메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

In Mycoplasma hominis the OppA-mediated cytoadhesion depends on its ATPase activity

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE INHIBITOR; OLIGOPEPTIDE; OPPA PROTEIN; PERMEASE; PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; LIPOPROTEIN; OLIGOPEPTIDE BINDING PROTEIN, BACTERIA; OLIGOPEPTIDE-BINDING PROTEIN, BACTERIA;

EID: 80051801145     PISSN: 14712180     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-11-185     Document Type: Article
Times cited : (28)

References (45)
  • 3
    • 0036065639 scopus 로고    scopus 로고
    • Choline-containing lipids in mycoplasmas
    • DOI 10.1016/S1286-4579(02)01622-2, PII S1286457902016222
    • Choline-containing lipids in mycoplasmas. Rottem S, Microbes Infect 2002 4 963 968 10.1016/S1286-4579(02)01622-2 12106789 (Pubitemid 34775238)
    • (2002) Microbes and Infection , vol.4 , Issue.9 , pp. 963-968
    • Rottem, S.1
  • 4
    • 4544363838 scopus 로고    scopus 로고
    • Mycoplasma fermentans binds to and invades HeLa cells: Involvement of plasminogen and urokinase
    • DOI 10.1128/IAI.72.9.5004-5011.2004
    • Mycoplasma fermentans binds to and invades HeLa cells: Involvement of plasminogen and urokinase. Yavlovich A, Katzenell A, Tarshis M, Higazi AAR, Rottem S, Infect Immun 2004 72 5004 5011 10.1128/IAI.72.9.5004-5011.2004 15321992 (Pubitemid 39223383)
    • (2004) Infection and Immunity , vol.72 , Issue.9 , pp. 5004-5011
    • Yavlovich, A.1    Katzenell, A.2    Tarshis, M.3    Higazi, A.A.-R.4    Rottem, S.5
  • 5
    • 0035812314 scopus 로고    scopus 로고
    • Characterization of Spiroplasma citri adhesion related protein SARP1, which contains a domain of a novel family designated sarpin
    • DOI 10.1016/S0378-1119(01)00655-2, PII S0378111901006552
    • Characterization of Spiroplasma citri adhesion related protein SARP1, which contains a domain of a novel family designated sarpin 1. Berg M, Melcher U, Fletcher J, Gene 2001 275 57 64 10.1016/S0378-1119(01)00655-2 11574152 (Pubitemid 32907326)
    • (2001) Gene , vol.275 , Issue.1 , pp. 57-64
    • Berg, M.1    Melcher, U.2    Fletcher, J.3
  • 7
    • 2142694393 scopus 로고    scopus 로고
    • Proteolytic Processing of the Mycoplasma hyopneumoniae Cilium Adhesin
    • DOI 10.1128/IAI.72.5.2791-2802.2004
    • Proteolytic processing of the Mycoplasma hyopneumoniae cilium adhesin. Djordjevic SP, Cordwell SJ, Djordjevic MA, Wilton J, Minion FC, Infect Immun 2004 72 2791 2802 10.1128/IAI.72.5.2791-2802.2004 15102789 (Pubitemid 38542407)
    • (2004) Infection and Immunity , vol.72 , Issue.5 , pp. 2791-2802
    • Djordjevic, S.P.1    Cordwell, S.J.2    Djordjevic, M.A.3    Wilton, J.4    Minion, F.C.5
  • 8
    • 0036720236 scopus 로고    scopus 로고
    • Identification and functional mapping of the mycoplasma fermentans P29 adhesin
    • 10.1128/IAI.70.9.4925-4935.2002 12183538
    • Identification and functional mapping of the mycoplasma fermentans P29 adhesin. Leigh SA, Wise KS, Infect Immun 2002 70 4925 4935 10.1128/IAI.70.9. 4925-4935.2002 12183538
    • (2002) Infect Immun , vol.70 , pp. 4925-4935
    • Leigh, S.A.1    Wise, K.S.2
  • 9
    • 67649313322 scopus 로고    scopus 로고
    • Oral vaccination against mycoplasmal pneumonia of swine using a live Erysipelothrix rhusiopathiae vaccine strain as a vector
    • 10.1016/j.vaccine.2009.04.081 19433128
    • Oral vaccination against mycoplasmal pneumonia of swine using a live Erysipelothrix rhusiopathiae vaccine strain as a vector. Ogawa Y, Oishi E, Muneta Y, Sano A, Hikono H, Shibahara T, Yagi Y, Shimoji Y, Vaccine 2009 27 4543 4550 10.1016/j.vaccine.2009.04.081 19433128
    • (2009) Vaccine , vol.27 , pp. 4543-4550
    • Ogawa, Y.1    Oishi, E.2    Muneta, Y.3    Sano, A.4    Hikono, H.5    Shibahara, T.6    Yagi, Y.7    Shimoji, Y.8
  • 10
    • 77954395126 scopus 로고    scopus 로고
    • RGD Motif of Lipoprotein T, Involved in Adhesion of Mycoplasma conjunctivae to Lamb Synovial Tissue Cells
    • 10.1128/JB.00253-10 20494988
    • RGD Motif of Lipoprotein T, Involved in Adhesion of Mycoplasma conjunctivae to Lamb Synovial Tissue Cells. Zimmermann L, Peterhans E, Frey J, J Bacteriol 2010 192 3773 3779 10.1128/JB.00253-10 20494988
    • (2010) J Bacteriol , vol.192 , pp. 3773-3779
    • Zimmermann, L.1    Peterhans, E.2    Frey, J.3
  • 12
    • 0029885953 scopus 로고    scopus 로고
    • Molecular basis of size and antigenic variation of a Mycoplasma hominis adhesin encoded by divergent vaa genes
    • Molecular basis of size and antigenic variation of a Mycoplasma hominis adhesin encoded by divergent vaa genes 1. Zhang QJ, Wise KS, Infect Immun 1996 64 2737 2744 8698503 (Pubitemid 26226841)
    • (1996) Infection and Immunity , vol.64 , Issue.7 , pp. 2737-2744
    • Zhang, Q.1    Wise, K.S.2
  • 13
    • 0032855674 scopus 로고    scopus 로고
    • The adherence-associated lipoprotein P100, encoded by an opp operon structure, functions as the oligopeptide-binding domain OppA of a putative oligopeptide transport system in Mycoplasma hominis
    • The adherence-associated lipoprotein P100, encoded by an opp operon structure, functions as the oligopeptide-binding domain OppA of a putative oligopeptide transport system in Mycoplasma hominis. Henrich B, Hopfe M, Kitzerow A, Hadding U, J Bacteriol 1999 181 4873 4878 10438757 (Pubitemid 29383516)
    • (1999) Journal of Bacteriology , vol.181 , Issue.16 , pp. 4873-4878
    • Henrich, B.1    Hopfe, M.2    Kitzerow, A.3    Hadding, U.4
  • 14
    • 1142310718 scopus 로고    scopus 로고
    • OppA, the Substrate-Binding Subunit of the Oligopeptide Permease, Is the Major Ecto-ATPase of Mycoplasma hominis
    • DOI 10.1128/JB.186.4.1021-1028.2004
    • OppA, the substrate-binding subunit of the oligopeptide permease, is the major ecto-ATPase of Mycoplasma hominis. Hopfe M, Henrich B, J Bacteriol 2004 186 1021 1028 10.1128/JB.186.4.1021-1028.2004 14761996 (Pubitemid 38209461)
    • (2004) Journal of Bacteriology , vol.186 , Issue.4 , pp. 1021-1028
    • Hopfe, M.1    Henrich, B.2
  • 15
    • 42249114677 scopus 로고    scopus 로고
    • OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells
    • OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells. Hopfe M, Henrich B, BMC Microbiol 2008 8
    • (2008) BMC Microbiol , vol.8
    • Hopfe, M.1    Henrich, B.2
  • 16
    • 33846688359 scopus 로고    scopus 로고
    • Structure and function of ABC transporters: The ATP switch provides flexible control
    • DOI 10.1007/s00424-006-0126-x, 20 years of ABC transporters
    • Structure and function of ABC transporters: the ATP switch provides flexible control. Linton KJ, Higgins CF, Pflugers Arch 2007 453 555 567 10.1007/s00424-006-0126-x 16937116 (Pubitemid 46192529)
    • (2007) Pflugers Archiv European Journal of Physiology , vol.453 , Issue.5 , pp. 555-567
    • Linton, K.J.1    Higgins, C.F.2
  • 17
    • 0001607723 scopus 로고
    • Distantly Related Sequences in the Alpha-Subunits and Beta-Subunits of Atp Synthase, Myosin, Kinases and Other Atp-Requiring Enzymes and A Common Nucleotide Binding Fold
    • 6329717
    • Distantly Related Sequences in the Alpha-Subunits and Beta-Subunits of Atp Synthase, Myosin, Kinases and Other Atp-Requiring Enzymes and A Common Nucleotide Binding Fold. Walker JE, Saraste M, Runswick MJ, Gay NJ, EMBO J 1982 1 945 951 6329717
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 18
    • 4644247731 scopus 로고    scopus 로고
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer
    • DOI 10.1016/j.jmb.2004.08.023, PII S0022283604010010
    • STAND, a class of P-loop NTPases including animal and plant regulators of programmed cell death: Multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer 1. Lelpe DD, Koonin EV, Aravind L, J Mol Biol 2004 343 1 28 10.1016/j.jmb.2004.08.023 15381417 (Pubitemid 39294573)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.1 , pp. 1-28
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 19
    • 0035033156 scopus 로고    scopus 로고
    • Ectonucleotidases: Some recent developments and a note on nomenclature
    • DOI 10.1002/ddr.1097
    • Ectonucleotidases: Some recent developments and a note on nomenclature. Zimmermann H, Drug Dev Res 2001 52 44 56 10.1002/ddr.1097 (Pubitemid 32401923)
    • (2001) Drug Development Research , vol.52 , Issue.1-2 , pp. 44-56
    • Zimmermann, H.1
  • 20
    • 0025177280 scopus 로고
    • Ecto-Atpase Activity in Cytolytic Lymphocytes-T - Protection from the Cytolytic Effects of Extracellular Atp
    • 2136737
    • Ecto-Atpase Activity in Cytolytic Lymphocytes-T-Protection from the Cytolytic Effects of Extracellular Atp. Filippini A, Taffs RE, Agui T, Sitkovsky MV, J Biol Chem 1990 265 334 340 2136737
    • (1990) J Biol Chem , vol.265 , pp. 334-340
    • Filippini, A.1    Taffs, R.E.2    Agui, T.3    Sitkovsky, M.V.4
  • 21
    • 0025721115 scopus 로고
    • Comparative-Studies of the Cytotoxic Lymphocyte-T-Mediated Cytotoxicity and of Extracellular Atp-Induced Cell-Lysis - Different Requirements in Extracellular Mg2+ and Ph
    • 1940362
    • Comparative-Studies of the Cytotoxic Lymphocyte-T-Mediated Cytotoxicity and of Extracellular Atp-Induced Cell-Lysis-Different Requirements in Extracellular Mg2+ and Ph. Redegeld F, Filippini A, Sitkovsky M, J Immunol 1991 147 3638 3645 1940362
    • (1991) J Immunol , vol.147 , pp. 3638-3645
    • Redegeld, F.1    Filippini, A.2    Sitkovsky, M.3
  • 22
    • 0028967657 scopus 로고
    • Ecto-Atpases - Identities and Functions
    • 7721538
    • Ecto-Atpases-Identities and Functions. Plesner L, Int Rev Cytol 1995 158 141 214 7721538
    • (1995) Int Rev Cytol , vol.158 , pp. 141-214
    • Plesner, L.1
  • 23
    • 33745357465 scopus 로고    scopus 로고
    • Stage-specific expression of P2Y receptors, ecto-apyrase, and ecto-5'-nucleotidase in myeloid leukocytes
    • Stage-specific expression of P2Y receptors, ecto-apyrase, and ecto-5'-nucleotidase in myeloid leukocytes. Clifford EE, Martin KA, Dalal P, Thomas R, Dubyak GR, Am J Physiol 1997 42 973 C987
    • (1997) Am J Physiol , vol.42
    • Clifford, E.E.1    Martin, K.A.2    Dalal, P.3    Thomas, R.4    Dubyak, G.R.5
  • 24
    • 0027661421 scopus 로고
    • Signal-Transduction via P2-Purinergic Receptors for Extracellular Atp and Other Nucleotides
    • 8214015
    • Signal-Transduction via P2-Purinergic Receptors for Extracellular Atp and Other Nucleotides. Dubyak GR, Elmoatassim C, Am J Physiol 1993 265 577 C606 8214015
    • (1993) Am J Physiol , vol.265
    • Dubyak, G.R.1    Elmoatassim, C.2
  • 25
    • 0242266131 scopus 로고    scopus 로고
    • Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction
    • DOI 10.1007/s00436-003-0965-8
    • Ecto-ATPase activity on the surface of Trypanosoma cruzi and its possible role in the parasite-host cell interaction. Bisaggio DFR, Peres-Sampaio CE, Meyer-Fernandes JR, Souto-Padron T, Parasitol Res 2003 91 273 282 10.1007/s00436-003-0965-8 14574556 (Pubitemid 37363621)
    • (2003) Parasitology Research , vol.91 , Issue.4 , pp. 273-282
    • Bisaggio, D.F.R.1    Peres-Sampaio, C.E.2    Meyer-Fernandes, J.R.3    Souto-Padron, T.4
  • 26
    • 0025903550 scopus 로고
    • Expression, Distribution, and Biochemistry of Human Cd39 - Role in Activation-Associated Homotypic Adhesion of Lymphocytes
    • 1672348
    • Expression, Distribution, and Biochemistry of Human Cd39-Role in Activation-Associated Homotypic Adhesion of Lymphocytes. Kansas GS, Wood GS, Tedder TF, J Immunol 1991 146 2235 2244 1672348
    • (1991) J Immunol , vol.146 , pp. 2235-2244
    • Kansas, G.S.1    Wood, G.S.2    Tedder, T.F.3
  • 27
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • DOI 10.1016/j.febslet.2005.11.079, PII S0014579305014572, ABC Transporters
    • ABC transporter architecture and regulatory roles of accessory domains. Biemans-Oldehinkel E, Doeven MK, Poolman B, FEBS Lett 2006 580 1023 1035 10.1016/j.febslet.2005.11.079 16375896 (Pubitemid 43186038)
    • (2006) FEBS Letters , vol.580 , Issue.4 , pp. 1023-1035
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 29
    • 0019973403 scopus 로고
    • Adherence of Mycoplasmas - Phenomena and Possible Role in the Pathogenesis of Disease
    • 10.1007/BF01640779 6809638
    • Adherence of Mycoplasmas-Phenomena and Possible Role in the Pathogenesis of Disease. Bredt W, Feldner J, Klaus B, Infection 1982 10 199 202 10.1007/BF01640779 6809638
    • (1982) Infection , vol.10 , pp. 199-202
    • Bredt, W.1    Feldner, J.2    Klaus, B.3
  • 30
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • DOI 10.1016/j.jmb.2003.08.040
    • Evolution and classification of P-loop kinases and related proteins. Leipe DD, Koonin EV, Aravind L, J Mol Biol 2003 333 781 815 10.1016/j.jmb.2003. 08.040 14568537 (Pubitemid 37268019)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 31
    • 79953297477 scopus 로고    scopus 로고
    • Cytoadherence-dependent induction of inflammatoryresponses by Mycoplasma pneumoniae
    • 10.1111/j.1365-2567.2011.03408.x
    • Cytoadherence-dependent induction of inflammatoryresponses by Mycoplasma pneumoniae. Shimizu TKYKK, Immunol 2011 133 51 61 10.1111/j.1365-2567.2011. 03408.x
    • (2011) Immunol , vol.133 , pp. 51-61
    • Shimizu, T.1
  • 32
    • 33749261659 scopus 로고    scopus 로고
    • Adenosine 5′-triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation
    • DOI 10.1016/j.pharmthera.2005.04.013, PII S0163725806000660
    • Adenosine 5'-triphosphate and adenosine as endogenous signaling molecules in immunity and inflammation. Bours MJL, Swennen ELR, Di Virgilio F, Cronstein BN, Dagnelie PC, Pharmacol Ther 2006 112 358 404 10.1016/j.pharmthera.2005.04. 013 16784779 (Pubitemid 44486409)
    • (2006) Pharmacology and Therapeutics , vol.112 , Issue.2 , pp. 358-404
    • Bours, M.J.L.1    Swennen, E.L.R.2    Di Virgilio, F.3    Cronstein, B.N.4    Dagnelie, P.C.5
  • 33
    • 34248349011 scopus 로고    scopus 로고
    • Effect of mycoplasmas on apoptosis of 32D cells is species-dependent
    • DOI 10.1007/s00284-006-0491-x
    • Effect of mycoplasmas on apoptosis of 32D cells is species- dependent. Zhang SM, Lo SC, Curr Microbiol 2007 54 388 395 10.1007/s00284-006-0491-x 17486403 (Pubitemid 46733875)
    • (2007) Current Microbiology , vol.54 , Issue.5 , pp. 388-395
    • Zhang, S.1    Lo, S.-C.2
  • 34
    • 67349167990 scopus 로고    scopus 로고
    • The P2X(7) receptor and intracellular pathogens: A continuing struggle
    • 10.1007/s11302-009-9130-x 19214779
    • The P2X(7) receptor and intracellular pathogens: a continuing struggle. Coutinho-Silva R, Correa G, Sater AA, Ojcius DM, Purinergic Signal 2009 5 197 204 10.1007/s11302-009-9130-x 19214779
    • (2009) Purinergic Signal , vol.5 , pp. 197-204
    • Coutinho-Silva, R.1    Correa, G.2    Sater, A.A.3    Ojcius, D.M.4
  • 35
    • 0030840444 scopus 로고    scopus 로고
    • 7) receptors
    • DOI 10.1016/S1074-7613(00)80364-7
    • ATP- induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X(7)) receptors. Lammas DA, Stober C, Harvey CJ, Kendrick N, Panchalingam S, Kumararatne DS, Immunity 1997 7 433 444 10.1016/S1074-7613(00) 80364-7 9324363 (Pubitemid 27446017)
    • (1997) Immunity , vol.7 , Issue.3 , pp. 433-444
    • Lammas, D.A.1    Stober, C.2    Harvey, C.J.3    Kendrick, N.4    Panchalingam, S.5    Kumararatne, D.S.6
  • 36
    • 0028136987 scopus 로고
    • Apoptosis, but Not Necrosis, of Infected Monocytes Is Coupled with Killing of Intracellular Bacillus-Calmette-Guerin
    • 10.1084/jem.180.4.1499 7931080
    • Apoptosis, But Not Necrosis, of Infected Monocytes Is Coupled with Killing of Intracellular Bacillus-Calmette-Guerin. Molloy A, Laochumroonvorapong P, Kaplan G, J Exp Med 1994 180 1499 1509 10.1084/jem.180.4.1499 7931080
    • (1994) J Exp Med , vol.180 , pp. 1499-1509
    • Molloy, A.1    Laochumroonvorapong, P.2    Kaplan, G.3
  • 37
    • 0026348862 scopus 로고
    • Intracellular locationof mycoplasmas in cultured cells demonstrated by immunocytochemistry and electronmicroscopy
    • 1768615
    • Intracellular locationof mycoplasmas in cultured cells demonstrated by immunocytochemistry and electronmicroscopy. Taylor-Robinson D, Davies HA, Sarathchandra P, Furr PM, Int J Exp Pathol 1991 72 705 714 1768615
    • (1991) Int J Exp Pathol , vol.72 , pp. 705-714
    • Taylor-Robinson, D.1    Davies, H.A.2    Sarathchandra, P.3    Furr, P.M.4
  • 38
    • 0035069028 scopus 로고    scopus 로고
    • Host and pathogen interaction during vaginal infection by Trichomonas vaginalis and Mycoplasma hominis or Ureaplasma urealyticum
    • DOI 10.1016/S0167-7012(01)00224-X, PII S016770120100224X
    • Host and pathogen interaction during vaginal infection by Trichomonas vaginalis and Mycoplasma hominis or Ureaplasma urealyticum. van der Schee C, Sluiters HJ, van der Meijden WI, van Beek P, Peerbooms P, Verbrugh H, van Belkum A, J Microbiol Methods 2001 45 61 67 10.1016/S0167-7012(01)00224-X 11295198 (Pubitemid 32268709)
    • (2001) Journal of Microbiological Methods , vol.45 , Issue.1 , pp. 61-67
    • Van Der Schee, C.1    Sluiters, H.J.F.2    Van Der Meijden, W.I.3    Van Beek, P.4    Peerbooms, P.5    Verbrugh, H.6    Van Belkum, A.7
  • 39
    • 33748998182 scopus 로고    scopus 로고
    • Mycoplasma hominis attaches to and locates intracellularly in human spermatozoa
    • DOI 10.1093/humrep/del032
    • Mycoplasma hominis attaches to and locates intracellularly in human spermatozoa. Diaz-Garcia FJ, Herrera-Mendoza AP, Giono-Cerezo S, Guerra-Infante FM, Hum Reprod 2006 21 1591 1598 10.1093/humrep/del032 16549424 (Pubitemid 44445041)
    • (2006) Human Reproduction , vol.21 , Issue.6 , pp. 1591-1598
    • Diaz-Garcia, F.J.1    Herrera-Mendoza, A.P.2    Giono-Cerezo, S.3    Guerra-Infante, F.M.4
  • 40
    • 0026531178 scopus 로고
    • Decreased Metabolism and Viability of Mycoplasma-Hominis Induced by Monoclonal Antibody-Mediated Agglutination
    • 1370272
    • Decreased Metabolism and Viability of Mycoplasma-Hominis Induced by Monoclonal Antibody-Mediated Agglutination. Feldmann RC, Henrich B, Kolbbachofen V, Hadding U, Infect Immun 1992 60 166 174 1370272
    • (1992) Infect Immun , vol.60 , pp. 166-174
    • Feldmann, R.C.1    Henrich, B.2    Kolbbachofen, V.3    Hadding, U.4
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding
    • A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding. Bradford MM, Anal Biochem 1976 7 248 254
    • (1976) Anal Biochem , vol.7 , pp. 248-254
    • Bradford, M.M.1
  • 42
    • 0014949207 scopus 로고
    • Cleavage of Structural Proteins during Assembly of Head of Bacteriophage-T4
    • 10.1038/227680a0 5432063
    • Cleavage of Structural Proteins During Assembly of Head of Bacteriophage-T4. Laemmli UK, Nature 1970 227 680 685 10.1038/227680a0 5432063
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • DOI 10.1016/0378-1119(89)90359-4
    • Engineering Hybrid Genes Without the Use of Restriction Enzymes-Gene-Splicing by Overlap Extension. Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR, Gene 1989 77 61 68 10.1016/0378-1119(89)90359-4 2744488 (Pubitemid 19125654)
    • (1989) Gene , vol.77 , Issue.1 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 45
    • 0022472836 scopus 로고
    • Enzyme-Linked-Immunosorbent-Assay for Adherence of Bacteria to Animal-Cells
    • 2877005
    • Enzyme-Linked-Immunosorbent-Assay for Adherence of Bacteria to Animal-Cells. Ofek I, Courtney HS, Schifferli DM, Beachey EH, J Clin Microbiol 1986 24 512 516 2877005
    • (1986) J Clin Microbiol , vol.24 , pp. 512-516
    • Ofek, I.1    Courtney, H.S.2    Schifferli, D.M.3    Beachey, E.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.