Chemical Communications, ISSN 1359-7345, 2008, Issue 37, pp. 4400 - 4412
Carbohydrate arrays (glycoarrays) have recently emerged as a high-throughput tool for studying carbohydrate-binding proteins and carbohydrate-processing...
LABEL-FREE | ENZYMATIC GLYCOSYLATION | SELF-ASSEMBLED MONOLAYERS | CHEMOENZYMATIC SYNTHESIS | SURFACE-PLASMON RESONANCE | OLIGOSACCHARIDE PROBES NEOGLYCOLIPIDS | GLYCAN-BINDING-PROTEINS | INFLUENZA-VIRUSES | CHEMISTRY, MULTIDISCIPLINARY | PLANT-CELL WALLS | MICROARRAY ANALYSIS | Enzymes - chemistry | Substrate Specificity | Proteins - chemistry | Carbohydrates - chemistry | Enzymes - metabolism
LABEL-FREE | ENZYMATIC GLYCOSYLATION | SELF-ASSEMBLED MONOLAYERS | CHEMOENZYMATIC SYNTHESIS | SURFACE-PLASMON RESONANCE | OLIGOSACCHARIDE PROBES NEOGLYCOLIPIDS | GLYCAN-BINDING-PROTEINS | INFLUENZA-VIRUSES | CHEMISTRY, MULTIDISCIPLINARY | PLANT-CELL WALLS | MICROARRAY ANALYSIS | Enzymes - chemistry | Substrate Specificity | Proteins - chemistry | Carbohydrates - chemistry | Enzymes - metabolism
Journal Article
Biochimie, ISSN 0300-9084, 09/2016, Volume 128-129, pp. 34 - 47
Occurrence of the adhesion/growth-regulatory galectins as family sets the challenge to achieve a complete network analysis. Along this route taken for a...
Fiber cells | In-source decay | Lectin | Phylogenesis | Lens | ADHESION/GROWTH-REGULATORY GALECTINS | GLYCAN-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | PANCREATIC-CARCINOMA MODEL | DOWN-REGULATION | CELL-GROWTH | GALACTOSIDE-BINDING LECTIN | STRUCTURAL FEATURES | ADHERENS JUNCTION PROTEIN | ANIMAL LECTINS | MOLECULAR-CLONING | Immunohistochemistry | Galectins - classification | Humans | Protein Multimerization | Phylogeny | Gene Regulatory Networks | Avian Proteins - chemistry | Lactose - metabolism | Eye Proteins - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Avian Proteins - metabolism | Lens, Crystalline - metabolism | Rats | Recombinant Proteins - chemistry | Gene Expression Profiling - methods | Binding Sites - genetics | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Sequence Homology, Amino Acid | Animals | Eye Proteins - classification | Eye Proteins - metabolism | Chickens | Protein Binding | Galectins - genetics | Galectins - metabolism | Avian Proteins - genetics | Genetic research | Lactose | Squamous cell carcinoma | Mass spectrometry | Analysis
Fiber cells | In-source decay | Lectin | Phylogenesis | Lens | ADHESION/GROWTH-REGULATORY GALECTINS | GLYCAN-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | PANCREATIC-CARCINOMA MODEL | DOWN-REGULATION | CELL-GROWTH | GALACTOSIDE-BINDING LECTIN | STRUCTURAL FEATURES | ADHERENS JUNCTION PROTEIN | ANIMAL LECTINS | MOLECULAR-CLONING | Immunohistochemistry | Galectins - classification | Humans | Protein Multimerization | Phylogeny | Gene Regulatory Networks | Avian Proteins - chemistry | Lactose - metabolism | Eye Proteins - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Avian Proteins - metabolism | Lens, Crystalline - metabolism | Rats | Recombinant Proteins - chemistry | Gene Expression Profiling - methods | Binding Sites - genetics | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Sequence Homology, Amino Acid | Animals | Eye Proteins - classification | Eye Proteins - metabolism | Chickens | Protein Binding | Galectins - genetics | Galectins - metabolism | Avian Proteins - genetics | Genetic research | Lactose | Squamous cell carcinoma | Mass spectrometry | Analysis
Journal Article
Journal of The American Society for Mass Spectrometry, ISSN 1044-0305, 7/2018, Volume 29, Issue 7, pp. 1493 - 1504
Catch-and-release electrospray ionization mass spectrometry (CaR-ESI-MS), implemented using model membranes (MMs), is a promising approach for the discovery of...
Biotechnology | Model membranes | Glycolipid | Screening | Chemistry | Analytical Chemistry | Proteomics | Glycan-binding protein | Picodiscs | Catch-and-release electrospray ionization mass spectrometry | Bioinformatics | Organic Chemistry | Nanodiscs | CHEMISTRY, ANALYTICAL | CHOLESTEROL | SCREENING GLYCOLIPIDS | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | RECEPTOR | MICELLES | IONIZATION-MASS-SPECTROMETRY | LIPID-BILAYERS | SPECTROSCOPY | CHOLERA-TOXIN BINDING | SAPOSIN | GANGLIOSIDE GM1 | Usage | Ionization | Lipids | Cholera toxin | Collisions (Nuclear physics) | Comparative analysis | Medical screening | Binding proteins | Mass spectrometry | Protein binding | Binding | Brain | Membranes | Ions | Phospholipids | Glycan | Proteins | Ligands | Cholera
Biotechnology | Model membranes | Glycolipid | Screening | Chemistry | Analytical Chemistry | Proteomics | Glycan-binding protein | Picodiscs | Catch-and-release electrospray ionization mass spectrometry | Bioinformatics | Organic Chemistry | Nanodiscs | CHEMISTRY, ANALYTICAL | CHOLESTEROL | SCREENING GLYCOLIPIDS | BIOCHEMICAL RESEARCH METHODS | CHEMISTRY, PHYSICAL | RECEPTOR | MICELLES | IONIZATION-MASS-SPECTROMETRY | LIPID-BILAYERS | SPECTROSCOPY | CHOLERA-TOXIN BINDING | SAPOSIN | GANGLIOSIDE GM1 | Usage | Ionization | Lipids | Cholera toxin | Collisions (Nuclear physics) | Comparative analysis | Medical screening | Binding proteins | Mass spectrometry | Protein binding | Binding | Brain | Membranes | Ions | Phospholipids | Glycan | Proteins | Ligands | Cholera
Journal Article
VIRUSES-BASEL, ISSN 1999-4915, 06/2016, Volume 8, Issue 6
Cyanovirin-N (CV-N) is an antiviral lectin with potent activity against enveloped viruses, including HIV. The mechanism of action involves high affinity...
Cyanovirin-N | oligomannose | RECOMBINANT VACCINIA VIRUS | CONTAINS 2 | CRYSTAL-STRUCTURE | ENVELOPE GLYCOPROTEIN | antiviral lectins | glycan-binding proteins | PRIMARY MACROPHAGES | VIROLOGY | TYPE-1 TROPISM | gp120 | HIV-INACTIVATING PROTEIN | DOMAIN-SWAPPED STRUCTURE | T-CELL LINES | CARBOHYDRATE-BINDING AGENTS | Antiviral Agents - pharmacology | Temperature | Magnetic Resonance Spectroscopy | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Protein Folding | Polysaccharides - metabolism | Carrier Proteins - genetics | Bacterial Proteins - pharmacology | Antiviral Agents - chemistry | Carrier Proteins - pharmacology | Protein Binding | Carrier Proteins - chemistry | Protein Stability | Circular Dichroism
Cyanovirin-N | oligomannose | RECOMBINANT VACCINIA VIRUS | CONTAINS 2 | CRYSTAL-STRUCTURE | ENVELOPE GLYCOPROTEIN | antiviral lectins | glycan-binding proteins | PRIMARY MACROPHAGES | VIROLOGY | TYPE-1 TROPISM | gp120 | HIV-INACTIVATING PROTEIN | DOMAIN-SWAPPED STRUCTURE | T-CELL LINES | CARBOHYDRATE-BINDING AGENTS | Antiviral Agents - pharmacology | Temperature | Magnetic Resonance Spectroscopy | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Protein Folding | Polysaccharides - metabolism | Carrier Proteins - genetics | Bacterial Proteins - pharmacology | Antiviral Agents - chemistry | Carrier Proteins - pharmacology | Protein Binding | Carrier Proteins - chemistry | Protein Stability | Circular Dichroism
Journal Article
ELECTROPHORESIS, ISSN 0173-0835, 06/2016, Volume 37, Issue 11, pp. 1437 - 1447
Glycosaminoglycans (GAGs) are linear, highly sulfated polysaccharides expressed by almost all animal cells. They occur as soluble molecules, or form...
Proteins | Glycosaminoglycan | Pull‐down | Glycan binding | Proteomics | Pull-down | COFACTOR ACTIVITY | CHEMISTRY, ANALYTICAL | BINDS HEPARIN | BIOCHEMICAL RESEARCH METHODS | FIBROBLAST-GROWTH-FACTOR | BRUCHS MEMBRANE | IDENTIFICATION | COMPLEMENT FACTOR-H | AFFINITY | BIOSYNTHESIS | ENDOTHELIAL-CELLS | HEPARAN-SULFATE PROTEOGLYCANS | Animals | Humans | Protein Binding | Ligands | Blood Proteins - chemistry | Proteins - chemistry | Proteomics - methods | Glycosaminoglycans - chemistry | Binding proteins | Sulfates | Cells | Blood proteins | Protein binding | Human | Binding | Affinity | Selectivity | Glycan
Proteins | Glycosaminoglycan | Pull‐down | Glycan binding | Proteomics | Pull-down | COFACTOR ACTIVITY | CHEMISTRY, ANALYTICAL | BINDS HEPARIN | BIOCHEMICAL RESEARCH METHODS | FIBROBLAST-GROWTH-FACTOR | BRUCHS MEMBRANE | IDENTIFICATION | COMPLEMENT FACTOR-H | AFFINITY | BIOSYNTHESIS | ENDOTHELIAL-CELLS | HEPARAN-SULFATE PROTEOGLYCANS | Animals | Humans | Protein Binding | Ligands | Blood Proteins - chemistry | Proteins - chemistry | Proteomics - methods | Glycosaminoglycans - chemistry | Binding proteins | Sulfates | Cells | Blood proteins | Protein binding | Human | Binding | Affinity | Selectivity | Glycan
Journal Article
Journal of Computational Chemistry, ISSN 0192-8651, 11/2014, Volume 35, Issue 30, pp. 2177 - 2183
Carbohydrate‐binding proteins (CBPs) are potential biomarkers and drug targets. However, the interactions between carbohydrates and proteins are challenging to...
carbohydrate binding | structural alignment | protein function prediction | glycan binding | statistical energy function | sugar binding | knowledge‐based energy function | Knowledge-based energy function | Sugar binding | Protein function prediction | Structural alignment | Statistical energy function | Carbohydrate binding | Glycan binding | RECOGNITION | CRYSTAL-STRUCTURE | CLASSIFICATION | knowledge-based energy function | GLYCOSYLATION | CHEMISTRY, MULTIDISCIPLINARY | DATABASE | ALIGNMENT | SITES | MICROARRAYS | DOMAINS | REVEALS | Models, Molecular | Protein Conformation | Receptors, Cell Surface - chemistry | Binding Sites | Binding proteins | Chemical properties | Protein binding
carbohydrate binding | structural alignment | protein function prediction | glycan binding | statistical energy function | sugar binding | knowledge‐based energy function | Knowledge-based energy function | Sugar binding | Protein function prediction | Structural alignment | Statistical energy function | Carbohydrate binding | Glycan binding | RECOGNITION | CRYSTAL-STRUCTURE | CLASSIFICATION | knowledge-based energy function | GLYCOSYLATION | CHEMISTRY, MULTIDISCIPLINARY | DATABASE | ALIGNMENT | SITES | MICROARRAYS | DOMAINS | REVEALS | Models, Molecular | Protein Conformation | Receptors, Cell Surface - chemistry | Binding Sites | Binding proteins | Chemical properties | Protein binding
Journal Article
Biopolymers, ISSN 0006-3525, 10/2013, Volume 99, Issue 10, pp. 796 - 806
ABSTRACT Interactions between proteins and soluble carbohydrates and/or surface displayed glycans are central to countless recognition, attachment and...
glycan binding | multivalent | oligomannose | complex‐type glycan | complex-type glycan | NOD FACTORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | POTENT | BIOPHYSICS | CYANOVIRIN-N | STRUCTURAL BASIS | TRANSFER DIFFERENCE NMR | DC-SIGN | HIV-INACTIVATING PROTEIN | LIGAND | STD NMR | BINDING | Polysaccharides - chemistry | Protein Binding | Proteins - chemistry | Carbohydrates - chemistry | Magnetic Resonance Spectroscopy | Binding Sites | Proteins | Nuclear magnetic resonance spectroscopy | Polysaccharides | Protein binding
glycan binding | multivalent | oligomannose | complex‐type glycan | complex-type glycan | NOD FACTORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | POTENT | BIOPHYSICS | CYANOVIRIN-N | STRUCTURAL BASIS | TRANSFER DIFFERENCE NMR | DC-SIGN | HIV-INACTIVATING PROTEIN | LIGAND | STD NMR | BINDING | Polysaccharides - chemistry | Protein Binding | Proteins - chemistry | Carbohydrates - chemistry | Magnetic Resonance Spectroscopy | Binding Sites | Proteins | Nuclear magnetic resonance spectroscopy | Polysaccharides | Protein binding
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 7/2011, Volume 80, Issue 1, pp. 797 - 823
In the last decade, glycan microarrays have revolutionized the analysis of the specificity of glycan-binding proteins (GBPs), providing information that...
glycan-binding protein | glycomics | lectin | carbohydrate | C-TYPE LECTIN | BLOOD-GROUP ANTIGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-SURFACE | PROTEIN-CARBOHYDRATE INTERACTIONS | RECEPTOR-BINDING SPECIFICITY | STRUCTURAL BASIS | SURFACE-PLASMON RESONANCE | ADAPTIVE IMMUNE-RESPONSES | INFLUENZA-VIRUSES | ARRAY-SCREENING-REVEALS | Carbohydrate Sequence | Microarray Analysis - methods | Glycomics - methods | Humans | Molecular Sequence Data | Polysaccharides - analysis | Animals | Proteins - metabolism | Protein Binding | Molecular Structure | Plant Lectins - chemistry | Proteins - chemistry | Carbohydrate Conformation | Plant Lectins - metabolism | Physiological aspects | Glycoproteins | Research | Proteomics | Lectin | Carbohydrate | Microarray | Glycan-Binding Protein | Glycomics | Glycan
glycan-binding protein | glycomics | lectin | carbohydrate | C-TYPE LECTIN | BLOOD-GROUP ANTIGENS | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-SURFACE | PROTEIN-CARBOHYDRATE INTERACTIONS | RECEPTOR-BINDING SPECIFICITY | STRUCTURAL BASIS | SURFACE-PLASMON RESONANCE | ADAPTIVE IMMUNE-RESPONSES | INFLUENZA-VIRUSES | ARRAY-SCREENING-REVEALS | Carbohydrate Sequence | Microarray Analysis - methods | Glycomics - methods | Humans | Molecular Sequence Data | Polysaccharides - analysis | Animals | Proteins - metabolism | Protein Binding | Molecular Structure | Plant Lectins - chemistry | Proteins - chemistry | Carbohydrate Conformation | Plant Lectins - metabolism | Physiological aspects | Glycoproteins | Research | Proteomics | Lectin | Carbohydrate | Microarray | Glycan-Binding Protein | Glycomics | Glycan
Journal Article