Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars.
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Fungal hemolysinsClostridium perfringens epsilon toxin: a malevolent molecule for animals and man?Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.Structure of a membrane-attack complex/perforin (MACPF) family protein from the human gut symbiont Bacteroides thetaiotaomicronStructural basis for sugar recognition, including the Tn carcinoma antigen, by the lectin SNA-II from Sambucus nigraCrystal Structure of Clostridium perfringens Enterotoxin Displays Features of -Pore-forming ToxinsStructures of Lysenin Reveal a Shared Evolutionary Origin for Pore-Forming Proteins And Its Mode of Sphingomyelin RecognitionBivalent Carbohydrate Binding Is Required for Biological Activity of Clitocybe nebularis Lectin (CNL), the N,N'-Diacetyllactosediamine (GalNAc 1-4GlcNAc, LacdiNAc)-specific Lectin from Basidiomycete C. nebularisPlasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence SystemGlycan Specificity of the Vibrio vulnificus Hemolysin Lectin Outlines Evolutionary History of Membrane Targeting by a Toxin FamilyCrystal structure of BinB: a receptor binding component of the binary toxin from Lysinibacillus sphaericusAtomic-resolution structure of the α-galactosyl binding Lyophyllum decastes lectin reveals a new protein family found in both fungi and plantsStructural basis for receptor recognition and pore formation of a zebrafish aerolysin-like proteinDe novo phasing with X-ray laser reveals mosquito larvicide BinAB structureX-ray and Cryo-electron Microscopy Structures of Monalysin Pore-forming Toxin Reveal Multimerization of the Pro-form.Hemolytic lectin CEL-III heptamerizes via a large structural transition from α-helices to a β-barrel during the transmembrane pore formation process.A rivet model for channel formation by aerolysin-like pore-forming toxinsExtending the aerolysin family: from bacteria to vertebrates.Structural insights into Bacillus thuringiensis Cry, Cyt and parasporin toxinsStructure and sequence analyses of Bacteroides proteins BVU_4064 and BF1687 reveal presence of two novel predominantly-beta domains, predicted to be involved in lipid and cell surface interactions.Functional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxinDietary Plant Lectins Appear to Be Transported from the Gut to Gain Access to and Alter Dopaminergic Neurons of Caenorhabditis elegans, a Potential Etiology of Parkinson's Disease.Coenzyme depletion by members of the aerolysin family of pore-forming toxins leads to diminished ATP levels and cell death.Molecular basis of toxicity of Clostridium perfringens epsilon toxin.Lectins from edible mushrooms.NMR studies on the interaction of sugars with the C-terminal domain of an R-type lectin from the earthworm Lumbricus terrestris.Mushroom lectins: specificity, structure and bioactivity relevant to human disease.Hitting the sweet spot-glycans as targets of fungal defense effector proteins.Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies.Isolation and characterization of a novel thermostable lectin from the wild edible mushroom Agaricus arvensis.Purification, characterization and cloning of a ricin B-like lectin from mushroom Clitocybe nebularis with antiproliferative activity against human leukemic T cells.Crystallization and preliminary crystallographic analysis of the catalytic module of endolysin from Cp-7, a phage infecting Streptococcus pneumoniae.Amaranthin-Like Proteins with Aerolysin Domains in Plants.A pore-forming protein implements VLR-activated complement cytotoxicity in lampreyStructural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family.Remediation capacity of Cd and Pb ions by mycelia of Imleria badia, Laetiporus sulphureus, and Agaricus bisporus in vitro cultures.β-Trefoil structure enables interactions between lectins and protease inhibitors that regulate their biological functions.A novel β-trefoil lectin from the parasol mushroom (Macrolepiota procera) is nematotoxic.
P2860
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P2860
Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars.
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Structural analysis of the Lae ...... lectin in complex with sugars.
@ast
Structural analysis of the Lae ...... lectin in complex with sugars.
@en
Structural analysis of the Lae ...... lectin in complex with sugars.
@nl
type
label
Structural analysis of the Lae ...... lectin in complex with sugars.
@ast
Structural analysis of the Lae ...... lectin in complex with sugars.
@en
Structural analysis of the Lae ...... lectin in complex with sugars.
@nl
prefLabel
Structural analysis of the Lae ...... lectin in complex with sugars.
@ast
Structural analysis of the Lae ...... lectin in complex with sugars.
@en
Structural analysis of the Lae ...... lectin in complex with sugars.
@nl
P2860
P50
P356
P1476
Structural analysis of the Lae ...... lectin in complex with sugars.
@en
P2093
Irwin J Goldstein
José M Mancheño
P2860
P304
17251-17259
P356
10.1074/JBC.M413933200
P407
P577
2005-02-01T00:00:00Z