고
    • Paramyxovirus fusion and entry: Multiple paths to a common end
    • Chang, A.; Dutch, R.E. Paramyxovirus fusion and entry: Multiple paths to a common end. Viruses, 2012, 4, 613-636.
    • (2012) Viruses , vol.4 , pp. 613-636
    • Chang, A.1    Dutch, R.E.2
  • 137
    • 84861309290 scopus 로고    scopus 로고
    • Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment
    • Diederich, S.; Sauerhering, L.; Weis, M.; Altmeppen, H.; Schaschke, N.; Reinheckel, T.; Erbar, S.; Maisner, A. Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment. J. Virol., 2012, 86, 3736-3745
    • (2012) J. Virol , vol.86 , pp. 3736-3745
    • Diederich, S.1    Sauerhering, L.2    Weis, M.3    Altmeppen, H.4    Schaschke, N.5    Reinheckel, T.6    Erbar, S.7    Maisner, A.8
  • 138
    • 0019522275 scopus 로고
    • Protein 1 is the reovirus cell attachment protein
    • Lee, P.W.K.; Hayes, E.C.; Joklik, W.K. Protein 1 is the reovirus cell attachment protein. Virology, 1981, 108, 156-163.
    • (1981) Virology , vol.8 , pp. 156-163
    • Lee, P.W.K.1    Hayes, E.C.2    Joklik, W.K.3
  • 139
    • 0019403390 scopus 로고
    • Reovirus: Evidence for a second step in the intracellular uncoating and transcriptase activation process
    • Borsa, J.; Sargent, M.D.; Lievaart, P.A.; Copps, T.P. Reovirus: Evidence for a second step in the intracellular uncoating and transcriptase activation process. Virology, 1981, 111, 191-200.
    • (1981) Virology , vol.111 , pp. 191-200
    • Borsa, J.1    Sargent, M.D.2    Lievaart, P.A.3    Copps, T.P.4


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