메뉴 건너뛰기




Volumn 8, Issue 1, 2008, Pages 53-61

Proteomics in leptospirosis research: Towards molecular diagnostics and vaccine development

Author keywords

Diagnostics; Immunoproteomics; Leptospirosis; Mass spectrometry; Proteome; Proteomics; Vaccine discovery

Indexed keywords

ACYL COENZYME A DEHYDROGENASE; CARRIER PROTEIN; CHAPERONE; DIHYDROLIPOAMIDE ACETYLTRANSFERASE; FLAGELLIN; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCOSIDASE; HEAT SHOCK PROTEIN; IMMUNOGLOBULIN; PROTEIN DNAK; RNA POLYMERASE; BACTERIAL VACCINE;

EID: 38149117068     PISSN: 14737159     EISSN: 17448352     Source Type: Journal    
DOI: 10.1586/14737159.8.1.53     Document Type: Review
Times cited : (20)

References (68)
  • 1
    • 0035072803 scopus 로고    scopus 로고
    • Leptospirosis
    • Levett PN. Leptospirosis. Clin. Microbiol. Rev. 14(2), 296-326 (2001).
    • (2001) Clin. Microbiol. Rev , vol.14 , Issue.2 , pp. 296-326
    • Levett, P.N.1
  • 2
    • 0027016462 scopus 로고
    • Typing leptospira from the perspective of a reference laboratory
    • Terpstra WJ. Typing leptospira from the perspective of a reference laboratory. Acta Leiden 60(2), 79-87 (1992).
    • (1992) Acta Leiden , vol.60 , Issue.2 , pp. 79-87
    • Terpstra, W.J.1
  • 3
    • 0032935785 scopus 로고    scopus 로고
    • Further determination of DNA relatedness between serogroups and serovars in the family Leptospiraceae with a proposal for Leptospira alexanderi sp. nov. and four new Leptospira genomospecies
    • Brenner DJ, Kaufmann AF, Sulzer KR, Steigerwalt AG, Rogers FC, Weyant RS. Further determination of DNA relatedness between serogroups and serovars in the family Leptospiraceae with a proposal for Leptospira alexanderi sp. nov. and four new Leptospira genomospecies. Int. J. Syst. Bacteriol. 49, 2839-2858 (1999).
    • (1999) Int. J. Syst. Bacteriol , vol.49 , pp. 2839-2858
    • Brenner, D.J.1    Kaufmann, A.F.2    Sulzer, K.R.3    Steigerwalt, A.G.4    Rogers, F.C.5    Weyant, R.S.6
  • 4
    • 0344983453 scopus 로고    scopus 로고
    • Leptospirosis: A zoonotic disease of global importance
    • Bharti AR, Nally JE, Ricaldi JN et al. Leptospirosis: a zoonotic disease of global importance. Lancet Infect. Dis. 3(12), 757-771 (2003).
    • (2003) Lancet Infect. Dis , vol.3 , Issue.12 , pp. 757-771
    • Bharti, A.R.1    Nally, J.E.2    Ricaldi, J.N.3
  • 5
    • 0037097534 scopus 로고    scopus 로고
    • Outbreak of leptospirosis among triathlon participants and community residents in Springfield, Illinois, 1998
    • Morgan J, Bornstein SL, Karpati AM et al. Outbreak of leptospirosis among triathlon participants and community residents in Springfield, Illinois, 1998. Clin. Infect. Dis. 34(12), 1593-1599 (2002).
    • (2002) Clin. Infect. Dis , vol.34 , Issue.12 , pp. 1593-1599
    • Morgan, J.1    Bornstein, S.L.2    Karpati, A.M.3
  • 6
    • 0027460367 scopus 로고
    • Active surveillance and risk factors for leptospirosis in Hawaii
    • Sasaki DM, Pang L, Minette HP et al. Active surveillance and risk factors for leptospirosis in Hawaii. Am. J. Trop. Med. Hyg. 48(1), 35-43 (1993).
    • (1993) Am. J. Trop. Med. Hyg , vol.48 , Issue.1 , pp. 35-43
    • Sasaki, D.M.1    Pang, L.2    Minette, H.P.3
  • 9
    • 0013862443 scopus 로고
    • Evaluation of Galton's macroscopic slide test for the serodiagnosis of leptospirosis in human serum samples
    • Wolff JW, Bohlander HJ. Evaluation of Galton's macroscopic slide test for the serodiagnosis of leptospirosis in human serum samples. Ann. Soc. Belg. Med. Trop. 46(1), 123-133 (1966).
    • (1966) Ann. Soc. Belg. Med. Trop , vol.46 , Issue.1 , pp. 123-133
    • Wolff, J.W.1    Bohlander, H.J.2
  • 10
    • 0031975286 scopus 로고    scopus 로고
    • Evaluation of the indirect hemagglutination assay for diagnosis of acute leptospirosis
    • Levett PN, Whittington CU. Evaluation of the indirect hemagglutination assay for diagnosis of acute leptospirosis. J. Clin. Microbiol. 36(1), 11-14 (1998).
    • (1998) J. Clin. Microbiol , vol.36 , Issue.1 , pp. 11-14
    • Levett, P.N.1    Whittington, C.U.2
  • 11
    • 0020049465 scopus 로고
    • Development of a simple serological method for diagnosing leptospirosis: A microcapsule agglutination test
    • Arimitsu Y, Kobayashi S, Akama K, Matuhasi T. Development of a simple serological method for diagnosing leptospirosis: a microcapsule agglutination test. J. Clin. Microbiol. 15(5), 835-841 (1982).
    • (1982) J. Clin. Microbiol , vol.15 , Issue.5 , pp. 835-841
    • Arimitsu, Y.1    Kobayashi, S.2    Akama, K.3    Matuhasi, T.4
  • 12
    • 0030797068 scopus 로고    scopus 로고
    • Evaluation of a commercial enzyme-linked immunosorbent assay for detection of immunoglobulin M antibody in diagnosis of human leptospiral infection
    • Winslow WE, Merry DJ, Pirc ML, Devine PL. Evaluation of a commercial enzyme-linked immunosorbent assay for detection of immunoglobulin M antibody in diagnosis of human leptospiral infection. J. Clin. Microbiol. 35(8), 1938-1942 (1997).
    • (1997) J. Clin. Microbiol , vol.35 , Issue.8 , pp. 1938-1942
    • Winslow, W.E.1    Merry, D.J.2    Pirc, M.L.3    Devine, P.L.4
  • 13
    • 28844468923 scopus 로고    scopus 로고
    • Laboratory diagnosis of leptospirosis
    • Ahmad SN, Shah S, Ahmad FM. Laboratory diagnosis of leptospirosis. J. Postgrad. Med. 51(3), 195-200 (2005).
    • (2005) J. Postgrad. Med , vol.51 , Issue.3 , pp. 195-200
    • Ahmad, S.N.1    Shah, S.2    Ahmad, F.M.3
  • 14
    • 34247608279 scopus 로고    scopus 로고
    • Leptospirosis: Pathogenesis, immunity, and diagnosis
    • Excellent review on the pathogenicity and diagnosis of leptospirosis, which also provides thoughtful perspectives on recent progress in the field, ••
    • Palaniappan RU, Ramanujam S, Chang YF. Leptospirosis: pathogenesis, immunity, and diagnosis. Curr. Opin. Infect. Dis. 20(3), 284-292 (2007). •• Excellent review on the pathogenicity and diagnosis of leptospirosis, which also provides thoughtful perspectives on recent progress in the field.
    • (2007) Curr. Opin. Infect. Dis , vol.20 , Issue.3 , pp. 284-292
    • Palaniappan, R.U.1    Ramanujam, S.2    Chang, Y.F.3
  • 15
    • 2942625703 scopus 로고    scopus 로고
    • A quantitative PCR (TaqMan) assay for pathogenic Leptospira spp
    • Smythe LD, Smith IL, Smith GA et al. A quantitative PCR (TaqMan) assay for pathogenic Leptospira spp. BMC. Infect. Dis. 2, 13 (2002).
    • (2002) BMC. Infect. Dis , vol.2 , pp. 13
    • Smythe, L.D.1    Smith, I.L.2    Smith, G.A.3
  • 18
    • 1842456788 scopus 로고    scopus 로고
    • Leptospiral immunoglobulin-like proteins elicit protective immunity
    • Koizumi N, Watanabe H. Leptospiral immunoglobulin-like proteins elicit protective immunity. Vaccine 22(11-12), 1545-1552 (2004).
    • (2004) Vaccine , vol.22 , Issue.11-12 , pp. 1545-1552
    • Koizumi, N.1    Watanabe, H.2
  • 19
    • 33644753762 scopus 로고    scopus 로고
    • Immunoprotection of recombinant leptospiral immunoglobulinlike protein A against Leptospira interrogans serovar Pomona infection
    • Palaniappan RU, McDonough SP, Divers TJ et al. Immunoprotection of recombinant leptospiral immunoglobulinlike protein A against Leptospira interrogans serovar Pomona infection. Infect. Immun. 74(3), 1745-1750 (2006).
    • (2006) Infect. Immun , vol.74 , Issue.3 , pp. 1745-1750
    • Palaniappan, R.U.1    McDonough, S.P.2    Divers, T.J.3
  • 20
    • 34447630469 scopus 로고    scopus 로고
    • The terminal portion of leptospiral immunoglobulin-like protein LigA confers protective immunity against lethal infection in the hamster model of leptospirosis
    • Silva EF, Medeiros MA, McBride AJ et al. The terminal portion of leptospiral immunoglobulin-like protein LigA confers protective immunity against lethal infection in the hamster model of leptospirosis. Vaccine 25(33), 6277-6286 (2007).
    • (2007) Vaccine , vol.25 , Issue.33 , pp. 6277-6286
    • Silva, E.F.1    Medeiros, M.A.2    McBride, A.J.3
  • 21
    • 21544445862 scopus 로고    scopus 로고
    • Protection against Leptospira interrogans sensu lato challenge by DNA immunization with the gene encoding hemolysin-associated protein 1
    • Branger C, Chatrenet B, Gauvrit A et al. Protection against Leptospira interrogans sensu lato challenge by DNA immunization with the gene encoding hemolysin-associated protein 1. Infect. Immun. 73(7), 4062-4069 (2005).
    • (2005) Infect. Immun , vol.73 , Issue.7 , pp. 4062-4069
    • Branger, C.1    Chatrenet, B.2    Gauvrit, A.3
  • 22
    • 0032702291 scopus 로고    scopus 로고
    • Leptospiral outer membrane proteins OmpL1 and LipL41 exhibit synergistic immunoprotection
    • Haake DA, Mazel MK, McCoy AM et al. Leptospiral outer membrane proteins OmpL1 and LipL41 exhibit synergistic immunoprotection. Infect. Immun. 67(12), 6572-6582 (1999).
    • (1999) Infect. Immun , vol.67 , Issue.12 , pp. 6572-6582
    • Haake, D.A.1    Mazel, M.K.2    McCoy, A.M.3
  • 23
    • 0037464546 scopus 로고    scopus 로고
    • Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing
    • Ren SX, Fu G, Jiang XG et al. Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing. Nature 422(6934), 888-893 (2003).
    • (2003) Nature , vol.422 , Issue.6934 , pp. 888-893
    • Ren, S.X.1    Fu, G.2    Jiang, X.G.3
  • 25
    • 33749249203 scopus 로고    scopus 로고
    • Genome reduction in Leptospira borgpetersenii reflects limited transmission potential
    • Bulach DM, Zuerner RL, Wilson P et al. Genome reduction in Leptospira borgpetersenii reflects limited transmission potential. Proc. Natl Acad. Sci. USA 103(39), 14560-14565 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.39 , pp. 14560-14565
    • Bulach, D.M.1    Zuerner, R.L.2    Wilson, P.3
  • 26
    • 0034912192 scopus 로고    scopus 로고
    • Leptospiral proteins recognized during the humoral immune response to leptospirosis in humans
    • A recent study to identify potential leptospiral immunogens using an immunoproteomics approach, •
    • Guerreiro H, Croda J, Flannery B et al. Leptospiral proteins recognized during the humoral immune response to leptospirosis in humans. Infect. Immun. 69(8), 4958-4968 (2001). • A recent study to identify potential leptospiral immunogens using an immunoproteomics approach.
    • (2001) Infect. Immun , vol.69 , Issue.8 , pp. 4958-4968
    • Guerreiro, H.1    Croda, J.2    Flannery, B.3
  • 27
    • 0036121913 scopus 로고    scopus 로고
    • Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai
    • A recent study to characterize leptospiral outer membrane proteins (OMPs) using a classical proteomics approach, •
    • Cullen PA, Cordwell SJ, Bulach DM, Haake DA, Adler B. Global analysis of outer membrane proteins from Leptospira interrogans serovar Lai. Infect. Immun. 70(5), 2311-2318 (2002). • A recent study to characterize leptospiral outer membrane proteins (OMPs) using a classical proteomics approach.
    • (2002) Infect. Immun , vol.70 , Issue.5 , pp. 2311-2318
    • Cullen, P.A.1    Cordwell, S.J.2    Bulach, D.M.3    Haake, D.A.4    Adler, B.5
  • 28
    • 13244249606 scopus 로고    scopus 로고
    • Purification and proteomic analysis of outer membrane vesicles from a clinical isolate of Leptospira interrogans serovar Copenhageni
    • A recent study to characterize leptospiral OMPs using a classical proteomics approach, •
    • Nally JE, Whitelegge JP, Aguilera R, Pereira MM, Blanco DR, Lovett MA. Purification and proteomic analysis of outer membrane vesicles from a clinical isolate of Leptospira interrogans serovar Copenhageni. Proteomics 5(1), 144-152 (2005). • A recent study to characterize leptospiral OMPs using a classical proteomics approach.
    • (2005) Proteomics , vol.5 , Issue.1 , pp. 144-152
    • Nally, J.E.1    Whitelegge, J.P.2    Aguilera, R.3    Pereira, M.M.4    Blanco, D.R.5    Lovett, M.A.6
  • 29
    • 33846814927 scopus 로고    scopus 로고
    • Characterization of the outer membrane proteome of Leptospira interrogans expressed during acute lethal infection
    • A recent study to characterize leptospiral OMPs using a classical proteomics approach, •
    • Nally JE, Whitelegge JP, Bassilian S, Blanco DR, Lovett MA. Characterization of the outer membrane proteome of Leptospira interrogans expressed during acute lethal infection. Infect. Immun. 75(2), 766-773 (2007). • A recent study to characterize leptospiral OMPs using a classical proteomics approach.
    • (2007) Infect. Immun , vol.75 , Issue.2 , pp. 766-773
    • Nally, J.E.1    Whitelegge, J.P.2    Bassilian, S.3    Blanco, D.R.4    Lovett, M.A.5
  • 30
    • 38149060098 scopus 로고    scopus 로고
    • Kositanont U, Saetun P, Krittanai C, Doungchawee G, Tribuddharat C, Thongboonkerd V. Application of immunoproteomics to leptospirosis: towards clinical diagnostics and vaccine discovery. Proteomics Clin. Appl. 1(4), 400-409 (2007). • A recent study to identify potential leptospiral immunogens using an immunoproteomics approach.
    • Kositanont U, Saetun P, Krittanai C, Doungchawee G, Tribuddharat C, Thongboonkerd V. Application of immunoproteomics to leptospirosis: towards clinical diagnostics and vaccine discovery. Proteomics Clin. Appl. 1(4), 400-409 (2007). • A recent study to identify potential leptospiral immunogens using an immunoproteomics approach.
  • 31
    • 0034101261 scopus 로고    scopus 로고
    • Proteomics in medical microbiology
    • Cash P. Proteomics in medical microbiology. Electrophoresis 21(6), 1187-1201 (2000).
    • (2000) Electrophoresis , vol.21 , Issue.6 , pp. 1187-1201
    • Cash, P.1
  • 32
    • 0035321652 scopus 로고    scopus 로고
    • Comparative proteomics of bacterial pathogens
    • Cordwell SJ, Nouwens AS, Walsh BJ. Comparative proteomics of bacterial pathogens. Proteomics 1(4), 461-472 (2001).
    • (2001) Proteomics , vol.1 , Issue.4 , pp. 461-472
    • Cordwell, S.J.1    Nouwens, A.S.2    Walsh, B.J.3
  • 33
    • 0032951971 scopus 로고    scopus 로고
    • A proteome analysis of livers from obese (ob/ob) mice treated with the peroxisome proliferator WY14,643
    • Edvardsson U, Alexandersson M, Brockenhuus von Löwenhielm H et al. A proteome analysis of livers from obese (ob/ob) mice treated with the peroxisome proliferator WY14,643. Electrophoresis 20(4-5), 935-942 (1999).
    • (1999) Electrophoresis , vol.20 , Issue.4-5 , pp. 935-942
    • Edvardsson, U.1    Alexandersson, M.2    Brockenhuus von Löwenhielm, H.3
  • 34
    • 0141720423 scopus 로고    scopus 로고
    • Proteomics of bacterial pathogens
    • Excellent review on microbial proteomics, ••
    • Cash P. Proteomics of bacterial pathogens. Adv. Biochem. Eng Biotechnol. 83, 93-115 (2003). •• Excellent review on microbial proteomics.
    • (2003) Adv. Biochem. Eng Biotechnol , vol.83 , pp. 93-115
    • Cash, P.1
  • 35
    • 17144410529 scopus 로고    scopus 로고
    • Bacterial proteomics and its role in antibacterial drug discovery
    • Brotz-Oesterhelt H, Bandow JE, Labischinski H. Bacterial proteomics and its role in antibacterial drug discovery. Mass Spectrom. Rev. 24(4), 549-565 (2005).
    • (2005) Mass Spectrom. Rev , vol.24 , Issue.4 , pp. 549-565
    • Brotz-Oesterhelt, H.1    Bandow, J.E.2    Labischinski, H.3
  • 36
    • 12344288395 scopus 로고    scopus 로고
    • Effectiveness and limitation of two-dimensional gel electrophoresis in bacterial membrane protein proteomics and perspectives
    • Bunai K, Yamane K. Effectiveness and limitation of two-dimensional gel electrophoresis in bacterial membrane protein proteomics and perspectives. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 815(1-2), 227-236 (2005).
    • (2005) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci , vol.815 , Issue.1-2 , pp. 227-236
    • Bunai, K.1    Yamane, K.2
  • 37
    • 22744458932 scopus 로고    scopus 로고
    • Proteomics meets microbiology: Technical advances in the global mapping of protein expression and function
    • Phillips CI, Bogyo M. Proteomics meets microbiology: technical advances in the global mapping of protein expression and function. Cell Microbiol. 7(8), 1061-1076 (2005).
    • (2005) Cell Microbiol , vol.7 , Issue.8 , pp. 1061-1076
    • Phillips, C.I.1    Bogyo, M.2
  • 38
    • 33744528308 scopus 로고    scopus 로고
    • Technologies for bacterial surface proteomics
    • Excellent review on microbial proteomics, ••
    • Cordwell SJ. Technologies for bacterial surface proteomics. Curr. Opin. Microbiol. 9(3), 320-329 (2006). •• Excellent review on microbial proteomics.
    • (2006) Curr. Opin. Microbiol , vol.9 , Issue.3 , pp. 320-329
    • Cordwell, S.J.1
  • 39
    • 0030895921 scopus 로고    scopus 로고
    • A comparison of selected mRNA and protein abundances in human liver
    • Anderson L, Seilhamer J. A comparison of selected mRNA and protein abundances in human liver. Electrophoresis 18(3-4), 533-537 (1997).
    • (1997) Electrophoresis , vol.18 , Issue.3-4 , pp. 533-537
    • Anderson, L.1    Seilhamer, J.2
  • 40
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi SP, Rochon Y, Franza BR, Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol. Cell Biol. 19(3), 1720-1730 (1999).
    • (1999) Mol. Cell Biol , vol.19 , Issue.3 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 41
    • 0037381261 scopus 로고    scopus 로고
    • Correlation study showing no concordance between EPAS-1/HIF-2α mRNA and protein expression in transitional cell cancer of the bladder
    • Ji P, Xuan JW, Onita T et al. Correlation study showing no concordance between EPAS-1/HIF-2α mRNA and protein expression in transitional cell cancer of the bladder. Urology 61(4), 851-857 (2003).
    • (2003) Urology , vol.61 , Issue.4 , pp. 851-857
    • Ji, P.1    Xuan, J.W.2    Onita, T.3
  • 44
    • 2642578228 scopus 로고    scopus 로고
    • Immunoproteomics: Mass spectrometry-based methods to study the targets of the immune response
    • Purcell AW, Gorman JJ. Immunoproteomics: mass spectrometry-based methods to study the targets of the immune response. Mol. Cell. Proteomics 3(3), 193-208 (2004).
    • (2004) Mol. Cell. Proteomics , vol.3 , Issue.3 , pp. 193-208
    • Purcell, A.W.1    Gorman, J.J.2
  • 45
    • 0037250739 scopus 로고    scopus 로고
    • Serological and proteomic evaluation of antibody responses in the identification of tumor antigens in renal cell carcinoma
    • Unwin RD, Harnden P, Pappin D et al. Serological and proteomic evaluation of antibody responses in the identification of tumor antigens in renal cell carcinoma. Proteomics 3(1), 45-55 (2003).
    • (2003) Proteomics , vol.3 , Issue.1 , pp. 45-55
    • Unwin, R.D.1    Harnden, P.2    Pappin, D.3
  • 46
    • 0035403554 scopus 로고    scopus 로고
    • Identification of tumor antigens in renal cell carcinoma by serological proteome analysis
    • Klade CS, Voss T, Krystek E et al. Identification of tumor antigens in renal cell carcinoma by serological proteome analysis. Proteomics 1(7), 890-898 (2001).
    • (2001) Proteomics , vol.1 , Issue.7 , pp. 890-898
    • Klade, C.S.1    Voss, T.2    Krystek, E.3
  • 47
    • 0036912713 scopus 로고    scopus 로고
    • Targeting of tumor associated antigens in renal cell carcinoma using proteome-based analysis and their clinical significance
    • Kellner R, Lichtenfels R, Atkins D et al. Targeting of tumor associated antigens in renal cell carcinoma using proteome-based analysis and their clinical significance. Proteomics 2(12), 1743-1751 (2002).
    • (2002) Proteomics , vol.2 , Issue.12 , pp. 1743-1751
    • Kellner, R.1    Lichtenfels, R.2    Atkins, D.3
  • 48
    • 1242295372 scopus 로고    scopus 로고
    • Identification of metabolic enzymes in renal cell carcinoma utilizing PROTEOMEX analyses
    • Lichtenfels R, Kellner R, Atkins D et al. Identification of metabolic enzymes in renal cell carcinoma utilizing PROTEOMEX analyses. Biochim. Biophys. Acta 1646(1-2), 21-31 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1646 , Issue.1-2 , pp. 21-31
    • Lichtenfels, R.1    Kellner, R.2    Atkins, D.3
  • 49
    • 10744230912 scopus 로고    scopus 로고
    • Identification of markers for the selection of patients undergoing renal cell carcinoma-specific immunotherapy
    • Seliger B, Menig M, Lichtenfels R et al. Identification of markers for the selection of patients undergoing renal cell carcinoma-specific immunotherapy. Proteomics 3(6), 979-990 (2003).
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 979-990
    • Seliger, B.1    Menig, M.2    Lichtenfels, R.3
  • 50
  • 51
    • 0031568420 scopus 로고    scopus 로고
    • Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level
    • McCormack AL, Schieltz DM, Goode B et al. Direct analysis and identification of proteins in mixtures by LC/MS/MS and database searching at the low-femtomole level. Anal. Chem. 69(4), 767-776 (1997).
    • (1997) Anal. Chem , vol.69 , Issue.4 , pp. 767-776
    • McCormack, A.L.1    Schieltz, D.M.2    Goode, B.3
  • 52
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu CC, MacCoss MJ, Howell KE, Yates JR III. A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 21(5), 532-538 (2003).
    • (2003) Nat. Biotechnol , vol.21 , Issue.5 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 53
    • 0036391454 scopus 로고    scopus 로고
    • Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags
    • Gygi SP, Rist B, Griffin TJ, Eng J, Aebersold R. Proteome analysis of low-abundance proteins using multidimensional chromatography and isotope-coded affinity tags. J. Proteome. Res. 1(1), 47-54 (2002).
    • (2002) J. Proteome. Res , vol.1 , Issue.1 , pp. 47-54
    • Gygi, S.P.1    Rist, B.2    Griffin, T.J.3    Eng, J.4    Aebersold, R.5
  • 54
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR III. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol. 19(3), 242-247 (2001).
    • (2001) Nat. Biotechnol , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 55
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu CC, Yates JR III. The application of mass spectrometry to membrane proteomics. Nat. Biotechnol. 21(3), 262-267 (2003).
    • (2003) Nat. Biotechnol , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 56
    • 31644438577 scopus 로고    scopus 로고
    • Large scale protein profiling by combination of protein fractionation and multidimensional protein identification technology (MudPIT)
    • Chen EI, Hewel J, Felding-Habermann B, Yates JR III. Large scale protein profiling by combination of protein fractionation and multidimensional protein identification technology (MudPIT). Mol. Cell. Proteomics 5(1), 53-56 (2006).
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.1 , pp. 53-56
    • Chen, E.I.1    Hewel, J.2    Felding-Habermann, B.3    Yates III, J.R.4
  • 57
    • 0020333627 scopus 로고
    • Profiling of urinary medium-sized peptides in normal and uremic urine by high-performance liquid chromatography
    • Mabuchi H, Nakahashi H. Profiling of urinary medium-sized peptides in normal and uremic urine by high-performance liquid chromatography. J. Chromatogr. 233, 107-113 (1982).
    • (1982) J. Chromatogr , vol.233 , pp. 107-113
    • Mabuchi, H.1    Nakahashi, H.2
  • 58
    • 0030800989 scopus 로고    scopus 로고
    • Mapping of peptides and protein fragments in human urine using liquid chromatography-mass spectrometry
    • Heine G, Raida M, Forssmann WG. Mapping of peptides and protein fragments in human urine using liquid chromatography-mass spectrometry. J. Chromatogr. A 776(1), 117-124 (1997).
    • (1997) J. Chromatogr. A , vol.776 , Issue.1 , pp. 117-124
    • Heine, G.1    Raida, M.2    Forssmann, W.G.3
  • 59
    • 19444387632 scopus 로고    scopus 로고
    • Advances in clinical cancer proteomics: SELDI-ToF-mass spectrometry and biomarker discovery
    • Seibert V, Ebert MP, Buschmann T. Advances in clinical cancer proteomics: SELDI-ToF-mass spectrometry and biomarker discovery. Brief Funct. Genomic. Proteomic. 4(1), 16-26 (2005).
    • (2005) Brief Funct. Genomic. Proteomic , vol.4 , Issue.1 , pp. 16-26
    • Seibert, V.1    Ebert, M.P.2    Buschmann, T.3
  • 60
    • 33646259958 scopus 로고    scopus 로고
    • Clinical proteomics: Searching for better tumour markers with SELDI-TOF mass spectrometry
    • Engwegen JY, Gast MC, Schellens JH, Beijnen JH. Clinical proteomics: searching for better tumour markers with SELDI-TOF mass spectrometry. Trends Pharmacol. Sci. 27(5), 251-259 (2006).
    • (2006) Trends Pharmacol. Sci , vol.27 , Issue.5 , pp. 251-259
    • Engwegen, J.Y.1    Gast, M.C.2    Schellens, J.H.3    Beijnen, J.H.4
  • 61
    • 33846934658 scopus 로고    scopus 로고
    • Poon TC. Opportunities and limitations of SELDI-TOF-MS in biomedical research: practical advices. Expert Rev. Proteomics 4(1), 51-65 (2007).
    • Poon TC. Opportunities and limitations of SELDI-TOF-MS in biomedical research: practical advices. Expert Rev. Proteomics 4(1), 51-65 (2007).
  • 62
    • 33645747471 scopus 로고    scopus 로고
    • Predicting the clinical outcome of congenital unilateral ureteropelvic junction obstruction in newborn by urinary proteome analysis
    • Decramer S, Wittke S, Mischak H et al. Predicting the clinical outcome of congenital unilateral ureteropelvic junction obstruction in newborn by urinary proteome analysis. Nat. Med. 12(4), 398-400 (2006).
    • (2006) Nat. Med , vol.12 , Issue.4 , pp. 398-400
    • Decramer, S.1    Wittke, S.2    Mischak, H.3
  • 63
    • 33344479181 scopus 로고    scopus 로고
    • Discovery and validation of new protein biomarkers for urothelial cancer: A prospective analysis
    • Theodorescu D, Wittke S, Ross MM et al. Discovery and validation of new protein biomarkers for urothelial cancer: a prospective analysis. Lancet Oncol. 7(3), 230-240 (2006).
    • (2006) Lancet Oncol , vol.7 , Issue.3 , pp. 230-240
    • Theodorescu, D.1    Wittke, S.2    Ross, M.M.3
  • 64
    • 18844370547 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery
    • Kolch W, Neususs C, Pelzing M, Mischak H. Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery. Mass Spectrom. Rev. 24(6), 959-977 (2005).
    • (2005) Mass Spectrom. Rev , vol.24 , Issue.6 , pp. 959-977
    • Kolch, W.1    Neususs, C.2    Pelzing, M.3    Mischak, H.4
  • 65
    • 34249300780 scopus 로고    scopus 로고
    • Urinary proteome profiling using microfluidic technology on a chip
    • Thongboonkerd V, Songtawee N, Sritippayawan S. Urinary proteome profiling using microfluidic technology on a chip. J. Proteome. Res. 6(5), 2011-2018 (2007).
    • (2007) J. Proteome. Res , vol.6 , Issue.5 , pp. 2011-2018
    • Thongboonkerd, V.1    Songtawee, N.2    Sritippayawan, S.3
  • 66
    • 4344632455 scopus 로고    scopus 로고
    • An integrated digital microfluidic lab-on-a-chip for clinical diagnostics on human physiological fluids
    • Srinivasan V, Pamula VK, Fair RB. An integrated digital microfluidic lab-on-a-chip for clinical diagnostics on human physiological fluids. Lab Chip. 4(4), 310-315 (2004).
    • (2004) Lab Chip , vol.4 , Issue.4 , pp. 310-315
    • Srinivasan, V.1    Pamula, V.K.2    Fair, R.B.3
  • 67
    • 27744509126 scopus 로고    scopus 로고
    • A lab-on-a-chip for spectrophotometric analysis of biological fluids
    • Minas G, Wolffenbuttel RF, Correia JH. A lab-on-a-chip for spectrophotometric analysis of biological fluids. Lab Chip. 5(11), 1303-1309 (2005).
    • (2005) Lab Chip , vol.5 , Issue.11 , pp. 1303-1309
    • Minas, G.1    Wolffenbuttel, R.F.2    Correia, J.H.3
  • 68
    • 33644777646 scopus 로고    scopus 로고
    • Lab-on-a-chip: Microfluidics in drug discovery
    • Dittrich PS, Manz A. Lab-on-a-chip: microfluidics in drug discovery. Nat. Rev. Drug Discov. 5(3), 210-218 (2006).
    • (2006) Nat. Rev. Drug Discov , vol.5 , Issue.3 , pp. 210-218
    • Dittrich, P.S.1    Manz, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.