Oligomerization of the Hemolytic Lectin CEL-III from the Marine InvertebrateCucumaria echinataInduced by the Binding of Carbohydrate Ligands

Oligomerization of the Hemolytic Lectin CEL-III from the Marine InvertebrateCucumaria echinataInduced by the Binding of Carbohydrate Ligands

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http://www.wikidata.org/entity/Q57838368
C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-III containing ricin-type -trefoil foldsHemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.Calcium ions stabilize a protein structure of hemolytic lectin CEL-III from marine invertebrate Cucumaria echinata.Molecular cloning, expression, and characterization of novel hemolytic lectins from the mushroom Laetiporus sulphureus, which show homology to bacterial toxins.Involvement of laser photo-CIDNP (chemically induced dynamic nuclear polarization)-reactive amino acid side chains in ligand binding by galactoside-specific lectins in solution.Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate.Animal lectins.Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata.Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism.Lectin from the Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni.Amino acid sequence and carbohydrate-binding analysis of the N-acetyl-D-galactosamine-specific C-type lectin, CEL-I, from the Holothuroidea, Cucumaria echinata.Characteristic recognition of N-acetylgalactosamine by an invertebrate C-type Lectin, CEL-I, revealed by X-ray crystallographic analysis.Effects of detergents on the oligomeric structures of hemolytic lectin CEL-III as determined by small-angle X-ray scattering.Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-III.Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III.Molecular cloning, functional expression, and characterization of isolectin genes of hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata.
P2860

Oligomerization of the Hemolytic Lectin CEL-III from the Marine InvertebrateCucumaria echinataInduced by the Binding of Carbohydrate Ligands

Item
http://www.wikidata.org/entity/Q57838368
description
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
im Juli 1996 veröffentlichter wissenschaftlicher Artikel
@de
scientific article published in Journal of Biological Chemistry
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в липні 1996
@uk
name
Oligomerization of the Hemolyt ...... inding of Carbohydrate Ligands
@en
Oligomerization of the Hemolyt ...... inding of Carbohydrate Ligands
@nl
type
label
Oligomerization of the Hemolyt ...... inding of Carbohydrate Ligands
@en
Oligomerization of the Hemolyt ...... inding of Carbohydrate Ligands
@nl
prefLabel
Oligomerization of the Hemolyt ...... inding of Carbohydrate Ligands
@en
Oligomerization of the Hemolyt ...... inding of Carbohydrate Ligands
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Oligomerization of the hemolyt ...... inding of carbohydrate ligands
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698