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Volumn 122, Issue 10, 2012, Pages 3665-3677

Cytokeratins mediate epithelial innate defense through their antimicrobial properties

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CARBOXY TERMINAL TELOPEPTIDE; CYTOKERATIN; CYTOKERATIN 6; CYTOKERATIN 6A; GLYCINE; GLYCINE RICH C TERMINAL FRAGMENT; KERATIN DERIVED ANTIMICROBIAL PEPTIDE; POLYPEPTIDE ANTIBIOTIC AGENT; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

EID: 84867186262     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI64416     Document Type: Article
Times cited : (76)

References (64)
  • 3
    • 33846827092 scopus 로고    scopus 로고
    • Sensing of bacteria: NOD a lonely job
    • DOI 10.1016/j.mib.2006.11.003, PII S1369527406001846
    • Kufer TA, Sansonetti PJ. Sensing of bacteria: NOD a lonely job. Curr Opin Microbiol. 2007;10(1):62-69. (Pubitemid 46216870)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.1 , pp. 62-69
    • Kufer, T.A.1    Sansonetti, P.J.2
  • 4
    • 77956025260 scopus 로고    scopus 로고
    • New insights into the regulation of signalling by toll-like receptors and nod-like receptors
    • Coll RC, O'Neill LA. New insights into the regulation of signalling by toll-like receptors and nod-like receptors. J Innate Immun. 2010;2(5):406-421.
    • (2010) J Innate Immun , vol.2 , Issue.5 , pp. 406-421
    • Coll, R.C.1    O'Neill, L.A.2
  • 5
    • 78149233514 scopus 로고    scopus 로고
    • The innate immune system in the intestine
    • Uematsu S, Fujimoto K. The innate immune system in the intestine. Microbiol Immunol. 2010; 54(11):645-657.
    • (2010) Microbiol Immunol , vol.54 , Issue.11 , pp. 645-657
    • Uematsu, S.1    Fujimoto, K.2
  • 6
    • 3142654210 scopus 로고    scopus 로고
    • Inferences, questions and possibilities in Toll-like receptor signalling
    • DOI 10.1038/nature02761
    • Beutler B. Inferences, questions and possibilities in Toll-like receptor signalling. Nature. 2004; 430(6996):257-263. (Pubitemid 38902439)
    • (2004) Nature , vol.430 , Issue.6996 , pp. 257-263
    • Beutler, B.1
  • 7
    • 58049193003 scopus 로고    scopus 로고
    • Microbe sensing, positive feedback loops, and the pathogenesis of inflammatory diseases
    • Beutler B. Microbe sensing, positive feedback loops, and the pathogenesis of inflammatory diseases. Immunol Rev. 2009;227(1):248-263.
    • (2009) Immunol Rev , vol.227 , Issue.1 , pp. 248-263
    • Beutler, B.1
  • 8
    • 42449118192 scopus 로고    scopus 로고
    • The incidence of contact lens-related microbial keratitis in Australia
    • Stapleton F, et al. The incidence of contact lens-related microbial keratitis in Australia. Ophthalmology. 2008;115(10):1655-1662.
    • (2008) Ophthalmology , vol.115 , Issue.10 , pp. 1655-1662
    • Stapleton, F.1
  • 10
    • 66549087843 scopus 로고    scopus 로고
    • Clearance of Pseudomonas aeruginosa from a healthy ocular surface involves surfactant protein D and is compromised by bacterial elastase in a murine null-infection model
    • Mun JJ, et al. Clearance of Pseudomonas aeruginosa from a healthy ocular surface involves surfactant protein D and is compromised by bacterial elastase in a murine null-infection model. Infect Immun. 2009;77(6):2392-2398.
    • (2009) Infect Immun , vol.77 , Issue.6 , pp. 2392-2398
    • Mun, J.J.1
  • 11
    • 0019509645 scopus 로고
    • Adherence of Pseudomonas aeruginosa to the injured cornea: A step in the pathogenesis of corneal infections
    • Ramphal R, McNiece MT, Polack FM. Adherence of Pseudomonas aeruginosa to the injured cornea: a step in the pathogenesis of corneal infections. Ann Ophthalmol. 1981;13(4):421-425. (Pubitemid 11073101)
    • (1981) Annals of Ophthalmology , vol.13 , Issue.4 , pp. 421-425
    • Ramphal, R.1    McNiece, M.T.2    Polack, F.M.3
  • 12
    • 79251524878 scopus 로고    scopus 로고
    • Role of defensins in corneal epithelial barrier function against Pseudomonas aeruginosa traversal
    • Augustin DK, et al. Role of defensins in corneal epithelial barrier function against Pseudomonas aeruginosa traversal. Infect Immun. 2011;79(2):595-605.
    • (2011) Infect Immun , vol.79 , Issue.2 , pp. 595-605
    • Augustin, D.K.1
  • 13
    • 58149103363 scopus 로고    scopus 로고
    • The role of antimicrobial peptides at the ocular surface
    • McDermott AM. The role of antimicrobial peptides at the ocular surface. Ophthalmic Res. 2009;41(2):60-75.
    • (2009) Ophthalmic Res , vol.41 , Issue.2 , pp. 60-75
    • McDermott, A.M.1
  • 14
    • 84857768770 scopus 로고    scopus 로고
    • Antimicrobial peptides in gastrointestinal inflammation
    • Jager S, Stange EF, Wehkamp J. Antimicrobial peptides in gastrointestinal inflammation. Int J Inflam. 2010;2010:910283.
    • (2010) Int J Inflam , vol.2010 , pp. 910283
    • Jager, S.1    Stange, E.F.2    Wehkamp, J.3
  • 16
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 2002;415(6870):389-395. (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 17
    • 26844575542 scopus 로고    scopus 로고
    • A dataset of human cornea proteins identified by peptide mass fingerprinting and tandem mass spectrometry
    • DOI 10.1074/mcp.D500003-MCP200
    • Karring H, Thogersen IB, Klintworth GK, Moller-Pedersen T, Enghild JJ. A dataset of human cornea proteins identified by Peptide mass fingerprinting and tandem mass spectrometry. Mol Cell Proteomics. 2005;4(9):1406-1408. (Pubitemid 41448726)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1406-1408
    • Karring, H.1    Thogersen, I.B.2    Klintworth, G.K.3    Moller-Pedersen, T.4    Enghild, J.J.5
  • 18
    • 78049266859 scopus 로고    scopus 로고
    • Correlation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides
    • Leptihn S, Har JY, Wohland T, Ding JL. Correlation of charge, hydrophobicity, and structure with antimicrobial activity of S1 and MIRIAM peptides. Biochemistry. 2010;49(43):9161-9170.
    • (2010) Biochemistry , vol.49 , Issue.43 , pp. 9161-9170
    • Leptihn, S.1    Har, J.Y.2    Wohland, T.3    Ding, J.L.4
  • 19
    • 51749085388 scopus 로고    scopus 로고
    • HELIQUEST: A web server to screen sequences with specific alpha-helical properties
    • Gautier R, Douguet D, Antonny B, Drin G. HELIQUEST: a web server to screen sequences with specific alpha-helical properties. Bioinformatics. 2008;24(18):2101-2102.
    • (2008) Bioinformatics , vol.24 , Issue.18 , pp. 2101-2102
    • Gautier, R.1    Douguet, D.2    Antonny, B.3    Drin, G.4
  • 20
    • 68949213019 scopus 로고    scopus 로고
    • A generic method for assignment of reliability scores applied to solvent accessibility predictions
    • Petersen B, Petersen TN, Andersen P, Nielsen M, Lundegaard C. A generic method for assignment of reliability scores applied to solvent accessibility predictions. BMC Struct Biol. 2009;9:51.
    • (2009) BMC Struct Biol , vol.9 , pp. 51
    • Petersen, B.1    Petersen, T.N.2    Andersen, P.3    Nielsen, M.4    Lundegaard, C.5
  • 21
    • 0000207681 scopus 로고
    • TMBASE - A database of membrane spanning protein segments
    • Hofmann K, Stoffel W. TMBASE - A database of membrane spanning protein segments. Biol Chem Hoppe-Seyler. 1993;374:166.
    • (1993) Biol Chem Hoppe-Seyler , vol.374 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 23
    • 77952626078 scopus 로고    scopus 로고
    • Novel synthetic, salt-resistant analogs of human beta-defensins 1 and 3 endowed with enhanced antimicrobial activity
    • Scudiero O, et al. Novel synthetic, salt-resistant analogs of human beta-defensins 1 and 3 endowed with enhanced antimicrobial activity. Antimicrob Agents Chemother. 2010;54(6):2312-2322.
    • (2010) Antimicrob Agents Chemother , vol.54 , Issue.6 , pp. 2312-2322
    • Scudiero, O.1
  • 25
    • 77951216438 scopus 로고    scopus 로고
    • Peptide fragments of a beta-defensin derivative with potent bactericidal activity
    • Reynolds NL, et al. Peptide fragments of a beta-defensin derivative with potent bactericidal activity. Antimicrob Agents Chemother. 2010;54(5):1922-1929.
    • (2010) Antimicrob Agents Chemother , vol.54 , Issue.5 , pp. 1922-1929
    • Reynolds, N.L.1
  • 26
    • 82955163216 scopus 로고    scopus 로고
    • Antimicrobial and antibiofilm activity of LL-37 and its truncated variants against Burkholderia pseudomallei
    • Kanthawong S, et al. Antimicrobial and antibiofilm activity of LL-37 and its truncated variants against Burkholderia pseudomallei. Int J Antimicrob Agents. 2012;39(1):39-44.
    • (2012) Int J Antimicrob Agents , vol.39 , Issue.1 , pp. 39-44
    • Kanthawong, S.1
  • 27
    • 0028289692 scopus 로고
    • The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core
    • Coyne MJ Jr, Russell KS, Coyle CL, Goldberg JB. The Pseudomonas aeruginosa algC gene encodes phosphoglucomutase, required for the synthesis of a complete lipopolysaccharide core. J Bacteriol. 1994; 176(12):3500-3507. (Pubitemid 24189649)
    • (1994) Journal of Bacteriology , vol.176 , Issue.12 , pp. 3500-3507
    • Coyne Jr., M.J.1    Russell, K.S.2    Coyle, C.L.3    Goldberg, J.B.4
  • 29
    • 34548041437 scopus 로고    scopus 로고
    • Analysis of the kinetics of folding of proteins and peptides using circular dichroism
    • Greenfield NJ. Analysis of the kinetics of folding of proteins and peptides using circular dichroism. Nat Protoc. 2006;1(6):2891-2899.
    • (2006) Nat Protoc , vol.1 , Issue.6 , pp. 2891-2899
    • Greenfield, N.J.1
  • 30
    • 58149187882 scopus 로고    scopus 로고
    • APD2: The updated antimicrobial peptide database and its application in peptide design
    • Wang G, Li X, Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 2009;37(Database issue):D933-D937.
    • (2009) Nucleic Acids Res , vol.37 , Issue.DATABASE ISSUE
    • Wang, G.1    Li, X.2    Wang, Z.3
  • 31
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • DOI 10.1124/pr.55.1.2
    • Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev. 2003;55(1):27-55. (Pubitemid 36268398)
    • (2003) Pharmacological Reviews , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 32
    • 0036467968 scopus 로고    scopus 로고
    • Inhibition of intracellular macromolecular synthesis in Staphylococcus aureus by thrombin-induced platelet microbicidal proteins
    • DOI 10.1086/338514
    • Xiong YQ, Bayer AS, Yeaman MR. Inhibition of intracellular macromolecular synthesis in Staphylococcus aureus by thrombin-induced platelet microbicidal proteins. J Infect Dis. 2002;185(3):348-356. (Pubitemid 34107248)
    • (2002) Journal of Infectious Diseases , vol.185 , Issue.3 , pp. 348-356
    • Xiong, Y.-Q.1    Bayer, A.S.2    Yeaman, M.R.3
  • 34
    • 0032719739 scopus 로고    scopus 로고
    • Structural features of helical antimicrobial peptides: Their potential to modulate activity on model membranes and biological cells
    • Dathe M, Wieprecht T. Structural features of helical antimicrobial peptides: their potential to modulate activity on model membranes and biological cells. Biochim Biophys Acta. 1999;1462(1-2):71-87.
    • (1999) Biochim Biophys Acta , vol.1462 , Issue.1-2 , pp. 71-87
    • Dathe, M.1    Wieprecht, T.2
  • 35
    • 0029069628 scopus 로고
    • Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides
    • Pathak N, et al. Comparison of the effects of hydrophobicity, amphiphilicity, and alpha-helicity on the activities of antimicrobial peptides. Proteins. 1995;22(2):182-186.
    • (1995) Proteins , vol.22 , Issue.2 , pp. 182-186
    • Pathak, N.1
  • 36
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • DOI 10.1038/nrmicro1098
    • Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol. 2005;3(3):238-250. (Pubitemid 40298223)
    • (2005) Nature Reviews Microbiology , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 37
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • DOI 10.1016/S0140-6736(97)80051-7
    • Hancock RE. Peptide antibiotics. Lancet. 1997; 349(9049):418-422. (Pubitemid 27077684)
    • (1997) Lancet , vol.349 , Issue.9049 , pp. 418-422
    • Hancock, R.E.W.1
  • 38
    • 79960782055 scopus 로고    scopus 로고
    • Antibiotic activities of host defense peptides: More to it than lipid bilayer perturbation
    • Wilmes M, Cammue BP, Sahl HG, Thevissen K. Antibiotic activities of host defense peptides: more to it than lipid bilayer perturbation. Nat Prod Rep. 2011;28(8):1350-1358.
    • (2011) Nat Prod Rep , vol.28 , Issue.8 , pp. 1350-1358
    • Wilmes, M.1    Cammue, B.P.2    Sahl, H.G.3    Thevissen, K.4
  • 41
    • 34548418612 scopus 로고    scopus 로고
    • Structure-activity study of the antibacterial peptide fallaxin
    • DOI 10.1110/ps.072966007
    • Nielsen SL, Frimodt-Moller N, Kragelund BB, Hansen PR. Structure-activity study of the antibacterial peptide fallaxin. Protein Sci. 2007;16(9):1969-1976. (Pubitemid 47367120)
    • (2007) Protein Science , vol.16 , Issue.9 , pp. 1969-1976
    • Nielsen, S.L.1    Frimodt-Moller, N.2    Kragelund, B.B.3    Hansen, P.R.4
  • 42
    • 79960690273 scopus 로고    scopus 로고
    • Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin, and maculatin
    • Chia CS, Gong Y, Bowie JH, Zuegg J, Cooper MA. Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin, and maculatin. Biopolymers. 2011;96(2):147-157.
    • (2011) Biopolymers , vol.96 , Issue.2 , pp. 147-157
    • Chia, C.S.1    Gong, Y.2    Bowie, J.H.3    Zuegg, J.4    Cooper, M.A.5
  • 43
    • 0023735907 scopus 로고
    • Synthetic magainin analogues with improved antimicrobial activity
    • Chen HC, Brown JH, Morell JL, Huang CM. Synthetic magainin analogues with improved antimicrobial activity. FEBS Lett. 1988;236(2):462-466.
    • (1988) FEBS Lett , vol.236 , Issue.2 , pp. 462-466
    • Chen, H.C.1    Brown, J.H.2    Morell, J.L.3    Huang, C.M.4
  • 44
    • 33344463202 scopus 로고    scopus 로고
    • Independent expansion of the keratin gene family in teleostean fish and mammals: An insight from phylogenetic analysis and radiation hybrid mapping of keratin genes in zebrafish
    • DOI 10.1016/j.gene.2005.09.016, PII S0378111905005974
    • Krushna Padhi B, Akimenko MA, Ekker M. Independent expansion of the keratin gene family in teleostean fish and mammals: an insight from phylogenetic analysis and radiation hybrid mapping of keratin genes in zebrafish. Gene. 2006;368:37-45. (Pubitemid 43290140)
    • (2006) Gene , vol.368 , Issue.1-2 , pp. 37-45
    • Krushna, P.B.1    Akimenko, M.-A.2    Ekker, M.3
  • 45
    • 78651397689 scopus 로고    scopus 로고
    • Keratins in health and cancer: More than mere epithelial cell markers
    • Karantza V. Keratins in health and cancer: more than mere epithelial cell markers. Oncogene. 2011; 30(2):127-138.
    • (2011) Oncogene , vol.30 , Issue.2 , pp. 127-138
    • Karantza, V.1
  • 46
    • 44149099717 scopus 로고    scopus 로고
    • The human keratins: Biology and pathology
    • Moll R, Divo M, Langbein L. The human keratins: biology and pathology. Histochem Cell Biol. 2008;129(6):705-733.
    • (2008) Histochem Cell Biol , vol.129 , Issue.6 , pp. 705-733
    • Moll, R.1    Divo, M.2    Langbein, L.3
  • 47
    • 34347232319 scopus 로고    scopus 로고
    • Wound re-epithelialization: Modulating keratinocyte migration in wound healing
    • Sivamani RK, Garcia MS, Isseroff RR. Wound re-epithelialization: modulating keratinocyte migration in wound healing. Front Biosci. 2007; 12:2849-2868.
    • (2007) Front Biosci , vol.12 , pp. 2849-2868
    • Sivamani, R.K.1    Garcia, M.S.2    Isseroff, R.R.3
  • 48
    • 41649084938 scopus 로고    scopus 로고
    • First evidence of the pore-forming properties of a keratin from skin mucus of rainbow trout (Oncorhynchus mykiss, formerly Salmo gairdneri)
    • DOI 10.1042/BJ20070801
    • Molle V, et al. First evidence of the pore-forming properties of a keratin from skin mucus of rainbow trout (Oncorhynchus mykiss, formerly Salmo gairdneri). Biochem J. 2008;411(1):33-40. (Pubitemid 351482344)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 33-40
    • Molle, V.1    Campagna, S.2    Bessin, Y.3    Ebran, N.4    Saint, N.5    Molle, G.6
  • 49
    • 21244442629 scopus 로고    scopus 로고
    • Transcriptional response of bronchial epithelial cells to Pseudomonas aeruginosa: Identification of early mediators of host defense
    • DOI 10.1152/physiolgenomics.00289.2004
    • Vos JB, et al. Transcriptional response of bronchial epithelial cells to Pseudomonas aeruginosa: identification of early mediators of host defense. Physiol Genomics. 2005;21(3):324-336. (Pubitemid 40898492)
    • (2005) Physiological Genomics , vol.21 , pp. 324-336
    • Vos, J.B.1    Van Sterkenburg, M.A.2    Rabe, K.F.3    Schalkwijk, J.4    Hiemstra, P.S.5    Datson, N.A.6
  • 50
    • 0242654921 scopus 로고    scopus 로고
    • Defense mechanisms of urinary bladder: Studies on antimicrobial polypeptides from bladder mucosa
    • Qi W, Boyao W. Defense mechanisms of urinary bladder: studies on antimicrobial polypeptides from bladder mucosa. Chin Med Sci J. 1999;14(1):17-22.
    • (1999) Chin Med Sci J , vol.14 , Issue.1 , pp. 17-22
    • Qi, W.1    Boyao, W.2
  • 51
    • 77954362765 scopus 로고    scopus 로고
    • The keratin-filament cycle of assembly and disassembly
    • Kolsch A, Windoffer R, Wurflinger T, Aach T, Leube RE. The keratin-filament cycle of assembly and disassembly. J Cell Sci. 2010;123(pt 13):2266-2272.
    • (2010) J Cell Sci , vol.123 , Issue.PART 13 , pp. 2266-2272
    • Kolsch, A.1    Windoffer, R.2    Wurflinger, T.3    Aach, T.4    Leube, R.E.5
  • 52
    • 0032234101 scopus 로고    scopus 로고
    • The wound repair-associated keratins 6, 16, and 17. Insights into the role of intermediate filaments in specifying keratinocyte cytoarchitecture
    • McGowan K, Coulombe PA. The wound repair-associated keratins 6, 16, and 17. Insights into the role of intermediate filaments in specifying keratinocyte cytoarchitecture. Subcell Biochem. 1998;31:173-204.
    • (1998) Subcell Biochem , vol.31 , pp. 173-204
    • McGowan, K.1    Coulombe, P.A.2
  • 53
    • 12344276291 scopus 로고    scopus 로고
    • Great promises yet to be fulfilled: Defining keratin intermediate filament function in vivo
    • DOI 10.1078/0171-9335-00443
    • Coulombe PA, Tong X, Mazzalupo S, Wang Z, Wong P. Great promises yet to be fulfilled: defining keratin intermediate filament function in vivo. Eur J Cell Biol. 2004;83(11-12):735-746. (Pubitemid 40123838)
    • (2004) European Journal of Cell Biology , vol.83 , Issue.11-12 , pp. 735-746
    • Coulombe, P.A.1    Tong, X.2    Mazzalupo, S.3    Wang, Z.4    Wong, P.5
  • 54
    • 7944229258 scopus 로고    scopus 로고
    • Keratin mutations and intestinal pathology
    • DOI 10.1002/path.1646
    • Owens DW, Lane EB. Keratin mutations and intestinal pathology. J Pathol. 2004;204(4):377-385. (Pubitemid 39468149)
    • (2004) Journal of Pathology , vol.204 , Issue.4 , pp. 377-385
    • Owens, D.W.1    Lane, E.B.2
  • 55
    • 54449101873 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-mediated degradation of keratin intermediate filaments in mechanically stimulated A549 cells
    • Jaitovich A, et al. Ubiquitin-proteasome-mediated degradation of keratin intermediate filaments in mechanically stimulated A549 cells. J Biol Chem. 2008;283(37):25348-25355.
    • (2008) J Biol Chem , vol.283 , Issue.37 , pp. 25348-25355
    • Jaitovich, A.1
  • 56
    • 77953264742 scopus 로고    scopus 로고
    • The role of the ubiquitin proteasome pathway in keratin intermediate filament protein degradation
    • Rogel MR, Jaitovich A, Ridge KM. The role of the ubiquitin proteasome pathway in keratin intermediate filament protein degradation. Proc Am Thorac Soc. 2010;7(1):71-76.
    • (2010) Proc Am Thorac Soc , vol.7 , Issue.1 , pp. 71-76
    • Rogel, M.R.1    Jaitovich, A.2    Ridge, K.M.3
  • 57
    • 84855398969 scopus 로고    scopus 로고
    • Rapid degradation of cyclooxygenase-1 and hematopoietic prostaglandin D synthase through ubiquitin-proteasome system in response to intracellular calcium level
    • Yazaki M, Kashiwagi K, Aritake K, Urade Y, Fujimori K. Rapid degradation of cyclooxygenase-1 and hematopoietic prostaglandin D synthase through ubiquitin-proteasome system in response to intracellular calcium level. Mol Biol Cell. 2012; 23(1):12-21.
    • (2012) Mol Biol Cell , vol.23 , Issue.1 , pp. 12-21
    • Yazaki, M.1    Kashiwagi, K.2    Aritake, K.3    Urade, Y.4    Fujimori, K.5
  • 58
    • 0023860482 scopus 로고
    • Purification and characterization of calpains from pig epidermis and their action on epidermal keratin
    • Ando Y, Miyachi Y, Imamura S, Kannagi R, Murachi T. Purification and characterization of calpains from pig epidermis and their action on epidermal keratin. J Invest Dermatol. 1988;90(1):26-30.
    • (1988) J Invest Dermatol , vol.90 , Issue.1 , pp. 26-30
    • Ando, Y.1    Miyachi, Y.2    Imamura, S.3    Kannagi, R.4    Murachi, T.5
  • 59
    • 0031743844 scopus 로고    scopus 로고
    • Degradation of cytokeratin intermediate filaments by calcium-activated proteases (calpains) in vitro: Implications for formation of Mallory bodies
    • Makowski GS, Ramsby ML. Degradation of cytokeratin intermediate filaments by calcium-activated proteases (calpains) in vitro: implications for formation of Mallory bodies. Res Commun Mol Pathol Pharmacol. 1998;101(3):211-223.
    • (1998) Res Commun Mol Pathol Pharmacol , vol.101 , Issue.3 , pp. 211-223
    • Makowski, G.S.1    Ramsby, M.L.2
  • 60
    • 0027300468 scopus 로고
    • Immunochemical localization of calpins and calpastatin in the rabbit eye
    • DOI 10.1016/0006-8993(93)90513-M
    • Persson H, Kawashima S, Karlsson JO. Immunohistochemical localization of calpains and calpastatin in the rabbit eye. Brain Res. 1993;611(2):272-278. (Pubitemid 23159695)
    • (1993) Brain Research , vol.611 , Issue.2 , pp. 272-278
    • Persson, H.1    Kawashima, S.2    Karlsson, J.-O.3
  • 61
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, MacCormak AL, Yates JR 3rd. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 1994;5(11):976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , Issue.11 , pp. 976-989
    • Eng, J.K.1    MacCormak, A.L.2    Yates III, J.R.3
  • 62
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR 3rd. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res. 2002;1(1):21-26.
    • (2002) J Proteome Res , vol.1 , Issue.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates III, J.R.3
  • 63
    • 80052067647 scopus 로고    scopus 로고
    • 3D quantitative imaging of unprocessed live tissue reveals epithelial defense against bacterial adhesion and subsequent traversal requires MyD88
    • Tam C, et al. 3D quantitative imaging of unprocessed live tissue reveals epithelial defense against bacterial adhesion and subsequent traversal requires MyD88. PLoS One. 2011;6(8):e24008.
    • (2011) PLoS One , vol.6 , Issue.8
    • Tam, C.1
  • 64
    • 0020587021 scopus 로고
    • Structure of the core oligosaccharide from the lipopolysaccharide of Pseudomonas aeruginosa PAC1R and its defective mutants
    • Rowe PS, Meadow PM. Structure of the core oligosaccharide from the lipopolysaccharide of Pseudomonas aeruginosa PAC1R and its defective mutants. Eur J Biochem. 1983;132(2):329-337. (Pubitemid 13093431)
    • (1983) European Journal of Biochemistry , vol.132 , Issue.2 , pp. 329-337
    • Rowe, P.S.N.1    Meadow, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.