Search Results - "Damager, I"
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1
Nanocoating of dental implants with pectins
Published in Bone (New York, N.Y.) (01-05-2011)Get full text
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Structural Insights into the Catalytic Mechanism of Trypanosoma cruzi trans-Sialidase
Published in Structure (London) (01-05-2004)“…Sialidases are a superfamily of sialic-acid-releasing enzymes that are of significant interest due to their implication as virulence factors in the…”
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Trypanosoma cruzi Trans-sialidase Operates through a Covalent Sialyl−Enzyme Intermediate: Tyrosine Is the Catalytic Nucleophile
Published in Journal of the American Chemical Society (25-06-2003)“…Modified sialic acid substrates have been used to label Trypanosoma cruzi trans-sialidase, demonstrating that the enzyme catalyses the transfer of sialic acid…”
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4
Functional characterisation of a putative rhamnogalacturonan II specific xylosyltransferase
Published in FEBS letters (22-09-2008)“…An Arabidopsis thaliana gene, At1g56550, was expressed in Pichia pastoris and the recombinant protein was shown to catalyse transfer of d-xylose from UDP-α-…”
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5
Affecting osteoblastic responses with in vivo engineered potato pectin fragments
Published in Journal of biomedical materials research. Part A (01-01-2012)“…Pectins, complex plant‐derived polysaccharides, are novel candidates for biomaterial nanocoatings. Pectic rhamnogalacturonan‐I regions (RG‐I) can be…”
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6
Chemical synthesis of 6‴-α-maltotriosyl-maltohexaose as substrate for enzymes in starch biosynthesis and degradation
Published in Carbohydrate research (20-07-1999)“…A branched nonasaccharide 6‴-α-maltotriosyl-maltohexaose was synthesised in 40 steps from d-glucose and maltose. Phenyl O-(2,3,4,6-tetra- O-benzyl-α-…”
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7
Modulation of activity and substrate binding modes by mutation of single and double subsites +1/+2 and −5/−6 of barley α‐amylase 1
Published in European journal of biochemistry (01-12-2001)“…Enzymatic properties of barley α‐amylase 1 (AMY1) are altered as a result of amino acid substitutions at subsites −5/−6 (Cys95→Ala/Thr) and +1/+2…”
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The action of starch synthase II on 6′′′‐α‐maltotriosyl‐maltohexaose comprising the branch point of amylopectin
Published in European journal of biochemistry (01-09-2001)“…The principle of using a chemically synthesized, well‐defined branched oligosaccharide to provide a more detailed knowledge of the substrate specificity of…”
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