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Volumn 18, Issue 6, 2012, Pages 782-788

Peptides in oral diseases

Author keywords

Antimicrobial peptides; Bacterial competence stimulating peptides; Cytokeratin peptides; Desmoglein 3 peptide; Oral infectious diseases; Oral squamous cell carcinomas; Pemphigus vulgaris

Indexed keywords

ADRENOMEDULLIN; BETA DEFENSIN; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; DESMOGLEIN 3; HISTATIN; POLYPEPTIDE ANTIBIOTIC AGENT;

EID: 84856458477     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/138161212799277842     Document Type: Article
Times cited : (7)

References (129)
  • 1
    • 79952065856 scopus 로고    scopus 로고
    • The role of bacteria in the caries process: Ecological perspectives
    • Takahashi N, Nyvad B. The role of bacteria in the caries process: ecological perspectives. J Dent Res 2011; 90: 294-303.
    • (2011) J Dent Res , vol.90 , pp. 294-303
    • Takahashi, N.1    Nyvad, B.2
  • 2
    • 77749237147 scopus 로고    scopus 로고
    • Changing concepts in caries microbiology
    • Russell RR. Changing concepts in caries microbiology. Am J Dent 2009; 22: 304-10.
    • (2009) Am J Dent , vol.22 , pp. 304-310
    • Russell, R.R.1
  • 3
    • 84861773841 scopus 로고    scopus 로고
    • Metagenomic analysis of the peri-implant and periodontal microflora in patients with clinical signs of gingivitis or mucositis
    • doi 10.1007/s00784-011-0561-8
    • Heuer W, Kettenring A, Stumpp SN, et al. Metagenomic analysis of the peri-implant and periodontal microflora in patients with clinical signs of gingivitis or mucositis. Clin Oral Investig Forthcoming 2011; doi 10.1007/s00784-011-0561-8.
    • (2011) Clin Oral Investig Forthcoming
    • Heuer, W.1    Kettenring, A.2    Stumpp, S.N.3
  • 4
    • 79958280944 scopus 로고    scopus 로고
    • Microbial shifts during dental biofilm re-development in the absence of oral hygiene in periodontal health and disease
    • Uzel NG, Teles FR, Teles RP, et al. Microbial shifts during dental biofilm re-development in the absence of oral hygiene in periodontal health and disease. J Clin Periodontol 2011; 38: 612-20.
    • (2011) J Clin Periodontol , vol.38 , pp. 612-620
    • Uzel, N.G.1    Teles, F.R.2    Teles, R.P.3
  • 5
    • 79951878895 scopus 로고    scopus 로고
    • Periodontal microbial complexes associated with specific cell and tissue responses
    • Kebschull M, Papapanou PN. Periodontal microbial complexes associated with specific cell and tissue responses. J Clin Periodontol 2011; 38: 17-27.
    • (2011) J Clin Periodontol , vol.38 , pp. 17-27
    • Kebschull, M.1    Papapanou, P.N.2
  • 7
    • 78649612848 scopus 로고    scopus 로고
    • Effects of Porphyromonas gingivalis infection on human gingival epithelial barrier function in vitro
    • Groeger S, Doman E, Chakraborty T, Meyle J. Effects of Porphyromonas gingivalis infection on human gingival epithelial barrier function in vitro. Eur J Oral Sci 2010; 118: 582-9.
    • (2010) Eur J Oral Sci , vol.118 , pp. 582-589
    • Groeger, S.1    Doman, E.2    Chakraborty, T.3    Meyle, J.4
  • 8
    • 78650186254 scopus 로고    scopus 로고
    • Oral biofilms: A reservoir of transferable, bacterial, antimicrobial resistance
    • Roberts AP, Mullany P. Oral biofilms: a reservoir of transferable, bacterial, antimicrobial resistance. Expert Rev Anti Infect Ther 2010; 8: 1441-50.
    • (2010) Expert Rev Anti Infect Ther , vol.8 , pp. 1441-1450
    • Roberts, A.P.1    Mullany, P.2
  • 10
    • 0033950176 scopus 로고    scopus 로고
    • Isolation and identification of Candida from the oral cavity
    • Williams DW, Lewis MA. Isolation and identification of Candida from the oral cavity. Oral Dis 2000; 6: 3-11.
    • (2000) Oral Dis , vol.6 , pp. 3-11
    • Williams, D.W.1    Lewis, M.A.2
  • 11
    • 77953792758 scopus 로고    scopus 로고
    • The screening of viral risk factors in tongue and pharyngolaryngeal squamous carcinoma
    • Zheng Y, Xia P, Zheng HC, Takahashi H, Masuda S, Takano Y. The screening of viral risk factors in tongue and pharyngolaryngeal squamous carcinoma. Anticancer Res 2010; 30: 1233-8.
    • (2010) Anticancer Res , vol.30 , pp. 1233-1238
    • Zheng, Y.1    Xia, P.2    Zheng, H.C.3    Takahashi, H.4    Masuda, S.5    Takano, Y.6
  • 12
    • 77955282693 scopus 로고    scopus 로고
    • HPV-associated head and neck cancer: A virus-related cancer epidemic
    • Marur S, D'Souza G, Westra WH, Forastiere AA. HPV-associated head and neck cancer: a virus-related cancer epidemic. Lancet Oncol 2010; 11: 781-9.
    • (2010) Lancet Oncol , vol.11 , pp. 781-789
    • Marur, S.1    D'Souza, G.2    Westra, W.H.3    Forastiere, A.A.4
  • 13
    • 77953609069 scopus 로고    scopus 로고
    • Relevance of human papilloma virus (HPV) infection to carcinogenesis of oral tongue cancer
    • Lee SY, Cho NH, Choi EC, et al. Relevance of human papilloma virus (HPV) infection to carcinogenesis of oral tongue cancer. Int J Oral Maxillofac Surg 2010; 39: 678-83.
    • (2010) Int J Oral Maxillofac Surg , vol.39 , pp. 678-683
    • Lee, S.Y.1    Cho, N.H.2    Choi, E.C.3
  • 14
    • 77952743400 scopus 로고    scopus 로고
    • Infectious and dietary risk factors of oral cancer
    • Meurman JH. Infectious and dietary risk factors of oral cancer. Oral Oncol 2010; 46: 411-13.
    • (2010) Oral Oncol , vol.46 , pp. 411-413
    • Meurman, J.H.1
  • 15
    • 84861594755 scopus 로고    scopus 로고
    • Revisiting the association between candidal infection and carcinoma, particularly oral squamous cell carcinoma
    • Bakri MM, Hussaini MH, Holmes RA, Cannon DR, Rich MA. Revisiting the association between candidal infection and carcinoma, particularly oral squamous cell carcinoma. J Oral Microbiol 2010; 21: 2.
    • (2010) J Oral Microbiol , vol.21 , pp. 2
    • Bakri, M.M.1    Hussaini, M.H.2    Holmes, R.A.3    Cannon, D.R.4    Rich, M.A.5
  • 16
    • 0030838115 scopus 로고    scopus 로고
    • Hepatitis C virus infection and lichen planus: A short review
    • Lodi G, Porter SR. Hepatitis C virus infection and lichen planus: a short review. Oral Dis 1997; 3: 77-81.
    • (1997) Oral Dis , vol.3 , pp. 77-81
    • Lodi, G.1    Porter, S.R.2
  • 17
    • 0030897029 scopus 로고    scopus 로고
    • The role of heat shock protein, microbial and autoimmune agents in the aetiology of Behçet's disease
    • Lehner T. The role of heat shock protein, microbial and autoimmune agents in the aetiology of Behçet's disease. Int Rev Immunol 1997; 14: 21-32.
    • (1997) Int Rev Immunol , vol.14 , pp. 21-32
    • Lehner, T.1
  • 20
    • 51549090562 scopus 로고    scopus 로고
    • Emergency department visits for antibiotic-associated adverse events
    • Shehab N, Patel PR, Srinivasan A, Budnitz DS. Emergency department visits for antibiotic-associated adverse events. Clin Infect Dis 2008; 47: 735-43.
    • (2008) Clin Infect Dis , vol.47 , pp. 735-743
    • Shehab, N.1    Patel, P.R.2    Srinivasan, A.3    Budnitz, D.S.4
  • 21
    • 0027448985 scopus 로고
    • A review of the adverse events profile of cefpirome
    • Rubinstein E, Labs R, Reeves A. A review of the adverse events profile of cefpirome. Drug Saf 1993; 9: 340-5.
    • (1993) Drug Saf , vol.9 , pp. 340-345
    • Rubinstein, E.1    Labs, R.2    Reeves, A.3
  • 22
    • 65449169610 scopus 로고    scopus 로고
    • The antimicrobial resistance profile of Streptococcus pneumoniae
    • Reinert RR. The antimicrobial resistance profile of Streptococcus pneumoniae. Clin Microbiol Infect 2009; 15: 7-11.
    • (2009) Clin Microbiol Infect , vol.15 , pp. 7-11
    • Reinert, R.R.1
  • 23
    • 0037842056 scopus 로고    scopus 로고
    • Antimicrobials: Modes of action and mechanisms of resistance
    • McDermott PF, Walker RD, White DG. Antimicrobials: modes of action and mechanisms of resistance. Int J Toxicol 2003; 22: 135-43.
    • (2003) Int J Toxicol , vol.22 , pp. 135-143
    • McDermott, P.F.1    Walker, R.D.2    White, D.G.3
  • 24
    • 0035884895 scopus 로고    scopus 로고
    • Antibiotic resistance: Consequences of inaction
    • Levy SB. Antibiotic resistance: consequences of inaction. Clin Infect Dis 2001; 33: S124-9.
    • (2001) Clin Infect Dis , vol.33
    • Levy, S.B.1
  • 25
    • 0030307207 scopus 로고    scopus 로고
    • Ins and outs of antimicrobial resistance: Era of the drug pumps
    • Jenkinson HF. Ins and outs of antimicrobial resistance: era of the drug pumps. J Dent Res 1996; 75: 736-42.
    • (1996) J Dent Res , vol.75 , pp. 736-742
    • Jenkinson, H.F.1
  • 26
    • 0021337427 scopus 로고
    • Current mechanisms of resistance to antimicrobial agents in microorganisms causing infection in the patient at risk for infection
    • Neu HC. Current mechanisms of resistance to antimicrobial agents in microorganisms causing infection in the patient at risk for infection. Am J Med 1984; 76: 11-27.
    • (1984) Am J Med , vol.76 , pp. 11-27
    • Neu, H.C.1
  • 28
    • 0031447774 scopus 로고    scopus 로고
    • Opportunistic fungal infections: Superficial and systemic candidiasis
    • Hedderwick S, Kauffman CA. Opportunistic fungal infections: superficial and systemic candidiasis. Geriatrics 1997; 52: 50-54, 59.
    • (1997) Geriatrics , vol.52
    • Hedderwick, S.1    Kauffman, C.A.2
  • 29
    • 0027142028 scopus 로고
    • Fungal infections of the oral cavity
    • Zegarelli DJ. Fungal infections of the oral cavity. Otolaryngol Clin North Am 1993; 26: 1069-89.
    • (1993) Otolaryngol Clin North Am , vol.26 , pp. 1069-1089
    • Zegarelli, D.J.1
  • 30
    • 33947375620 scopus 로고    scopus 로고
    • Candida glabrata: An emerging oral opportunistic pathogen
    • Li L, Redding S, Dongari-Bagtzoglou A. Candida glabrata: an emerging oral opportunistic pathogen. J Dent Res 2007; 86: 204-15.
    • (2007) J Dent Res , vol.86 , pp. 204-215
    • Li, L.1    Redding, S.2    Dongari-Bagtzoglou, A.3
  • 31
    • 79958058721 scopus 로고    scopus 로고
    • Prevention and treatment of Clostridium difficile infection
    • Gouliouris T, Brown NM, Aliyu SH. Prevention and treatment of Clostridium difficile infection. Clin Med 2011; 11: 75-9.
    • (2011) Clin Med , vol.11 , pp. 75-79
    • Gouliouris, T.1    Brown, N.M.2    Aliyu, S.H.3
  • 32
    • 78651397723 scopus 로고    scopus 로고
    • Differences in the in vitro susceptibility of planktonic and biofilm-associated Escherichia coli strains to antimicrobial agents
    • Naves P, Del Prado G, Ponte C, Soriano F. Differences in the in vitro susceptibility of planktonic and biofilm-associated Escherichia coli strains to antimicrobial agents. J Chemother 2010; 22: 312-7.
    • (2010) J Chemother , vol.22 , pp. 312-317
    • Naves, P.1    del Prado, G.2    Ponte, C.3    Soriano, F.4
  • 33
    • 77957760025 scopus 로고    scopus 로고
    • Modality of bacterial growth presents unique targets: How do we treat biofilm-mediated infections?
    • Fey PD. Modality of bacterial growth presents unique targets: how do we treat biofilm-mediated infections? Curr Opin Microbiol 2010; 13: 610-5.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 610-615
    • Fey, P.D.1
  • 34
    • 36448961979 scopus 로고    scopus 로고
    • Peptidology: Short amino acid modules in cell biology and immunology
    • Lucchese G, Stufano A, Trost B, Kusalik A, Kanduc D. Peptidology: short amino acid modules in cell biology and immunology. Amino Acids 2007; 33: 703-7.
    • (2007) Amino Acids , vol.33 , pp. 703-707
    • Lucchese, G.1    Stufano, A.2    Trost, B.3    Kusalik, A.4    Kanduc, D.5
  • 35
    • 31644438026 scopus 로고    scopus 로고
    • Peptimmunology: Immunogenic peptides and sequence redundancy
    • Kanduc D. Peptimmunology: immunogenic peptides and sequence redundancy. Curr Drug Discov Technol 2005; 2: 239-44.
    • (2005) Curr Drug Discov Technol , vol.2 , pp. 239-244
    • Kanduc, D.1
  • 36
    • 33646131438 scopus 로고    scopus 로고
    • Defining peptide sequences: From antigenicity to immunogenicity through redundancy
    • Kanduc D. Defining peptide sequences: from antigenicity to immunogenicity through redundancy. Curr Pharmacogenomics 2006; 4: 33-7.
    • (2006) Curr Pharmacogenomics , vol.4 , pp. 33-37
    • Kanduc, D.1
  • 37
    • 0032871752 scopus 로고    scopus 로고
    • Molecular mimicry of phage displayed peptides mimicking GD3 ganglioside
    • Willers J, Lucchese A, Kanduc D, Ferrone S. Molecular mimicry of phage displayed peptides mimicking GD3 ganglioside. Peptides 1999; 20: 1021-6.
    • (1999) Peptides , vol.20 , pp. 1021-1026
    • Willers, J.1    Lucchese, A.2    Kanduc, D.3    Ferrone, S.4
  • 38
    • 0033667726 scopus 로고    scopus 로고
    • Computer-assisted analysis of molecular mimicry between HPV16 E7 oncoprotein and human protein sequences
    • Natale C, Giannini T, Lucchese A, Kanduc D. Computer-assisted analysis of molecular mimicry between HPV16 E7 oncoprotein and human protein sequences. Immunol Cell Biol 2000; 78: 580-5.
    • (2000) Immunol Cell Biol , vol.78 , pp. 580-585
    • Natale, C.1    Giannini, T.2    Lucchese, A.3    Kanduc, D.4
  • 39
    • 0037051685 scopus 로고    scopus 로고
    • Monoclonal and polyclonal humoral immune response to EC HER-2/NEU peptides with low similarity to the host's proteome
    • Mittelman A, Lucchese A, Sinha AA, Kanduc D. Monoclonal and polyclonal humoral immune response to EC HER-2/NEU peptides with low similarity to the host's proteome. Int J Cancer 2002; 98: 741-7.
    • (2002) Int J Cancer , vol.98 , pp. 741-747
    • Mittelman, A.1    Lucchese, A.2    Sinha, A.A.3    Kanduc, D.4
  • 40
    • 4043057315 scopus 로고    scopus 로고
    • Non-self-discrimination as a driving concept in the identification of an immunodominant HMW-MAA epitopic peptide sequence by autoantibodies from melanoma cancer patients
    • Dummer R, Mittelman A, Fanizzi FP, Lucchese G, Willers J, Kanduc D. Non-self-discrimination as a driving concept in the identification of an immunodominant HMW-MAA epitopic peptide sequence by autoantibodies from melanoma cancer patients. Int J Cancer 2004; 111: 720-6.
    • (2004) Int J Cancer , vol.111 , pp. 720-726
    • Dummer, R.1    Mittelman, A.2    Fanizzi, F.P.3    Lucchese, G.4    Willers, J.5    Kanduc, D.6
  • 42
    • 4644309011 scopus 로고    scopus 로고
    • Identification of monoclonal anti-HMW-MAA antibody linear peptide epitope by proteomic database mining
    • Mittelman A, Tiwari R, Lucchese G, Willers J, Dummer R, Kanduc D. Identification of monoclonal anti-HMW-MAA antibody linear peptide epitope by proteomic database mining. J Invest Dermat 2004; 123: 670-5.
    • (2004) J Invest Dermat , vol.123 , pp. 670-675
    • Mittelman, A.1    Tiwari, R.2    Lucchese, G.3    Willers, J.4    Dummer, R.5    Kanduc, D.6
  • 43
    • 21244498559 scopus 로고    scopus 로고
    • Definition of anti-tyrosinase MAb T311 linear determinant by proteome-based similarity analysis
    • Willers J, Lucchese A, Mittelman A, Dummer R, Kanduc D. Definition of anti-tyrosinase MAb T311 linear determinant by proteome-based similarity analysis. Exp Dermatol 2005; 14: 543-50.
    • (2005) Exp Dermatol , vol.14 , pp. 543-550
    • Willers, J.1    Lucchese, A.2    Mittelman, A.3    Dummer, R.4    Kanduc, D.5
  • 44
    • 27744523641 scopus 로고    scopus 로고
    • Proteomic scan for tyrosinase peptide antigenic pattern in vitiligo and melanoma. Role of sequence similarity and HLA-DR1 affinity
    • Lucchese A, Willers J, Mittelman A, Kanduc D, Dummer R. Proteomic scan for tyrosinase peptide antigenic pattern in vitiligo and melanoma. Role of sequence similarity and HLA-DR1 affinity. J Immunol 2005; 175: 7009-20.
    • (2005) J Immunol , vol.175 , pp. 7009-7020
    • Lucchese, A.1    Willers, J.2    Mittelman, A.3    Kanduc, D.4    Dummer, R.5
  • 45
    • 33748935159 scopus 로고    scopus 로고
    • LL-37, the only human member of the cathelicidin family of antimicrobial peptides
    • Durr UHN, Sudheendra US, Ramamoorthy A. LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim Biophys Acta 2006; 1758: 1408-25.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1408-1425
    • Durr, U.H.N.1    Sudheendra, U.S.2    Ramamoorthy, A.3
  • 46
    • 0029007198 scopus 로고
    • Hcap-18, a cathelin/probacternecin-like protein of human neutrophil specific granules
    • Cowland JB, Johnsen AH, Borregaard N. hCAP-18, a cathelin/probacternecin-like protein of human neutrophil specific granules. FEBS Lett 1995; 368: 173-6.
    • (1995) FEBS Lett , vol.368 , pp. 173-176
    • Cowland, J.B.1    Johnsen, A.H.2    Borregaard, N.3
  • 47
    • 0030602220 scopus 로고    scopus 로고
    • Structural, functional analysis and localization of human CAP18 gene
    • Larrick JW, Lee J, Ma S, Li X, Francke U, Wright SC et al. Structural, functional analysis and localization of human CAP18 gene. FEBS Lett 1996; 398: 74-80.
    • (1996) FEBS Lett , vol.398 , pp. 74-80
    • Larrick, J.W.1    Lee, J.2    Ma, S.3    Li, X.4    Francke, U.5    Wright, S.C.6
  • 48
    • 78751567920 scopus 로고    scopus 로고
    • Cathelicidins-Therapeutic antimicrobial and antitumor host defense peptides for oral diseases
    • Okumura K. Cathelicidins-Therapeutic antimicrobial and antitumor host defense peptides for oral diseases. Jpn Dent Sci Rev 2011; 47: 67-81.
    • (2011) Jpn Dent Sci Rev , vol.47 , pp. 67-81
    • Okumura, K.1
  • 49
    • 0032903987 scopus 로고    scopus 로고
    • The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, is present in human squamous epithelia and colocalizes with interleukin-6
    • Nilsson-Frohm M, Sandstedt B, Sorenson O, Weber G, Borregaard N, Stahle-Backdahl M. The human cationic antimicrobial protein (hCAP18), a peptide antibiotic, is present in human squamous epithelia and colocalizes with interleukin-6. Infect Immun 1999; 67: 2561-6.
    • (1999) Infect Immun , vol.67 , pp. 2561-2566
    • Nilsson-Frohm, M.1    Sandstedt, B.2    Sorenson, O.3    Weber, G.4    Borregaard, N.5    Stahle-Backdahl, M.6
  • 50
    • 0036891933 scopus 로고    scopus 로고
    • Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva
    • Murakami M, Dorschner RA, Gallo RL. Cathelicidin antimicrobial peptides are expressed in salivary glands and saliva. J Dent Res 2002; 81: 845-52.
    • (2002) J Dent Res , vol.81 , pp. 845-852
    • Murakami, M.1    Dorschner, R.A.2    Gallo, R.L.3
  • 51
    • 0141918814 scopus 로고    scopus 로고
    • Antimicrobial peptides in defence of the oral and respiratory tracts
    • Devine DA. Antimicrobial peptides in defence of the oral and respiratory tracts. Mol Immunol 2003; 40: 431-43.
    • (2003) Mol Immunol , vol.40 , pp. 431-443
    • Devine, D.A.1
  • 52
    • 0041736471 scopus 로고    scopus 로고
    • Sensitivity of genera Porphyromonas and Prevotella to the bactericidal action of C-terminal domain of human CAP18 and its analogues
    • Isogai E, Isogai H, Matuo K, et al. Sensitivity of genera Porphyromonas and Prevotella to the bactericidal action of C-terminal domain of human CAP18 and its analogues. Oral Microbiol Immunol 2003; 18: 329-32.
    • (2003) Oral Microbiol Immunol , vol.18 , pp. 329-332
    • Isogai, E.1    Isogai, H.2    Matuo, K.3
  • 53
    • 0033926971 scopus 로고    scopus 로고
    • Sensitivity of Actinobacillus actinomycetemcomitans and Capnocytophaga spp. to the bactericidal action of LL-37: A cathelicidin found in human leukocytes and epithelium
    • Tanaka D, Miyasaki KT, Lehrer RI. Sensitivity of Actinobacillus actinomycetemcomitans and Capnocytophaga spp. to the bactericidal action of LL-37: a cathelicidin found in human leukocytes and epithelium. Oral Microbiol Immunol 2000; 15: 226-31.
    • (2000) Oral Microbiol Immunol , vol.15 , pp. 226-231
    • Tanaka, D.1    Miyasaki, K.T.2    Lehrer, R.I.3
  • 54
    • 21244433198 scopus 로고    scopus 로고
    • Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, {beta}-defensins and LL37, produced by human epithelial cells
    • Ouhara K, Komatsuzawa H, Yamada S, Shiba H, Fujiwara T, Ohara M, et al. Susceptibilities of periodontopathogenic and cariogenic bacteria to antibacterial peptides, {beta}-defensins and LL37, produced by human epithelial cells. J Antimicrob Chemother 2005; 55: 888-96.
    • (2005) J Antimicrob Chemother , vol.55 , pp. 888-896
    • Ouhara, K.1    Komatsuzawa, H.2    Yamada, S.3    Shiba, H.4    Fujiwara, T.5    Ohara, M.6
  • 55
  • 56
    • 0346996865 scopus 로고    scopus 로고
    • The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor
    • Tjabringa GS, Aarbiou J, Ninaber DK, et al. The antimicrobial peptide LL-37 activates innate immunity at the airway epithelial surface by transactivation of the epidermal growth factor receptor. J Immunol 2003; 171: 6690-6.
    • (2003) J Immunol , vol.171 , pp. 6690-6696
    • Tjabringa, G.S.1    Aarbiou, J.2    Ninaber, D.K.3
  • 57
    • 0036240209 scopus 로고    scopus 로고
    • A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis
    • Niyonsaba F, Iwabuchi K, Someya A, et al. A cathelicidin family of human antibacterial peptide LL-37 induces mast cell chemotaxis. Immunology 2002; 106: 20-6.
    • (2002) Immunology , vol.106 , pp. 20-26
    • Niyonsaba, F.1    Iwabuchi, K.2    Someya, A.3
  • 58
    • 0035058454 scopus 로고    scopus 로고
    • Evaluation of the effects of peptide antibiotics human beta-defensins-1/-2 and LL-37 on histamine release and prostaglandin D(2) production from mast cells
    • Niyonsaba F, Someya A, Hirata M, Ogawa H, Nagaoka I. Evaluation of the effects of peptide antibiotics human beta-defensins-1/-2 and LL-37 on histamine release and prostaglandin D(2) production from mast cells. Eur J Immunol 2001; 31: 1066-75.
    • (2001) Eur J Immunol , vol.31 , pp. 1066-1075
    • Niyonsaba, F.1    Someya, A.2    Hirata, M.3    Ogawa, H.4    Nagaoka, I.5
  • 59
    • 0037335205 scopus 로고    scopus 로고
    • The cathelicidin antimicrobial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium
    • Heilborn JD, Nilsson MF, Kratz G, et al. The cathelicidin antimicrobial peptide LL-37 is involved in re-epithelialization of human skin wounds and is lacking in chronic ulcer epithelium. J Invest Dermatol 2003; 120: 379-89.
    • (2003) J Invest Dermatol , vol.120 , pp. 379-389
    • Heilborn, J.D.1    Nilsson, M.F.2    Kratz, G.3
  • 60
    • 0035884820 scopus 로고    scopus 로고
    • Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells
    • Nagaoka I, Hirota S, Niyonsaba F, et al. Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells. J Immunol 2001; 167: 3329-38.
    • (2001) J Immunol , vol.167 , pp. 3329-3338
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3
  • 61
    • 0036731921 scopus 로고    scopus 로고
    • Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacement with hydrophobic and cationic amino acid residues
    • Nagaoka I, Hirota S, Niyonsaba F, et al. Augmentation of the lipopolysaccharide-neutralizing activities of human cathelicidin CAP18/LL-37-derived antimicrobial peptides by replacement with hydrophobic and cationic amino acid residues. Clin Diagn Lab Immunol 2002; 9: 972-82.
    • (2002) Clin Diagn Lab Immunol , vol.9 , pp. 972-982
    • Nagaoka, I.1    Hirota, S.2    Niyonsaba, F.3
  • 62
    • 0031046311 scopus 로고    scopus 로고
    • Biological function of the dTDP-rhamnose synthesis pathway in Streptococcus mutans
    • Tsukioka Y, Yamashita Y, Oho T, Nakano Y, Koga TD. Biological function of the dTDP-rhamnose synthesis pathway in Streptococcus mutans. J Bacteriol 1997; 179: 1126-34.
    • (1997) J Bacteriol , vol.179 , pp. 1126-1134
    • Tsukioka, Y.1    Yamashita, Y.2    Oho, T.3    Nakano, Y.4    Koga, T.D.5
  • 64
    • 0030272902 scopus 로고    scopus 로고
    • Microbial/host interactions in health and disease: Who controls the cytokine network?
    • Henderson B, Poole S, Wilson M. Microbial/host interactions in health and disease: who controls the cytokine network? Immunopharmacology 1996; 35: 1-21.
    • (1996) Immunopharmacology , vol.35 , pp. 1-21
    • Henderson, B.1    Poole, S.2    Wilson, M.3
  • 65
  • 69
    • 79952009518 scopus 로고    scopus 로고
    • Salivary infectious agents and periodontal disease status
    • Saygun I, Nizam N, Keskiner I, et al. Salivary infectious agents and periodontal disease status. J Periodontal Res 2011; 46: 235-9.
    • (2011) J Periodontal Res , vol.46 , pp. 235-239
    • Saygun, I.1    Nizam, N.2    Keskiner, I.3
  • 70
    • 34447119498 scopus 로고    scopus 로고
    • Isolation and characterization of the mutans streptococci from the dental plaques in Koreans
    • Yoo SY, Park SJ, Jeong DK, et al. Isolation and characterization of the mutans streptococci from the dental plaques in Koreans. J Microbiol 2007; 45: 246-55.
    • (2007) J Microbiol , vol.45 , pp. 246-255
    • Yoo, S.Y.1    Park, S.J.2    Jeong, D.K.3
  • 71
    • 52849096623 scopus 로고    scopus 로고
    • Streptococcus mutans and Streptococcus sanguinis colonization correlated with caries experience in children
    • Ge Y, Caufield PW, Fisch GS, Li Y. Streptococcus mutans and Streptococcus sanguinis colonization correlated with caries experience in children. Caries Res 2008; 42: 444-8.
    • (2008) Caries Res , vol.42 , pp. 444-448
    • Ge, Y.1    Caufield, P.W.2    Fisch, G.S.3    Li, Y.4
  • 72
    • 0034116709 scopus 로고    scopus 로고
    • Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides
    • Yashin B, Pang M, Turner JS, et al. Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides. Eur J Clin Microbiol Infect Dis 2000; 19: 187-94.
    • (2000) Eur J Clin Microbiol Infect Dis , vol.19 , pp. 187-194
    • Yashin, B.1    Pang, M.2    Turner, J.S.3
  • 74
    • 31944451136 scopus 로고    scopus 로고
    • Human alpha-defensins block papillomavirus infection
    • Buck CB, Day PM, Thompson CD, et al. Human alpha-defensins block papillomavirus infection. Proc Natl Acad Sci USA 2006; 103: 1516-21.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1516-1521
    • Buck, C.B.1    Day, P.M.2    Thompson, C.D.3
  • 75
    • 77954552752 scopus 로고    scopus 로고
    • Human papillomavirus-mediated carcinogenesis and HPV-associated oral and oropharyngeal squamous cell carcinoma. Part 1: Human papillomavirus-mediated carcinogenesis
    • Feller L, Wood NH, Khammissa RA, Lemmer J. Human papillomavirus-mediated carcinogenesis and HPV-associated oral and oropharyngeal squamous cell carcinoma. Part 1: human papillomavirus-mediated carcinogenesis. Head Face Med 2010; 6: 14.
    • (2010) Head Face Med , vol.6 , pp. 14
    • Feller, L.1    Wood, N.H.2    Khammissa, R.A.3    Lemmer, J.4
  • 76
    • 77954555333 scopus 로고    scopus 로고
    • Human papillomavirus-mediated carcinogenesis and HPV-associated oral and oropharyngeal squamous cell carcinoma. Part 2: Human papillomavirus associated oral and oropharyngeal squamous cell carcinoma
    • Feller L, Wood NH, Khammissa RA, Lemmer J. Human papillomavirus-mediated carcinogenesis and HPV-associated oral and oropharyngeal squamous cell carcinoma. Part 2: Human papillomavirus associated oral and oropharyngeal squamous cell carcinoma. Head Face Med 2010; 6: 15.
    • (2010) Head Face Med , vol.6 , pp. 15
    • Feller, L.1    Wood, N.H.2    Khammissa, R.A.3    Lemmer, J.4
  • 77
    • 77957268782 scopus 로고    scopus 로고
    • Cancer genes alterations and HPV infection in oral squamous cell carcinoma
    • Popovi B, Jeki B, Novakovi I, et al. Cancer genes alterations and HPV infection in oral squamous cell carcinoma. Int J Oral Maxillofac Surg 2010; 39: 909-15.
    • (2010) Int J Oral Maxillofac Surg , vol.39 , pp. 909-915
    • Popovi, B.1    Jeki, B.2    Novakovi, I.3
  • 79
    • 62649167961 scopus 로고    scopus 로고
    • Effect of SP3 silencing on cytokeratin expression pattern in HPV-positive cells
    • Lucchese A, Serpico R. Effect of SP3 silencing on cytokeratin expression pattern in HPV-positive cells. Int J Immunopathol Pharmacol 2009; 22: 163-8.
    • (2009) Int J Immunopathol Pharmacol , vol.22 , pp. 163-168
    • Lucchese, A.1    Serpico, R.2
  • 80
    • 4043145072 scopus 로고    scopus 로고
    • Possible association between HPV16 E7 protein level and cytokeratin 19
    • Favia G, Kanduc D, Lo Muzio L, Lucchese A, Serpico R. Possible association between HPV16 E7 protein level and cytokeratin 19. Int J Cancer 2004; 111: 795-7.
    • (2004) Int J Cancer , vol.111 , pp. 795-797
    • Favia, G.1    Kanduc, D.2    lo Muzio, L.3    Lucchese, A.4    Serpico, R.5
  • 81
    • 84856506085 scopus 로고    scopus 로고
    • An in vitro multistep carcinogenesis model for both HPV-positive and -negative human oral squamous cell carcinomas
    • Zushi Y, Narisawa-Saito M, Noguchi K, et al. An in vitro multistep carcinogenesis model for both HPV-positive and -negative human oral squamous cell carcinomas. Am J Cancer Res 2011; 1: 869-81.
    • (2011) Am J Cancer Res , vol.1 , pp. 869-881
    • Zushi, Y.1    Narisawa-Saito, M.2    Noguchi, K.3
  • 82
    • 80051552897 scopus 로고    scopus 로고
    • Beta-defensins: What are they REALLY doing in the oral cavity?
    • Diamond G, Ryan L. Beta-defensins: what are they REALLY doing in the oral cavity? Oral Dis 2011; 17: 628-35.
    • (2011) Oral Dis , vol.17 , pp. 628-635
    • Diamond, G.1    Ryan, L.2
  • 84
    • 36248993535 scopus 로고    scopus 로고
    • Antimicrobial peptides in oral cancer
    • Meyer JE, Harder J. Antimicrobial peptides in oral cancer. Curr Pharm Des 2007; 13: 3119-30.
    • (2007) Curr Pharm Des , vol.13 , pp. 3119-3130
    • Meyer, J.E.1    Harder, J.2
  • 85
    • 0027197671 scopus 로고
    • Adrenomedullin: A novel hypotensive peptide isolated from human pheochromocytoma
    • Kitamura K, Kangawa K, Kawamoto M, et al. Adrenomedullin: a novel hypotensive peptide isolated from human pheochromocytoma. Biochem Biophys Res Commun 1993; 192: 553-60.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 553-560
    • Kitamura, K.1    Kangawa, K.2    Kawamoto, M.3
  • 86
    • 77958454620 scopus 로고    scopus 로고
    • The first clinical pilot study of intravenous adrenomedullin administration in patients with acute myocardial infarction
    • Kataoka Y, Miyazaki S, Yasuda S, et al. The first clinical pilot study of intravenous adrenomedullin administration in patients with acute myocardial infarction. J Cardiovasc Pharmacol 2010; 56: 413-9.
    • (2010) J Cardiovasc Pharmacol , vol.56 , pp. 413-419
    • Kataoka, Y.1    Miyazaki, S.2    Yasuda, S.3
  • 88
    • 77955927484 scopus 로고    scopus 로고
    • Attenuation of renal ischemia and reperfusion injury by human adrenomedullin and its binding protein
    • Shah KG, Rajan D, Jacob A, et al. Attenuation of renal ischemia and reperfusion injury by human adrenomedullin and its binding protein. J Surg Res 2010; 163: 110-7.
    • (2010) J Surg Res , vol.163 , pp. 110-117
    • Shah, K.G.1    Rajan, D.2    Jacob, A.3
  • 89
    • 77954597743 scopus 로고    scopus 로고
    • Adrenomedullin regulates sperm motility and oviductal ciliary beat via cyclic adenosine 5'- monophosphate/protein kinase A and nitric oxide
    • Chiu PC, Liao S, Lam KK, et al. Adrenomedullin regulates sperm motility and oviductal ciliary beat via cyclic adenosine 5'- monophosphate/protein kinase A and nitric oxide. Endocrinology 2010; 151: 3336-47.
    • (2010) Endocrinology , vol.151 , pp. 3336-3347
    • Chiu, P.C.1    Liao, S.2    Lam, K.K.3
  • 90
    • 74349118931 scopus 로고    scopus 로고
    • Adrenomedullin is expressed during rodent dental tissue development and promotes cell growth and mineralization
    • Musson DS, McLachlan JL, Sloan AJ, Smith AJ, Cooper PR. Adrenomedullin is expressed during rodent dental tissue development and promotes cell growth and mineralization. Biol Cell 2010; 102: 145-57.
    • (2010) Biol Cell , vol.102 , pp. 145-157
    • Musson, D.S.1    McLachlan, J.L.2    Sloan, A.J.3    Smith, A.J.4    Cooper, P.R.5
  • 91
  • 92
    • 43349099628 scopus 로고    scopus 로고
    • Adrenomedullin suppresses tumour necrosis factor alpha-induced CXC chemokine ligand 10 production by human gingival fibroblasts
    • Hosokawa I, Hosokawa Y, Ozaki K, Nakae H, Matsuo T. Adrenomedullin suppresses tumour necrosis factor alpha-induced CXC chemokine ligand 10 production by human gingival fibroblasts. Clin Exp Immunol 2008; 152: 568-75.
    • (2008) Clin Exp Immunol , vol.152 , pp. 568-575
    • Hosokawa, I.1    Hosokawa, Y.2    Ozaki, K.3    Nakae, H.4    Matsuo, T.5
  • 93
    • 0034888528 scopus 로고    scopus 로고
    • Adrenomedullin expression in pathogen-challenged oral epithelial cells
    • Kapas S, Bansal A, Bhargava V, et al. Adrenomedullin expression in pathogen-challenged oral epithelial cells. Peptides 2001; 22: 1485-9.
    • (2001) Peptides , vol.22 , pp. 1485-1489
    • Kapas, S.1    Bansal, A.2    Bhargava, V.3
  • 94
    • 0037445828 scopus 로고    scopus 로고
    • Adrenomedullin and mucosal defence: Interaction between host and microorganism
    • Allaker RP, Kapas S. Adrenomedullin and mucosal defence: interaction between host and microorganism. Regul Pept 2003; 112: 147-52.
    • (2003) Regul Pept , vol.112 , pp. 147-152
    • Allaker, R.P.1    Kapas, S.2
  • 95
    • 0032319580 scopus 로고    scopus 로고
    • Human Salivary histatins: Promising antifungal therapeutic agents
    • Tsai H, Bobek LA. Human Salivary histatins: promising antifungal therapeutic agents. Crit Rev Oral Biol Med 1998; 9: 480-97.
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 480-497
    • Tsai, H.1    Bobek, L.A.2
  • 96
    • 0025137692 scopus 로고
    • Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva
    • Sugiyama K, Ogino T, Ogata K. Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva. Arch Oral Biol 1990; 35: 415-9.
    • (1990) Arch Oral Biol , vol.35 , pp. 415-419
    • Sugiyama, K.1    Ogino, T.2    Ogata, K.3
  • 97
    • 0023888810 scopus 로고
    • Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans
    • Oppenheim FG, Xu T, McMillian FM, et al. Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. J Biol Chem 1988; 263: 7472-7.
    • (1988) J Biol Chem , vol.263 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3
  • 98
    • 4744347696 scopus 로고    scopus 로고
    • A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway
    • Castagnola M, Inzitari R, Rossetti DV, et al. A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway. J Biol Chem 2004; 279: 41436-43.
    • (2004) J Biol Chem , vol.279 , pp. 41436-41443
    • Castagnola, M.1    Inzitari, R.2    Rossetti, D.V.3
  • 99
    • 0021280786 scopus 로고
    • Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans
    • MacKay BJ, Denepitiya L, Iacono VJ, Krost SB, Pollock JJ. Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans. Infect Immun 1984; 44: 695-701.
    • (1984) Infect Immun , vol.44 , pp. 695-701
    • Mackay, B.J.1    Denepitiya, L.2    Iacono, V.J.3    Krost, S.B.4    Pollock, J.J.5
  • 100
    • 11144232372 scopus 로고    scopus 로고
    • Human salivary peptides derived from histatins
    • Lupi A, Schininà ME, Denotti G, et al. Human salivary peptides derived from histatins. Eur J Morphol 2003; 41: 99-102.
    • (2003) Eur J Morphol , vol.41 , pp. 99-102
    • Lupi, A.1    Schininà, M.E.2    Denotti, G.3
  • 101
    • 0035115443 scopus 로고    scopus 로고
    • Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease
    • Gusman H, Travis J, Helmerhorst EJ, Potempa J, Troxler RF, Oppenheim FG. Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease. Infect Immun 2001; 69: 1402-8.
    • (2001) Infect Immun , vol.69 , pp. 1402-1408
    • Gusman, H.1    Travis, J.2    Helmerhorst, E.J.3    Potempa, J.4    Troxler, R.F.5    Oppenheim, F.G.6
  • 102
    • 0029851698 scopus 로고    scopus 로고
    • Candidacidal activity of recombinant human salivary histatin-5 and variants
    • Tsai H, Raj PA, Bobek LA. Candidacidal activity of recombinant human salivary histatin-5 and variants. Infect Immun 1996; 64: 5000-7.
    • (1996) Infect Immun , vol.64 , pp. 5000-5007
    • Tsai, H.1    Raj, P.A.2    Bobek, L.A.3
  • 103
    • 0030670607 scopus 로고    scopus 로고
    • Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans
    • Tsai H., Bobek LA. Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans. Biochim Biophys Acta 1997; 1336: 367-9.
    • (1997) Biochim Biophys Acta , vol.1336 , pp. 367-369
    • Tsai, H.1    Bobek, L.A.2
  • 104
    • 18044401756 scopus 로고    scopus 로고
    • Clinical and microbial evaluation of a histatin containing mouthrinse in humans with experimental gingivitis
    • Mickels N, McManus C, Massaro J, et al. Clinical and microbial evaluation of a histatin containing mouthrinse in humans with experimental gingivitis. J Clin Periodontol 2001; 28: 404-10.
    • (2001) J Clin Periodontol , vol.28 , pp. 404-410
    • Mickels, N.1    McManus, C.2    Massaro, J.3
  • 105
    • 0035032562 scopus 로고    scopus 로고
    • Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5
    • Rothstein DM, Spacciapoli P, Tran LT, et al. Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5. Antimicrob Agents Chemother 2001; 45: 1367-73.
    • (2001) Antimicrob Agents Chemother , vol.45 , pp. 1367-1373
    • Rothstein, D.M.1    Spacciapoli, P.2    Tran, L.T.3
  • 106
    • 0035172093 scopus 로고    scopus 로고
    • Induction of histamine release from rat peritoneal mast cells by histatins
    • Yoshida M, Kimura T, Kitaichi K, et al. Induction of histamine release from rat peritoneal mast cells by histatins. Biol Pharm Bull 2001; 24: 1267-70.
    • (2001) Biol Pharm Bull , vol.24 , pp. 1267-1270
    • Yoshida, M.1    Kimura, T.2    Kitaichi, K.3
  • 107
    • 0032911047 scopus 로고    scopus 로고
    • Reactivation of Mutant p53 through Interaction of a C-terminal peptide with the core domain
    • Selivanova G, Ryabchenko L, Jansson E, Iotsova V, Wiman KG. Reactivation of Mutant p53 through Interaction of a C-terminal peptide with the core domain. Mol Cel Biol 1999; 19: 3395-402.
    • (1999) Mol Cel Biol , vol.19 , pp. 3395-3402
    • Selivanova, G.1    Ryabchenko, L.2    Jansson, E.3    Iotsova, V.4    Wiman, K.G.5
  • 108
    • 34247605962 scopus 로고    scopus 로고
    • Expression of Bcl-xL, Bax, and p53 in primary tumors and lymph node metastases in oral squamous cell carcinoma
    • Baltaziak M, Duraj E, Koda M, et al. Expression of Bcl-xL, Bax, and p53 in primary tumors and lymph node metastases in oral squamous cell carcinoma. Ann N Y Acad Sci. 2006; 1090:18-25.
    • (2006) Ann N Y Acad Sci , vol.1090 , pp. 18-25
    • Baltaziak, M.1    Duraj, E.2    Koda, M.3
  • 109
    • 84855465861 scopus 로고    scopus 로고
    • Role of human papillomavirus infection in carcinogenesis of oral squamous cell carcinoma with evidences of prognostic association
    • doi: 10.1111/j.1600-0714.2011.01046.x
    • Chen SF, Yu FS, Chang YC, Fu E, Nieh S, Lin YS. Role of human papillomavirus infection in carcinogenesis of oral squamous cell carcinoma with evidences of prognostic association. J Oral Pathol Med Forthcoming 2011; doi: 10.1111/j.1600-0714.2011.01046.x.
    • (2011) J Oral Pathol Med Forthcoming
    • Chen, S.F.1    Yu, F.S.2    Chang, Y.C.3    Fu, E.4    Nieh, S.5    Lin, Y.S.6
  • 110
    • 80053526676 scopus 로고    scopus 로고
    • Expression form of p53 and PCNA at the invasive front in oral squamous cell carcinoma: Correlation with clinicopathological features and prognosis
    • doi: 10.1111/j.1600-0714.2011.01032.x
    • Kato K, Kawashiri S, Yoshizawa K, et al. Expression form of p53 and PCNA at the invasive front in oral squamous cell carcinoma: correlation with clinicopathological features and prognosis. J Oral Pathol Med Forthcoming 2011; doi: 10.1111/j.1600-0714.2011.01032.x.
    • (2011) J Oral Pathol Med Forthcoming
    • Kato, K.1    Kawashiri, S.2    Yoshizawa, K.3
  • 111
    • 4243226455 scopus 로고    scopus 로고
    • E7 protein of human papillomaviruses and its interaction with cellular pathways
    • P. Bannasch, D. Kanduc, S. Papa, and J. M. Tager Ed., Birkhäuser Verlag, Basel, Switzerland
    • Zehbe I, Ciccolini F, Dell'Orco M, et al. E7 protein of human papillomaviruses and its interaction with cellular pathways, In P. Bannasch, D. Kanduc, S. Papa, and J. M. Tager Ed., Cell growth and oncogenesis. Birkhäuser Verlag, Basel, Switzerland. 1998; 97-107.
    • (1998) Cell Growth and Oncogenesis , pp. 97-107
    • Zehbe, I.1    Ciccolini, F.2    Dell'Orco, M.3
  • 112
    • 45149130644 scopus 로고    scopus 로고
    • Human papillomavirus as a risk factor in oral carcinogenesis: A study using in situ hybridization with signal amplification
    • Acay R, Rezende N, Fontes A, Aburad A, Nunes F, Sousa S. Human papillomavirus as a risk factor in oral carcinogenesis: a study using in situ hybridization with signal amplification. Oral Microbiol Immunol 2008; 23: 271-4.
    • (2008) Oral Microbiol Immunol , vol.23 , pp. 271-274
    • Acay, R.1    Rezende, N.2    Fontes, A.3    Aburad, A.4    Nunes, F.5    Sousa, S.6
  • 113
    • 0036635470 scopus 로고    scopus 로고
    • Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)- globin and human cytokeratin 7
    • Kanduc D. Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)- globin and human cytokeratin 7. J Virol 2002; 76: 7040-8.
    • (2002) J Virol , vol.76 , pp. 7040-7048
    • Kanduc, D.1
  • 114
    • 60349123060 scopus 로고    scopus 로고
    • Human papillomavirus vaccine safety in pediatric patients: An evaluation of the Vaccine Adverse Event Reporting
    • Borja-Hart NL, Benavides S, Christensen C. Human papillomavirus vaccine safety in pediatric patients: an evaluation of the Vaccine Adverse Event Reporting. Ann Pharmacother 2009; 43: 356-9.
    • (2009) Ann Pharmacother , vol.43 , pp. 356-359
    • Borja-Hart, N.L.1    Benavides, S.2    Christensen, C.3
  • 115
    • 38449105360 scopus 로고    scopus 로고
    • Adverse events reported for HPV vaccine
    • Eggertson L. Adverse events reported for HPV vaccine. CMAJ 2007; 177: 1169-70.
    • (2007) CMAJ , vol.177 , pp. 1169-1170
    • Eggertson, L.1
  • 116
    • 70349132570 scopus 로고    scopus 로고
    • Quantifying the possible cross-reactivity risk of an HPV16 vaccine
    • Kanduc D. Quantifying the possible cross-reactivity risk of an HPV16 vaccine. J Exp Ther Oncol 2009; 8: 65-76.
    • (2009) J Exp Ther Oncol , vol.8 , pp. 65-76
    • Kanduc, D.1
  • 117
    • 79951779703 scopus 로고    scopus 로고
    • Syncope and seizures following human papillomavirus vaccination: A retrospective case series
    • Crawford NW, Clothier HJ, Elia S, Lazzaro T, Royle J, Buttery JP. Syncope and seizures following human papillomavirus vaccination: a retrospective case series. Med J Aust 2011; 194: 16-8.
    • (2011) Med J Aust , vol.194 , pp. 16-18
    • Crawford, N.W.1    Clothier, H.J.2    Elia, S.3    Lazzaro, T.4    Royle, J.5    Buttery, J.P.6
  • 118
    • 45149120630 scopus 로고    scopus 로고
    • A predatory mechanism dramatically increases the efficiency of lateral gene transfer in Streptococcus pneumoniae and related commensal species
    • Johnsborg O, Eldholm V, Bjørnstad ML, Håvarstein LS. A predatory mechanism dramatically increases the efficiency of lateral gene transfer in Streptococcus pneumoniae and related commensal species. Mol Microbiol 2008; 69: 245-53.
    • (2008) Mol Microbiol , vol.69 , pp. 245-253
    • Johnsborg, O.1    Eldholm, V.2    Bjørnstad, M.L.3    Håvarstein, L.S.4
  • 119
    • 25644434423 scopus 로고    scopus 로고
    • Peptide pheromone induced cell death of Streptococcus mutans
    • Qi F, Kreth J, Lévesque CM, Kay O, et al. Peptide pheromone induced cell death of Streptococcus mutans. FEMS Microbiol Lett 2005; 251: 321-6.
    • (2005) FEMS Microbiol Lett , vol.251 , pp. 321-326
    • Qi, F.1    Kreth, J.2    Lévesque, C.M.3    Kay, O.4
  • 121
    • 77954578574 scopus 로고    scopus 로고
    • The CS1 segment of fibronectin is involved in human OSCC pathogenesis by mediating OSCC cell spreading, migration, and invasion
    • Kamarajan P, Garcia-Pardo A, D'Silva NJ, Kapila YL. The CS1 segment of fibronectin is involved in human OSCC pathogenesis by mediating OSCC cell spreading, migration, and invasion. BMC Cancer 2010; 10: 330.
    • (2010) BMC Cancer , vol.10 , pp. 330
    • Kamarajan, P.1    Garcia-Pardo, A.2    D'Silva, N.J.3    Kapila, Y.L.4
  • 122
    • 74749088094 scopus 로고    scopus 로고
    • Cyclic alphavbeta6-targeting peptide selected from biopanning with clinical potential for head and neck squamous cell carcinoma
    • Hsiao JR, Chang Y, Chen YL, et al. Cyclic alphavbeta6-targeting peptide selected from biopanning with clinical potential for head and neck squamous cell carcinoma. Head Neck 2001; 32: 160-72.
    • (2001) Head Neck , vol.32 , pp. 160-172
    • Hsiao, J.R.1    Chang, Y.2    Chen, Y.L.3
  • 123
    • 78649325107 scopus 로고    scopus 로고
    • Circulating cycloxygenase-2 in patients with tobacco-related intraoral squamous cell carcinoma and evaluation of its peptide inhibitors as potential antitumor agent
    • Kapoor V, Singh AK, Dey S, Sharma SC, Das SN. Circulating cycloxygenase-2 in patients with tobacco-related intraoral squamous cell carcinoma and evaluation of its peptide inhibitors as potential antitumor agent. J Cancer Res Clin Oncol 2001; 136: 1795-804.
    • (2001) J Cancer Res Clin Oncol , vol.136 , pp. 1795-1804
    • Kapoor, V.1    Singh, A.K.2    Dey, S.3    Sharma, S.C.4    Das, S.N.5
  • 124
    • 0034544554 scopus 로고    scopus 로고
    • Isolation of a peptide for targeted drug delivery into human head and neck solid tumors
    • Hong FD, Clayman GL. Isolation of a peptide for targeted drug delivery into human head and neck solid tumors. Cancer Res 2000; 60: 6551-6.
    • (2000) Cancer Res , vol.60 , pp. 6551-6556
    • Hong, F.D.1    Clayman, G.L.2
  • 125
    • 34249941306 scopus 로고    scopus 로고
    • Novel cell-surface peptides specific to human oral squamous cell carcinoma using an
    • Kawai N, Asaumi J, Murakami J, et al. Novel cell-surface peptides specific to human oral squamous cell carcinoma using an E. coli peptide display library. Oncol Rep 2007; 17: 787-91.
    • (2007) E. Coli Peptide Display Library. Oncol Rep , vol.17 , pp. 787-791
    • Kawai, N.1    Asaumi, J.2    Murakami, J.3
  • 126
    • 33750703178 scopus 로고    scopus 로고
    • Preliminary data on Pemphigus vulgaris treatment by a proteomics-defined peptide: A case report
    • Angelini G, Bonamonte D, Lucchese A, et al. Preliminary data on Pemphigus vulgaris treatment by a proteomics-defined peptide: a case report. J Transl Med 2006; 4: 43.
    • (2006) J Transl Med , vol.4 , pp. 43
    • Angelini, G.1    Bonamonte, D.2    Lucchese, A.3
  • 127
    • 33749556727 scopus 로고    scopus 로고
    • Proteomic definition of a desmoglein linear determinant common to Pemphigus vulgaris and Pemphigus foliaceous
    • Lucchese A, Mittelman A, Tessitore L, Serpico R, Sinha AA, Kanduc D. Proteomic definition of a desmoglein linear determinant common to Pemphigus vulgaris and Pemphigus foliaceous. J Transl Med 2006; 4: 37.
    • (2006) J Transl Med , vol.4 , pp. 37
    • Lucchese, A.1    Mittelman, A.2    Tessitore, L.3    Serpico, R.4    Sinha, A.A.5    Kanduc, D.6
  • 128
    • 23044474907 scopus 로고    scopus 로고
    • Characterization of polyclonal antibodies raised against a linear peptide determinant of desmoglein-3
    • Angelini G, Bonamonte D, Lin MS, et al. Characterization of polyclonal antibodies raised against a linear peptide determinant of desmoglein-3. J Exp Ther Oncol 2005; 5: 1-7.
    • (2005) J Exp Ther Oncol , vol.5 , pp. 1-7
    • Angelini, G.1    Bonamonte, D.2    Lin, M.S.3
  • 129
    • 18144371672 scopus 로고    scopus 로고
    • Epitope definition by proteomic similarity analysis: Identification of the linear determinant of the anti-Dsg3 MAb 5H10
    • Lucchese A, Mittelman A, Lin MS, Kanduc D, Sinha AA. Epitope definition by proteomic similarity analysis: identification of the linear determinant of the anti-Dsg3 MAb 5H10. J Transl Med 2004; 2: 43.
    • (2004) J Transl Med , vol.2 , pp. 43
    • Lucchese, A.1    Mittelman, A.2    Lin, M.S.3    Kanduc, D.4    Sinha, A.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.