about
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretionCellular Functions and X-ray Structure of Anthrolysin O, a Cholesterol-dependent Cytolysin Secreted by Bacillus anthracisSecondary structure reshuffling modulates glycosyltransferase function at the membraneDisorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretionBacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes.Deciphering membrane insertion of the diphtheria toxin T domain by specular neutron reflectometry and solid-state NMR spectroscopy.Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxinClostridium septicum alpha-toxin forms pores and induces rapid cell necrosis.Calcium, acylation, and molecular confinement favor folding of Bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic formBee venom phospholipase A2 as a membrane-binding vector for cell surface display or internalization of soluble proteins.The Translocation Domain of Botulinum Neurotoxin A Moderates the Propensity of the Catalytic Domain to Interact with Membranes at Acidic pHExposure to Bordetella pertussis adenylate cyclase toxin affects integrin-mediated adhesion and mechanics in alveolar epithelial cells.Alteration of the tertiary structure of the major bee venom allergen Api m 1 by multiple mutations is concomitant with low IgE reactivityThe Tip of the Four N-Terminal α-Helices of Clostridium sordellii Lethal Toxin Contains the Interaction Site with Membrane Phosphatidylserine Facilitating Small GTPases GlucosylationBordetella pertussis adenylate cyclase toxin translocation across a tethered lipid bilayerMEMHDX: an interactive tool to expedite the statistical validation and visualization of large HDX-MS datasets.Interaction between the two subdomains of the C-terminal part of the botulinum neurotoxin A is essential for the generation of protective antibodies.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Prolonged display or rapid internalization of the IgG-binding protein ZZ anchored to the surface of cells using the diphtheria toxin T domain.Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studiesMolecular Basis of Membrane Association by the Phosphatidylinositol Mannosyltransferase PimA Enzyme from Mycobacteria.Correction: The Translocation Domain of Botulinum Neurotoxin A Moderates the Propensity of the Catalytic Domain to Interact with Membranes at Acidic pH.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Interactions of apomyoglobin with membranes: mechanisms and effects on heme uptake.Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the bordetella pertussis adenylate cyclase toxin.Calmodulin-induced conformational and hydrodynamic changes in the catalytic domain of Bordetella pertussis adenylate cyclase toxin.Membrane Interaction of botulinum neurotoxin A translocation (T) domain. The belt region is a regulatory loop for membrane interaction.Molecular crowding stabilizes both the intrinsically disordered calcium-free state and the folded calcium-bound state of a repeat in toxin (RTX) protein.Clostridium perfringens iota toxin. Mapping of the Ia domain involved in docking with Ib and cellular internalization.Characterization of wild-type recombinant Bet v 1a as a candidate vaccine against birch pollen allergy.Side chain resonances in static oriented proton-decoupled 15N solid-state NMR spectra of membrane proteins.RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion.Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region.Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Synthesis and characterization of tethered lipid assemblies for membrane protein reconstitution (Review).SEC-SAXS and HDX-MS: A powerful combination. The case of the calcium-binding domain of a bacterial toxin.The catalytic domains of Clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid.Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis.Type III secretion effectors of the IpaH family are E3 ubiquitin ligases.
P50
Q27308665-CE833464-F023-43FA-9D54-38D0983DD692Q27654239-9E5684EE-B795-4E35-B806-2F5496779839Q27696184-5D2EE8D5-31C1-4EF3-B3A5-DE29790D556FQ28083580-7967AD26-879B-43E0-A14D-FBF161C899AFQ30843322-1E18C2A8-8A0D-4133-B951-E9184F9844DCQ33478095-64A16A43-7CF0-4432-8299-BF90C56368A9Q34388681-48F868CD-C4C2-4782-9469-1C0275724D01Q34994070-9445F504-B0D0-4BDB-833D-4B20BD73C3DDQ35260287-9E522947-03E4-4714-AED6-B2FE631DB5A8Q35740362-026DB3C8-7FCA-49FE-B09C-ABE2652C4247Q35987067-476BB050-BB34-4742-A4F5-F3B586031D9BQ36396610-07FF5EDC-07B2-4796-B55A-500C4D5FB762Q36526262-09538B21-791A-42E5-BF97-18C0E0A5B513Q36846081-38F0C2C6-1582-4F4D-9520-BD2E39339484Q37409405-5D3A2EC3-1226-4E34-A280-05529CED2A09Q37529995-12320BC8-CABC-4AFD-AA4E-B124E727B37BQ38337915-51F90C43-B2EF-4282-822F-78079736D3EEQ39412993-7E8AF14D-B64A-4528-8F6A-4E7584155299Q40789624-41747B52-5980-47FC-B804-F00FE8AB4DAAQ41882978-81D9FB43-CD2C-4227-8AD9-E3842351C411Q41891782-FC175287-AD5C-48AD-97FC-3AD503D0D642Q42151620-DF9B2F7F-8D29-4029-9B89-AF1D4611A2CBQ42346791-091F1152-0C4D-4D83-8D1B-D755E9316A5DQ42917720-A5B900D8-0BB3-476C-8601-0591151EF334Q42958287-D826A84D-8394-459B-9FAC-80EDB7BF557BQ43185587-A8EA5BC8-9763-4EFF-80C0-1CDC55EE5F89Q43226338-DE7D1FB8-7398-44FD-BBA6-2912CD2C8CB6Q43960895-81A0D8BB-4CD1-4ED4-B63D-06BC83F1705AQ44091121-2DD5A841-2E07-43BA-AD43-F3D546512670Q44131368-BC1C3C6C-9150-4E54-A685-78F464CD52FFQ45275973-1D8157E9-D415-4F53-97BA-4B2703B3D2E3Q46047171-997B0D24-654E-4AAC-A30C-CD3B8082DCE0Q46241353-DDA1A7A2-E65F-42EA-9EF2-F1AF46737CA5Q47128421-FC1CC1A2-DF93-4D75-88AD-BF7AE8C783B5Q47401954-E16A4B58-DC0E-4A05-9D8F-D7A1E29A64ABQ47622142-60A45E81-872F-4679-82ED-0D7A139B32B1Q47997009-07179644-AB76-4610-B997-6D1A12A26613Q48225911-369FA4CA-90E1-48B4-AAD5-7355B0F0EF3DQ48331099-A55A7FA0-C210-40E2-96F8-211D412A6056Q50066742-404727D5-E2B3-4FD2-BFCB-F2D6919E0FAB
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Alexandre Chenal
@ast
Alexandre Chenal
@en
Alexandre Chenal
@es
Alexandre Chenal
@nl
Alexandre Chenal
@sl
type
label
Alexandre Chenal
@ast
Alexandre Chenal
@en
Alexandre Chenal
@es
Alexandre Chenal
@nl
Alexandre Chenal
@sl
prefLabel
Alexandre Chenal
@ast
Alexandre Chenal
@en
Alexandre Chenal
@es
Alexandre Chenal
@nl
Alexandre Chenal
@sl
P106
P21
P31
P496
0000-0002-4959-1003