메뉴 건너뛰기




Volumn 362, Issue 9, 2015, Pages

Allicin from garlic inhibits the biofilm formation and urease activity of Proteus mirabilis in vitro

Author keywords

Allicin; Antimicrobial; Biofilm; Hemolysin; Proteus mirabilis; Urease

Indexed keywords

ALLICIN; HEMOLYSIN; UREASE; SULFINIC ACID DERIVATIVE;

EID: 84955165736     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1093/femsle/fnv049     Document Type: Article
Times cited : (46)

References (58)
  • 1
    • 0030765775 scopus 로고    scopus 로고
    • Allicin from garlic strongly inhibits cysteine proteinases and cytopathic effects of Entamoeba histolytica
    • Ankri S, Miron T, Rabinkov A, et al. Allicin from garlic strongly inhibits cysteine proteinases and cytopathic effects of Entamoeba histolytica. Antimicrob Agents Ch 1997;41:2286-8
    • (1997) Antimicrob Agents Ch. , vol.41 , pp. 2286-2288
    • Ankri, S.1    Miron, T.2    Rabinkov, A.3
  • 2
    • 79955608879 scopus 로고    scopus 로고
    • Conjugates of daidzeinalliinase as a targeted pro-drug enzyme system against ovarian carcinoma
    • Appel E, Rabinkov A, Neeman M, et al. Conjugates of daidzeinalliinase as a targeted pro-drug enzyme system against ovarian carcinoma. J Drug Target 2011;19:326-35
    • (2011) J Drug Target. , vol.19 , pp. 326-335
    • Appel, E.1    Rabinkov, A.2    Neeman, M.3
  • 3
    • 14844286972 scopus 로고    scopus 로고
    • Apoptotic killing of Bchronic lymphocytic leukemia tumor cells by allicin generated in situ using a rituximab-alliinase conjugate
    • Arditti FD, Rabinkov A, Miron T, et al. Apoptotic killing of Bchronic lymphocytic leukemia tumor cells by allicin generated in situ using a rituximab-alliinase conjugate. Mol Cancer Ther 2005;4:325-31
    • (2005) Mol Cancer Ther. , vol.4 , pp. 325-331
    • Arditti, F.D.1    Rabinkov, A.2    Miron, T.3
  • 4
    • 77956555178 scopus 로고    scopus 로고
    • Inhibition of streptolysin O by allicin-an active component of garlic
    • Arzanlou M, Bohlooli S. Inhibition of streptolysin O by allicin-an active component of garlic. J Med Microbiol 2010a;59:1044-9
    • (2010) J Med Microbiol. , vol.59 , pp. 1044-1049
    • Arzanlou, M.1    Bohlooli, S.2
  • 5
    • 71349087630 scopus 로고    scopus 로고
    • Introducing of green garlic plant as a new source of allicin
    • Arzanlou M, Bohlooli S. Introducing of green garlic plant as a new source of allicin. Food Chem 2010b;120:179-83
    • (2010) Food Chem. , vol.120 , pp. 179-183
    • Arzanlou, M.1    Bohlooli, S.2
  • 6
    • 79952362439 scopus 로고    scopus 로고
    • Allicin from garlic neutralizes the hemolytic activity of intra-and extra-cellular pneumolysin O in vitro
    • Arzanlou M, Bohlooli S, Jannati E, et al. Allicin from garlic neutralizes the hemolytic activity of intra-and extra-cellular pneumolysin O in vitro. Toxicon 2011;57:540-5
    • (2011) Toxicon , vol.57 , pp. 540-545
    • Arzanlou, M.1    Bohlooli, S.2    Jannati, E.3
  • 8
    • 80052721620 scopus 로고    scopus 로고
    • Garlic allicin as a potential agent for controlling oral pathogens
    • Bachrach G, Jamil A, Naor R, et al. Garlic allicin as a potential agent for controlling oral pathogens. J Med Food 2011;14: 1338-43
    • (2011) J Med Food. , vol.14 , pp. 1338-1343
    • Bachrach, G.1    Jamil, A.2    Naor, R.3
  • 9
    • 0031042034 scopus 로고    scopus 로고
    • Synthesis and activity of Helicobacter pylori urease and catalase at low pH
    • Bauerfeind P, Garner R, Dunn BE, et al. Synthesis and activity of Helicobacter pylori urease and catalase at low pH. Gut 1997;40:25-30
    • (1997) Gut. , vol.40 , pp. 25-30
    • Bauerfeind, P.1    Garner, R.2    Dunn, B.E.3
  • 10
    • 0034039960 scopus 로고    scopus 로고
    • Bacterial ureases in infectious diseases
    • Burne RA, Chen YY. Bacterial ureases in infectious diseases. Microbes Infect 2000;2:533-42
    • (2000) Microbes Infect. , vol.2 , pp. 533-542
    • Burne, R.A.1    Chen, Y.Y.2
  • 11
    • 34548454935 scopus 로고    scopus 로고
    • Antibacterial activity of allicin alone and in combination with beta-lactams against Staphylococcus spp. and Pseudomonas aeruginosa
    • Cai Y, Wang R, Pei F, et al. Antibacterial activity of allicin alone and in combination with beta-lactams against Staphylococcus spp. and Pseudomonas aeruginosa. J Antibiot 2007;60:335-8
    • (2007) J Antibiot. , vol.60 , pp. 335-338
    • Cai, Y.1    Wang, R.2    Pei, F.3
  • 12
    • 80051897122 scopus 로고    scopus 로고
    • Inhibition of development, swarming differentiation and virulence factors in Proteus mirabilis by an extract of Lithrea molleoides and its active principle (Z,Z)-5-(trideca-4',7'-dienyl)-resorcinol
    • Carpinella MC, DeBellis L, Joray MB, et al. Inhibition of development, swarming differentiation and virulence factors in Proteus mirabilis by an extract of Lithrea molleoides and its active principle (Z,Z)-5-(trideca-4',7'-dienyl)-resorcinol. Phytomedicine 2011;18:994-7
    • (2011) Phytomedicine. , vol.18 , pp. 994-997
    • Carpinella, M.C.1    DeBellis, L.2    Joray, M.B.3
  • 14
    • 84895867429 scopus 로고    scopus 로고
    • Anti-Proteus activity of some South African medicinal plants: Their potential for the prevention of rheumatoid arthritis
    • Cock IE, van Vuuren SF. Anti-Proteus activity of some South African medicinal plants: their potential for the prevention of rheumatoid arthritis. Inflammopharmacology 2014;22:23-36
    • (2014) Inflammopharmacology. , vol.22 , pp. 23-36
    • Cock, I.E.1    Van Vuuren, S.F.2
  • 15
    • 0033763785 scopus 로고    scopus 로고
    • Pathogenesis of Proteus mirabilis urinary tract infection
    • Coker C, Poore CA, Li X, et al. Pathogenesis of Proteus mirabilis urinary tract infection. Microbes Infect 2000;2:1497-505
    • (2000) Microbes Infect. , vol.2 , pp. 497-505
    • Coker, C.1    Poore, C.A.2    Li, X.3
  • 16
    • 79955755873 scopus 로고    scopus 로고
    • Fighting bacterial infections-future treatment options
    • Fernebro J. Fighting bacterial infections-future treatment options. Drug Resist Update 2011;14:125-39
    • (2011) Drug Resist Update. , vol.14 , pp. 125-139
    • Fernebro, J.1
  • 17
    • 77951659581 scopus 로고    scopus 로고
    • Ureases as a target for the treatment of gastric and urinary infections
    • Follmer C. Ureases as a target for the treatment of gastric and urinary infections. J Clin Pathol 2010;63:424-30
    • (2010) J Clin Pathol. , vol.63 , pp. 424-430
    • Follmer, C.1
  • 18
    • 0000817158 scopus 로고
    • Garlic chemistry: Stability of S-(2- propenyl)-2-propene-1-sulfinothioate (allicin) in blood, solvents, and simulated physiological fluids
    • Freeman F, Kodera Y. Garlic chemistry: Stability of S-(2- propenyl)-2-propene-1-sulfinothioate (allicin) in blood, solvents, and simulated physiological fluids. J Agr Food Chem 1995;43:2332-8
    • (1995) J Agr Food Chem. , vol.43 , pp. 2332-2338
    • Freeman, F.1    Kodera, Y.2
  • 19
    • 0024383733 scopus 로고
    • Optimization of a medium for the rapid urease test for detection of Campylobacter pylori in gastric antral biopsie
    • Goldie J, Veldhuyzen van Zanten SJ, Jalali S, et al. Optimization of a medium for the rapid urease test for detection of Campylobacter pylori in gastric antral biopsies. J Clin Microbiol 1989;27:2080-2
    • (1989) J Clin Microbiol. , vol.27 , pp. 2080-2082
    • Goldie, J.1    Veldhuyzen van Zanten, S.J.2    Jalali, S.3
  • 20
    • 0017238988 scopus 로고
    • The primary cause of infection-induced urinary stones
    • Griffith DP, Musher DM, Itin C. Urease. The primary cause of infection-induced urinary stones. Invest Urol 1976;13:346-50
    • (1976) Invest Urol. , vol.13 , pp. 346-350
    • Griffith, D.P.1    Musher, D.M.2    Itin, C.U.3
  • 22
    • 80053912099 scopus 로고    scopus 로고
    • Proteus mirabilis biofilms and catheterassociated urinary tract infections
    • Jacobsen SM, Shirtliff ME. Proteus mirabilis biofilms and catheterassociated urinary tract infections. Virulence 2011;2:460-5
    • (2011) Virulence. , Issue.2 , pp. 460-465
    • Jacobsen, S.M.1    Shirtliff, M.E.2
  • 23
    • 0025220411 scopus 로고
    • Construction of a urease-negative mutant of Proteus mirabilis: Analysis of virulence in a mouse model of ascending urinary tract infection
    • Jones BD, Lockatell CV, Johnson DE, et al. Construction of a urease-negative mutant of Proteus mirabilis: analysis of virulence in a mouse model of ascending urinary tract infection. Infect Immun 1990;58:1120-3
    • (1990) Infect Immun. , vol.58 , pp. 1120-1123
    • Jones, B.D.1    Lockatell, C.V.2    Johnson, D.E.3
  • 25
    • 82755189409 scopus 로고    scopus 로고
    • Comparison between allicin and fluconazole in Candida albicans biofilm inhibition and in suppression of HWP1 gene expression
    • Khodavandi A, Harmal NS, Alizadeh F, et al. Comparison between allicin and fluconazole in Candida albicans biofilm inhibition and in suppression of HWP1 gene expression. Phytomedicine 2011;19:56-63
    • (2011) Phytomedicine. , vol.19 , pp. 56-63
    • Khodavandi, A.1    Harmal, N.S.2    Alizadeh, F.3
  • 26
    • 84885961359 scopus 로고    scopus 로고
    • Characteristics of bacteremia caused by extended-spectrum beta-lactamase-producing Proteus mirabilis
    • Kurihara Y, Hitomi S, Oishi T, et al. Characteristics of bacteremia caused by extended-spectrum beta-lactamase-producing Proteus mirabilis. J Infect Chemother 2013;19:799-805
    • (2013) J Infect Chemother. , vol.19 , pp. 799-805
    • Kurihara, Y.1    Hitomi, S.2    Oishi, T.3
  • 27
    • 80053231200 scopus 로고    scopus 로고
    • Allicin reduces the production of alpha-toxin by Staphylococcus aureus
    • Leng BF, Qiu JZ, Dai XH, et al. Allicin reduces the production of alpha-toxin by Staphylococcus aureus. Molecules 2011;16: 7958-68
    • (2011) Molecules. , vol.16 , pp. 7958-7968
    • Leng, B.F.1    Qiu, J.Z.2    Dai, X.H.3
  • 28
    • 84886784548 scopus 로고    scopus 로고
    • Effects of allicin on the formation of Pseudomonas aeruginosa biofinm and the production of quorum-sensing controlled virulence factors
    • Lihua L, Jianhuit W, Jialini Y, et al. Effects of allicin on the formation of Pseudomonas aeruginosa biofinm and the production of quorum-sensing controlled virulence factors. Pol J Microbiol 2013;62:243-51
    • (2013) Pol J Microbiol. , vol.62 , pp. 243-251
    • Lihua, L.1    Jianhuit, W.2    Jialini, Y.3
  • 29
    • 0033973286 scopus 로고    scopus 로고
    • The mode of action of allicin: its ready permeability through phospholipid membranes may contribute to its biological activity
    • Miron T, Rabinkov A, Mirelman D, et al. The mode of action of allicin: its ready permeability through phospholipid membranes may contribute to its biological activity. Biochim Biophys Acta 2000;1463:20-30
    • (2000) Biochim Biophys Acta. , vol.1463 , pp. 20-30
    • Miron, T.1    Rabinkov, A.2    Mirelman, D.3
  • 30
    • 0025758569 scopus 로고
    • Cytotoxicity of the HpmA hemolysin and urease of Proteus mirabilis and Proteus vulgaris against cultured human renal proximal tubular epithelial cells
    • Mobley HL, Chippendale GR, Swihart KG, et al. Cytotoxicity of the HpmA hemolysin and urease of Proteus mirabilis and Proteus vulgaris against cultured human renal proximal tubular epithelial cells. Infect Immun 1991;59:2036-42
    • (1991) Infect Immun. , vol.59 , pp. 2036-2042
    • Mobley, H.L.1    Chippendale, G.R.2    Swihart, K.G.3
  • 31
    • 0023636563 scopus 로고
    • Urease-positive bacteriuria and obstruction of long-term urinary catheters
    • Mobley HL, Warren JW. Urease-positive bacteriuria and obstruction of long-term urinary catheters. J Clin Microbiol 1987;25:2216-7
    • (1987) J Clin Microbiol. , vol.25 , pp. 2216-2217
    • Mobley, H.L.1    Warren, J.W.2
  • 32
    • 84869086220 scopus 로고    scopus 로고
    • Integrons, betalactamase and qnr genes in multidrug resistant clinical isolates of Proteusmirabilis and P.vulgaris,
    • Mokracka J, Gruszczynska B, Kaznowski A. Integrons, betalactamase and qnr genes in multidrug resistant clinical isolates of Proteusmirabilis and P. vulgaris. APMIS 2012;120:950-8
    • (2012) APMIS. , vol.120 , pp. 950-958
    • Mokracka, J.1    Gruszczynska, B.2    Kaznowski, A.3
  • 33
    • 0031688581 scopus 로고    scopus 로고
    • The effect of urease inhibitors on the encrustation of urethral catheters
    • Morris NS, Stickler DJ. The effect of urease inhibitors on the encrustation of urethral catheters. APMIS 1998;26:275-9
    • (1998) APMIS. , vol.26 , pp. 275-279
    • Morris, N.S.1    Stickler, D.J.2
  • 34
    • 0016465937 scopus 로고
    • Role of urease in pyelonephritis resulting from urinary tract infection with Proteus
    • Musher DM, Griffith DP, Yawn D, et al. Role of urease in pyelonephritis resulting from urinary tract infection with Proteus. J Infect Dis 1975;131:177-81
    • (1975) J Infect Dis. , vol.131 , pp. 177-181
    • Musher, D.M.1    Griffith, D.P.2    Yawn, D.3
  • 35
    • 0027405296 scopus 로고
    • Potent inhibitory action of the gastric proton pump inhibitor lansoprazole against urease activity of Helicobacter pylori: Unique action selective for H.pylori cells
    • Nagata K, Satoh H, Iwahi T, et al. Potent inhibitory action of the gastric proton pump inhibitor lansoprazole against urease activity of Helicobacter pylori: unique action selective for H. pylori cells. Antimicrob Agents Ch 1993;37:769-74
    • (1993) Antimicrob Agents Ch. , vol.37 , pp. 769-774
    • Nagata, K.1    Satoh, H.2    Iwahi, T.3
  • 36
    • 0031707478 scopus 로고    scopus 로고
    • Urease plays an important role in the chemotactic motility of Helicobacter pylori in a viscous environment
    • Nakamura H, Yoshiyama H, Takeuchi H, et al. Urease plays an important role in the chemotactic motility of Helicobacter pylori in a viscous environment. Infect Immun 1998;66:4832-7
    • (1998) Infect Immun. , vol.66 , pp. 4832-4837
    • Nakamura, H.1    Yoshiyama, H.2    Takeuchi, H.3
  • 37
    • 0017123983 scopus 로고
    • A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe
    • Norris R, Brocklehurst K. A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe. Biochem J 1976;159:245-57
    • (1976) Biochem J. , vol.159 , pp. 245-257
    • Norris, R.1    Brocklehurst, K.2
  • 38
    • 34247221584 scopus 로고    scopus 로고
    • Effects of oregano, carvacrol and thymol on Staphylococcus aureus and Staphylococcus epidermidis biofilms
    • Nostro A, Sudano Roccaro A, Bisignano G, et al. Effects of oregano, carvacrol and thymol on Staphylococcus aureus and Staphylococcus epidermidis biofilms. J Med Microbiol 2007;56:519-23
    • (2007) J Med Microbiol. , vol.56 , pp. 519-523
    • Nostro, A.1    Sudano Roccaro, A.2    Bisignano, G.3
  • 40
    • 84888303148 scopus 로고    scopus 로고
    • Inhibition of biofilm development of uropathogens by curcumin, an anti-quorum sensing agent from Curcuma longa
    • Packiavathy IASV, Priya S, Pandia SK, et al. Inhibition of biofilm development of uropathogens by curcumin, an anti-quorum sensing agent from Curcuma longa. Food Chem 2014;148: 453-60
    • (2014) Food Chem. , vol.148 , pp. 453-460
    • Packiavathy, I.A.S.V.1    Priya, S.2    Pandia, S.K.3
  • 41
    • 23244464263 scopus 로고    scopus 로고
    • Biofilms and antimicrobial resistance
    • Patel R. Biofilms and antimicrobial resistance. Clin Orthop Relat R 2005;437:41-7
    • (2005) Clin Orthop Relat R. , vol.437 , pp. 41-47
    • Patel, R.1
  • 42
    • 17144464125 scopus 로고    scopus 로고
    • In vitro activity of allicin against Staphylococcus epidermidis and influence of subinhibitory concentrations on biofilm formation
    • Perez-Giraldo C, Cruz-Villalon G, Sanchez-Silos R, et al. In vitro activity of allicin against Staphylococcus epidermidis and influence of subinhibitory concentrations on biofilm formation. J Appl Microbiol 2003;95:709-11
    • (2003) J Appl Microbiol. , vol.95 , pp. 709-711
    • Perez-Giraldo, C.1    Cruz-Villalon, G.2    Sanchez-Silos, R.3
  • 43
    • 0032472767 scopus 로고    scopus 로고
    • The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins
    • Rabinkov A, Miron T, Konstantinovski L, et al. The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. Biochim Biophys Acta 1998;1379:233-44
    • (1998) Biochim Biophys Acta. , vol.1379 , pp. 233-244
    • Rabinkov, A.1    Miron, T.2    Konstantinovski, L.3
  • 44
    • 0025054422 scopus 로고
    • Nickel availability and urease expression in Proteus mirabilis
    • Rando D, Steglitz U, Morsdorf G, et al. Nickel availability and urease expression in Proteus mirabilis. Arch Microbiol 1990;154:428-32
    • (1990) Arch Microbiol. , vol.154 , pp. 428-432
    • Rando, D.1    Steglitz, U.2    Morsdorf, G.3
  • 45
    • 0035126237 scopus 로고    scopus 로고
    • Determination of allicin, S-allylcysteine and volatile metabolites of garlic in breath, plasma or simulated gastric fluids
    • Rosen RT, Hiserodt RD, Fukuda EK, et al. Determination of allicin, S-allylcysteine and volatile metabolites of garlic in breath, plasma or simulated gastric fluids. J Nutr 2001;131:968S-71S
    • (2001) J Nutr. , vol.131 , pp. 968S-971S
    • Rosen, R.T.1    Hiserodt, R.D.2    Fukuda, E.K.3
  • 46
    • 0022824215 scopus 로고
    • Cell invasiveness of Proteus mirabilis and Proteus vulgaris strains
    • Rozalski A, Dlugonska H, Kotelko K. Cell invasiveness of Proteus mirabilis and Proteus vulgaris strains. Arch Immunol Ther Ex 1986;34:505-12
    • (1986) Arch Immunol Ther Ex. , vol.34 , pp. 505-512
    • Rozalski, A.1    Dlugonska, H.2    Kotelko, K.3
  • 48
    • 0027196715 scopus 로고
    • Proteus mirabilis urease: histidine 320 of UreC is essential for urea hydrolysis and nickel ion binding within the native enzyme
    • Sriwanthana B, Mobley HL. Proteus mirabilis urease: histidine 320 of UreC is essential for urea hydrolysis and nickel ion binding within the native enzyme. Infect Immun 1993;61:2570-7
    • (1993) Infect Immun. , vol.61 , pp. 2570-2577
    • Sriwanthana, B.1    Mobley, H.L.2
  • 49
    • 53749104267 scopus 로고    scopus 로고
    • Quantification of Proteus mirabilis virulence factors and modulation by acylated homoserine lactones
    • Stankowska D, Kwinkowski M, Kaca W. Quantification of Proteus mirabilis virulence factors and modulation by acylated homoserine lactones. J Microbiol Immunol 2008;41:243-53
    • (2008) J Microbiol Immunol. , vol.41 , pp. 243-253
    • Stankowska, D.1    Kwinkowski, M.2    Kaca, W.3
  • 50
    • 0025374682 scopus 로고
    • Cytotoxic activity of the Proteus hemolysin HpmA
    • Swihart KG, Welch RA. Cytotoxic activity of the Proteus hemolysin HpmA. Infect Immun 1990;58:1861-9
    • (1990) Infect Immun. , vol.58 , pp. 1861-1869
    • Swihart, K.G.1    Welch, R.A.2
  • 51
    • 0141756326 scopus 로고    scopus 로고
    • Urease inhibitory activity of simple alpha,beta-unsaturated ketones
    • Tanaka T, Kawase M, Tani S. Urease inhibitory activity of simple alpha,beta-unsaturated ketones. Life Sci 2003;73:2985-90
    • (2003) Life Sci. , vol.73 , pp. 2985-2990
    • Tanaka, T.1    Kawase, M.2    Tani, S.3
  • 52
    • 0029114569 scopus 로고
    • Helicobacter pylori urease inhibition by rabeprazole, a proton pump inhibitor
    • TsuchiyaM, Imamura L, Park JB, et al. Helicobacter pylori urease inhibition by rabeprazole, a proton pump inhibitor. Biol Pharm Bull 1995;18:1053-6
    • (1995) Biol Pharm Bull. , vol.18 , pp. 1053-1056
    • Tsuchiya, M.1    Imamura, L.2    Park, J.B.3
  • 53
  • 54
    • 84919338477 scopus 로고    scopus 로고
    • Garlic revisited: antimicrobial activity of allicin-containing garlic extracts against Burkholderia cepacia comple
    • Wallock-Richards D, Doherty CJ, Doherty L, et al. Garlic revisited: antimicrobial activity of allicin-containing garlic extracts against Burkholderia cepacia complex. PLoS One 2014;9:e112726
    • (2014) PLoS One. , vol.9 , pp. 112726
    • Wallock-Richards, D.1    Doherty, C.J.2    Doherty, L.3
  • 55
    • 33750457654 scopus 로고    scopus 로고
    • Inhibition of swarming and virulence factor expression in Proteus mirabilis by resveratrol
    • Wang WB, Lai HC, Hsueh PR, et al. Inhibition of swarming and virulence factor expression in Proteus mirabilis by resveratrol. J Med Microbiol 2006;55:1313-21
    • (2006) J Med Microbiol. , vol.55 , pp. 1313-1321
    • Wang, W.B.1    Lai, H.C.2    Hsueh, P.R.3
  • 56
    • 84857815530 scopus 로고    scopus 로고
    • Antimicrobial activities against biofilm formed by Proteus mirabilis isolates from wound and urinary tract infections
    • Wasfi R, Abd El-Rahman OA, Mansour LE, et al. Antimicrobial activities against biofilm formed by Proteus mirabilis isolates from wound and urinary tract infections. Indian J Med Microbi 2012;30:76-80
    • (2012) Indian J Med Microbi. , vol.30 , pp. 76-80
    • Wasfi, R.1    Abd El-Rahman, O.A.2    Mansour, L.E.3
  • 57
    • 69249201386 scopus 로고    scopus 로고
    • Structural and functional studies of truncated hemolysin A from Proteus mirabilis
    • Weaver TM, Smith JA, Hocking JM, et al. Structural and functional studies of truncated hemolysin A from Proteus mirabilis. J Biol Chem 2009;284:22297-309
    • (2009) J Biol Che. , vol.284 , pp. 22297-22309
    • Weaver, T.M.1    Smith, J.A.2    Hocking, J.M.3
  • 58
    • 0001404835 scopus 로고
    • Enzyme inhibition by allicin, the active principle of garlic
    • Wills ED. Enzyme inhibition by allicin, the active principle of garlic. Biochem J 1956;63:514-20
    • (1956) Biochem J. , vol.63 , pp. 514-520
    • Wills, E.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.