Resistance to a bacterial toxin is mediated by removal of a conserved glycosylation pathway required for toxin-host interactions.
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The genome of the heartworm, Dirofilaria immitis, reveals drug and vaccine targetsWorms and flies as genetically tractable animal models to study host-pathogen interactionsRole of receptors in Bacillus thuringiensis crystal toxin activityDiversity and specificity in the interaction between Caenorhabditis elegans and the pathogen Serratia marcescensPromotion of bone morphogenetic protein signaling by tetraspanins and glycosphingolipidsNeuronal Goα and CAPS regulate behavioral and immune responses to bacterial pore-forming toxinsCandidate genes revealed by a genome scan for mosquito resistance to a bacterial insecticide: sequence and gene expression variationsStructure and Glycolipid Binding Properties of the Nematicidal Protein Cry5BMechanistic and single-dose in vivo therapeutic studies of Cry5B anthelmintic action against hookwormsBacillus thuringiensis-derived Cry5B has potent anthelmintic activity against Ascaris suumThe Drosophila melanogaster homologue of the human histo-blood group Pk gene encodes a glycolipid-modifying alpha1,4-N-acetylgalactosaminyltransferasesrf-3, a mutant of Caenorhabditis elegans, resistant to bacterial infection and to biofilm binding, is deficient in glycoconjugates.Activation of the unfolded protein response is required for defenses against bacterial pore-forming toxin in vivo.Hypoxia and the hypoxic response pathway protect against pore-forming toxins in C. elegans.The Caenorhabditis elegans bus-2 mutant reveals a new class of O-glycans affecting bacterial resistance.Protist-type lysozymes of the nematode Caenorhabditis elegans contribute to resistance against pathogenic Bacillus thuringiensisThe pore-forming protein Cry5B elicits the pathogenicity of Bacillus sp. against Caenorhabditis elegans.In vitro uptake of 140 kDa Bacillus thuringiensis nematicidal crystal proteins by the second stage juvenile of Meloidogyne haplaNew positive regulators of lin-12 activity in Caenorhabditis elegans include the BRE-5/Brainiac glycosphingolipid biosynthesis enzyme.Glycosylation genes expressed in seam cells determine complex surface properties and bacterial adhesion to the cuticle of Caenorhabditis elegans.RAB-5- and RAB-11-dependent vesicle-trafficking pathways are required for plasma membrane repair after attack by bacterial pore-forming toxin.Mos1 mutagenesis reveals a diversity of mechanisms affecting response of Caenorhabditis elegans to the bacterial pathogen Microbacterium nematophilum.Bacillus thuringiensis Crystal Protein Cry6Aa Triggers Caenorhabditis elegans Necrosis Pathway Mediated by Aspartic Protease (ASP-1).Single amino acid mutation in an ATP-binding cassette transporter gene causes resistance to Bt toxin Cry1Ab in the silkworm, Bombyx mori.Molecular cloning and functional characterization of a Lepidopteran insect beta4-N-acetylgalactosaminyltransferase with broad substrate specificity, a functional role in glycoprotein biosynthesis, and a potential functional role in glycolipid biosynA novel sphingolipid-TORC1 pathway critically promotes postembryonic development in Caenorhabditis elegans.Caenorhabditis elegans: an emerging model in biomedical and environmental toxicology.Expression of ceramide glucosyltransferases, which are essential for glycosphingolipid synthesis, is only required in a small subset of C. elegans cells.Mitogen-activated protein kinase pathways defend against bacterial pore-forming toxins.Bacterial pore-forming proteins as anthelmintics.HLH-30/TFEB-mediated autophagy functions in a cell-autonomous manner for epithelium intrinsic cellular defense against bacterial pore-forming toxin in C. elegans.Bacillus thuringiensis: A story of a successful bioinsecticide.Glycosphingolipids in signaling and development: from liposomes to model organisms.Molecular Cloning, Expression, and Identification of Bre Genes Involved in Glycosphingolipids Synthesis in Helicoverpa armigera (Lepidoptera: Noctuidae).The directed migration of gonadal distal tip cells in Caenorhabditis elegans requires NGAT-1, a ß1,4-N-acetylgalactosaminyltransferase enzyme.Combining Human Epigenetics and Sleep Studies in Caenorhabditis elegans: A Cross-Species Approach for Finding Conserved Genes Regulating Sleep.Structure elucidation of neutral, di-, tri-, and tetraglycosylceramides from High Five cells: identification of a novel (non-arthro-series) glycosphingolipid pathway.A two-domain protein triggers heat shock pathway and necrosis pathway both in model plant and nematode.A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resistance to Cry1Ab.Determining the involvement of two aminopeptidase Ns in the resistance of Plutella xylostella to the Bt toxin Cry1Ac: cloning and study of in vitro function.
P2860
Q22065964-EB02B4A1-1B0F-41B6-B817-39FA3E5D32B6Q24531940-0B96EABF-B0EF-4C23-9E0B-3A15E43A2661Q24683647-FF729C7F-22A5-41CA-8F27-FCB414EE12C3Q24804560-1CC71728-E639-4E96-8872-C87DA2FBE239Q27311143-96BF27B9-58E9-4070-A72D-BEAB91D2E4BBQ27318747-99E99E95-540E-4145-B40F-5D403CEEB130Q27490690-3C1ACFDC-8D28-4206-9E22-53E8CC8E50C7Q27675127-8637783E-E44B-4A73-98AD-58B9FD4220B0Q28484987-C6232E93-20C6-4FFC-AA4A-8B7A2BAE3B0FQ28534011-2CCC320E-3EA7-46A8-8BC4-C03C5CC541F2Q33202664-E02F4B50-AEF6-4EFC-94B0-CF6E3A016FC0Q33207429-5322A6C8-1845-4834-8A2A-DA3A4D651E6AQ33375026-50B57A85-2336-44D5-AFE1-8150D6FAFEAEQ33518501-120139DA-537F-4164-8505-978462A3F5BAQ33885210-B2BDEA91-5F0E-4FAF-B2FB-65A458331CE5Q34023766-46E813BD-B19A-47DB-86F7-D0BDFB8DDD72Q34117229-7AD65B58-FBBF-4C06-94C5-90C3D28CEAC8Q34318332-CE71F4BD-FDE7-4190-AB48-2933C012D2A0Q34424915-2A21DB9E-8303-4D5B-87A8-E190B0503A80Q34477569-7B1FDC9B-55BE-40B6-8D23-19C44ACBB98FQ34673172-A62A83EC-FE35-4CD7-A16D-24984539956DQ35641565-50B17E26-C7D4-4643-91F4-919618360C61Q35900236-7BB14A6D-B246-4611-82F3-6F99BA7AC012Q36056339-98EA2DF0-BBA9-4AFB-9656-47DD658A99E0Q36723748-AEE412AF-9942-4898-B7D9-01F2FD3301BCQ36864868-1311657D-0133-4831-A976-035D5B90281EQ36927018-1CBF2F97-1D23-4237-9FC4-80949023B0F6Q37271606-5A05C53A-41DA-4B2F-AFD8-8A76DF868C75Q37285144-C2638FF2-235F-4018-B95B-8BA38245E715Q37469105-E79856E3-7493-4F6E-BA21-BBE29DC08D60Q37664475-1AF6C8A7-9862-40DB-9A46-75EC897DD308Q37849891-DAB4DE7D-27F6-4CA5-A302-51F0BF24CA70Q37950975-880B57E2-9A47-43CC-B218-F56AE8D4234FQ38770232-874B81A4-26AB-4320-BCEF-2E2D09D60001Q39757304-CA9F689E-2F33-4F46-8C53-30FBC5DB9EF8Q40232748-7ABF784F-0E03-47D8-AD2C-17DC0B66E20BQ40398097-FBB17178-3DE0-422C-A7A2-6087925AFB11Q40765879-DE7D4BE0-47AC-45AA-A03D-A8C1DA13DBFDQ42008155-ABAFFF5F-9D3E-47F1-82CE-8142E4668B9BQ42014067-350E6DA2-830D-47DB-A4FC-8C19A05BC3FE
P2860
Resistance to a bacterial toxin is mediated by removal of a conserved glycosylation pathway required for toxin-host interactions.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@en
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@nl
type
label
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@en
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@nl
prefLabel
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@en
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@nl
P2093
P2860
P356
P1476
Resistance to a bacterial toxi ...... d for toxin-host interactions.
@en
P2093
Brad D Barrows
Danielle L Huffman
Jeffrey D Esko
Jillian R Brown
Joel S Griffitts
Johanna L Whitacre
Lisa D Marroquin
Raffi V Aroian
Reto Müller
Thierry Hennet
P2860
P304
45594-45602
P356
10.1074/JBC.M308142200
P407
P577
2003-08-27T00:00:00Z