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Volumn 19, Issue 10, 2012, Pages 1045-1053

Structural and Dynamic properties of incomplete immunoglobulin-like fold domains

Author keywords

Adhesins; Immunoglobulin fold; Molecular dynamics; MSCRAMM; Pili

Indexed keywords

ADHESIN; BACTERIAL PROTEIN; COLLAGEN; FIBRINOGEN; IMMUNOGLOBULIN; PROTEIN CAF1; PROTEIN CAF1M; PROTEIN PRKC; UNCLASSIFIED DRUG;

EID: 84867279669     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986612802762732     Document Type: Article
Times cited : (10)

References (32)
  • 2
    • 33746300776 scopus 로고    scopus 로고
    • Protein-protein interaction through betastrand addition
    • Remaut, H.; Waksman, G. Protein-protein interaction through betastrand addition. Trends Biochem. Sci., 2006, 31, 436-444.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 436-444
    • Remaut, H.1    Waksman, G.2
  • 3
    • 0036108484 scopus 로고    scopus 로고
    • 3d domain swapping: As domains continue to swap
    • Liu, Y. Eisenberg, D. 3d domain swapping: As domains continue to swap. Protein Sci., 2002, 11, 1285-1299.
    • (2002) Protein Sci , vol.11 , pp. 1285-1299
    • Liu, Y.1    Eisenberg, D.2
  • 4
    • 33744497267 scopus 로고    scopus 로고
    • Runaway domain swapping in amyloid-like fibrils of t7 endonuclease i
    • Guo, Z.; Eisenberg, D. Runaway domain swapping in amyloid-like fibrils of t7 endonuclease i. Proc. Natl. Acad. Sci. USA, 2006, 103, 8042-8047.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8042-8047
    • Guo, Z.1    Eisenberg, D.2
  • 5
    • 66749095282 scopus 로고    scopus 로고
    • New insight into serpin polymerization and aggregation
    • Huntington, J.A.; Sendall, T.J.; Yamasaki, M. New insight into serpin polymerization and aggregation. Prion, 2009, 3, 12-14.
    • (2009) Prion , vol.3 , pp. 12-14
    • Huntington, J.A.1    Sendall, T.J.2    Yamasaki, M.3
  • 6
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki, M.; Li, W.; Johnson, D.J.; Huntington, J.A. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature, 2008, 455, 1255-1258.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 9
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson, J.S.; Richardson, D.C. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA, 2002, 99, 2754-2759.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 10
    • 50349099883 scopus 로고    scopus 로고
    • Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses
    • De Simone, A.; Esposito, L.; Pedone, C.; Vitagliano, L. Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses. Biophys. J., 2008, 95, 1965-1973.
    • (2008) Biophys. J , vol.95 , pp. 1965-1973
    • De Simone, A.1    Esposito, L.2    Pedone, C.3    Vitagliano, L.4
  • 11
    • 43849090507 scopus 로고    scopus 로고
    • Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations
    • Esposito, L.; Paladino, A.; Pedone, C.; Vitagliano, L. Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations. Biophys. J., 2008, 94, 4031-4040.
    • (2008) Biophys. J , vol.94 , pp. 4031-4040
    • Esposito, L.1    Paladino, A.2    Pedone, C.3    Vitagliano, L.4
  • 12
    • 0028172534 scopus 로고
    • The immunoglobulin fold. Structural classification, sequence patterns and common core
    • Bork, P.; Holm, L.; Sander, C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol., 1994, 242, 309-320.
    • (1994) J. Mol. Biol , vol.242 , pp. 309-320
    • Bork, P.1    Holm, L.2    Sander, C.3
  • 13
    • 0029443827 scopus 로고
    • Cell adhesion molecules 1: Immunoglobulin superfamily
    • Brummendorf, T.; Rathjen, F.G. Cell adhesion molecules 1: Immunoglobulin superfamily. Protein Profile, 1995, 2, 963-1108.
    • (1995) Protein Profile , vol.2 , pp. 963-1108
    • Brummendorf, T.1    Rathjen, F.G.2
  • 16
    • 79952848730 scopus 로고    scopus 로고
    • X-ray structural studies of the entire extracellular region of the serine/threonine kinase prkc from staphylococcus aureus
    • Ruggiero, A.; Squeglia, F.; Marasco, D.; Marchetti, R.; Molinaro, A.; Berisio, R. X-ray structural studies of the entire extracellular region of the serine/threonine kinase prkc from staphylococcus aureus. Biochem. J., 2011, 435, 33-41.
    • (2011) Biochem. J , vol.435 , pp. 33-41
    • Ruggiero, A.1    Squeglia, F.2    Marasco, D.3    Marchetti, R.4    Molinaro, A.5    Berisio, R.6
  • 17
    • 70350211420 scopus 로고    scopus 로고
    • Structural biology of the chaperoneusher pathway of pilus biogenesis
    • Waksman, G.; Hultgren, S.J. Structural biology of the chaperoneusher pathway of pilus biogenesis. Nat. Rev. Microbiol., 2009, 7, 765-774.
    • (2009) Nat. Rev. Microbiol , vol.7 , pp. 765-774
    • Waksman, G.1    Hultgren, S.J.2
  • 18
    • 34250332241 scopus 로고    scopus 로고
    • Fgl chaperone- assembled fimbrial polyadhesins: Anti-immune armament of gram-negative bacterial pathogens
    • Zavialov, A.; Zav'yalova, G.; Korpela, T.; Zav'yalov, V. Fgl chaperone- assembled fimbrial polyadhesins: Anti-immune armament of gram-negative bacterial pathogens. FEMS Microbiol. Rev., 2007, 31, 478-514.
    • (2007) FEMS Microbiol. Rev , vol.31 , pp. 478-514
    • Zavialov, A.1    Zav'Yalova, G.2    Korpela, T.3    Zav'Yalov, V.4
  • 19
    • 77950384104 scopus 로고    scopus 로고
    • Adhesive organelles of gram-negative pathogens assembled with the classical chaperone/usher machinery: Structure and function from a clinical standpoint
    • Zav'yalov, V.; Zavialov, A.; Zav'yalova, G.; Korpela, T. Adhesive organelles of gram-negative pathogens assembled with the classical chaperone/usher machinery: Structure and function from a clinical standpoint. FEMS Microbiol. Rev., 2010, 34, 317-378.
    • (2010) FEMS Microbiol. Rev , vol.34 , pp. 317-378
    • Zav'Yalov, V.1    Zavialov, A.2    Zav'Yalova, G.3    Korpela, T.4
  • 21
    • 33847716307 scopus 로고    scopus 로고
    • A molecular dynamics study of pilus subunits: Insights into pilus biogenesis
    • Vitagliano, L.; Ruggiero, A.; Pedone, C.; Berisio, R. A molecular dynamics study of pilus subunits: Insights into pilus biogenesis. J. Mol. Biol., 2007, 367, 935-941.
    • (2007) J. Mol. Biol , vol.367 , pp. 935-941
    • Vitagliano, L.1    Ruggiero, A.2    Pedone, C.3    Berisio, R.4
  • 22
    • 45449098666 scopus 로고    scopus 로고
    • Conformational states and association mechanism of yersinia pestis caf1 subunits
    • Vitagliano, L.; Ruggiero, A.; Pedone, C.; Berisio, R. Conformational states and association mechanism of yersinia pestis caf1 subunits. Biochem. Biophys. Res. Commun., 2008, 372, 804-810.
    • (2008) Biochem. Biophys. Res. Commun , vol.372 , pp. 804-810
    • Vitagliano, L.1    Ruggiero, A.2    Pedone, C.3    Berisio, R.4
  • 23
    • 63449138207 scopus 로고    scopus 로고
    • Molecular dynamics studies of the p pilus rod subunit papa
    • Vitagliano, L.; Ruggiero, A.; Pedone, C.; Berisio, R. Molecular dynamics studies of the p pilus rod subunit papa. J. Pept. Sci., 2009, 15, 192-199.
    • (2009) J. Pept. Sci , vol.15 , pp. 192-199
    • Vitagliano, L.1    Ruggiero, A.2    Pedone, C.3    Berisio, R.4
  • 24
    • 37349025742 scopus 로고    scopus 로고
    • Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics
    • Rose, R.J.; Welsh, T.S.; Waksman, G.; Ashcroft, A.E.; Radford, S.E.; Paci, E. Donor-strand exchange in chaperone-assisted pilus assembly revealed in atomic detail by molecular dynamics. J. Mol. Biol., 2008, 375, 908-919.
    • (2008) J. Mol. Biol , vol.375 , pp. 908-919
    • Rose, R.J.1    Welsh, T.S.2    Waksman, G.3    Ashcroft, A.E.4    Radford, S.E.5    Paci, E.6
  • 25
    • 33751534447 scopus 로고    scopus 로고
    • Molecular mechanism of p pilus termination in uropathogenic escherichia coli
    • Verger, D.; Miller, E.; Remaut, H.; Waksman, G.; Hultgren, S. Molecular mechanism of p pilus termination in uropathogenic escherichia coli. EMBO Rep., 2006, 7, 1228-1232.
    • (2006) EMBO Rep , vol.7 , pp. 1228-1232
    • Verger, D.1    Miller, E.2    Remaut, H.3    Waksman, G.4    Hultgren, S.5
  • 26
    • 0038820383 scopus 로고    scopus 로고
    • Structure and biogenesis of the capsular f1 antigen from yersinia pestis: Preserved folding energy drives fiber formation
    • Zavialov, A.V.; Berglund, J.; Pudney, A.F.; Fooks, L.J.; Ibrahim, T.M.; MacIntyre, S.; Knight, S.D. Structure and biogenesis of the capsular f1 antigen from yersinia pestis: Preserved folding energy drives fiber formation. Cell, 2003, 113, 587-596.
    • (2003) Cell , vol.113 , pp. 587-596
    • Zavialov, A.V.1    Berglund, J.2    Pudney, A.F.3    Fooks, L.J.4    Ibrahim, T.M.5    MacIntyre, S.6    Knight, S.D.7
  • 27
    • 0027960065 scopus 로고
    • Mscrammmediated adherence of microorganisms to host tissues
    • Patti, J.M.; Allen, B.L.; McGavin, M.J.; Hook, M. Mscrammmediated adherence of microorganisms to host tissues. Annu. Rev. Microbiol., 1994, 48, 585-617.
    • (1994) Annu. Rev. Microbiol , vol.48 , pp. 585-617
    • Patti, J.M.1    Allen, B.L.2    McGavin, M.J.3    Hook, M.4
  • 28
    • 16644375299 scopus 로고    scopus 로고
    • Mscramm-targeted vaccines and immunotherapy for staphylococcal infection
    • Rivas, J.M.; Speziale, P.; Patti, J.M.; Hook, M. Mscramm-targeted vaccines and immunotherapy for staphylococcal infection. Curr. Opin. Drug Discov. Devel., 2004, 7, 223-227.
    • (2004) Curr. Opin. Drug Discov. Devel , vol.7 , pp. 223-227
    • Rivas, J.M.1    Speziale, P.2    Patti, J.M.3    Hook, M.4
  • 30
    • 57149093798 scopus 로고    scopus 로고
    • A structural model of the staphylococcus aureus clfa-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics
    • Ganesh, V.K.; Rivera, J.J.; Smeds, E.; Ko, Y.P.; Bowden, M.G.; Wann, E.R.; Gurusiddappa, S.; Fitzgerald, J.R.; Hook, M. A structural model of the staphylococcus aureus clfa-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. PLoS Pathog., 2008, 4, e1000226.
    • (2008) PLoS Pathog , vol.4
    • Ganesh, V.K.1    Rivera, J.J.2    Smeds, E.3    Ko, Y.P.4    Bowden, M.G.5    Wann, E.R.6    Gurusiddappa, S.7    Fitzgerald, J.R.8    Hook, M.9
  • 31
    • 38049166003 scopus 로고    scopus 로고
    • Evidence for the dock, lock, and latch ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (mscramm) sdrg
    • Bowden, M.G.; Heuck, A.P.; Ponnuraj, K.; Kolosova, E.; Choe, D.; Gurusiddappa, S.; Narayana, S.V.; Johnson, A.E.; Hook, M. Evidence for the dock, lock, and latch ligand binding mechanism of the staphylococcal microbial surface component recognizing adhesive matrix molecules (mscramm) sdrg. J. Biol. Chem., 2008, 283, 638-647.
    • (2008) J. Biol. Chem , vol.283 , pp. 638-647
    • Bowden, M.G.1    Heuck, A.P.2    Ponnuraj, K.3    Kolosova, E.4    Choe, D.5    Gurusiddappa, S.6    Narayana, S.V.7    Johnson, A.E.8    Hook, M.9
  • 32
    • 79959717409 scopus 로고    scopus 로고
    • Role of hydration in collagen recognition by bacterial adhesins
    • Vitagliano, L.; Berisio, R.; De Simone, A. Role of hydration in collagen recognition by bacterial adhesins. Biophys. J., 2011, 100, 2253-2261.
    • (2011) Biophys. J , vol.100 , pp. 2253-2261
    • Vitagliano, L.1    Berisio, R.2    De Simone, A.3


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