An integrated computational analysis of the structure, dynamics, and ligand binding interactions of the human galectin network

Galectins, a family of evolutionarily conserved animal lectins, have been shown to modulate signaling processes leading to inflammation, apoptosis, immunoregulation, and angiogenesis through their ability to interact with poly-N-acetyllactosamine-enriched glycoconjugates. To date 16 human galectin c...

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Guardado en:
Detalles Bibliográficos
Autores principales: Guardia, Carlos Manuel Alberto, Gauto, Diego Fernando, Martí, Marcelo Adrián, Estrin, Dario Ariel
Publicado: 2011
Materias:
Angiogenesis
Carbohydrate-recognition domains
Classical molecular dynamics
Computational analysis
Dynamics characteristic
Entropy value
Galectins
Glycoconjugates
Immunoregulation
Ligand affinity
Ligand binding
Molecular levels
Protein-ligand interactions
Sequence analysis
Signaling process
Specific inhibitors
Structural differences
Structural information
Binding energy
Binding sites
Carbohydrates
Cell death
Computational methods
Dynamics
Glucose
Molecular dynamics
Proteins
Structural analysis
Tissue
Ligands
epitope
galectin
galectin 12, human
galectin 4
LGALS13 protein, human
ligand
placenta protein
poly N acetyllactosamine
poly-N-acetyllactosamine
polysaccharide
amino acid sequence
article
binding site
chemical structure
chemistry
entropy
human
immunology
metabolism
methodology
molecular dynamics
molecular genetics
nuclear magnetic resonance spectroscopy
phylogeny
physiology
protein binding
protein database
protein tertiary structure
sequence homology
signal transduction
systems biology
X ray crystallography
Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
Databases, Protein
Entropy
Epitopes
Galectin 4
Humans
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Dynamics Simulation
Molecular Sequence Data
Phylogeny
Polysaccharides
Pregnancy Proteins
Protein Binding
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Signal Transduction
Systems Biology
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15499596_v51_n8_p1918_Guardia
http://hdl.handle.net/20.500.12110/paper_15499596_v51_n8_p1918_Guardia
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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