Monica M. Palcic spends much of her time researching Biochemistry, Enzyme, Glycosyltransferase, Stereochemistry and Oligosaccharide. Her work on Biochemistry is being expanded to include thematically relevant topics such as Rational design. Monica M. Palcic interconnects Biocatalysis, Cell culture and Nucleotide in the investigation of issues within Enzyme.
Her Glycosyltransferase research is multidisciplinary, incorporating elements of Fucosyltransferase, Residue, Mutant, Antigen and Escherichia coli. Her Disaccharide study in the realm of Stereochemistry connects with subjects such as Acceptor. Her work deals with themes such as Fucosyltransferases, Glycoconjugate, Chemical synthesis and Polyacrylamide, which intersect with Oligosaccharide.
Stereochemistry, Biochemistry, Enzyme, Glycosyltransferase and Chromatography are her primary areas of study. Her biological study spans a wide range of topics, including Oligosaccharide and Substrate. Her Oligosaccharide research is multidisciplinary, relying on both Glycosylation and Enzymatic synthesis.
Her Biochemistry study combines topics in areas such as Molecular biology and Antigen. Her work deals with themes such as Residue and Nucleotide, which intersect with Enzyme. In her study, Crystal structure is inextricably linked to Mutant, which falls within the broad field of Glycosyltransferase.
Monica M. Palcic focuses on Biochemistry, Glycosyltransferase, Stereochemistry, Enzyme and Active site. Her Glycosyltransferase research includes themes of Glycosyl, Crystallography, Trisaccharide, Glycosylation and Glycolipid. Her Stereochemistry study incorporates themes from H antigen, Substrate, Mutant and ABO blood group system.
Her Enzyme study combines topics from a wide range of disciplines, such as Glycoconjugate and Galactose. Her Active site research incorporates themes from Transferase and Binding site. Her study in Binding site is interdisciplinary in nature, drawing from both Amino acid and Catalytic cycle.
Monica M. Palcic mainly investigates Biochemistry, Capillary electrophoresis, Glycosyltransferase, Starch and Glycosphingolipid. Her work on Enzyme, Metabolic pathway, Molecular model and Mode of action as part of general Biochemistry study is frequently connected to Molecular targets, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. Her primary area of study in Enzyme is in the field of Biosynthesis.
The Glycosyltransferase study combines topics in areas such as Covalent bond, Trisaccharide, Anomer, Stereochemistry and Glycobiology. She works on Stereochemistry which deals in particular with Glycosyl. Monica M. Palcic interconnects BODIPY, Chromatography and Fluorescence spectroscopy in the investigation of issues within Glycosphingolipid.
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The use of hydrophobic synthetic glycosides as acceptors in glycosyltransferase assays
Monica M Palcic;Louis D Heerze;Michael Pierce;Ole Hindsgaul.
Glycoconjugate Journal (1988)
The structural basis for specificity in human ABO(H) blood group biosynthesis
Sonia I. Patenaude;Nina O.L. Seto;Nina O.L. Seto;Svetlana N. Borisova;Adam Szpacenko.
Nature Structural & Molecular Biology (2002)
A continuous spectrophotometric assay for monoamine oxidase and related enzymes in tissue homogenates
Andrew Holt;Dennis F. Sharman;Glen B. Baker;Monica M. Palcic.
Analytical Biochemistry (1997)
Acceptor-substrate recognition by N-acetylglucosaminyltransferase-V: Critical role of the 4″-hydroxyl group in β-d-GlcpNAc-(1 → 2)-α-d-Manp(1 → 6)-β-d-Glcp-OR
Osamu Kanie;Suzanne C. Crawley;Monica M. Palcic;Ole Hindsgaul.
Carbohydrate Research (1993)
Recent structures, evolution and mechanisms of glycosyltransferases.
Christelle Breton;Sylvie Fournel-Gigleux;Monica M Palcic.
Current Opinion in Structural Biology (2012)
Identification of topaquinone and its consensus sequence in copper amine oxidases.
S. M. Janes;M. M. Palcic;C. H. Scaman;A. J. Smith.
Acceptor specificity of different length constructs of human recombinant alpha 1,3/4-fucosyltransferases. Replacement of the stem region and the transmembrane domain of fucosyltransferase V by protein A results in an enzyme with GDP-fucose hydrolyzing activity.
Theodora de Vries;Theodora de Vries;Cheryl A. Srnka;Monica M. Palcic;Stuart J. Swiedler.
Journal of Biological Chemistry (1995)
α-Glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
C. Stewart Gillmor;C. Stewart Gillmor;Patricia Poindexter;Justin L. Lorieau;Monica M. Palcic.
Journal of Cell Biology (2002)
Biocatalytic synthesis of oligosaccharides.
Monica M Palcic.
Current Opinion in Biotechnology (1999)
A Continuous Spectrophotometric Assay for Glycosyltransferases
S. Gosselin;M. Alhussaini;M.B. Streiff;K. Takabayashi.
Analytical Biochemistry (1994)
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