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Volumn 10, Issue 2, 2011, Pages 646-655

Influence of histatin 5 on Candida albicans mitochondrial protein expression assessed by quantitative mass spectrometry

Author keywords

Antifungal mechanism; Candida albicans; Histatin; ICAT; Mitochondrial proteome; mTRAQ; Quantitative proteomics

Indexed keywords

CYTOCHROME; ELONGATION FACTOR 1ALPHA; HISTATIN 5; MITOCHONDRIAL PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

EID: 79955433491     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100861k     Document Type: Article
Times cited : (22)

References (55)
  • 1
    • 0034060385 scopus 로고    scopus 로고
    • Pathology and clinical correlates in oral candidiasis and its variants: A review
    • Reichart, P. A.; Samaranayake, L. P.; Philipsen, H. P. Pathology and clinical correlates in oral candidiasis and its variants: a review. Oral Dis. 2000, 6 (2), 85-91. (Pubitemid 30159035)
    • (2000) Oral Diseases , vol.6 , Issue.2 , pp. 85-91
    • Reichart, P.A.1    Samaranayake, L.P.2    Philipsen, H.P.3
  • 2
    • 68949214450 scopus 로고    scopus 로고
    • The effects of orthodontic appliances on Candida in the human mouth
    • Hibino, K.; Wong, R. W.; Hagg, U.; Samaranayake, L. P. The effects of orthodontic appliances on Candida in the human mouth. Int. J. Paediatr. Dent. 2009, 19 (5), 301-8.
    • (2009) Int. J. Paediatr. Dent. , vol.19 , Issue.5 , pp. 301-308
    • Hibino, K.1    Wong, R.W.2    Hagg, U.3    Samaranayake, L.P.4
  • 3
    • 6544293463 scopus 로고    scopus 로고
    • Host defense against oropharyngeal and vaginal candidiasis: Site- specific differences
    • Fidel, P. L., Jr. Host defense against oropharyngeal and vaginal candidiasis: Site-specific differences. Rev. Iberoam. Micol. 1999, 16 (1), 8-15. (Pubitemid 29166851)
    • (1999) Revista Iberoamericana de Micologia , vol.16 , Issue.1 , pp. 8-15
    • Fidel Jr., P.L.1
  • 8
    • 0033501533 scopus 로고    scopus 로고
    • Therapeutic experience with fluconazole in the treatment of fungal infections in diabetic patients
    • Penk, A.; Pittrow, L. Therapeutic experience with fluconazole in the treatment of fungal infections in diabetic patients. Mycoses. 1999, 42 (Suppl, 2), 97-100. (Pubitemid 30253119)
    • (1999) Mycoses, Supplement , vol.42 , Issue.2 , pp. 97-100
    • Penk, A.1    Pittrow, L.2
  • 9
    • 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, F. G.; Xu, T.; McMillian, F. M.; Levitz, S. M.; Diamond, R. D.; Offner, G. D.; Troxler, R. F. 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 (16), 7472-7.
    • (1988) J. Biol. Chem. , vol.263 , Issue.16 , pp. 7472-7477
    • Oppenheim, F.G.1    Xu, T.2    McMillian, F.M.3    Levitz, S.M.4    Diamond, R.D.5    Offner, G.D.6    Troxler, R.F.7
  • 10
    • 0030670607 scopus 로고    scopus 로고
    • Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans
    • DOI 10.1016/S0304-4165(97)00076-7, PII S0304416597000767
    • Tsai, H.; Bobek, L. A. Human salivary histatin-5 exerts potent fungicidal activity against Cryptococcus neoformans. Biochim. Biophys. Acta 1997, 1336 (3), 367-9. (Pubitemid 27467037)
    • (1997) Biochimica et Biophysica Acta - General Subjects , vol.1336 , Issue.3 , pp. 367-369
    • Tsai, H.1    Bobek, L.A.2
  • 11
    • 0032979798 scopus 로고    scopus 로고
    • Amphotericin B- and fluconazole-resistant Candida spp., Aspergillus fumigatus, and other newly emerging pathogenic fungi are susceptible to basic antifungal peptides
    • Helmerhorst, E. J.; Reijnders, I. M.; van't, Hof, W.; Simoons-Smit, I.; Veerman, E. C.; Amerongen, A. V. Amphotericin B-and fluconazole-resistant Candida spp., Aspergillus fumigatus, and other newly emerging pathogenic fungi are susceptible to basic antifungal peptides. Antimicrob. Agents Chemother. 1999, 43 (3), 702-4. (Pubitemid 29109547)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.3 , pp. 702-704
    • Helmerhorst, E.J.1    Reijnders, I.M.2    Van 'T Hof, W.3    Simoons-Smit, I.4    Veerman, E.C.I.5    Amerongen, A.V.N.6
  • 12
    • 0032952474 scopus 로고    scopus 로고
    • A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides
    • DOI 10.1016/S0014-5793(99)00411-1, PII S0014579399004111
    • Helmerhorst, E. J.; Reijnders, I. M.; van't, Hof, W.; Veerman, E. C.; Nieuw, Amerongen, A. V. A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides. FEBS Lett. 1999, 449 (2-3), 105-10. (Pubitemid 29192887)
    • (1999) FEBS Letters , vol.449 , Issue.2-3 , pp. 105-110
    • Helmerhorst, E.J.1    Reijnders, I.M.2    Van 'T Hof, W.3    Veerman, E.C.I.4    Nieuw Amerongen, A.V.5
  • 13
    • 33644653705 scopus 로고    scopus 로고
    • The antifungal mechanisms of antimicrobial peptides
    • Devine, D. A., Hancok, R. E. W., Eds.; Cambridge University Press: New York
    • Helmerhorst, E. J.; Oppenheim, F. G. The antifungal mechanisms of antimicrobial peptides. In Mamalian Host Defense peptides; Devine, D. A., Hancok, R. E. W., Eds.; Cambridge University Press: New York, 2004; Vol 6, pp 245-77.
    • (2004) Mamalian Host Defense Peptides , vol.6 , pp. 245-277
    • Helmerhorst, E.J.1    Oppenheim, F.G.2
  • 15
    • 0032958766 scopus 로고    scopus 로고
    • Antifungal peptides: Novel therapeutic compounds against emerging pathogens
    • De Lucca, A. J.; Walsh, T. J. Antifungal peptides: novel therapeutic compounds against emerging pathogens. Antimicrob. Agents Chemother. 1999, 43 (1), 1-11. (Pubitemid 29069190)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.1 , pp. 1-11
    • De Lucca, A.J.1    Walsh, T.J.2
  • 16
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. U.S.A. 1987, 84 (15), 5449-53. (Pubitemid 17129018)
    • (1987) Proceedings of the National Academy of Sciences of the United States of America , vol.84 , Issue.15 , pp. 5449-5453
    • Zasloff, M.1
  • 17
    • 0021854511 scopus 로고
    • Activity of rabbit leukocyte peptides against Candida albicans
    • Selsted, M. E.; Szklarek, D.; Ganz, T.; Lehrer, R. I. Activity of rabbit leukocyte peptides against Candida albicans. Infect. Immun. 1985, 49 (1), 202-6. (Pubitemid 15062889)
    • (1985) Infection and Immunity , vol.49 , Issue.1 , pp. 202-206
    • Selsted, M.E.1    Szklarek, D.2    Ganz, T.3    Lehrer, R.I.4
  • 18
    • 0141919277 scopus 로고    scopus 로고
    • Human salivary MUC7 mucin peptides: Effect of size, charge and cysteine residues on antifungal activity
    • DOI 10.1042/BJ20030779
    • Situ, H.; Wei, G.; Smith, C. J.; Mashhoon, S.; Bobek, L. A. Human salivary MUC7 mucin peptides: effect of size, charge and cysteine residues on antifungal activity. Biochem. J. 2003, 375 (Pt 1), 175-82. (Pubitemid 37255393)
    • (2003) Biochemical Journal , vol.375 , Issue.1 , pp. 175-182
    • Situ, H.1    Wei, G.2    Smith, C.J.3    Mashhoon, S.4    Bobek, L.A.5
  • 19
    • 0035937109 scopus 로고    scopus 로고
    • Characterization of histatin 5 with respect to amphipathicity hydrophobicity and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation
    • Helmerhorst, E. J.; van't, Hof, W.; Breeuwer, P.; Veerman, E. C.; Abee, T.; Troxler, R. F.; Amerongen, A. V.; Oppenheim, F. G. Characterization of histatin 5 with respect to amphipathicity, hydrophobicity, and effects on cell and mitochondrial membrane integrity excludes a candidacidal mechanism of pore formation. J. Biol. Chem. 2001 , 276 (8), 5643-9.
    • (2001) J. Biol. Chem. , vol.276 , Issue.8 , pp. 5643-5649
    • Helmerhorst, E.J.1    Van'T Hof, W.2    Breeuwer, P.3    Veerman, E.C.4    Abee, T.5    Troxler, R.F.6    Amerongen, A.V.7    Oppenheim, F.G.8
  • 21
    • 0032493760 scopus 로고    scopus 로고
    • Candidacidal activity of salivary histatins: Identification of a histatin 5-binding protein on Candida albicans
    • DOI 10.1074/jbc.273.32.20438
    • Edgerton, M.; Koshlukova, S. E.; Lo, T. E.; Chrzan, B. G.; Straubinger, R. M.; Raj, P. A. Candidacidal activity of salivary histatins. Identification of a histatin 5-binding protein on Candida albicans. J. Biol. Chem. 1998, 273 (32), 20438-47. (Pubitemid 28377611)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 20438-20447
    • Edgerton, M.1    Koshlukova, S.E.2    Lo, T.E.3    Chrzan, B.G.4    Straubinger, R.M.5    Raj, P.A.6
  • 22
    • 33747331132 scopus 로고    scopus 로고
    • Candida albicans cell wall ssa proteins bind and facilitate import of salivary histatin 5 required for toxicity
    • Li, X. S.; Sun, J. N.; Okamoto-Shibayama, K.; Edgerton, M. Candida albicans cell wall ssa proteins bind and facilitate import of salivary histatin 5 required for toxicity. J. Biol. Chem. 2006, 281 (32), 22453-63.
    • (2006) J. Biol. Chem. , vol.281 , Issue.32 , pp. 22453-22463
    • Li, X.S.1    Sun, J.N.2    Okamoto-Shibayama, K.3    Edgerton, M.4
  • 23
    • 55549117176 scopus 로고    scopus 로고
    • Uptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain
    • Sun, J. N.; Li, W.; Jang, W. S.; Nayyar, N.; Sutton, M. D.; Edgerton, M. Uptake of the antifungal cationic peptide Histatin 5 by Candida albicans Ssa2p requires binding to non-conventional sites within the ATPase domain. Mol. Microbiol. 2008, 70 (5), 1246-60.
    • (2008) Mol. Microbiol. , vol.70 , Issue.5 , pp. 1246-1260
    • Sun, J.N.1    Li, W.2    Jang, W.S.3    Nayyar, N.4    Sutton, M.D.5    Edgerton, M.6
  • 24
    • 0033516461 scopus 로고    scopus 로고
    • Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death
    • Koshlukova, S. E.; Lloyd, T. L.; Araujo, M. W.; Edgerton, M. Salivary histatin 5 induces non-lytic release of ATP from Candida albicans leading to cell death. J. Biol. Chem. 1999, 274 (27), 18872-9.
    • (1999) J. Biol. Chem. , vol.274 , Issue.27 , pp. 18872-18879
    • Koshlukova, S.E.1    Lloyd, T.L.2    Araujo, M.W.3    Edgerton, M.4
  • 27
    • 0034438935 scopus 로고    scopus 로고
    • Pellicle precursor protein crosslinking: Characterization of an adduct between acidic proline-rich protein (PRP-1) and statherin generated by transglutaminase
    • Yao, Y.; Lamkin, M. S.; Oppenheim, F. G. Pellicle precursor protein crosslinking characterization of an adduct between acidic prolinerich protein (PRP-1) and statherin generated by transglutaminase. J. Dent. Res. 2000, 79 (4), 930-8. (Pubitemid 32501304)
    • (2000) Journal of Dental Research , vol.79 , Issue.4 , pp. 930-938
    • Yao, Y.1    Lamkin, M.S.2    Oppenheim, F.G.3
  • 28
    • 53049096977 scopus 로고    scopus 로고
    • Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues
    • DeSouza, L. V.; Taylor, A. M.; Li, W.; Minkoff, M. S.; Romaschin, A. D.; Colgan, T. J.; Siu, K. W. Multiple reaction monitoring of mTRAQ-labeled peptides enables absolute quantification of endogenous levels of a potential cancer marker in cancerous and normal endometrial tissues. J. Proteome Res. 2008, 7 (8), 3525-34.
    • (2008) J. Proteome Res. , vol.7 , Issue.8 , pp. 3525-3534
    • Desouza, L.V.1    Taylor, A.M.2    Li, W.3    Minkoff, M.S.4    Romaschin, A.D.5    Colgan, T.J.6    Siu, K.W.7
  • 29
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • DOI 10.1038/13690
    • Gygi, S. P.; Rist, B.; Gerber, S. A.; Turecek, F.; Gelb, M. H.; Aebersold, R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 1999, 17 (10), 994-9. (Pubitemid 29474856)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 31
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates, J. R.; Eng, J. K.; McCormack, A. L.; Schieltz, D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal. Chem. 1995, 67 (8), 1426-36.
    • (1995) Anal. Chem. , vol.67 , Issue.8 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 33
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • UniProt Consortium.
    • UniProt Consortium. The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res. 2010, 38 (Database issue), D142-8.
    • (2010) Nucleic Acids Res. , vol.38 , Issue.DATABASE ISSUE
  • 36
    • 33745851905 scopus 로고    scopus 로고
    • Toward the complete yeast mitochondrial proteome: Multidimensional separation techniques for mitochondrial proteomics
    • DOI 10.1021/pr050477f
    • Reinders, J.; Zahedi, R. P.; Pfanner, N.; Meisinger, C.; Sickmann, A. Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J. Proteome Res. 2006, 5 (7), 1543-54. (Pubitemid 44036128)
    • (2006) Journal of Proteome Research , vol.5 , Issue.7 , pp. 1543-1554
    • Reinders, J.1    Zahedi, R.P.2    Pfanner, N.3    Meisinger, C.4    Sickmann, A.5
  • 40
    • 20444452944 scopus 로고    scopus 로고
    • The concomitant expression and availability of conventional and alternative, cyanide-insensitive, respiratory pathways in Candida albicans
    • DOI 10.1016/j.mito.2005.04.001, PII S1567724905000553
    • Helmerhorst, E. J.; Stan, M.; Murphy, M. P.; Sherman, F.; Oppenheim, F. G. The concomitant expression and availability of conventional and alternative, cyanide-insensitive, respiratorypathways in Candida albicans. Mitochondrion 2005, 5 (3), 200-11. (Pubitemid 40823307)
    • (2005) Mitochondrion , vol.5 , Issue.3 , pp. 200-211
    • Helmerhorst, E.J.1    Stan, M.2    Murphy, M.P.3    Sherman, F.4    Oppenheim, F.G.5
  • 41
    • 0347992031 scopus 로고    scopus 로고
    • Human Salivary Histatin 5 Fungicidal Action Does Not Induce Programmed Cell Death Pathways in Candida albicans
    • DOI 10.1128/AAC.48.1.110-115.2004
    • Wunder, D.; Dong, J.; Baev, D.; Edgerton, M. Human salivary histatin 5 fungicidal action does not induce programmed cell death pathways in Candida albicans. Antimicrob. Agents Chemother. 2004, 48 (1)), 110-5. (Pubitemid 38040185)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.1 , pp. 110-115
    • Wunder, D.1    Dong, J.2    Baev, D.3    Edgerton, M.4
  • 42
    • 18844393429 scopus 로고    scopus 로고
    • Genome-wide expression profiling of the response to azole, polyene, echinocandin, and pyrimidine antifungal agents in Candida albicans
    • DOI 10.1128/AAC.49.6.2226-2236.2005
    • Liu, T. T.; Lee, R. E.; Barker, K. S.; Lee, R. E.; Wei, L.; Homayouni, R.; Rogers, P. D. Genome-wide expression profiling of the response to azole, polyene, echinocandin, and pyrimidine antifungal agents in Candida albicans. Antimicrob. Agents Chemother. 2005, 49 (6), 2226-36. (Pubitemid 40734449)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.6 , pp. 2226-2236
    • Liu, T.T.1    Lee, R.E.B.2    Barker, K.S.3    Lee, R.E.4    Wei, L.5    Homayouni, R.6    Rogers, P.D.7
  • 44
    • 33747186667 scopus 로고    scopus 로고
    • Multivariate approach to comparing whole-cell proteomes of Bacillus cereus indicates a biofilm-specific proteome
    • DOI 10.1021/pr050402b
    • Vilain, S.; Brözel, V. S. Multivariate approach to comparing wholecell proteomes of Bacillus cereus indicates a biofilm-specific proteome. J. Proteome Res. 2006, 5 (8), 1924-30. (Pubitemid 44232705)
    • (2006) Journal of Proteome Research , vol.5 , Issue.8 , pp. 1924-1930
    • Vilain, S.1    Brozel, V.S.2
  • 45
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner, F.; Foster, L. J.; Campanaro, S.; Valle, G.; Mann, M. Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol. Cell. Proteomics 2006, 5 (4), 608-19.
    • (2006) Mol. Cell. Proteomics , vol.5 , Issue.4 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 46
    • 41649119244 scopus 로고    scopus 로고
    • The malate-aspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast
    • DOI 10.1101/gad.1648308
    • Easlon, E.; Tsang, F.; Skinner, C.; Wang, C.; Lin, Su-Ju. The malateaspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast. Genes Dev. 2008, 22 (7), 931-44. (Pubitemid 351482846)
    • (2008) Genes and Development , vol.22 , Issue.7 , pp. 931-944
    • Easlon, E.1    Tsang, F.2    Skinner, C.3    Wang, C.4    Lin, S.-J.5
  • 47
    • 1342286842 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle and activation of glyoxylate cycle in the course of chronological aging of Saccharomyces cerevisiae. Compensatory role of succinate oxidation
    • DOI 10.1016/j.biochi.2003.10.019
    • Samokhvalov, V.; Ignatov, V.; Kondrashova, M. Inhibition of Krebs cycle and activation of glyoxylate cycle in the course of chronological aging of Saccharomyces cerevisiae. Compensatory role of succinate oxidation. Biochimie 2004, 86 (1), 39-46. (Pubitemid 38264277)
    • (2004) Biochimie , vol.86 , Issue.1 , pp. 39-46
    • Samokhvalov, V.1    Ignatov, V.2    Kondrashova, M.3
  • 49
    • 70350362952 scopus 로고    scopus 로고
    • ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis
    • Mnatsakanyan, N.; Hook, J. A.; Quisenberry, L.; Weber, J. ATP synthase with its gamma subunit reduced to the N-terminal helix can still catalyze ATP synthesis. J. Biol. Chem. 2009, 284 (39), 26519-25.
    • (2009) J. Biol. Chem. , vol.284 , Issue.39 , pp. 26519-26525
    • Mnatsakanyan, N.1    Hook, J.A.2    Quisenberry, L.3    Weber, J.4
  • 50
    • 0029154909 scopus 로고
    • The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an e site factor
    • Triana-Alonso, F. J.; Chakraburtty, K.; Nierhaus, K. H. The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J. Biol. Chem. 1995, 270 (35), 20473-8.
    • (1995) J. Biol. Chem. , vol.270 , Issue.35 , pp. 20473-20478
    • Triana-Alonso, F.J.1    Chakraburtty, K.2    Nierhaus, K.H.3
  • 51
    • 0242317676 scopus 로고    scopus 로고
    • Assessing functional divergence in EF-1α and its paralogs in eukaryotes and archaebacteria
    • DOI 10.1093/nar/gkg440
    • Inagaki, Y.; Blouin, C.; Susko, E.; Roger, A. Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria. J. Nucleic. Acids Res. 2003, 31 (14), 4227-37. (Pubitemid 37442302)
    • (2003) Nucleic Acids Research , vol.31 , Issue.14 , pp. 4227-4237
    • Inagaki, Y.1    Blouin, C.2    Susko, E.3    Roger, A.J.4
  • 53
    • 0035049593 scopus 로고    scopus 로고
    • Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast
    • Munshi, R.; Kandl, K. A.; Carr-Schmid, A.; Whitacre, J. L.; Adams, A. E.; Kinzy, T. G. Overexpression of translation elongation factor 1α affects the organization and function of the actin cytoskeleton in yeast. Genetics 2001, 157 (4), 1425-36. (Pubitemid 32298814)
    • (2001) Genetics , vol.157 , Issue.4 , pp. 1425-1436
    • Munshi, R.1    Kandl, K.A.2    Carr-Schmid, A.3    Whitacre, J.L.4    Adams, A.E.M.5    Kinzy, T.G.6
  • 54
    • 33644873111 scopus 로고    scopus 로고
    • Loss of NAD(H) from swollen yeast mitochondria
    • Bradshaw, P. C.; Pfeiffer, D. R. Loss of NAD(H) from swollen yeast mitochondria. BMC Biochem. 2006, 7,3.
    • (2006) BMC Biochem. , vol.7 , pp. 3
    • Bradshaw, P.C.1    Pfeiffer, D.R.2
  • 55
    • 33750618079 scopus 로고    scopus 로고
    • Oral fluid proteolytic effects on histatin 5 structure and function
    • DOI 10.1016/j.archoralbio.2006.06.005, PII S0003996906001579
    • Helmerhorst, E. J.; Alagl, A. S.; Siqueira, W. L.; Oppenheim, F. G. Oral fluid proteolytic effects on histatin 5 structure and function. Arch. Oral Biol. 2006, 51 (12), 1061-70. (Pubitemid 44692651)
    • (2006) Archives of Oral Biology , vol.51 , Issue.12 , pp. 1061-1070
    • Helmerhorst, E.J.1    Alagl, A.S.2    Siqueira, W.L.3    Oppenheim, F.G.4


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