-
1
-
-
43049115291
-
Trends in biotechnological production of fuel ethanol from different feedstocks
-
10.1016/j.biortech.2007.11.013 18158236
-
Trends in biotechnological production of fuel ethanol from different feedstocks. Sánchez OJ, Cardona CA, Bioresour Technol 2008 99 13 5270 5295 10.1016/j.biortech.2007.11.013 18158236
-
(2008)
Bioresour Technol
, vol.99
, Issue.13
, pp. 5270-5295
-
-
Sánchez, O.J.1
Cardona, C.A.2
-
2
-
-
36448945474
-
Cassava as an alternative feedstocks in the production of renewable transportation fuel
-
Cassava as an alternative feedstocks in the production of renewable transportation fuel. Shetty JK, Chotani G, Gang D, Bates D, Int Sugar J 2007 109 1307 3 11
-
(2007)
Int Sugar J
, vol.109
, Issue.1307
, pp. 3-11
-
-
Shetty, J.K.1
Chotani, G.2
Gang, D.3
Bates, D.4
-
3
-
-
77956806266
-
Application of microbial α-amylase in industry-A review
-
Application of microbial α-amylase in industry-a review. de Souza PM, Magalhues PO, Brazilian J Microbiol 2010 41 4 850 861
-
(2010)
Brazilian J Microbiol
, vol.41
, Issue.4
, pp. 850-861
-
-
De Souza, P.M.1
Magalhues, P.O.2
-
4
-
-
77949913204
-
α-Amylase: An ideal representative of thermostable enzymes
-
10.1007/s12010-009-8735-4 19763902
-
α-Amylase: an ideal representative of thermostable enzymes. Prakash O, Jaiswal N, Appl Biochem Biotechnol 2010 160 8 2401 2414 10.1007/s12010-009- 8735-4 19763902
-
(2010)
Appl Biochem Biotechnol
, vol.160
, Issue.8
, pp. 2401-2414
-
-
Prakash, O.1
Jaiswal, N.2
-
5
-
-
76349122941
-
Structure of Bacillus amyloliquefaciens α-amylase at high resolution: Implications for thermal stability
-
10.1107/S1744309109051938
-
Structure of Bacillus amyloliquefaciens α-amylase at high resolution: implications for thermal stability. Alikhajeh J, Khajeh K, Ranjbar B, Naderi-Manesh H, Lin YH, Liu E, Guan HH, Hsieh YC, Chuankhayan P, Huang YC, Jeyaraman J, Liu MY, Chen CJ, Acta Crystallograph Sect F Struct Biol Cryst Commun 2010 66 2 121 129 10.1107/S1744309109051938
-
(2010)
Acta Crystallograph Sect F Struct Biol Cryst Commun
, vol.66
, Issue.2
, pp. 121-129
-
-
Alikhajeh, J.1
Khajeh, K.2
Ranjbar, B.3
Naderi-Manesh, H.4
Lin, Y.H.5
Liu, E.6
Guan, H.H.7
Hsieh, Y.C.8
Chuankhayan, P.9
Huang, Y.C.10
Jeyaraman, J.11
Liu, M.Y.12
Chen, C.J.13
-
6
-
-
3342983714
-
Adaptation of class-13 α-amylases to diverse living conditions
-
DOI 10.1002/cbic.200300734
-
Adaptation of class-13 α-amylases to diverse living conditions. Linden A, Wilmanns M, Chembiochem 2004 5 2 231 239 10.1002/cbic.200300734 14760745 (Pubitemid 39256238)
-
(2004)
ChemBioChem
, vol.5
, Issue.2
, pp. 231-239
-
-
Linden, A.1
Wilmanns, M.2
-
7
-
-
0037393130
-
Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis
-
DOI 10.1128/AEM.69.4.2383-2385.2003
-
Improving the thermostability of raw-starch-digesting amylase from a Cytophaga sp. by site-directed mutagenesis. Shiau RJ, Hung HC, Jeang CL, Appl Environ Microbiol 2003 69 4 2383 2385 10.1128/AEM.69.4.2383-2385.2003 12676725 (Pubitemid 36443662)
-
(2003)
Applied and Environmental Microbiology
, vol.69
, Issue.4
, pp. 2383-2385
-
-
Shiau, R.-J.1
Hung, H.-C.2
Jeang, C.-L.3
-
8
-
-
0033025132
-
Close evolutionary relatedness of α-amylases from archaea and plants
-
Close evolutionary relatedness of α-amylases from archaea and plants. Janeček S, Lévêque E, Belarbi A, Haye B, J Mol Evol 1999 48 4 421 426 10.1007/PL00006486 10079280 (Pubitemid 29153361)
-
(1999)
Journal of Molecular Evolution
, vol.48
, Issue.4
, pp. 421-426
-
-
Janecek, S.1
Leveque, E.2
Belarbi, A.3
Haye, B.4
-
9
-
-
33745836733
-
α-Amylases from microbial sources - An overview on recent developments
-
α-Amylases from microbial sources-an overview on recent developments. Sivaramakrishnan S, Gangadharan D, Nampoothiri KM, Soccol CR, Pandey A, Food Technol Biotech 2006 44 2 173 184 (Pubitemid 44033841)
-
(2006)
Food Technology and Biotechnology
, vol.44
, Issue.2
, pp. 173-184
-
-
Sivaramakrishnan, S.1
Gangadharan, D.2
Nampoothiri, K.M.3
Soccol, C.R.4
Pandey, A.5
-
10
-
-
0003112117
-
Starch conversion
-
New York: Stockton Press Godfrey T, West SI
-
Starch conversion. Bentley IS, Williams EC, Industrial enzymology New York: Stockton Press, Godfrey T, West SI, 1996 339 357
-
(1996)
Industrial Enzymology
, pp. 339-357
-
-
Bentley, I.S.1
Williams, E.C.2
-
11
-
-
0028943302
-
Purification and properties of extracellular amylase from the hyperthermophilic archaeon Thermococcus profundus DT5432
-
16534999
-
Purification and properties of extracellular amylase from the hyperthermophilic archaeon Thermococcus profundus DT5432. Chung YC, Kobayashi T, Kanai H, Akiba T, Kudo T, Appl Environ Microbiol 1995 61 4 1502 1506 16534999
-
(1995)
Appl Environ Microbiol
, vol.61
, Issue.4
, pp. 1502-1506
-
-
Chung, Y.C.1
Kobayashi, T.2
Kanai, H.3
Akiba, T.4
Kudo, T.5
-
12
-
-
0030826555
-
Cloning, sequencing, and expression of the gene encoding extracellular α-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme
-
Cloning, sequencing, and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus and biochemical characterization of the recombinant enzyme. Dong G, Vieille C, Savchenko A, Zeikus JG, Appl Environ Microbiol 1997 63 9 3569 3576 9293008 (Pubitemid 27383154)
-
(1997)
Applied and Environmental Microbiology
, vol.63
, Issue.9
, pp. 3569-3576
-
-
Dong, G.1
Vieille, C.2
Savchenko, A.3
Zeikus, J.G.4
-
13
-
-
0025890307
-
Purification and properties of a hyperthermoactive α-amylase from the archaeobacterium Pyrococcus woesei
-
10.1007/BF00245352
-
Purification and properties of a hyperthermoactive α-amylase from the archaeobacterium Pyrococcus woesei. Koch R, Spreinat A, Lemke K, Antranikian G, Arch Microbiol 1991 155 6 572 578 10.1007/BF00245352
-
(1991)
Arch Microbiol
, vol.155
, Issue.6
, pp. 572-578
-
-
Koch, R.1
Spreinat, A.2
Lemke, K.3
Antranikian, G.4
-
14
-
-
2542510221
-
Cloning and expression of an α-amylase encoding gene from the hyperthermophilic archaebacterium Thermococcus hydrothermalis and biochemical characterisation of the recombinant enzyme
-
DOI 10.1016/S0378-1097(00)00117-8, PII S0378109700001178
-
Cloning and expression of an α-amylase encoding gene from the hyperthermophilic archaebacterium Thermococcus hydrothermalis and biochemical characterization of the recombinant enzyme. Lévêque E, Haye B, Belarbi A, FEMS Microbiol Lett 2000 186 1 67 71 10779714 (Pubitemid 30211743)
-
(2000)
FEMS Microbiology Letters
, vol.186
, Issue.1
, pp. 67-71
-
-
Leveque, E.1
Haye, B.2
Belarbi, A.3
-
15
-
-
0037984394
-
Differential regulation of a hyperthermophilic α-amylase with a novel (Ca,Zn) two-metal center by zinc
-
DOI 10.1074/jbc.M211339200
-
Differential regulation of a hyperthermophilic α-amylase with a novel (Ca, Zn) two-metal center by zinc. Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M, J Biol Chem 2003 278 11 9875 9884 10.1074/jbc.M211339200 12482867 (Pubitemid 36800491)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.11
, pp. 9875-9884
-
-
Linden, A.1
Mayans, O.2
Meyer-Klaucke, W.3
Antranikian, G.4
Wilmanns, M.5
-
16
-
-
33746893814
-
Comparison of the wild-type α-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus α-amylase
-
DOI 10.1093/jb/mvj107
-
Comparison of the wild-type α-amylase and its variant enzymes in Bacillus amyloliquefaciens in activity and thermal stability, and insights into engineering the thermal stability of Bacillus α-amylase. Lee S, Mouri Y, Minoda M, Oneda H, Inouye K, J Biochem 2006 139 6 1007 1015 10.1093/jb/mvj107 16788051 (Pubitemid 44196877)
-
(2006)
Journal of Biochemistry
, vol.139
, Issue.6
, pp. 1007-1015
-
-
Lee, S.1
Mouri, Y.2
Minoda, M.3
Oneda, H.4
Inouye, K.5
-
17
-
-
0031925343
-
Glycosyl hydrolases from hyperthermophilic microorganisms
-
DOI 10.1016/S0958-1669(98)80106-7
-
Glycosyl hydrolases from hyperthermophilic microorganisms. Bauer MW, Driskill LE, Kelly RM, Curr Opin Biotechnol 1998 9 2 141 145 10.1016/S0958-1669(98)80106-7 9588002 (Pubitemid 28194999)
-
(1998)
Current Opinion in Biotechnology
, vol.9
, Issue.2
, pp. 141-145
-
-
Bauer, M.W.1
Driskill, L.E.2
Kelly, R.M.3
-
18
-
-
81055147824
-
Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues
-
10.1007/s10930-011-9348-7 21786160
-
Sequence-structural features and evolutionary relationships of family GH57 α-amylases and their putative α-amylase-like homologues. Janeček S, Blesak K, Protein J 2011 30 6 429 435 10.1007/s10930-011-9348- 7 21786160
-
(2011)
Protein J
, vol.30
, Issue.6
, pp. 429-435
-
-
Janeček, S.1
Blesak, K.2
-
19
-
-
0026055308
-
A classification of glycosyl hydrolases based on amino acid sequence similarities
-
A classification of glycosyl hydrolases based on amino acid sequence similarities. Henrissat B, J Biochem 1991 280 2 309 316
-
(1991)
J Biochem
, vol.280
, Issue.2
, pp. 309-316
-
-
Henrissat, B.1
-
20
-
-
58149200943
-
The Carbohydrate-Active EnZymes database (CAZy): An expert resource for glycogenomics
-
The Carbohydrate-Active EnZymes database (CAZy): an expert resource for glycogenomics. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B, Nucleic Acids Res 2009 37 1 233 238
-
(2009)
Nucleic Acids Res
, vol.37
, Issue.1
, pp. 233-238
-
-
Cantarel, B.L.1
Coutinho, P.M.2
Rancurel, C.3
Bernard, T.4
Lombard, V.5
Henrissat, B.6
-
21
-
-
33845665889
-
Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of α-amylase-related proteins
-
DOI 10.1093/protein/gzl044
-
Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Stam MR, Danchin EG, Corinne R, Coutinho PM, Henrissat B, Protein Eng Des Sel 2006 19 12 555 562 10.1093/protein/gzl044 17085431 (Pubitemid 44950461)
-
(2006)
Protein Engineering, Design and Selection
, vol.19
, Issue.12
, pp. 555-562
-
-
Stam, M.R.1
Danchin, E.G.J.2
Rancurel, C.3
Coutinho, P.M.4
Henrissat, B.5
-
22
-
-
84872127693
-
Tracing the evolution of the α-amylase subfamily GH13-36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases
-
23313816
-
Tracing the evolution of the α-amylase subfamily GH13-36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases. Majzlová K, Pukajová Z, Janeček S, Carbohydr Res 2013 367 15 48 57 23313816
-
(2013)
Carbohydr Res
, vol.367
, Issue.15
, pp. 48-57
-
-
Majzlová, K.1
Pukajová, Z.2
Janeček, S.3
-
23
-
-
77955094931
-
Amylolytic enzymes-focus on the alpha-amylases from archaea and plants
-
Amylolytic enzymes-focus on the alpha-amylases from archaea and plants. Janeček S, Nova Biotechnol 2009 9 1 5 25
-
(2009)
Nova Biotechnol
, vol.9
, Issue.1
, pp. 5-25
-
-
Janeček, S.1
-
24
-
-
0032960271
-
Amylase and 16S rRNA genes from a hyperthermophilic archaebacterium
-
DOI 10.1046/j.1365-2672.1999.00642.x
-
Amylase and 16S rRNA genes from a hyperthermophilic archaeabacterium. Jones RA, Jermiin LS, Easteal S, Patel BK, Beacham IR, J Appl Microbiol 1999 86 1 93 107 10.1046/j.1365-2672.1999.00642.x 10030014 (Pubitemid 29055018)
-
(1999)
Journal of Applied Microbiology
, vol.86
, Issue.1
, pp. 93-107
-
-
Jones, R.A.1
Jermiin, L.S.2
Easteal, S.3
Patel, B.K.C.4
Beacham, I.R.5
-
25
-
-
84899863334
-
α-Amylase: An enzyme specificity found in various families of glycoside hydrolases
-
doi: 10.1007/s00018-013-1388-z
-
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Janeček S, Svensson B, MacGregor EA, Cell Mol Life Sci 2013 doi: 10.1007/s00018-013-1388-z
-
(2013)
Cell Mol Life Sci
-
-
Janeček, S.1
Svensson, B.2
Macgregor, E.A.3
-
26
-
-
84874830199
-
Sinomicrobium oceani gen. Nov., sp. Nov., a novel member of the family Flavobacteriaceae isolated from marine sediment
-
22707529
-
Sinomicrobium oceani gen. nov., sp. nov., a novel member of the family Flavobacteriaceae isolated from marine sediment. Xu Y, Tian XP, Liu YJ, Li J, Kim CJ, Yin H, Li WJ, Zhang S, Int J Syst Evol Microbiol 2013 63 3 1045 1050 22707529
-
(2013)
Int J Syst Evol Microbiol
, vol.63
, Issue.3
, pp. 1045-1050
-
-
Xu, Y.1
Tian, X.P.2
Liu, Y.J.3
Li, J.4
Kim, C.J.5
Yin, H.6
Li, W.J.7
Zhang, S.8
-
27
-
-
0030910823
-
Cloning, sequencing, characterization, and expression of an extracellular α-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis
-
DOI 10.1074/jbc.272.26.16335
-
Cloning, sequencing, characterization, and expression of an extracellular alpha-amylase from the hyperthermophilic archaeon Pyrococcus furiosus in Escherichia coli and Bacillus subtilis. Jørgensen S, Vorgias CE, Antranikian G, J Biol Chem 1997 272 26 16335 16342 10.1074/jbc.272.26.16335 9195939 (Pubitemid 27276457)
-
(1997)
Journal of Biological Chemistry
, vol.272
, Issue.26
, pp. 16335-16342
-
-
Jorgensen, S.1
Vorgias, C.E.2
Antranikian, G.3
-
28
-
-
1642458395
-
Horizontal gene transfer from Eukarya to Bacteria and domain shuffling: The α-amylase model
-
DOI 10.1007/s00018-003-3334-y
-
Horizontal gene transfer from Eukarya to bacteria and domain shuffling: the α-amylase model. Da Lage JL, Feller G, Janeček S, Cell Mol Life Sci 2004 61 1 97 109 10.1007/s00018-003-3334-y 14704857 (Pubitemid 38121903)
-
(2004)
Cellular and Molecular Life Sciences
, vol.61
, Issue.1
, pp. 97-109
-
-
Da Lage, J.-L.1
Feller, G.2
Janecek, S.3
-
29
-
-
0029953633
-
Crystal structure of pig pancreatic α-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose
-
Crystal structure of pig pancreatic α-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose. Gilles C, Astier JP, Marchis-Mouren G, Cambillau C, Payan F, Eur J Biochem 1996 238 2 561 569 10.1111/j.1432-1033.1996.0561z.x 8681972 (Pubitemid 26191164)
-
(1996)
European Journal of Biochemistry
, vol.238
, Issue.2
, pp. 561-569
-
-
Gilles, C.1
Astier, J.-P.2
Marchis-Mouren, G.3
Cambillau, C.4
Payan, F.5
-
30
-
-
0028198814
-
The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution
-
DOI 10.1021/bi00186a031
-
The active center of mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor derived from the X-ray structure analysis to 2.2 Å resolution. Qian M, Haser R, Buisson G, Duée E, Payan F, Biochemistry 1994 33 20 6284 6294 10.1021/bi00186a031 8193143 (Pubitemid 24190783)
-
(1994)
Biochemistry
, vol.33
, Issue.20
, pp. 6284-6294
-
-
Qian, M.1
Haser, R.2
Buisson, G.3
Duee, E.4
Payan, F.5
-
31
-
-
0029931070
-
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å Resolution. Implications for product specificity
-
DOI 10.1021/bi952339h
-
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity. Strokopytov B, Knegtel MA, Penninga D, Rozenboom HJ, Kalk KH, Dijkhuizen L, Dijkstra BW, Biochemistry 1996 35 13 4241 4249 10.1021/bi952339h 8672460 (Pubitemid 26113482)
-
(1996)
Biochemistry
, vol.35
, Issue.13
, pp. 4241-4249
-
-
Strokopytov, B.1
Knegtel, R.M.A.2
Penninga, D.3
Rozeboom, H.J.4
Kalk, K.H.5
Dijkhuizen, L.6
Dijkstra, B.W.7
-
32
-
-
0028021627
-
Sequence similarities and evolutionary relationships of microbial, plant and animal α-amylases
-
Sequence similarities and evolutionary relationships of microbial, plant and animal α-amylases. Janeček S, Eur J Biochem 1994 224 2 519 524 10.1111/j.1432-1033.1994.00519.x 7925367 (Pubitemid 24282835)
-
(1994)
European Journal of Biochemistry
, vol.224
, Issue.2
, pp. 519-524
-
-
Janecek, S.1
-
33
-
-
77951753263
-
Tyrosine 39 of GH13 α-amylase from Thermococcus hydrothermalis contributes to its thermostability
-
10.2478/s11756-010-0030-x
-
Tyrosine 39 of GH13 α-amylase from Thermococcus hydrothermalis contributes to its thermostability. Godány A, Majzlová K, Horváthová V, Janeček S, Biologia 2010 65 3 408 415 10.2478/s11756-010-0030-x
-
(2010)
Biologia
, vol.65
, Issue.3
, pp. 408-415
-
-
Godány, A.1
Majzlová, K.2
Horváthová, V.3
Janeček, S.4
-
34
-
-
0028933531
-
Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
-
10.1006/jmbi.1994.0106 7877175
-
Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. Machius M, Wiegand G, Huber R, J Mol Biol 1995 246 4 545 559 10.1006/jmbi.1994.0106 7877175
-
(1995)
J Mol Biol
, vol.246
, Issue.4
, pp. 545-559
-
-
Machius, M.1
Wiegand, G.2
Huber, R.3
-
35
-
-
0030778420
-
α-Amylase family: Molecular biology and evolution
-
DOI 10.1016/S0079-6107(97)00015-1, PII S0079610797000151
-
α-Amylase family: molecular biology and evolution. Janeček S, Progr Biophys Mol Biol 1997 67 1 67 97 10.1016/S0079-6107(97)00015-1 (Pubitemid 27491749)
-
(1997)
Progress in Biophysics and Molecular Biology
, vol.67
, Issue.1
, pp. 67-97
-
-
Janecek, S.1
-
36
-
-
0034714134
-
Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase
-
10.1006/jmbi.2000.4025 10966804
-
Probing structural determinants specifying high thermostability in Bacillus licheniformis α-amylase. Declerck N, Machius M, Wiegand G, Huber R, Gaillardin C, J Mol Biol 2000 301 4 1041 1057 10.1006/jmbi.2000.4025 10966804
-
(2000)
J Mol Biol
, vol.301
, Issue.4
, pp. 1041-1057
-
-
Declerck, N.1
Machius, M.2
Wiegand, G.3
Huber, R.4
Gaillardin, C.5
-
37
-
-
0028359337
-
Refined molecular structure of pig pancreatic α-Amylase at 2.1 Å resolution
-
DOI 10.1006/jmbi.1994.1107
-
Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution. Larson SB, Greenwood A, Cascio D, Day J, McPherson A, J Mol Biol 1994 235 5 1560 1584 10.1006/jmbi.1994.1107 8107092 (Pubitemid 24150405)
-
(1994)
Journal of Molecular Biology
, vol.235
, Issue.5
, pp. 1560-1584
-
-
Larson, S.B.1
Greenwood, A.2
Cascio, D.3
Day, J.4
McPherson, A.5
-
38
-
-
13144305048
-
Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
-
10.1016/S0969-2126(98)00032-X 9551551
-
Activation of Bacillus licheniformis α-amylase through a disorder → order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Machius M, Declerck N, Huber R, Wiegand G, Structure 1998 6 3 281 292 10.1016/S0969-2126(98)00032-X 9551551
-
(1998)
Structure
, vol.6
, Issue.3
, pp. 281-292
-
-
Machius, M.1
Declerck, N.2
Huber, R.3
Wiegand, G.4
-
39
-
-
0033748784
-
Production and partial characterization of thermostable and calcium-independent α-amylase of an extreme thermophile Bacillus thermooleovorans NP54
-
10.1046/j.1472-765x.2000.00830.x 11069641
-
Production and partial characterization of thermostable and calcium-independent α-amylase of an extreme thermophile Bacillus thermooleovorans NP54. Malhotra R, Noorwez SM, Satyanarayana T, Lett Appl Microbiol 2000 31 5 378 384 10.1046/j.1472-765x.2000.00830.x 11069641
-
(2000)
Lett Appl Microbiol
, vol.31
, Issue.5
, pp. 378-384
-
-
Malhotra, R.1
Noorwez, S.M.2
Satyanarayana, T.3
-
40
-
-
0025061657
-
Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus
-
Extremely thermostable amylolytic enzyme from the archaebacterium Pyrococcus furiosus. Koch R, Zablowski P, Spreinat A, Antranikian G, FEMS Microbiol Lett 1990 71 1-2 21 26 (Pubitemid 20256268)
-
(1990)
FEMS Microbiology Letters
, vol.71
, Issue.1-2
, pp. 21-26
-
-
Koch, R.1
Zablowski, P.2
Spreinat, A.3
Antranikian, G.4
-
41
-
-
14544282884
-
A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104
-
A Ca-independent α-amylase that is active and stable at low pH from the Bacillus sp. KR-8104. Sajedi RH, Naderi-Manesh H, Khajeh K, Ahmadvand R, Ranjbar B, Asoodeh A, Moradian F, Enzyme Microb Technol 2005 36 5-6 671 671
-
(2005)
Enzyme Microb Technol
, vol.36
, Issue.5-6
, pp. 671-671
-
-
Sajedi, R.H.1
Naderi-Manesh, H.2
Khajeh, K.3
Ahmadvand, R.4
Ranjbar, B.5
Asoodeh, A.6
Moradian, F.7
-
42
-
-
0037076543
-
Pyrococcus furiosus α-amylase is stabilized by calcium and zinc
-
DOI 10.1021/bi012106s
-
Pyrococcus furiosus α-amylase is stabilized by calcium and zinc. Savchenko A, Vieille C, Kang S, Zeikus JG, Biochemistry 2002 41 19 6193 6201 10.1021/bi012106s 11994016 (Pubitemid 34498927)
-
(2002)
Biochemistry
, vol.41
, Issue.19
, pp. 6193-6201
-
-
Savchenko, A.1
Vieille, C.2
Kang, S.3
Zeikus, J.G.4
-
43
-
-
34548472445
-
Critical factors to high thermostability of an α-amylase from hyperthermophilic archaeon Thermococcus onnurineus NA1
-
Critical factors to high thermostability of an α-amylase from hyperthermophilic archaeon Thermococcus onnurineus NA1. Lim JK, Lee HS, Kim YJ, Bae SS, Jeon JH, Kang SG, Lee JH, J Microbiol Biotechnol 2007 17 8 1242 1248 18051591 (Pubitemid 47377389)
-
(2007)
Journal of Microbiology and Biotechnology
, vol.17
, Issue.8
, pp. 1242-1248
-
-
Lim, J.K.1
Lee, H.S.2
Kim, Y.J.3
Bae, S.S.4
Jeon, J.H.5
Kang, S.G.6
Lee, J.-H.7
-
44
-
-
34748886064
-
The 'pair of sugar tongs' site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity
-
DOI 10.1111/j.1742-4658.2007.06024.x
-
The 'pair of sugar tongs' site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity. Bozonnet S, Jensen MT, Nielsen MM, Aghajari N, Jensen MH, Kramhøft B, Willemoes M, Tranier S, Haser R, Svensson B, FEBS J 2007 274 19 5055 5067 10.1111/j.1742-4658.2007.06024.x 17803687 (Pubitemid 47481177)
-
(2007)
FEBS Journal
, vol.274
, Issue.19
, pp. 5055-5067
-
-
Bozonnet, S.1
Jensen, M.T.2
Nielsen, M.M.3
Aghajari, N.4
Jensen, M.H.5
Kramhoft, B.6
Willemoes, M.7
Tranier, S.8
Haser, R.9
Svensson, B.10
-
45
-
-
0032847990
-
Characteristics of two forms of α-amylases and structural implication
-
10508102
-
Characteristics of two forms of α-amylases and structural implication. Ohdan K, Kuriki T, Kaneko H, Shimada J, Takada T, Fujimoto Z, Mizuno H, Okada S, Appl Environ Microbiol 1999 65 10 4652 4658 10508102
-
(1999)
Appl Environ Microbiol
, vol.65
, Issue.10
, pp. 4652-4658
-
-
Ohdan, K.1
Kuriki, T.2
Kaneko, H.3
Shimada, J.4
Takada, T.5
Fujimoto, Z.6
Mizuno, H.7
Okada, S.8
-
46
-
-
0028091811
-
C-terminal truncations of a thermostable Bacillus stearothermophilus α-amylase
-
C-terminal truncations of a thermostable Bacillus stearothermophilus α-amylase. Vihinen M, Peltonen T, Iitiä A, Suominen I, Mäntsälä P, Protein Eng 1994 7 10 1255 1259 10.1093/protein/7.10. 1255 7855141 (Pubitemid 24319404)
-
(1994)
Protein Engineering
, vol.7
, Issue.10
, pp. 1255-1259
-
-
Vihinen, M.1
Peltonen, T.2
Iitia, A.3
Suominen, I.4
Mantsala, P.5
-
47
-
-
0032483304
-
Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution
-
DOI 10.1006/jmbi.1998.1992
-
Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution. Katsuya Y, Mezaki Y, Kubota M, Matsuura Y, J Mol Biol 1998 281 5 885 897 10.1006/jmbi.1998.1992 9719642 (Pubitemid 28408436)
-
(1998)
Journal of Molecular Biology
, vol.281
, Issue.5
, pp. 885-897
-
-
Katsuya, Y.1
Mezaki, Y.2
Kubota, M.3
Matsuura, Y.4
-
48
-
-
0033856840
-
Comparative characterization of complete and truncated forms of Lactobacillus amylovorus α-amylase and role of the c-terminal direct repeats in raw-starch binding
-
DOI 10.1128/AEM.66.8.3350-3356.2000
-
Comparative characterization of complete and truncated forms of Lactobacillus amylovorus α-amylase and the role of the C-terminal direct repeats in raw starch binding. Sanoja RR, Morlon-Guyot J, Jore J, Pintado J, Juge N, Guyot JP, Appl Environ Microbiol 2000 66 8 3350 3356 10.1128/AEM.66.8.3350-3356.2000 10919790 (Pubitemid 30624576)
-
(2000)
Applied and Environmental Microbiology
, vol.66
, Issue.8
, pp. 3350-3356
-
-
Rodriguez Sanoja, R.1
Morlon-Guyot, J.2
Jore, J.3
Pintado, J.4
Juge, N.5
Guyot, J.P.6
-
49
-
-
0032551748
-
Improved thermostability of a bacillus α-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding
-
DOI 10.1006/bbrc.1998.8970
-
Improved thermostability of a Bacillus α-amylase by deletion of an arginine-glycine residue is caused by enhanced calcium binding. Igarashi K, Hatada Y, Ikawa K, Araki H, Ozawa T, Kobayashi T, Ozaki K, Ito S, Biochem Biophys Res Commun 1998 248 2 372 377 10.1006/bbrc.1998.8970 9675143 (Pubitemid 28386429)
-
(1998)
Biochemical and Biophysical Research Communications
, vol.248
, Issue.2
, pp. 372-377
-
-
Igarashi, K.1
Hatada, Y.2
Ikawa, K.3
Araki, H.4
Ozawa, T.5
Kobayashi, T.6
Ozaki, K.7
Ito, S.8
-
50
-
-
0023424403
-
Purification and characterization of the extracellular α-amylase activity of the yeast Schwanniomyces alluvius
-
10.1139/o87-116 3502323
-
Purification and characterization of the extracellular α-amylase activity of the yeast Schwanniomyces alluvius. Moranelli F, Yaguchi M, Calleja GB, Nasim A, Biochem Cell Biol 1987 65 10 899 908 10.1139/o87-116 3502323
-
(1987)
Biochem Cell Biol
, vol.65
, Issue.10
, pp. 899-908
-
-
Moranelli, F.1
Yaguchi, M.2
Calleja, G.B.3
Nasim, A.4
-
52
-
-
0001857117
-
16S/23S rRNA sequencing
-
Hoboken, NJ: John Wiley & Sons Stackebrandt E, Goodfellow M
-
16S/23S rRNA sequencing. Lane D, Nucleic acid techniques in bacterial systematics Hoboken, NJ: John Wiley & Sons, Stackebrandt E, Goodfellow M, 1991 115 175
-
(1991)
Nucleic Acid Techniques in Bacterial Systematics
, pp. 115-175
-
-
Lane, D.1
-
53
-
-
40549120596
-
The RAST Server: Rapid annotations using subsystems technology
-
DOI 10.1186/1471-2164-9-75
-
The RAST server: rapid annotations using subsystems technology. Aziz RK, Bartels D, Best AA, DeJongh M, Disz T, Edwards RA, Formsma K, Gerdes S, Glass EM, Kubal M, Meyer F, Olsen GJ, Olson R, Osterman AL, Overbeek RA, McNeil LK, Paarmann D, Paczian T, Parrello B, Pusch GD, Reich C, Stevens R, Vassieva O, Vonstein V, Wilke A, Zagnitko O, BMC Genomics 2008 9 75 10.1186/1471-2164-9-75 18261238 (Pubitemid 351356785)
-
(2008)
BMC Genomics
, vol.9
, pp. 75
-
-
Aziz, R.K.1
Bartels, D.2
Best, A.3
DeJongh, M.4
Disz, T.5
Edwards, R.A.6
Formsma, K.7
Gerdes, S.8
Glass, E.M.9
Kubal, M.10
Meyer, F.11
Olsen, G.J.12
Olson, R.13
Osterman, A.L.14
Overbeek, R.A.15
McNeil, L.K.16
Paarmann, D.17
Paczian, T.18
Parrello, B.19
Pusch, G.D.20
Reich, C.21
Stevens, R.22
Vassieva, O.23
Vonstein, V.24
Wilke, A.25
Zagnitko, O.26
more..
-
54
-
-
0031574072
-
The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
-
DOI 10.1093/nar/25.24.4876
-
The CLUSTAL-X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG, Nucleic Acids Res 1997 25 24 4876 4882 10.1093/nar/25.24.4876 9396791 (Pubitemid 28022245)
-
(1997)
Nucleic Acids Research
, vol.25
, Issue.24
, pp. 4876-4882
-
-
Thompson, J.D.1
Gibson, T.J.2
Plewniak, F.3
Jeanmougin, F.4
Higgins, D.G.5
-
55
-
-
34547781750
-
MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
-
DOI 10.1093/molbev/msm092
-
MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Tamura K, Dudley J, Nei M, Kumar S, Mol Biol Evol 2007 24 8 1596 1599 10.1093/molbev/msm092 17488738 (Pubitemid 47236692)
-
(2007)
Molecular Biology and Evolution
, vol.24
, Issue.8
, pp. 1596-1599
-
-
Tamura, K.1
Dudley, J.2
Nei, M.3
Kumar, S.4
-
56
-
-
0029004590
-
Protein modeling by e-mail
-
10.1038/nbt0795-658
-
Protein modeling by e-mail. Peitsch MC, Nat Biotechnol 1995 13 658 660 10.1038/nbt0795-658
-
(1995)
Nat Biotechnol
, vol.13
, pp. 658-660
-
-
Peitsch, M.C.1
-
57
-
-
0042622380
-
SWISS-MODEL: An automated protein homology-modeling server
-
DOI 10.1093/nar/gkg520
-
SWISS-MODEL: an automated protein homology-modeling server. Schwede T, Kopp J, Guex N, Peitsch MC, Nucleic Acids Res 2003 31 13 3381 3385 10.1093/nar/gkg520 12824332 (Pubitemid 37442164)
-
(2003)
Nucleic Acids Research
, vol.31
, Issue.13
, pp. 3381-3385
-
-
Schwede, T.1
Kopp, J.2
Guex, N.3
Peitsch, M.C.4
-
58
-
-
33747333106
-
Use of dinitrosalicylic acid reagent for determination of reducing sugar
-
10.1021/ac60147a030
-
Use of dinitrosalicylic acid reagent for determination of reducing sugar. Miller GL, Anal Chem 1959 31 3 426 428 10.1021/ac60147a030
-
(1959)
Anal Chem
, vol.31
, Issue.3
, pp. 426-428
-
-
Miller, G.L.1
-
59
-
-
0035318737
-
Novel α-Amylase That Is Highly Resistant to Chelating Reagents and Chemical Oxidants from the Alkaliphilic Bacillus Isolate KSM-K38
-
DOI 10.1128/AEM.67.4.1744-1750.2001
-
Novel α-amylase that is highly resistant to chelating reagents and chemical oxidants from the alkaliphilic Bacillus isolate KSM-K38. Hagihara H, Igarashi K, Hayashi Y, Endo K, Ikawa-Kitayama K, Ozaki K, Kawai S, Ito S, Appl Environ Microbiol 2001 67 4 1744 1750 10.1128/AEM.67.4.1744-1750.2001 11282629 (Pubitemid 33644947)
-
(2001)
Applied and Environmental Microbiology
, vol.67
, Issue.4
, pp. 1744-1750
-
-
Hagihara, H.1
Igarashi, K.2
Hayashi, Y.3
Endo, K.4
Ikawa-Kitayama, K.5
Ozaki, K.6
Kawai, S.7
Ito, S.8
|