메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

Actinomycetes: A repertory of green catalysts with a potential revenue resource

Author keywords

[No Author keywords available]

Indexed keywords

AMYLASE; BACTERIAL ENZYME; CELLULASE; CHITINASE; GLUCOSE OXIDASE; INDUSTRIAL ENZYME; LIPOXYGENASE; PEROXIDASE; PHYTASE; POLYGALACTURONASE; PROTEINASE; TRIACYLGLYCEROL LIPASE; XYLAN ENDO 1,3 BETA XYLOSIDASE; ENZYME;

EID: 84877252497     PISSN: 23146133     EISSN: 23146141     Source Type: Journal    
DOI: 10.1155/2013/264020     Document Type: Review
Times cited : (70)

References (58)
  • 2
    • 84877260933 scopus 로고    scopus 로고
    • http://naturebiochem.com/downloads/Enzymes-Pharma-applications
  • 3
    • 84877293258 scopus 로고    scopus 로고
    • http://ec.europa.eu/food/fs/sc/scan/out85-en.pdf
  • 5
    • 84877276228 scopus 로고    scopus 로고
    • Collection of information on enzymes, Final Report "Collection of Information on Enzymes", 2002
    • Collection of information on enzymes, Final Report "Collection of Information on Enzymes" 2002, http://ec.europa.eu/environment/archives/ dansub/pdfs/enzymerepcomplete.pdf
  • 7
    • 80053101081 scopus 로고    scopus 로고
    • Cloning, expression and characterization of an alkaline thermostable GH9 endoglucanase from Thermobifida halotolerans YIM, 90462 T
    • Zhang F., Chen J. J., Ren W. Z., Nie G. X., Ming H., Tang S. K., Li W. J., Cloning, expression and characterization of an alkaline thermostable GH9 endoglucanase from Thermobifida halotolerans YIM, 90462 T. Bioresource Technology 2011 102 21 10143 10146
    • (2011) Bioresource Technology , vol.102 , Issue.21 , pp. 10143-10146
    • Zhang, F.1    Chen, J.J.2    Ren, W.Z.3    Nie, G.X.4    Ming, H.5    Tang, S.K.6    Li, W.J.7
  • 9
    • 0035314559 scopus 로고    scopus 로고
    • Studies on carboxymethyl cellulase produced by an alkalothermophilic actinomycete
    • DOI 10.1016/S0960-8524(00)00150-4, PII S0960852400001504
    • George S. P., Ahmad A., Rao M. B., Studies on carboxymethyl cellulase produced by an alkalothermophilic actinomycete. Bioresource Technology 2001 77 2 171 175 2-s2.0-0035314559 10.1016/S0960-8524(00)00150-4 (Pubitemid 32012531)
    • (2001) Bioresource Technology , vol.77 , Issue.2 , pp. 171-175
    • George, S.P.1    Ahmad, A.2    Rao, M.B.3
  • 10
    • 77957997241 scopus 로고    scopus 로고
    • Optimization, economization and characterization of cellulase produced by marine Streptomyces ruber
    • 2-s2.0-77957997241
    • El-Sersy N. A., Abd-Elnaby H., Abou-Elela G. M., Ibrahim H. A. H., El-Toukhy N. M. K., Optimization, economization and characterization of cellulase produced by marine Streptomyces ruber. African Journal of Biotechnology 2010 9 38 6355 6364 2-s2.0-77957997241
    • (2010) African Journal of Biotechnology , vol.9 , Issue.38 , pp. 6355-6364
    • El-Sersy, N.A.1    Abd-Elnaby, H.2    Abou-Elela, G.M.3    Ibrahim, H.A.H.4    El-Toukhy, N.M.K.5
  • 12
    • 79955975799 scopus 로고    scopus 로고
    • Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw
    • 2-s2.0-79955975799 10.1186/1754-6834-4-12
    • Zhang J., Siika-Aho M., Puranen T., Tang M., Tenkanen M., Viikari L., Thermostable recombinant xylanases from Nonomuraea flexuosa and Thermoascus aurantiacus show distinct properties in the hydrolysis of xylans and pretreated wheat straw. Biotechnology for Biofuels 2011 4, article 12 2-s2.0-79955975799 10.1186/1754-6834-4-12
    • (2011) Biotechnology for Biofuels , vol.412
    • Zhang, J.1    Siika-Aho, M.2    Puranen, T.3    Tang, M.4    Tenkanen, M.5    Viikari, L.6
  • 14
    • 84877247149 scopus 로고    scopus 로고
    • Efficient utilization of xylanase and lipase producing thermophilic marine actinomycetes (Streptomyces albus and Streptomyces hygroscopicus) in the production of ecofriendly alternative energy from waste
    • Priya B. S., Stalin T., Selvam K., Efficient utilization of xylanase and lipase producing thermophilic marine actinomycetes (Streptomyces albus and Streptomyces hygroscopicus) in the production of ecofriendly alternative energy from waste. African Journal of Biotechnology 2012 11 78 14320 14325
    • (2012) African Journal of Biotechnology , vol.11 , Issue.78 , pp. 14320-14325
    • Priya, B.S.1    Stalin, T.2    Selvam, K.3
  • 16
    • 44349160190 scopus 로고    scopus 로고
    • Statistical optimization of α-amylase production by Streptomyces erumpens MTCC 7317 cells in calcium alginate beads using response surface methodology
    • Kar S., Ray R. C., Statistical optimization of α -amylase production by Streptomyces erumpens MTCC 7317 cells in calcium alginate beads using response surface methodology. Polish Journal of Microbiology 2008 57 1 49 57 2-s2.0-44349160190 (Pubitemid 351729694)
    • (2008) Polish Journal of Microbiology , vol.57 , Issue.1 , pp. 49-57
    • Kar, S.1    Ray, R.C.2
  • 17
    • 0242473815 scopus 로고    scopus 로고
    • Production and characterization of a thermostable α -amylase from Nocardiopsis sp. endophyte of yam bean
    • 2-s2.0-0242473815 10.1016/S0960-8524(00)00089-4
    • Stamford T. L. M., Stamford N. P., Coelho L. C. B. B., Araújo J. M., Production and characterization of a thermostable α -amylase from Nocardiopsis sp. endophyte of yam bean. Bioresource Technology 2001 76 2 137 141 2-s2.0-0242473815 10.1016/S0960-8524(00)00089-4
    • (2001) Bioresource Technology , vol.76 , Issue.2 , pp. 137-141
    • Stamford, T.L.M.1    Stamford, N.P.2    Coelho, L.C.B.B.3    Araújo, J.M.4
  • 18
    • 3142642544 scopus 로고    scopus 로고
    • Purification and properties of a maltotriose-producing α-amylase from Thermobifida fusca
    • DOI 10.1016/j.enzmictec.2004.05.004, PII S0141022904001310
    • Yang C.-H., Liu W.-H., Purification and properties of a maltotriose-producing alpha-amylase from Thermobifida fusca. Enzyme and Microbial Technology 2004 35 254 260 (Pubitemid 38901003)
    • (2004) Enzyme and Microbial Technology , vol.35 , Issue.2-3 , pp. 254-260
    • Yang, C.-H.1    Liu, W.-H.2
  • 19
    • 80051642813 scopus 로고    scopus 로고
    • An overview of cold-active microbial alpha-amylase: Adaptation strategies and biotechnological potentials
    • Kuddus M., Roohi J. M., Arif J. M., Ramteke P. W., An overview of cold-active microbial alpha-amylase: adaptation strategies and biotechnological potentials. Biotechnology 2011 10 246 258
    • (2011) Biotechnology , vol.10 , pp. 246-258
    • Kuddus, M.1    Roohi, J.M.2    Arif, J.M.3    Ramteke, P.W.4
  • 20
    • 43849085759 scopus 로고    scopus 로고
    • Purification and partial characterization of polygalacturonase from Streptomyces lydicus
    • DOI 10.1016/j.biortech.2007.10.002, PII S0960852407008395
    • Jacob N., Asha Poorna C., Prema P., Purification and partial characterization of polygalacturonase from Streptomyces lydicus. Bioresource Technology 2008 99 14 6697 6701 2-s2.0-43849085759 10.1016/j.biortech.2007.10. 002 (Pubitemid 351697711)
    • (2008) Bioresource Technology , vol.99 , Issue.14 , pp. 6697-6701
    • Jacob, N.1    Asha Poorna, C.2    Prema, P.3
  • 21
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles: Some applications of their products for biotechnology
    • 2-s2.0-0032712358
    • Horikoshi K., Alkaliphiles: some applications of their products for biotechnology. Microbiology and Molecular Biology Reviews 1999 63 4 735 750 2-s2.0-0032712358
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.4 , pp. 735-750
    • Horikoshi, K.1
  • 23
    • 29244457833 scopus 로고    scopus 로고
    • An extracellular protease with depilation activity from Streptomyces nogalator
    • Mitra P., Chakrabartty P. K., An extracellular protease with depilation activity from Streptomyces nogalator. Journal of Scientific and Industrial Research 2005 64 12 978 983 2-s2.0-29244457833 (Pubitemid 41825413)
    • (2005) Journal of Scientific and Industrial Research , vol.64 , Issue.12 , pp. 978-983
    • Mitra, P.1    Chakrabartty, P.K.2
  • 24
    • 48349145890 scopus 로고    scopus 로고
    • Bacterial keratinases: Useful enzymes for bioprocessing agroindustrial wastes and beyond
    • 2-s2.0-48349145890 10.1007/s11947-007-0025-y
    • Brandelli A., Bacterial keratinases: useful enzymes for bioprocessing agroindustrial wastes and beyond. Food and Bioprocess Technology 2008 1 2 105 116 2-s2.0-48349145890 10.1007/s11947-007-0025-y
    • (2008) Food and Bioprocess Technology , vol.1 , Issue.2 , pp. 105-116
    • Brandelli, A.1
  • 25
    • 77954536499 scopus 로고    scopus 로고
    • Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents
    • 2-s2.0-77954536499 10.1016/j.biortech.2010.05.066
    • Jaouadi B., Abdelmalek B., Fodil D., Ferradji F. Z., Rekik H., Zaraî N., Bejar S., Purification and characterization of a thermostable keratinolytic serine alkaline proteinase from Streptomyces sp. strain AB1 with high stability in organic solvents. Bioresource Technology 2010 101 21 8361 8369 2-s2.0-77954536499 10.1016/j.biortech.2010.05.066
    • (2010) Bioresource Technology , vol.101 , Issue.21 , pp. 8361-8369
    • Jaouadi, B.1    Abdelmalek, B.2    Fodil, D.3    Ferradji, F.Z.4    Rekik, H.5    Zaraî, N.6    Bejar, S.7
  • 26
    • 33947230782 scopus 로고    scopus 로고
    • Bacterial chitinases: Properties and potential
    • DOI 10.1080/07388550601168223, PII 773237085
    • Bhattacharya D., Nagpure A., Gupta R. K., Bacterial chitinases: properties and potential. Critical Reviews in Biotechnology 2007 27 1 21 28 2-s2.0-33947230782 10.1080/07388550601168223 (Pubitemid 46425932)
    • (2007) Critical Reviews in Biotechnology , vol.27 , Issue.1 , pp. 21-28
    • Bhattacharya, D.1    Nagpure, A.2    Gupta, R.K.3
  • 27
    • 0036444826 scopus 로고    scopus 로고
    • Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2
    • DOI 10.1046/j.1365-2672.2002.01766.x
    • Nawani N. N., Kapadnis B. P., Das A. D., Rao A. S., Mahajan S. K., Purification and characterization of a thermophilic and acidophilic chitinase from Microbispora sp. V2. Journal of Applied Microbiology 2002 93 6 965 975 2-s2.0-0036444826 10.1046/j.1365-2672.2002.01766.x (Pubitemid 35408571)
    • (2002) Journal of Applied Microbiology , vol.93 , Issue.6 , pp. 965-975
    • Nawani, N.N.1    Kapadnis, B.P.2    Das, A.D.3    Rao, A.S.4    Mahajan, S.K.5
  • 28
    • 84877267438 scopus 로고    scopus 로고
    • 2011
    • 2011, http://www.reportlinker.com/p0747897-summary/World-Enzymes- Industry.html
  • 29
    • 84877257814 scopus 로고    scopus 로고
    • Industry Study with Forecasts for 2015 and 2020
    • The Freedonia group, Industry Study with Forecasts for 2015 and 2020. Study 2011 2824
    • (2011) Study , Issue.2824
    • Freedonia Group, T.1
  • 30
    • 84877300639 scopus 로고    scopus 로고
    • Global markets for enzymes in industrial applications (BIO030G)
    • Dewan S. S., Global markets for enzymes in industrial applications (BIO030G). BCC Research, 2011
    • (2011) BCC Research
    • Dewan, S.S.1
  • 31
    • 84877268865 scopus 로고    scopus 로고
    • Global Markets and Technologies for Biofuel Enzymes (EGY099A)
    • Dewan S. S., Global Markets and Technologies for Biofuel Enzymes (EGY099A). BCC Research, 2012
    • (2012) BCC Research
    • Dewan, S.S.1
  • 32
    • 84877290496 scopus 로고    scopus 로고
    • World Intellectual Property Organization
    • World Intellectual Property Organization, http://www.wipo.int
  • 33
    • 84877248466 scopus 로고    scopus 로고
    • http://www.specialtyenzymes.com/seb-group-usa
  • 34
    • 84877261590 scopus 로고    scopus 로고
    • 2010
    • 2010, http://www.newstatesman.com/healthcare-and-pharmaceuticals/2010/11/ specialty-enzymes-global
  • 35
    • 84877302543 scopus 로고    scopus 로고
    • 2012
    • 2012, http://forbesindia.com/article/breakpoint/novozyme-makes-enzymes- for-a-better-lifes/32760/1
  • 36
    • 77149175624 scopus 로고    scopus 로고
    • Isolation and characterization of marine antagonistic actinomycetes from west coast of India
    • Remya M., Vijayakumar R., Isolation and characterization of marine antagonistic actinomycetes from west coast of India. Medicine and Biology 2008 15 1 13 19
    • (2008) Medicine and Biology , vol.15 , Issue.1 , pp. 13-19
    • Remya, M.1    Vijayakumar, R.2
  • 37
    • 15044360123 scopus 로고    scopus 로고
    • Thermostable cellulases from Streptomyces sp.: Scale-up production in a 50-l fermenter
    • DOI 10.1007/s10529-004-8356-5
    • Jang H. D., Chang K. S., Thermostable cellulases from Streptomyces sp.: scale-up production in a 50-l fermenter. Biotechnology Letters 2005 27 4 239 242 2-s2.0-15044360123 10.1007/s10529-004-8356-5 (Pubitemid 40374624)
    • (2005) Biotechnology Letters , vol.27 , Issue.4 , pp. 239-242
    • Jang, H.-D.1    Chang, K.-S.2
  • 38
    • 84856466552 scopus 로고    scopus 로고
    • Cellulase Enzyme Production by Streptomyces Sp. Using Fruit Waste as Substrate
    • Rathan R. K., Ambili M., Cellulase Enzyme Production by Streptomyces Sp. Using Fruit Waste as Substrate. Australian Journal of Basic and Applied Sciences 2011 5 12 1114 1118
    • (2011) Australian Journal of Basic and Applied Sciences , vol.5 , Issue.12 , pp. 1114-1118
    • Rathan, R.K.1    Ambili, M.2
  • 39
    • 31744446283 scopus 로고    scopus 로고
    • Production of xylanases by Streptomyces species and their bleaching effect on rice straw pulp
    • Rifaat H. M., Nagieb Z. A., Ahmed Y. M., Production of xylanases by Streptomyces species and their bleaching effect on rice straw pulp. Applied Ecology and Environmental Research 2006 4 1 151 160 2-s2.0-31744446283 (Pubitemid 43175684)
    • (2006) Applied Ecology and Environmental Research , vol.4 , Issue.1 , pp. 151-160
    • Rifaat, H.M.1    Nagieb, Z.A.2    Ahmed, Y.M.3
  • 40
    • 79953267462 scopus 로고    scopus 로고
    • Single step purification and characterization of a thermostable and calcium independent α -amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam hot spring reservoir, Gujarat (India)
    • 2-s2.0-79953267462 10.1016/j.ijbiomac.2011.02.010
    • Kikani B. A., Singh S. P., Single step purification and characterization of a thermostable and calcium independent α -amylase from Bacillus amyloliquifaciens TSWK1-1 isolated from Tulsi Shyam hot spring reservoir, Gujarat (India). International Journal of Biological Macromolecules 2011 48 4 676 681 2-s2.0-79953267462 10.1016/j.ijbiomac.2011.02.010
    • (2011) International Journal of Biological Macromolecules , vol.48 , Issue.4 , pp. 676-681
    • Kikani, B.A.1    Singh, S.P.2
  • 41
    • 0035216323 scopus 로고    scopus 로고
    • Antimicrobial effect of chitooligosaccharides produced by bioreactor
    • DOI 10.1016/S0144-8617(00)00200-9
    • Jeon Y. J., Park P. J., Kim S. K., Antimicrobial effect of chitooligosaccharides produced by bioreactor. Carbohydrate Polymers 2001 44 1 71 76 2-s2.0-0035216323 10.1016/S0144-8617(00)00200-9 (Pubitemid 33375928)
    • (2001) Carbohydrate Polymers , vol.44 , Issue.1 , pp. 71-76
    • Jeon, Y.-J.1    Park, P.-J.2    Kim, S.-K.3
  • 42
    • 77950593857 scopus 로고    scopus 로고
    • Conversion of squid pen by Pseudomonas aeruginosa K187 fermentation for the production of N-acetyl chitooligosaccharides and biofertilizers
    • 2-s2.0-77950593857 10.1016/j.carres.2010.01.025
    • Wang S. L., Hsu W. H., Liang T. W., Conversion of squid pen by Pseudomonas aeruginosa K187 fermentation for the production of N-acetyl chitooligosaccharides and biofertilizers. Carbohydrate Research 2010 345 7 880 885 2-s2.0-77950593857 10.1016/j.carres.2010.01.025
    • (2010) Carbohydrate Research , vol.345 , Issue.7 , pp. 880-885
    • Wang, S.L.1    Hsu, W.H.2    Liang, T.W.3
  • 43
    • 33749239274 scopus 로고    scopus 로고
    • New model substrates for enzymes hydrolysing polyethyleneterephthalate and polyamide fibres
    • DOI 10.1016/j.jbbm.2006.02.005, PII S0165022X06000340, Proceedings of the 8th International Symposium on Instrumental Analysis
    • Heumann S., Eberl A., Pobeheim H., Liebminger S., Fischer-Colbrie G., Almansa E., Cavaco-Paulo A., Gübitz G. M., New model substrates for enzymes hydrolysing polyethyleneterephthalate and polyamide fibres. Journal of Biochemical and Biophysical Methods 2006 69 1-2 89 99 2-s2.0-33749239274 10.1016/j.jbbm.2006.02.005 (Pubitemid 44486418)
    • (2006) Journal of Biochemical and Biophysical Methods , vol.69 , Issue.1-2 , pp. 89-99
    • Heumann, S.1    Eberl, A.2    Pobeheim, H.3    Liebminger, S.4    Fischer-Colbrie, G.5    Almansa, E.6    Cavaco-Paulo, A.7    Gubitz, G.M.8
  • 44
    • 84877260706 scopus 로고    scopus 로고
    • Therapeutically active biomolecules from marine actinomycetes
    • Jayaprakashvel M., Therapeutically active biomolecules from marine actinomycetes. Journal of Modern Biotechnology 2012 1 1 1 7
    • (2012) Journal of Modern Biotechnology , vol.1 , Issue.1 , pp. 1-7
    • Jayaprakashvel, M.1
  • 47
    • 0036900864 scopus 로고    scopus 로고
    • Screening for novel enzymes for biocatalytic processes: Accessing the metagenome as a resource of novel functional sequence space
    • DOI 10.1016/S0958-1669(02)00345-2
    • Lorenz P., Liebeton K., Niehaus F., Eck J., Screening for novel enzymes for biocatalytic processes: accessing the metagenome as a resource of novel functional sequence space. Current Opinion in Biotechnology 2002 13 6 572 577 (Pubitemid 35448058)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.6 , pp. 572-577
    • Lorenz, P.1    Liebeton, K.2    Niehaus, F.3    Eck, J.4
  • 49
    • 0033904795 scopus 로고    scopus 로고
    • High-throughput screening of enzyme libraries
    • DOI 10.1016/S0958-1669(00)00108-7
    • Olsen M., Iverson B., Georgiou G., High-throughput screening of enzyme libraries. Current Opinion in Biotechnology 2000 11 4 331 337 2-s2.0-0033904795 10.1016/S0958-1669(00)00108-7 (Pubitemid 30598926)
    • (2000) Current Opinion in Biotechnology , vol.11 , Issue.4 , pp. 331-337
    • Olsen, M.1    Iverson, B.2    Georgiou, G.3
  • 50
    • 79958708794 scopus 로고    scopus 로고
    • Assessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis
    • 2-s2.0-79958708794 10.4155/fmc.11.48
    • Nannemann D. P., Birmingham W. R., Scism R. A., Bachmann B. O., Assessing directed evolution methods for the generation of biosynthetic enzymes with potential in drug biosynthesis. Future Medicinal Chemistry 2011 3 7 803 819 2-s2.0-79958708794 10.4155/fmc.11.48
    • (2011) Future Medicinal Chemistry , vol.3 , Issue.7 , pp. 803-819
    • Nannemann, D.P.1    Birmingham, W.R.2    Scism, R.A.3    Bachmann, B.O.4
  • 51
    • 73149119826 scopus 로고    scopus 로고
    • Ultrahigh-throughput FACS-based screening for directed enzyme evolution
    • 2-s2.0-73149119826 10.1002/cbic.200900384
    • Yang G., Withers S. G., Ultrahigh-throughput FACS-based screening for directed enzyme evolution. ChemBioChem 2009 10 17 2704 2715 2-s2.0-73149119826 10.1002/cbic.200900384
    • (2009) ChemBioChem , vol.10 , Issue.17 , pp. 2704-2715
    • Yang, G.1    Withers, S.G.2
  • 54
    • 84934439990 scopus 로고    scopus 로고
    • GFP reporter screens for the engineering of amino acid degrading enzymes from libraries expressed in bacteria
    • Paley O., Agnello G., Cantor J., Yoo T. H., Georgiou E Stone G., GFP reporter screens for the engineering of amino acid degrading enzymes from libraries expressed in bacteria. Methods in Molecular Biology 2013 978 31 44
    • (2013) Methods in Molecular Biology , vol.978 , pp. 31-44
    • Paley, O.1    Agnello, G.2    Cantor, J.3    Yoo, T.H.4    Georgiou Stone E, G.5
  • 55
    • 84873985413 scopus 로고    scopus 로고
    • Flow cytometry-based ultra-high-throughput screening assay for cellulase activity
    • Ostafe R., Prodanovic R., Commandeur U., Fischer R., Flow cytometry-based ultra-high-throughput screening assay for cellulase activity. Analytical Biochemsitry 2013 435 1 93 98
    • (2013) Analytical Biochemsitry , vol.435 , Issue.1 , pp. 93-98
    • Ostafe, R.1    Prodanovic, R.2    Commandeur, U.3    Fischer, R.4
  • 57
    • 84876253828 scopus 로고    scopus 로고
    • Sensitive, high throughput detection of proteins in individual, surfactant stabilized picoliter droplets using NanoESI mass spectrometry
    • 10.1021/ac400453t
    • Smith C., Li X., Mize T., Sharpe T., Graziani E. I., Abell C., Huck W. T., Sensitive, high throughput detection of proteins in individual, surfactant stabilized picoliter droplets using NanoESI mass spectrometry. Analytical Chemistry 2013 10.1021/ac400453t
    • (2013) Analytical Chemistry
    • Smith, C.1    Li, X.2    Mize, T.3    Sharpe, T.4    Graziani, E.I.5    Abell, C.6    Huck, W.T.7
  • 58
    • 58149102483 scopus 로고    scopus 로고
    • Development of predictive 3D-QSAR CoMFA and CoMSIA models for β -aminohydroxamic acid-derived tumor necrosis factor- α converting enzyme inhibitors
    • 2-s2.0-58149102483 10.1111/j.1747-0285.2008.00737.x
    • Murumkar P. R., Gupta S. D., Zambre V. P., Giridhar R., Yadav M. R., Development of predictive 3D-QSAR CoMFA and CoMSIA models for β -aminohydroxamic acid-derived tumor necrosis factor- α converting enzyme inhibitors. Chemical Biology and Drug Design 2009 73 1 97 107 2-s2.0-58149102483 10.1111/j.1747-0285.2008.00737.x
    • (2009) Chemical Biology and Drug Design , vol.73 , Issue.1 , pp. 97-107
    • Murumkar, P.R.1    Gupta, S.D.2    Zambre, V.P.3    Giridhar, R.4    Yadav, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.