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Crystallographic evidence for substrate ring distortion and protein conformational changes during catalysis in cellobiohydrolase Ce16A from trichoderma reeseiStructural basis for enantiomer binding and separation of a common beta-blocker: crystal structure of cellobiohydrolase Cel7A with bound (S)-propranolol at 1.9 A resolutionThe X-ray crystal structure of the Trichoderma reesei family 12 endoglucanase 3, Cel12A, at 1.9 A resolutionEngineering of a glycosidase Family 7 cellobiohydrolase to more alkaline pH optimum: the pH behaviour of Trichoderma reesei Cel7A and its E223S/ A224H/L225V/T226A/D262G mutantFamily 7 cellobiohydrolases from Phanerochaete chrysosporium: crystal structure of the catalytic module of Cel7D (CBH58) at 1.32 A resolution and homology models of the isozymesThe active site of cellobiohydrolase Cel6A from Trichoderma reesei: the roles of aspartic acids D221 and D175Dextranase from Penicillium minioluteum: reaction course, crystal structure, and product complexEngineering the exo-loop of Trichoderma reesei cellobiohydrolase, Cel7A. A comparison with Phanerochaete chrysosporium Cel7DX-ray crystal structures of Phanerochaete chrysosporium Laminarinase 16A in complex with products from lichenin and laminarin hydrolysisSynthesis of cyclic beta-glucan using laminarinase 16A glycosynthase mutant from the basidiomycete Phanerochaete chrysosporiumStructural, Biochemical, and Computational Characterization of the Glycoside Hydrolase Family 7 Cellobiohydrolase of the Tree-killing Fungus Heterobasidion irregulareCrystal Structure and Computational Characterization of the Lytic Polysaccharide Monooxygenase GH61D from the Basidiomycota Fungus Phanerochaete chrysosporiumLoop Motions Important to Product Expulsion in the Thermobifida fusca Glycoside Hydrolase Family 6 Cellobiohydrolase from Structural and Computational StudiesRational design, synthesis, evaluation and enzyme-substrate structures of improved fluorogenic substrates for family 6 glycoside hydrolasesThe structure of a bacterial cellobiohydrolase: the catalytic core of the Thermobifida fusca family GH6 cellobiohydrolase Cel6BStructural and Electronic Snapshots during the Transition from a Cu(II) to Cu(I) Metal Center of a Lytic Polysaccharide Monooxygenase by X-ray PhotoreductionThe mechanism of cellulose hydrolysis by a two-step, retaining cellobiohydrolase elucidated by structural and transition path sampling studiesStructural insights into the inhibition of cellobiohydrolase Cel7A by xylo-oligosaccharidesSequencing, biochemical characterization, crystal structure and molecular dynamics of cellobiohydrolase Cel7A from Geotrichum candidum 3CThe three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reeseiActivity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reeseiThe crystal structure of the catalytic core domain of endoglucanase I from Trichoderma reesei at 3.6 A resolution, and a comparison with related enzymesHigh-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reeseiAdsorption and synergism of cellobiohydrolase I and II of Trichoderma reesei during hydrolysis of microcrystalline celluloseProduct binding varies dramatically between processive and nonprocessive cellulase enzymes.Glycosylated linkers in multimodular lignocellulose-degrading enzymes dynamically bind to celluloseCrystal complex structures reveal how substrate is bound in the -4 to the +2 binding sites of Humicola grisea Cel12A.Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes.The putative endoglucanase PcGH61D from Phanerochaete chrysosporium is a metal-dependent oxidative enzyme that cleaves cellulose.Hypocrea jecorina CEL6A protein engineering.Identification of functionally important amino acids in the cellulose-binding domain of Trichoderma reesei cellobiohydrolase I.Biochemical and Structural Characterizations of Two Dictyostelium Cellobiohydrolases from the Amoebozoa Kingdom Reveal a High Level of Conservation between Distant Phylogenetic Trees of Life.Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism.Towards a molecular-level theory of carbohydrate processivity in glycoside hydrolases.Structures of Phanerochaete chrysosporium Cel7D in complex with product and inhibitors.EGIII, a new endoglucanase from Trichoderma reesei: the characterization of both gene and enzyme.Airtight storage of moist wheat grain improves bioethanol yields.Expression, crystal structure and cellulase activity of the thermostable cellobiohydrolase Cel7A from the fungus Humicola grisea var. thermoidea.Characterization of protein glycoforms with N-linked neutral and phosphorylated oligosaccharides: studies on the glycosylation of endoglucanase 1 (Cel7B) from Trichoderma reesei.Crystallization and X-ray analysis of native and selenomethionyl beta-mannanase Man5A from blue mussel, Mytilus edulis, expressed in Pichia pastoris.
P50
Q27619885-E050733E-678A-42AA-B937-FDC4F5DA28C3Q27628896-F45D1959-AAC4-4C12-98C0-ECA274B9297EQ27631438-9EAE7CC4-C6F9-422A-AA52-280EEE8400E8Q27631586-CCA7F994-89A9-49DD-B49E-422887DFE3A0Q27636841-DDFACDEA-3BEC-4D70-A2A2-8C6DA3724827Q27639510-F7170074-F15D-4F53-871F-33F597425376Q27641985-85B3F6DF-FFF7-44DA-AB00-E03B4BA5C568Q27642386-625DD6A4-AB96-486D-9205-35CE1191D05DQ27657497-009D3705-34CD-4A6F-B70C-FDCD678020B3Q27658973-315C862B-2B36-471C-AC52-EB4ABC5723C7Q27675853-C6FCFD77-0818-4A11-93B9-6B47A2500CBAQ27677016-D8B9ACC6-2E0F-4C4F-8C24-032FCAFD7E9FQ27680122-E520933F-099C-4A50-AA78-B853C16662F2Q27683296-605921DF-4001-44F9-890A-C70608EEBF1DQ27683571-D6E642A9-9912-4D38-9781-C831178E70E6Q27683785-14509A6D-7C26-4226-BA98-A5B9A8D62E80Q27687984-B47ABF0B-66B6-4FDE-84DF-CFB12DBA742EQ27698477-2726D4E5-9610-4F2B-A620-C34AC37AD970Q27702143-ECE7715A-89EC-4937-8B5F-E2C626C5D6F7Q27730832-4CD3B4FD-5B9E-41FE-B63C-B2702CF8C56BQ27734116-8B175976-C763-4691-8470-FA28F636658AQ27745581-A21BFEF7-2E3A-4431-A86F-0DB606471BADQ27748854-246D8B7A-A638-4AFB-B968-5B0862215C08Q28287020-6085F04D-796F-4453-868D-723FE008B2D2Q30418292-21C1DCD4-EA90-418E-B088-EFAA680478EBQ30544331-46CC0911-CE40-48A7-91EE-A5702EEAAD3EQ31111616-AEB5ADA5-BE5D-4B51-AA62-DA00017B1F5AQ33216880-47AE2542-3634-4E74-BCBA-7196A9D28779Q34087898-F7C1CF72-37F5-4618-8533-ECF458CBEEC6Q34154286-1784B144-9ACC-46B4-A0DD-1F7255031FADQ36279202-CEC2ABB5-3134-430C-9C2D-3ED470E39FEBQ37122308-3FA4FF49-CF10-4910-8206-787DA9B48ABAQ37475167-7F3A4CE2-9DB1-47C8-92F3-F8637EF8D7DBQ38215156-ADA6863D-1215-4B2B-AC32-04B333C77637Q38328256-EDD481CC-A806-4741-A0B5-5D63DC8359FDQ41438195-115D556B-4219-4B19-B9C0-397B2947811CQ42149521-71C65B8A-27C8-41C4-9B60-9972989B932CQ42868330-741DF3B8-378A-446A-95AC-E576193FAABBQ43561923-29A524AE-8E4F-43F8-ABC5-5D6D2194D987Q45714189-7D12C594-6319-40E8-B87E-1B013FF981CF
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Jerry Ståhlberg
@ast
Jerry Ståhlberg
@en
Jerry Ståhlberg
@es
Jerry Ståhlberg
@nl
Jerry Ståhlberg
@sl
type
label
Jerry Ståhlberg
@ast
Jerry Ståhlberg
@en
Jerry Ståhlberg
@es
Jerry Ståhlberg
@nl
Jerry Ståhlberg
@sl
altLabel
Jerry Stahlberg
@en
prefLabel
Jerry Ståhlberg
@ast
Jerry Ståhlberg
@en
Jerry Ståhlberg
@es
Jerry Ståhlberg
@nl
Jerry Ståhlberg
@sl
P1053
D-4163-2013
P106
P21
P31
P3829
P496
0000-0003-4059-8580