-
1
-
-
0041663295
-
The structure of barley α-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs
-
Robert X., Haser R., Gottschalk T.E., Ratajczak F., Driguez H., Svensson B., and Aghajari N. The structure of barley α-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs. Structure 11 (2003) 973-984
-
(2003)
Structure
, vol.11
, pp. 973-984
-
-
Robert, X.1
Haser, R.2
Gottschalk, T.E.3
Ratajczak, F.4
Driguez, H.5
Svensson, B.6
Aghajari, N.7
-
2
-
-
25444484215
-
Oligosaccharide binding to barley α-amylase 1
-
Robert X., Haser R., Mori H., Svensson B., and Aghajari N. Oligosaccharide binding to barley α-amylase 1. J. Biol. Chem. 280 (2005) 32968-32978
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 32968-32978
-
-
Robert, X.1
Haser, R.2
Mori, H.3
Svensson, B.4
Aghajari, N.5
-
3
-
-
34748886064
-
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 M.T., Nielsen M.M., Aghajari N., Jensen M.H., Kramhøft B., Willemoës M., Tranier S., Haser R., and Svensson B. The "pair of sugar tongs" site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity. FEBS J. 274 (2007) 5055-5067
-
(2007)
FEBS J.
, vol.274
, pp. 5055-5067
-
-
Bozonnet, S.1
Jensen, M.T.2
Nielsen, M.M.3
Aghajari, N.4
Jensen, M.H.5
Kramhøft, B.6
Willemoës, M.7
Tranier, S.8
Haser, R.9
Svensson, B.10
-
4
-
-
1642321719
-
Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1
-
Bak-Jensen K.S., André G., Gottschalk T.E., Paës G., Tran V., and Svensson B. Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1. J. Biol. Chem. 279 (2004) 10093-10102
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 10093-10102
-
-
Bak-Jensen, K.S.1
André, G.2
Gottschalk, T.E.3
Paës, G.4
Tran, V.5
Svensson, B.6
-
5
-
-
33748328058
-
Mapping of barley α-amylases and outer subsite mutants reveals dynamic high-affinity subsites and barriers in the long substrate binding cleft
-
Kandra L., Abou Hachem M., Gyémánt G., Kramhøft B., and Svensson B. Mapping of barley α-amylases and outer subsite mutants reveals dynamic high-affinity subsites and barriers in the long substrate binding cleft. FEBS Lett. 580 (2006) 5049-5053
-
(2006)
FEBS Lett.
, vol.580
, pp. 5049-5053
-
-
Kandra, L.1
Abou Hachem, M.2
Gyémánt, G.3
Kramhøft, B.4
Svensson, B.5
-
6
-
-
13544266212
-
Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylose by barley alpha-amylase
-
Kramhøft B., Bak-Jensen K.S., Mori H., Juge N., Nøhr J., and Svensson B. Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylose by barley alpha-amylase. Biochemistry 44 (2005) 1824-1832
-
(2005)
Biochemistry
, vol.44
, pp. 1824-1832
-
-
Kramhøft, B.1
Bak-Jensen, K.S.2
Mori, H.3
Juge, N.4
Nøhr, J.5
Svensson, B.6
-
7
-
-
33748517440
-
Structure of Bacillus halmapalus α-amylase crystallized with and without the substrate analogue acarbose and maltose
-
Lyhne-Iversen L., Hobley T.J., Kaasgaard S.G., and Harris P. Structure of Bacillus halmapalus α-amylase crystallized with and without the substrate analogue acarbose and maltose. Acta Crystallogr., Sect. F 62 (2006) 849-854
-
(2006)
Acta Crystallogr., Sect. F
, vol.62
, pp. 849-854
-
-
Lyhne-Iversen, L.1
Hobley, T.J.2
Kaasgaard, S.G.3
Harris, P.4
-
8
-
-
33747177331
-
Monoclinic crystal form of Aspergillus niger α-amylase in complex with maltose at 1.8 Å resolution
-
Vujicic-Žagar A., and Dijkstra B.W. Monoclinic crystal form of Aspergillus niger α-amylase in complex with maltose at 1.8 Å resolution. Acta Crystallogr., Sect. F 62 (2006) 716-721
-
(2006)
Acta Crystallogr., Sect. F
, vol.62
, pp. 716-721
-
-
Vujicic-Žagar, A.1
Dijkstra, B.W.2
-
10
-
-
0035660447
-
Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley α-amylase 1
-
Mori H., Sass Bak-Jensen K., Gottschalk T.E., Motawia S.M., Damager I., Lindberg Møller B., and Svensson B. Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and -5/-6 of barley α-amylase 1. Eur. J. Biochem. 268 (2001) 6545-6558
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 6545-6558
-
-
Mori, H.1
Sass Bak-Jensen, K.2
Gottschalk, T.E.3
Motawia, S.M.4
Damager, I.5
Lindberg Møller, B.6
Svensson, B.7
-
11
-
-
0030250653
-
Overexpression, purification, and characterization of recombinant barley α-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris
-
Juge N., Andersen J.S., Tull D., Roepstorff P., and Svensson B. Overexpression, purification, and characterization of recombinant barley α-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 8 (1996) 204-214
-
(1996)
Protein Expr. Purif.
, vol.8
, pp. 204-214
-
-
Juge, N.1
Andersen, J.S.2
Tull, D.3
Roepstorff, P.4
Svensson, B.5
-
12
-
-
0346826288
-
Kinetics and energetics of the binding between barley α-amylase/subtilisin inhibitor and barley α-amylase 2 analyzed by surface plasmon resonance and isothermal titration calorimetry
-
Nielsen P.K., Bønsager B.C., Berland C.R., Sigurskjold B.W., and Svensson B. Kinetics and energetics of the binding between barley α-amylase/subtilisin inhibitor and barley α-amylase 2 analyzed by surface plasmon resonance and isothermal titration calorimetry. Biochemistry 42 (2003) 1478-1487
-
(2003)
Biochemistry
, vol.42
, pp. 1478-1487
-
-
Nielsen, P.K.1
Bønsager, B.C.2
Berland, C.R.3
Sigurskjold, B.W.4
Svensson, B.5
-
13
-
-
0036005625
-
Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds
-
Robert X., Gottschalk T.E., Haser R., Svensson B., and Aghajari N. Expression, purification and preliminary crystallographic studies of alpha-amylase isozyme 1 from barley seeds. Acta Crystallogr., Sect. D-Biol. Crystallogr. 58 (2002) 683-686
-
(2002)
Acta Crystallogr., Sect. D-Biol. Crystallogr.
, vol.58
, pp. 683-686
-
-
Robert, X.1
Gottschalk, T.E.2
Haser, R.3
Svensson, B.4
Aghajari, N.5
-
14
-
-
0027879008
-
Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
-
Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
-
(1993)
J. Appl. Crystallogr.
, vol.26
, pp. 795-800
-
-
Kabsch, W.1
-
15
-
-
3543012707
-
Crystallography & NMR system: A new software suite for macromolecular structure determination
-
Brünger A.T., Adams P.D., Clore G.M., Delano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr., Sect. D - Biol. Crystallogr. 54 (1998) 905-921
-
(1998)
Acta Crystallogr., Sect. D - Biol. Crystallogr.
, vol.54
, pp. 905-921
-
-
Brünger, A.T.1
Adams, P.D.2
Clore, G.M.3
Delano, W.L.4
Gros, P.5
Grosse-Kunstleve, R.W.6
Jiang, J.S.7
Kuszewski, J.8
Nilges, M.9
Pannu, N.S.10
Read, R.J.11
Rice, L.M.12
Simonson, T.13
Warren, G.L.14
-
16
-
-
46949099232
-
-
Roussel, A. and Cambillau, C. (1989) TURBO-FRODO, in: Silicon Graphics Geometry Partner Directory, Silicon Graphics, Mountain View, CA, pp. 77-78.
-
Roussel, A. and Cambillau, C. (1989) TURBO-FRODO, in: Silicon Graphics Geometry Partner Directory, Silicon Graphics, Mountain View, CA, pp. 77-78.
-
-
-
-
17
-
-
0026597444
-
Free R-value - a novel statistical quantity for assessing the accuracy of crystal-structures
-
Brünger A.T. Free R-value - a novel statistical quantity for assessing the accuracy of crystal-structures. Nature 355 (1992) 472-475
-
(1992)
Nature
, vol.355
, pp. 472-475
-
-
Brünger, A.T.1
-
18
-
-
0141815501
-
On the mechanism of α-amylase - acarbose and cyclodextrin inhibition of barley amylase isozymes
-
Oudjeriouat N., Moreau Y., Santimone M., Svensson B., Marchis-Mouren G., and Desseaux V. On the mechanism of α-amylase - acarbose and cyclodextrin inhibition of barley amylase isozymes. Eur. J. Biochem. 270 (2003) 3871-3879
-
(2003)
Eur. J. Biochem.
, vol.270
, pp. 3871-3879
-
-
Oudjeriouat, N.1
Moreau, Y.2
Santimone, M.3
Svensson, B.4
Marchis-Mouren, G.5
Desseaux, V.6
-
19
-
-
0031897880
-
Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis
-
Irwin D., Shin D.H., Zhang S., Barr B.K., Sakon J., Karplus P.A., and Wilson D.B. Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis. J. Bacteriol. 180 (1998) 1709-1714
-
(1998)
J. Bacteriol.
, vol.180
, pp. 1709-1714
-
-
Irwin, D.1
Shin, D.H.2
Zhang, S.3
Barr, B.K.4
Sakon, J.5
Karplus, P.A.6
Wilson, D.B.7
-
20
-
-
33644530353
-
The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase
-
Juge N., Nøhr J., Le Gal-Coëffet M.F., Kramhøft B., Furniss C.S.M., Planchot V., Archer D.B., Williamson G., and Svensson B. The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. Biochim. Biophys. Acta - Proteins Proteom. 1764 (2006) 275-284
-
(2006)
Biochim. Biophys. Acta - Proteins Proteom.
, vol.1764
, pp. 275-284
-
-
Juge, N.1
Nøhr, J.2
Le Gal-Coëffet, M.F.3
Kramhøft, B.4
Furniss, C.S.M.5
Planchot, V.6
Archer, D.B.7
Williamson, G.8
Svensson, B.9
-
21
-
-
0025831189
-
Interaction of β-cyclodextrin with the granular starch binding domain of glucoamylase
-
Belshaw N.J., and Williamson G. Interaction of β-cyclodextrin with the granular starch binding domain of glucoamylase. Biochim. Biophys. Acta 1078 (1991) 117-120
-
(1991)
Biochim. Biophys. Acta
, vol.1078
, pp. 117-120
-
-
Belshaw, N.J.1
Williamson, G.2
-
22
-
-
0027425535
-
Site-directed mutagenesis of histidine-93, aspartic acid-180, glutamic acid-205, histidine-290, and aspartic acid-291 at the active-site and tryptophan-279 at the raw starch binding-site in barley alpha-amylase 1
-
Søgaard M., Kadziola A., Haser R., and Svensson B. Site-directed mutagenesis of histidine-93, aspartic acid-180, glutamic acid-205, histidine-290, and aspartic acid-291 at the active-site and tryptophan-279 at the raw starch binding-site in barley alpha-amylase 1. J. Biol. Chem. 268 (1993) 22480-22484
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 22480-22484
-
-
Søgaard, M.1
Kadziola, A.2
Haser, R.3
Svensson, B.4
-
23
-
-
0032562777
-
Molecular structure of a barley α-amylase-inhibitor complex: Implications for starch binding and catalysis
-
Kadziola A., Søgaard M., Svensson B., and Haser R. Molecular structure of a barley α-amylase-inhibitor complex: Implications for starch binding and catalysis. J. Mol. Biol. 278 (1998) 205-217
-
(1998)
J. Mol. Biol.
, vol.278
, pp. 205-217
-
-
Kadziola, A.1
Søgaard, M.2
Svensson, B.3
Haser, R.4
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