메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Host-derived extracellular RNA promotes adhesion of Streptococcus pneumoniae to endothelial and epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENOLASE; GLYCINE; LYSINE; NUCLEOTIDE; PANCREATIC RIBONUCLEASE; RNA;

EID: 84999816175     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep37758     Document Type: Article
Times cited : (22)

References (59)
  • 3
    • 65449169610 scopus 로고    scopus 로고
    • The antimicrobial resistance profile of Streptococcus pneumoniae
    • Reinert, R. R. The antimicrobial resistance profile of Streptococcus pneumoniae. Clin Microbiol Infect 15 Suppl 3, 7-11 (2009).
    • (2009) Clin Microbiol Infect 15 Suppl , vol.3 , pp. 7-11
    • Reinert, R.R.1
  • 4
    • 0034727809 scopus 로고    scopus 로고
    • Increasing prevalence of multidrug-resistant Streptococcus pneumoniae in the United States
    • Whitney, C. G. et al. Increasing prevalence of multidrug-resistant Streptococcus pneumoniae in the United States. The New England journal of medicine 343, 1917-1924 (2000).
    • (2000) The New England Journal of Medicine , vol.343 , pp. 1917-1924
    • Whitney, C.G.1
  • 5
    • 84938895447 scopus 로고    scopus 로고
    • Effects of Infant Pneumococcal Conjugate Vaccination on Serotype Distribution in Invasive Pneumococcal Disease among Children and Adults in Germany
    • van der Linden, M., Falkenhorst, G., Perniciaro, S. & Imohl, M. Effects of Infant Pneumococcal Conjugate Vaccination on Serotype Distribution in Invasive Pneumococcal Disease among Children and Adults in Germany. PloS one 10, e0131494 (2015).
    • (2015) PloS One , vol.10
    • Van Der Linden, M.1    Falkenhorst, G.2    Perniciaro, S.3    Imohl, M.4
  • 6
    • 40949162838 scopus 로고    scopus 로고
    • The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease
    • Kadioglu, A., Weiser, J. N., Paton, J. C. & Andrew, P. W. The role of Streptococcus pneumoniae virulence factors in host respiratory colonization and disease. Nat Rev Microbiol 6, 288-301 (2008).
    • (2008) Nat Rev Microbiol , vol.6 , pp. 288-301
    • Kadioglu, A.1    Weiser, J.N.2    Paton, J.C.3    Andrew, P.W.4
  • 7
    • 1342304130 scopus 로고    scopus 로고
    • Ectodomains 3 and 4 of human polymeric Immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium
    • Elm, C. et al. Ectodomains 3 and 4 of human polymeric Immunoglobulin receptor (hpIgR) mediate invasion of Streptococcus pneumoniae into the epithelium. The Journal of biological chemistry 279, 6296-6304 (2004).
    • (2004) The Journal of Biological Chemistry , vol.279 , pp. 6296-6304
    • Elm, C.1
  • 8
    • 34247485877 scopus 로고    scopus 로고
    • E-cadherin is a receptor for the common protein pneumococcal surface adhesin A (PsaA) of Streptococcus pneumoniae
    • Anderton, J. M. et al. E-cadherin is a receptor for the common protein pneumococcal surface adhesin A (PsaA) of Streptococcus pneumoniae. Microbial pathogenesis 42, 225-236 (2007).
    • (2007) Microbial Pathogenesis , vol.42 , pp. 225-236
    • Anderton, J.M.1
  • 10
    • 34247573934 scopus 로고    scopus 로고
    • The host immune regulator factor H interacts via two contact sites with the PspC protein of Streptococcus pneumoniae and mediates adhesion to host epithelial cells
    • Hammerschmidt, S. et al. The host immune regulator factor H interacts via two contact sites with the PspC protein of Streptococcus pneumoniae and mediates adhesion to host epithelial cells. Journal of immunology 178, 5848-5858 (2007).
    • (2007) Journal of Immunology , vol.178 , pp. 5848-5858
    • Hammerschmidt, S.1
  • 11
    • 48749094614 scopus 로고    scopus 로고
    • Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge
    • Rose, L. et al. Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge. J Infect Dis 198, 375-383 (2008).
    • (2008) J Infect Dis , vol.198 , pp. 375-383
    • Rose, L.1
  • 12
    • 0348110222 scopus 로고    scopus 로고
    • Evolution of sfbI encoding streptococcal fibronectin-binding protein I: Horizontal genetic transfer and gene mosaic structure
    • Towers, R. J. et al. Evolution of sfbI encoding streptococcal fibronectin-binding protein I: horizontal genetic transfer and gene mosaic structure. J Clin Microbiol 41, 5398-5406 (2003).
    • (2003) J Clin Microbiol , vol.41 , pp. 5398-5406
    • Towers, R.J.1
  • 13
    • 0034786512 scopus 로고    scopus 로고
    • The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence
    • Holmes, A. R. et al. The pavA gene of Streptococcus pneumoniae encodes a fibronectin-binding protein that is essential for virulence. Molecular microbiology 41, 1395-1408 (2001).
    • (2001) Molecular Microbiology , vol.41 , pp. 1395-1408
    • Holmes, A.R.1
  • 14
    • 0026682564 scopus 로고
    • A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    • Pancholi, V. & Fischetti, V. A. A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. The Journal of experimental medicine 176, 415-426 (1992).
    • (1992) The Journal of Experimental Medicine , vol.176 , pp. 415-426
    • Pancholi, V.1    Fischetti, V.A.2
  • 15
    • 42949153528 scopus 로고    scopus 로고
    • Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions
    • Kinnby, B., Booth, N. A. & Svensater, G. Plasminogen binding by oral streptococci from dental plaque and inflammatory lesions. Microbiology 154, 924-931 (2008).
    • (2008) Microbiology , vol.154 , pp. 924-931
    • Kinnby, B.1    Booth, N.A.2    Svensater, G.3
  • 16
    • 1842535489 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein
    • Bergmann, S., Rohde, M. & Hammerschmidt, S. Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein. Infection and immunity 72, 2416-2419 (2004).
    • (2004) Infection and Immunity , vol.72 , pp. 2416-2419
    • Bergmann, S.1    Rohde, M.2    Hammerschmidt, S.3
  • 17
    • 0034931519 scopus 로고    scopus 로고
    • Alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)- binding protein displayed on the bacterial cell surface
    • Bergmann, S., Rohde, M., Chhatwal, G. S. & Hammerschmidt, S. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)- binding protein displayed on the bacterial cell surface. Molecular microbiology 40, 1273-1287 (2001).
    • (2001) Molecular Microbiology , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 18
    • 0025819231 scopus 로고
    • Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor
    • Miles, L. A. et al. Role of cell-surface lysines in plasminogen binding to cells: identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 30, 1682-1691 (1991).
    • (1991) Biochemistry , vol.30 , pp. 1682-1691
    • Miles, L.A.1
  • 19
    • 0038501069 scopus 로고    scopus 로고
    • Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae
    • Bergmann, S. et al. Identification of a novel plasmin(ogen)-binding motif in surface displayed alpha-enolase of Streptococcus pneumoniae. Molecular microbiology 49, 411-423 (2003).
    • (2003) Molecular Microbiology , vol.49 , pp. 411-423
    • Bergmann, S.1
  • 21
    • 84871978237 scopus 로고    scopus 로고
    • Fighting against the dark side of neutrophil extracellular traps in disease: Manoeuvres for host protection
    • Saffarzadeh, M. & Preissner, K. T. Fighting against the dark side of neutrophil extracellular traps in disease: manoeuvres for host protection. Current opinion in hematology 20, 3-9 (2013).
    • (2013) Current Opinion in Hematology , vol.20 , pp. 3-9
    • Saffarzadeh, M.1    Preissner, K.T.2
  • 22
    • 53149116721 scopus 로고    scopus 로고
    • Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation, and prolong survival upon infection in insects
    • Altincicek, B., Stotzel, S., Wygrecka, M., Preissner, K. T. & Vilcinskas, A. Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation, and prolong survival upon infection in insects. Journal of immunology 181, 2705-2712 (2008).
    • (2008) Journal of Immunology , vol.181 , pp. 2705-2712
    • Altincicek, B.1    Stotzel, S.2    Wygrecka, M.3    Preissner, K.T.4    Vilcinskas, A.5
  • 24
    • 84867252647 scopus 로고    scopus 로고
    • Extracellular RNA promotes leukocyte recruitment in the vascular system by mobilising proinflammatory cytokines
    • Fischer, S. et al. Extracellular RNA promotes leukocyte recruitment in the vascular system by mobilising proinflammatory cytokines. Thrombosis and haemostasis 108, 730-741 (2012).
    • (2012) Thrombosis and Haemostasis , vol.108 , pp. 730-741
    • Fischer, S.1
  • 25
    • 84882581773 scopus 로고    scopus 로고
    • Extracellular RNA liberates tumor necrosis factor-alpha to promote tumor cell trafficking and progression
    • Fischer, S. et al. Extracellular RNA liberates tumor necrosis factor-alpha to promote tumor cell trafficking and progression. Cancer research 73, 5080-5089 (2013).
    • (2013) Cancer Research , vol.73 , pp. 5080-5089
    • Fischer, S.1
  • 26
    • 84898612000 scopus 로고    scopus 로고
    • Role of extracellular RNA and TLR3-Trif signaling in myocardial ischemia-reperfusion injury
    • Chen, C. et al. Role of extracellular RNA and TLR3-Trif signaling in myocardial ischemia-reperfusion injury. J Am Heart Assoc 3, e000683 (2014).
    • (2014) J Am Heart Assoc , vol.3
    • Chen, C.1
  • 27
    • 84945945891 scopus 로고    scopus 로고
    • Cardiac RNA induces inflammatory responses in cardiomyocytes and immune cells via Toll-like receptor 7 signaling
    • Feng, Y. et al. Cardiac RNA induces inflammatory responses in cardiomyocytes and immune cells via Toll-like receptor 7 signaling. The Journal of biological chemistry 290, 26688-26698 (2015).
    • (2015) The Journal of Biological Chemistry , vol.290 , pp. 26688-26698
    • Feng, Y.1
  • 28
    • 31544473809 scopus 로고    scopus 로고
    • The role of positively charged amino acids and electrostatic interactions in the complex of U1A protein and U1 hairpin II RNA
    • Law, M. J. et al. The role of positively charged amino acids and electrostatic interactions in the complex of U1A protein and U1 hairpin II RNA. Nucleic acids research 34, 275-285 (2006).
    • (2006) Nucleic Acids Research , vol.34 , pp. 275-285
    • Law, M.J.1
  • 29
    • 84887618763 scopus 로고    scopus 로고
    • The interaction between bacterial enolase and plasminogen promotes adherence of Streptococcus pneumoniae to epithelial and endothelial cells
    • Bergmann, S., Schoenen, H. & Hammerschmidt, S. The interaction between bacterial enolase and plasminogen promotes adherence of Streptococcus pneumoniae to epithelial and endothelial cells. Int J Med Microbiol 303, 452-462 (2013).
    • (2013) Int J Med Microbiol , vol.303 , pp. 452-462
    • Bergmann, S.1    Schoenen, H.2    Hammerschmidt, S.3
  • 30
    • 5144224570 scopus 로고    scopus 로고
    • Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: Crystal structure and evaluation of plasmin(ogen)-binding sites
    • Ehinger, S., Schubert, W. D., Bergmann, S., Hammerschmidt, S. & Heinz, D. W. Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites. Journal of molecular biology 343, 997-1005 (2004).
    • (2004) Journal of Molecular Biology , vol.343 , pp. 997-1005
    • Ehinger, S.1    Schubert, W.D.2    Bergmann, S.3    Hammerschmidt, S.4    Heinz, D.W.5
  • 31
    • 0346881417 scopus 로고    scopus 로고
    • Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci
    • Derbise, A., Song, Y. P., Parikh, S., Fischetti, V. A. & Pancholi, V. Role of the C-terminal lysine residues of streptococcal surface enolase in Glu- and Lys-plasminogen-binding activities of group A streptococci. Infection and immunity 72, 94-105 (2004).
    • (2004) Infection and Immunity , vol.72 , pp. 94-105
    • Derbise, A.1    Song, Y.P.2    Parikh, S.3    Fischetti, V.A.4    Pancholi, V.5
  • 33
    • 0025831155 scopus 로고
    • Structure and biological role of vitronectin
    • Preissner, K. T. Structure and biological role of vitronectin. Annu Rev Cell Biol 7, 275-310 (1991).
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 275-310
    • Preissner, K.T.1
  • 34
    • 72449147268 scopus 로고    scopus 로고
    • Proteoglycans: From structural compounds to signaling molecules
    • Schaefer, L. & Schaefer, R. M. Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res 339, 237-246 (2010).
    • (2010) Cell Tissue Res , vol.339 , pp. 237-246
    • Schaefer, L.1    Schaefer, R.M.2
  • 35
    • 72449207034 scopus 로고    scopus 로고
    • The interaction of Thrombospondins with extracellular matrix proteins
    • Tan, K. & Lawler, J. The interaction of Thrombospondins with extracellular matrix proteins. J Cell Commun Signal 3, 177-187 (2009).
    • (2009) J Cell Commun Signal , vol.3 , pp. 177-187
    • Tan, K.1    Lawler, J.2
  • 36
    • 84894193386 scopus 로고    scopus 로고
    • Repeating structures of the major staphylococcal autolysin are essential for the interaction with human thrombospondin 1 and vitronectin
    • Kohler, T. P. et al. Repeating structures of the major staphylococcal autolysin are essential for the interaction with human thrombospondin 1 and vitronectin. The Journal of biological chemistry 289, 4070-4082 (2014).
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 4070-4082
    • Kohler, T.P.1
  • 37
    • 61949389320 scopus 로고    scopus 로고
    • Integrin-linked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells
    • Bergmann, S. et al. Integrin-linked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells. Journal of cell science 122, 256-267 (2009).
    • (2009) Journal of Cell Science , vol.122 , pp. 256-267
    • Bergmann, S.1
  • 38
    • 0034604055 scopus 로고    scopus 로고
    • ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: Relationship with Myc promoter-binding protein 1 (MBP-1)
    • Feo, S., Arcuri, D., Piddini, E., Passantino, R. & Giallongo, A. ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS letters 473, 47-52 (2000).
    • (2000) FEBS Letters , vol.473 , pp. 47-52
    • Feo, S.1    Arcuri, D.2    Piddini, E.3    Passantino, R.4    Giallongo, A.5
  • 39
    • 23744464766 scopus 로고    scopus 로고
    • The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration
    • Bergmann, S., Rohde, M., Preissner, K. T. & Hammerschmidt, S. The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration. Thrombosis and haemostasis 94, 304-311 (2005).
    • (2005) Thrombosis and Haemostasis , vol.94 , pp. 304-311
    • Bergmann, S.1    Rohde, M.2    Preissner, K.T.3    Hammerschmidt, S.4
  • 40
    • 32944482526 scopus 로고    scopus 로고
    • An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps
    • Beiter, K. et al. An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Current biology: CB 16, 401-407 (2006).
    • (2006) Current Biology: CB , vol.16 , pp. 401-407
    • Beiter, K.1
  • 41
    • 84904510702 scopus 로고    scopus 로고
    • Tuf of Streptococcus pneumoniae is a surface displayed human complement regulator binding protein
    • Mohan, S. et al. Tuf of Streptococcus pneumoniae is a surface displayed human complement regulator binding protein. Molecular immunology 62, 249-264 (2014).
    • (2014) Molecular Immunology , vol.62 , pp. 249-264
    • Mohan, S.1
  • 42
    • 84901608607 scopus 로고    scopus 로고
    • Proteomic analysis of the interaction of Bifidobacterium longum NCC2705 with the intestine cells Caco-2 and identification of plasminogen receptors
    • Wei, X. et al. Proteomic analysis of the interaction of Bifidobacterium longum NCC2705 with the intestine cells Caco-2 and identification of plasminogen receptors. Journal of proteomics 108, 89-98 (2014).
    • (2014) Journal of Proteomics , vol.108 , pp. 89-98
    • Wei, X.1
  • 43
    • 34948857581 scopus 로고    scopus 로고
    • Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis
    • Xolalpa, W. et al. Identification of novel bacterial plasminogen-binding proteins in the human pathogen Mycobacterium tuberculosis. Proteomics 7, 3332-3341 (2007).
    • (2007) Proteomics , vol.7 , pp. 3332-3341
    • Xolalpa, W.1
  • 44
    • 0023190457 scopus 로고
    • Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu
    • Faulhammer, H. G. & Joshi, R. L. Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu. FEBS letters 217, 203-211 (1987).
    • (1987) FEBS Letters , vol.217 , pp. 203-211
    • Faulhammer, H.G.1    Joshi, R.L.2
  • 45
    • 84866386143 scopus 로고    scopus 로고
    • Intravascular neutrophil extracellular traps capture bacteria from the bloodstream during sepsis
    • McDonald, B., Urrutia, R., Yipp, B. G., Jenne, C. N. & Kubes, P. Intravascular neutrophil extracellular traps capture bacteria from the bloodstream during sepsis. Cell Host Microbe 12, 324-333 (2012).
    • (2012) Cell Host Microbe , vol.12 , pp. 324-333
    • McDonald, B.1    Urrutia, R.2    Yipp, B.G.3    Jenne, C.N.4    Kubes, P.5
  • 46
    • 34147188469 scopus 로고    scopus 로고
    • Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood
    • Clark, S. R. et al. Platelet TLR4 activates neutrophil extracellular traps to ensnare bacteria in septic blood. Nature medicine 13, 463-469 (2007).
    • (2007) Nature Medicine , vol.13 , pp. 463-469
    • Clark, S.R.1
  • 47
    • 34547586304 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 is an inhibitor of factor VII-activating protease in patients with acute respiratory distress syndrome
    • Wygrecka, M. et al. Plasminogen activator inhibitor-1 is an inhibitor of factor VII-activating protease in patients with acute respiratory distress syndrome. The Journal of biological chemistry 282, 21671-21682 (2007).
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 21671-21682
    • Wygrecka, M.1
  • 48
    • 34948826463 scopus 로고    scopus 로고
    • Extracellular RNA mediates endothelial-cell permeability via vascular endothelial growth factor
    • Fischer, S. et al. Extracellular RNA mediates endothelial-cell permeability via vascular endothelial growth factor. Blood 110, 2457-2465 (2007).
    • (2007) Blood , vol.110 , pp. 2457-2465
    • Fischer, S.1
  • 49
    • 42249111711 scopus 로고    scopus 로고
    • Current view on alveolar coagulation and fibrinolysis in acute inflammatory and chronic interstitial lung diseases
    • Wygrecka, M., Jablonska, E., Guenther, A., Preissner, K. T. & Markart, P. Current view on alveolar coagulation and fibrinolysis in acute inflammatory and chronic interstitial lung diseases. Thrombosis and haemostasis 99, 494-501 (2008).
    • (2008) Thrombosis and Haemostasis , vol.99 , pp. 494-501
    • Wygrecka, M.1    Jablonska, E.2    Guenther, A.3    Preissner, K.T.4    Markart, P.5
  • 50
    • 84930883815 scopus 로고    scopus 로고
    • Distinct molecular phenotypes of direct vs indirect ARDS in single-center and multicenter studies
    • Calfee, C. S. et al. Distinct molecular phenotypes of direct vs indirect ARDS in single-center and multicenter studies. Chest 147, 1539-1548 (2015).
    • (2015) Chest , vol.147 , pp. 1539-1548
    • Calfee, C.S.1
  • 51
    • 70349745535 scopus 로고    scopus 로고
    • Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7
    • Abtin, A. et al. Degradation by stratum corneum proteases prevents endogenous RNase inhibitor from blocking antimicrobial activities of RNase 5 and RNase 7. The Journal of investigative dermatology 129, 2193-2201 (2009).
    • (2009) The Journal of Investigative Dermatology , vol.129 , pp. 2193-2201
    • Abtin, A.1
  • 52
    • 33947513637 scopus 로고    scopus 로고
    • The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity
    • Huang, Y. C. et al. The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity. The Journal of biological chemistry 282, 4626-4633 (2007).
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 4626-4633
    • Huang, Y.C.1
  • 53
    • 65249140613 scopus 로고    scopus 로고
    • Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7
    • Torrent, M. et al. Comparison of the membrane interaction mechanism of two antimicrobial RNases: RNase 3/ECP and RNase 7. Biochimica et biophysica acta 1788, 1116-1125 (2009).
    • (2009) Biochimica et Biophysica Acta , vol.1788 , pp. 1116-1125
    • Torrent, M.1
  • 54
    • 0037340434 scopus 로고    scopus 로고
    • Angiogenins: A new class of microbicidal proteins involved in innate immunity
    • Hooper, L. V., Stappenbeck, T. S., Hong, C. V. & Gordon, J. I. Angiogenins: a new class of microbicidal proteins involved in innate immunity. Nature immunology 4, 269-273 (2003).
    • (2003) Nature Immunology , vol.4 , pp. 269-273
    • Hooper, L.V.1    Stappenbeck, T.S.2    Hong, C.V.3    Gordon, J.I.4
  • 55
    • 84895067360 scopus 로고    scopus 로고
    • Role of extracellular RNA in atherosclerotic plaque formation in mice
    • Simsekyilmaz, S. et al. Role of extracellular RNA in atherosclerotic plaque formation in mice. Circulation 129, 598-606 (2014).
    • (2014) Circulation , vol.129 , pp. 598-606
    • Simsekyilmaz, S.1
  • 56
    • 84942995150 scopus 로고    scopus 로고
    • RNase1 as a potential mediator of remote ischaemic preconditioning for cardioprotectiondagger
    • discussion 737
    • Cabrera-Fuentes, H. A. et al. RNase1 as a potential mediator of remote ischaemic preconditioning for cardioprotectiondagger. Eur J Cardiothorac Surg 48, 732-737, discussion 737 (2015).
    • (2015) Eur J Cardiothorac Surg , vol.48 , pp. 732-737
    • Cabrera-Fuentes, H.A.1
  • 57
    • 84914140035 scopus 로고    scopus 로고
    • RNase1 prevents the damaging interplay between extracellular RNA and tumour necrosis factor-alpha in cardiac ischaemia/reperfusion injury
    • Cabrera-Fuentes, H. A. et al. RNase1 prevents the damaging interplay between extracellular RNA and tumour necrosis factor-alpha in cardiac ischaemia/reperfusion injury. Thrombosis and haemostasis 112, 1110-1119 (2014).
    • (2014) Thrombosis and Haemostasis , vol.112 , pp. 1110-1119
    • Cabrera-Fuentes, H.A.1
  • 58
    • 0034061865 scopus 로고    scopus 로고
    • Species-specific binding of human secretory component to SpsA protein of Streptococcus pneumoniae via a hexapeptide motif
    • Hammerschmidt, S., Tillig, M. P., Wolff, S., Vaerman, J. P. & Chhatwal, G. S. Species-specific binding of human secretory component to SpsA protein of Streptococcus pneumoniae via a hexapeptide motif. Molecular microbiology 36, 726-736 (2000).
    • (2000) Molecular Microbiology , vol.36 , pp. 726-736
    • Hammerschmidt, S.1    Tillig, M.P.2    Wolff, S.3    Vaerman, J.P.4    Chhatwal, G.S.5
  • 59
    • 84900513575 scopus 로고    scopus 로고
    • The interaction of enolase-1 with caveolae-associated proteins regulates its subcellular localization
    • Zakrzewicz, D. et al. The interaction of enolase-1 with caveolae-associated proteins regulates its subcellular localization. The Biochemical journal 460, 295-307 (2014).
    • (2014) The Biochemical Journal , vol.460 , pp. 295-307
    • Zakrzewicz, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.