about
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretionDefining a protective epitope on factor H binding protein, a key meningococcal virulence factor and vaccine antigenMolecular Basis of Ligand-Dependent Regulation of NadR, the Transcriptional Repressor of Meningococcal Virulence Factor NadAPrepore Stability Controls Productive Folding of the BAM-independent Multimeric Outer Membrane Secretin PulD.The Abl SH2-kinase linker naturally adopts a conformation competent for SH3 domain binding.Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex.Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchiiMEMHDX: an interactive tool to expedite the statistical validation and visualization of large HDX-MS datasets.Aspartic proteinases in Antarctic fish.Proteomics for Allergy: from Proteins to the Patients.Neisseria meningitis GNA1030 is a ubiquinone-8 binding protein.Structure and allosteric inhibition of excitatory amino acid transporter 1.The marine natural product adociasulfate-2 as a tool to identify the MT-binding region of kinesins.The stress sigma factor of RNA polymerase RpoS/σS is a solvent exposed open molecule in solution.Structural disorder and induced folding within two cereal, ABA stress and ripening (ASR) proteins.Calcium-dependent disorder-to-order transitions are central to the secretion and folding of the CyaA toxin of Bordetella pertussis, the causative agent of whooping cough.Structural Characterization of Whirlin Reveals an Unexpected and Dynamic Supramodule Conformation of Its PDZ Tandem.SEC-SAXS and HDX-MS: A powerful combination. The case of the calcium-binding domain of a bacterial toxin.Characterization of epitope specificities of reference antibodies used for the quantification of the birch pollen allergen Bet v 1.Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis.Two cross-reactive monoclonal antibodies recognize overlapping epitopes on Neisseria meningitidis factor H binding protein but have different functional propertiesConsensus designs and thermal stability determinants of a human glutamate transporterDynamics of a type 2 secretion system pseudopilus unraveled by complementary approachesMolecular dissection of the inhibitor binding pocket of mitotic kinesin Eg5 reveals mutants that confer resistance to antimitotic agentsUse of hydrogen/deuterium exchange mass spectrometry and mutagenesis as a tool to identify the binding region of inhibitors targeting the human mitotic kinesin Eg5Post-translational acylation controls the folding and functions of the CyaA RTX toxinRecommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experimentsTranslocation and calmodulin-activation of the adenylate cyclase toxin (CyaA) of Bordetella pertussis
P50
Q27308665-FD4EE010-1944-4307-B209-31BFE36DF183Q27676318-37E4C27C-1342-47B2-8F10-520FAFB1B34BQ28551548-7FD33516-CD9A-428D-A166-EF7848AAE3A8Q30152695-532AEF7F-5328-4385-B880-660E90067831Q30158039-A3745FE5-ED06-43F8-8C5E-768818B22B13Q33622210-B46F4708-F754-4DB5-9894-649B38170638Q36871250-A84D12ED-8ACF-4261-BBF9-649B86CB467DQ37529995-1685F31C-F0A8-45B3-8383-51D72F4A34F4Q37907423-B89BF32F-82F6-4AFE-9F7B-0E30B65E19BAQ38930142-485E6D39-C39C-4F91-BA58-85CD82067627Q41354112-0AE04E3F-867B-4094-8DF9-407D3D46C0AAQ42356946-F2271B38-BBBE-4284-8816-39B350236A8DQ42505706-4C290B82-A7D3-4B32-9A3F-E46E1E615ECBQ47305089-2FA8E2A0-DFBD-4282-8DFD-F6ED07FEB0C0Q47401954-B0B27595-2B1E-4E1A-9AFB-5DBCC03AB09DQ47656080-ADB6360E-03A0-4915-883E-5682FB81FEE8Q47718694-78C41540-7959-47D7-ACA1-6E4FB01DAB9AQ47997009-4969FAD0-A786-43C9-BFB5-8BCF82FAEE02Q48240468-50863072-BB36-4D0C-B58B-2F24E357E8ACQ48331099-0B5CBD6A-0E10-425C-8BFA-73D7935BFEE8Q57836539-66A70FAE-2C5C-4B57-8CBE-C95CE4CACD64Q58595127-09044145-327C-4B80-8A06-E03B0BDEB34EQ64448200-11C48959-F5BB-4A65-B0C1-4464F8B16DAFQ79741869-F6D71BD8-6F86-47EA-86E9-476F8DC32B8DQ82216852-D0D5CBE1-C133-44B6-B1F9-968F67F9C62DQ92935721-384DA35E-4B29-4CB5-A363-231835ED45F4Q93089051-D4DAED0D-DAE2-4F0D-A678-FFD3C67F839FQ93211663-84D78985-06CE-4F18-A967-EEF79923E25F
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Sébastien Brier
@ast
Sébastien Brier
@en
Sébastien Brier
@es
Sébastien Brier
@nl
type
label
Sébastien Brier
@ast
Sébastien Brier
@en
Sébastien Brier
@es
Sébastien Brier
@nl
prefLabel
Sébastien Brier
@ast
Sébastien Brier
@en
Sébastien Brier
@es
Sébastien Brier
@nl
P108
P106
P31
P496
0000-0003-1758-8237