about
What the Myddosome structure tells us about the initiation of innate immunityEstrogen receptor transcription and transactivation: Structure-function relationship in DNA- and ligand-binding domains of estrogen receptorsCrystal structure of a mutant hERalpha ligand-binding domain reveals key structural features for the mechanism of partial agonismOverexpression, purification, and crystal structure of native ER alpha LBDFunctional Insights from the Crystal Structure of the N-Terminal Domain of the Prototypical Toll ReceptorLiesegang-like patterns of Toll crystals grown in gel.Cytokine Spatzle binds to the Drosophila immunoreceptor Toll with a neurotrophin-like specificity and couples receptor activationMolecular mechanism that induces activation of Spätzle, the ligand for the Drosophila Toll receptorThree-tier regulation of cell number plasticity by neurotrophins and Tolls in Drosophila.LPS ligand and culture additives improve production of monomeric MD-1 and 2 in Pichia pastoris by decreasing aggregation and intermolecular disulfide bondingIdentification of key residues that confer Rhodobacter sphaeroides LPS activity at horse TLR4/MD-2.Baseless assumptions: activation of TLR9 by DNA.Different dimerisation mode for TLR4 upon endosomal acidification?Assembly and localization of Toll-like receptor signalling complexes.Elucidation of the MD-2/TLR4 interface required for signaling by lipid IVa.Structural insight into the mechanism of activation of the Toll receptor by the dimeric ligand Spätzle.Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway.Critical residues involved in Toll-like receptor 4 activation by cationic lipid nanocarriers are not located at the lipopolysaccharide-binding interface.Toll-like receptor 2 promiscuity is responsible for the immunostimulatory activity of nucleic acid nanocarriers.Allergens as immunomodulatory proteins: the cat dander protein Fel d 1 enhances TLR activation by lipid ligands.The molecular basis for recognition of bacterial ligands at equine TLR2, TLR1 and TLR6.MD-2: the Toll 'gatekeeper' in endotoxin signalling.The molecular basis of the host response to lipopolysaccharide.Role of the Spatzle Pro-domain in the generation of an active toll receptor ligand.Peptidoglycan-Sensing Receptors Trigger the Formation of Functional Amyloids of the Adaptor Protein Imd to Initiate Drosophila NF-κB Signaling.Bioinformatic analysis of Toll-like receptor sequences and structures.Toll-like receptors as molecular switches.Activation of insect and vertebrate toll signaling: from endogenous cytokine ligand to direct recognition of pathogen patterns.Bioinformatic Analysis of Toll-Like Receptor Sequences and StructuresIIV-6 Inhibits NF-κB Responses in Drosophila.Conserved mechanisms of signal transduction by Toll and Toll-like receptorsSaturation of acyl chains converts cardiolipin from an antagonist to an activator of Toll-like receptor-4Correction to: Saturation of acyl chains converts cardiolipin from an antagonist to an activator of Toll-like receptor-4
P50
Q24338472-82120E66-2D1D-48EF-938A-C61EB7351E52Q24800777-5CCEA9AD-7CA5-4EE7-AE7A-5F0C313A8F9CQ27630889-F3394121-91FB-421E-B313-163D5F63007EQ27632980-31766FB6-2B6F-421E-95ED-1D56D4B93C0CQ27675519-40D5F4E6-35FF-4F5C-96AB-2026F585C29CQ27677443-63F0487D-BE84-4F72-A655-C9E3D51C65F7Q27680692-CC73532C-36BD-4BDB-91A4-C33DD620CCFEQ28751608-94FF196A-20C4-4E2A-857F-5C504A73A80BQ33625318-1704249E-849F-4732-A58C-B5075FE4923BQ34544374-8658AD10-28A0-44AC-A98B-47C4794A0398Q35176850-89EDBC1A-8632-4216-B69B-847EE3AC7F19Q37110387-223E26F4-7577-4D61-AE9A-DE6E7C8289ABQ37971120-9657758F-4FEA-4BA7-A38F-2E2E36721434Q38233769-9D450BCD-EFE9-4313-99E0-B4D8DA6F538DQ39964197-A7D2AA5B-FA28-4933-8BC1-ACE8B818BF17Q40001553-501587A9-5085-487E-8C44-C171C6E759B9Q40442019-B4702F29-89B0-4E04-BD50-3E21057DBE2EQ40959256-13C6BC39-EBE4-4FE0-9C58-55799602505EQ41762712-2AD4446B-3A6C-4EC2-A330-FC95CCBFFFC9Q42755753-5BCB6607-7246-4D2C-8DE2-3F16BBCF9926Q43084726-DDDE5CCD-A5E7-474A-8B28-FE4FE1F054D4Q45345605-0B6C0BC0-61FE-4FFA-AD0D-0B8C14E2EA74Q45811531-7A64D8A0-4658-4B13-9780-AD55F6960DDBQ47071124-498FA9B1-051A-488D-9229-4426523FF339Q47432395-7758D436-2034-4CA1-8E94-D63236F30D08Q47982870-A11D9DC9-F91B-4769-9607-BBA6BC7D1675Q48546511-A26DE40F-301A-4397-934D-F5B3B65080C0Q48550476-01C5D4FF-3590-4773-9BB7-6C7C57A77CDDQ62054619-5FDE10C1-2C0B-4934-853F-B0A0D7440935Q64935347-37987AB7-F497-4E67-8142-FD62D4318595Q81428083-EDCBDF21-A08A-48F3-9DC1-E63AAD7AE611Q91810336-4FF19FCD-0370-454E-806A-BC1787E122E0Q92138899-18DD5873-6433-4D30-8618-00110D7F0C3D
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Monique Gangloff
@ast
Monique Gangloff
@en
Monique Gangloff
@es
Monique Gangloff
@nl
Monique Gangloff
@sl
type
label
Monique Gangloff
@ast
Monique Gangloff
@en
Monique Gangloff
@es
Monique Gangloff
@nl
Monique Gangloff
@sl
prefLabel
Monique Gangloff
@ast
Monique Gangloff
@en
Monique Gangloff
@es
Monique Gangloff
@nl
Monique Gangloff
@sl
P106
P1153
6602539986
P21
P31
P496
0000-0001-6131-0115