about
Interaction of human complement with Sbi, a staphylococcal immunoglobulin-binding protein: indications of a novel mechanism of complement evasion by Staphylococcus aureusStructure-function analysis of the C3 binding region of Staphylococcus aureus immune subversion protein SbiA structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3dStructural features and ligand binding properties of tandem WW domains from YAP and TAZ, nuclear effectors of the Hippo pathwayHigh-resolution solution structure of reduced parsley plastocyaninHuman general transcription factor TFIIB: conformational variability and interaction with VP16 activation domainExtracellular Fibrinogen-binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet-Leukocyte ComplexesSolution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding proteinAlternate routes to conformational specificity in a Greek key beta barrel protein.Equilibrium folding intermediates of a Greek key beta-barrel protein.Solution structure of the epithelial cadherin domain responsible for selective cell adhesion.Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment.Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens.S. aureus IgG-binding proteins SpA and Sbi: host specificity and mechanisms of immune complex formation.YAP is essential for tissue tension to ensure vertebrate 3D body shapeSubunit interactions change the heme active-site geometry in p-cresol methylhydroxylase.The Hippo pathway: key interaction and catalytic domains in organ growth control, stem cell self-renewal and tissue regeneration.Transient expression in HEK 293 cells: an alternative to E. coli for the production of secreted and intracellular mammalian proteins.Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement receptor 2 (CR2) share overlapping contact residues on C3d: implications for the controversy regarding the CR2/C3d cocrystal structure.Characterisation of receptor binding by the chemotaxis inhibitory protein of Staphylococcus aureus and the effects of the host immune responseComparative genomic analysis reveals 2-oxoacid dehydrogenase complex lipoylation correlation with aerobiosis in archaea.Post-translational modification in the archaea: structural characterization of multi-enzyme complex lipoylation.A unique lipoylation system in the Archaea. Lipoylation in Thermoplasma acidophilum requires two proteins.Structural analysis of Salmonella enterica effector protein SopD.Biophysical characterization of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei.Assignment of the 1H, 13C and 15N resonances of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei.Unusual helix-containing greek keys in development-specific Ca(2+)-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy.A Modular Bioplatform Based on a Versatile Supramolecular Multienzyme Complex Directly Attached to Graphene.TFIIA-TAF regulatory interplay: NMR evidence for overlapping binding sites on TBP.Distinctive phosphoinositide and Ca2+ binding properties of normal and cognitive performance-linked variant forms of KIBRA C2 domain.Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherinThe complex formed between plastocyanin and cytochrome c. Investigation by NMR spectroscopyThe Histone Folds in Transcription Factor TFIIDDirect electrochemistry of protein-protein complexes involving cytochrome c, cytochrome b5, and plastocyaninThe button test: a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMREvolution of the genetic triplet code via two types of doublet codons
P50
Q24646878-212A9BAF-93CA-4DF4-89CF-AF4A6256957AQ24649766-3FC43B1F-1C97-4072-98B7-4AD1C998E88AQ27665619-91E70460-AA52-4507-8EB0-38851F4525D4Q27667018-3E788DA3-A6F5-4E07-882A-05A6254F49F7Q27731421-49A864B2-5AE8-49B8-B0AF-C17B5852CBAEQ27758094-20398524-6DB0-4229-9FDB-849931BFE8FBQ28115532-AFFC827F-3FBA-40DD-BC0C-E5D8578FD4DEQ28118266-B53CB697-5049-488A-9DFD-282768F83E1DQ30167960-54631F15-FE6D-41DD-822E-9A71857BEDE6Q30176227-FED0F0D1-55A1-4CBF-BE4B-AB4DA36E4DB3Q30193717-F3BD8719-1DB7-475E-A560-20FCC01457A3Q33576331-429BF1C5-589E-40CA-9A5F-532BEFAAF4A2Q34341216-4563B30A-73FE-4CCA-8135-11B6B25AC858Q34722335-A1412B2E-9FF1-46E3-BE34-AED5A9721CEBQ36483518-283FF002-27A5-4D88-B593-835D05C2E5F0Q37611000-82B86CEB-2066-4F00-97EE-4824EEEFC72CQ38038638-43BF10A7-EEEC-40F0-B4B5-1E991295BA43Q38275230-36374F4D-175F-4C6C-886C-1B8AE85F25D6Q39750608-4CC6A8AC-547C-4F81-8B8B-98B2F90048CDQ41773639-F9C4BC4D-E9AE-4366-B4D0-FC1A8E7AE218Q41896709-C90C3881-E6F0-4F8E-A3B7-2A300B30C396Q43016865-BA9F6C40-EAFB-4FC0-B663-C6C8E0EC0B43Q43027137-63E9ADE5-D175-4764-ACFD-C4F1DAC7E5F5Q47629058-2CCFDCB6-01A7-43AC-B1D6-3D73EBCD0C57Q47824038-E7393814-8597-4AFF-BBD4-B03D2609C4D8Q47968042-50620367-8924-40DF-917A-18F9FDBF69D3Q48157823-4B4BD2A2-CD01-4454-8D8C-4F7E4685F04AQ49161898-F96356BD-0149-40DC-8DA6-7607AE9A2489Q52576836-3DB827E4-A9F1-42FB-AA0E-3411A2C83096Q52801344-891D3854-0496-4802-B883-32D04421F588Q57800438-7F9F18EC-C417-43DA-B8B9-4D23F7DA7801Q57889998-424037DA-ECA3-441F-9A8B-73CB581C9976Q58484446-61CBEF99-6FEC-4B42-ADE5-59C07A773B89Q68458324-C598F0CE-5396-4B1E-A0F1-FFB132DFED75Q73924705-4C3C339D-E96C-46CB-8242-DEBDDD043FC7Q80972521-3ABA0CA6-47AE-4CC2-B46D-3A907FC5F042
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Stefan Bagby
@ast
Stefan Bagby
@en
Stefan Bagby
@es
Stefan Bagby
@nl
Stefan Bagby
@sl
type
label
Stefan Bagby
@ast
Stefan Bagby
@en
Stefan Bagby
@es
Stefan Bagby
@nl
Stefan Bagby
@sl
prefLabel
Stefan Bagby
@ast
Stefan Bagby
@en
Stefan Bagby
@es
Stefan Bagby
@nl
Stefan Bagby
@sl
P106
P1153
7003784631
P21
P31
P496
0000-0003-2302-9511