about
beta-Glycosyl azides as substrates for alpha-glycosynthases: preparation of efficient alpha-L-fucosynthasesA new archaeal beta-glycosidase from Sulfolobus solfataricus: seeding a novel retaining beta-glycan-specific glycoside hydrolase family along with the human non-lysosomal glucosylceramidase GBA2Recoding in archaea.Interrupted genes in extremophilic archaea: mechanisms of gene expression in early organisms.The alpha-L-fucosidase from Sulfolobus solfataricus.High-level expression of thermostable cellulolytic enzymes in tobacco transplastomic plants and their use in hydrolysis of an industrially pretreated Arundo donax L. biomass.Engineering the stability and the activity of a glycoside hydrolase.Glycosynthases as tools for the production of glycan analogs of natural products.Translational recoding in archaea.The molecular characterization of a novel GH38 α-mannosidase from the crenarchaeon Sulfolobus solfataricus revealed its ability in de-mannosylating glycoproteins.The gene of an archaeal alpha-L-fucosidase is expressed by translational frameshifting.Novel thermophilic hemicellulases for the conversion of lignocellulose for second generation biorefineries.Pharmacological enhancement of α-glucosidase by the allosteric chaperone N-acetylcysteine.Structure of human lysosomal acid α-glucosidase-a guide for the treatment of Pompe disease.Identification of an archaeal alpha-L-fucosidase encoded by an interrupted gene. Production of a functional enzyme by mutations mimicking programmed -1 frameshifting.Thermophilic glycosynthases for oligosaccharides synthesis.Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering.The identification and molecular characterization of the first archaeal bifunctional exo-β-glucosidase/N-acetyl-β-glucosaminidase demonstrate that family GH116 is made of three functionally distinct subfamilies.A comparative infrared spectroscopic study of glycoside hydrolases from extremophilic archaea revealed different molecular mechanisms of adaptation to high temperatures.Activity and stability of hyperthermophilic enzymes: a comparative study on two archaeal beta-glycosidases.Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant.RNA editing and modifications of RNAs might have favoured the evolution of the triplet genetic code from an ennuplet code.Functional characterization and high-throughput proteomic analysis of interrupted genes in the archaeon Sulfolobus solfataricus.Probing the catalytically essential residues of the alpha-L-fucosidase from the hyperthermophilic archaeon Sulfolobus solfataricus.A novel α-d-galactosynthase from Thermotoga maritima converts β-d-galactopyranosyl azide to α-galacto-oligosaccharidesExtremophilic (Hemi)cellulolytic Microorganisms and EnzymesExploitation of β-glycosyl azides for the preparation of α-glycosynthasesCorrigendum: Glycosynthases in BiocatalysisGlycosynthases in BiocatalysisCarbohydrate-Active Enzymes from Hyperthermophiles: Biochemistry and ApplicationsDesign of new reaction conditions for characterization of a mutant thermophilicα-l-fucosidaseStructural basis of the destabilization produced by an amino-terminal tag in the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricusRecent Advances in the Oligosaccharide Synthesis Promoted by Catalytically Engineered GlycosidasesRecent Developments in the Synthesis of Oligosaccharides by Hyperthermophilic GlycosidasesTwo-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding eApplications in Biocatalysis of Glycosyl Hydrolases from the Hyperthermophilic ArchaeonSulfolobus solfataricusIonic network at the C-terminus of the ?-glycosidase from the hyperthermophilic archaeonSulfolobus solfataricus: Functional role in the quaternary structure thermal stabilizationBiotechnologyIdentification of a novel esterase from the thermophilic bacterium Geobacillus thermodenitrificans NG80-2GlcNAc De-N-Acetylase from the Hyperthermophilic Archaeon Sulfolobus solfataricus
P50
Q27658017-E7AE01AB-D73A-40B0-A068-1AD68CBFE4E1Q33567476-02DBBF51-E88C-49CE-B765-690EBCAC2BCDQ36013846-F35A93D4-0DD2-45BB-9E32-E0280235A5D9Q36660530-BEFBA016-5276-48D0-89F4-37063A6E8EE9Q36905499-03FD5BD9-32ED-4230-AA4C-AAF09A242840Q37119438-61CCFC03-6E7E-4F04-BF06-0AA44293BD0EQ37803473-DF0B677F-C8A6-44A7-82D6-8A3038E2875BQ38002738-C0D78A27-F35B-432B-919C-7772F2F10E5CQ38046766-2B7D53CB-FC86-45FD-87DB-074B490F4D7BQ38341817-E91621B5-92D6-48B8-951B-36B7DACCC928Q38756317-22538B59-2FEC-4392-A426-ED17521A47A3Q40691209-93CDB9AD-B5C5-4287-8DC2-4217F2619260Q41912890-EB08112F-B453-4F67-9A6C-E5C9006FE537Q42645986-511376C2-C4B5-4FA2-8F53-6972C15111DAQ42694224-04221C14-4244-4F16-BCBE-7986F6009CF4Q43015478-043E32A8-5491-4FB0-B155-A950D130B51DQ43015917-E7E10B77-A21D-4077-9F0F-32F7761F3404Q43019539-A73A586B-0BC5-46AB-8217-7189D7BDC57AQ43022305-4FB8AFF8-92A2-4FCD-8B89-1204BC51C4EDQ43027742-6BE95EF7-3755-4844-AB6D-1CC6A796620CQ44544829-DFD6ED4C-B8CD-476B-8F18-9E4583B6A3F9Q46882145-2F111673-ECA7-4498-BFB6-23DD933461D3Q46953049-665325BE-6C6E-4CB7-B969-BCA1CD0641F9Q54170368-EED02262-EDB1-4071-87F6-69E7D048C313Q57436452-CE93E597-71EC-49D8-B71F-647B1BDF397EQ58412958-E77E1F48-34E9-4BAA-ABA7-C77A59E852C2Q58412972-E5ECFCAC-17A4-4FB5-B5AC-0C759DB1D95DQ58412980-0CC625EF-70F2-47D9-B470-A09AD296A1F8Q58412984-2CEF7BE7-097C-4F42-8AE8-B17DBA588968Q58412996-8F7A0936-DC25-445B-87FD-01D967534F37Q58413025-E239232A-A310-4FB4-A00A-216C28B26F7EQ58413038-D81670C0-FFEA-4E92-8EED-47832D37688BQ58413049-8C59B450-19C2-4959-AB2B-C9B7E257804EQ58413054-F35060FC-09CA-414A-A6A6-D7B28593825AQ58413066-BFC13323-6690-4E34-9AFF-00E7FE76CD8DQ58413077-F9B543DA-A811-4978-A0AB-1D4495011346Q58413098-07980AEC-C9B4-4E6E-9A9D-BA885EBA14F2Q58413116-24E87220-AE54-41CE-815B-1593C7C0C46DQ91753506-316D4C21-9BB6-4CFD-83CA-4FE899C9662DQ93183361-B22D4D27-84E6-4706-9557-436D6540B8C5
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Beatrice Cobucci-Ponzano
@ast
Beatrice Cobucci-Ponzano
@en
Beatrice Cobucci-Ponzano
@es
Beatrice Cobucci-Ponzano
@nl
Beatrice Cobucci-Ponzano
@sl
type
label
Beatrice Cobucci-Ponzano
@ast
Beatrice Cobucci-Ponzano
@en
Beatrice Cobucci-Ponzano
@es
Beatrice Cobucci-Ponzano
@nl
Beatrice Cobucci-Ponzano
@sl
altLabel
Beatrice Cobucci Ponzano
@en
Beatrice CobucciPonzano
@en
prefLabel
Beatrice Cobucci-Ponzano
@ast
Beatrice Cobucci-Ponzano
@en
Beatrice Cobucci-Ponzano
@es
Beatrice Cobucci-Ponzano
@nl
Beatrice Cobucci-Ponzano
@sl
P106
P1153
6603003946
P21
P31
P496
0000-0002-8211-2297