about
Purification of bacterial membrane sensor kinases and biophysical methods for determination of their ligand and inhibitor interactionsLigand- and drug-binding studies of membrane proteins revealed through circular dichroism spectroscopySolution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificityStructure of the response regulator VicR DNA-binding domainContext effects on misreading and suppression at UAG codons in human cells.Activation of the global gene regulator PrrA (RegA) from Rhodobacter sphaeroides.Quality control and biophysical characterisation data of VanSA.Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complexCharacterisation of the selective binding of antibiotics vancomycin and teicoplanin by the VanS receptor regulating type A vancomycin resistance in the enterococci.Full hydrodynamic reversibility of the weak dimerization of vancomycin and elucidation of its interaction with VanS monomers at clinical concentration.Hydrodynamics of the VanA-type VanS histidine kinase: an extended solution conformation and first evidence for interactions with vancomycin.Cloning and nucleotide sequence of regA, a putative response regulator gene of Rhodobacter sphaeroides.Characterisation of a Rrhodobacter sphaeroides gene that encodes a product resembling Eescherichia coli cytochrome b(561) and R. sphaeroides cytochrome b(562).Sequence, chromophore extraction and 3-D model of the photoactive yellow protein from Rhodobacter sphaeroides.Evaluation of a biochemical test scheme for identifying clinical isolates of Enterococcus faecalis and Enterococcus faecium.Expression, purification and characterisation of full-length histidine protein kinase RegB from Rhodobacter sphaeroides.Interactions of the intact FsrC membrane histidine kinase with the tricyclic peptide inhibitor siamycin I revealed through synchrotron radiation circular dichroism.Collection and characterisation of bacterial membrane proteins.Interactions of the intact FsrC membrane histidine kinase with its pheromone ligand GBAP revealed through synchrotron radiation circular dichroism.Expression, purification and activities of the entire family of intact membrane sensor kinases from Enterococcus faecalis.Antimicrobial resistance (AMR) nanomachines-mechanisms for fluoroquinolone and glycopeptide recognition, efflux and/or deactivation.Anti-HIV siamycin I directly inhibits autophosphorylation activity of the bacterial FsrC quorum sensor and other ATP-dependent enzyme activities.Redox-responsive in vitro modulation of the signalling state of the isolated PrrB sensor kinase of Rhodobacter sphaeroides NCIB 8253.Cytolysin gene expression in Enterococcus faecalis is regulated in response to aerobiosis conditions.Use of a lux reporter system for monitoring rapid changes in alpha-toxin gene expression in Clostridium perfringens during growth.The 3' codon context effect on UAG suppressor tRNA is different in Escherichia coli and human cells.Structural and biophysical characterisation of membrane protein–ligand bindingNMR assignment of the Rhodobacter sphaeroides fasciclin-1 domain protein (Fdp)Use of a lux reporter system for monitoring rapid changes in α-toxin gene expression in Clostridium perfringens during growthIntroduction of recombinant DNA into Clostridium sppProduction of membrane proteins for characterisation of their pheromone-sensing and antimicrobial resistance functionsThe discovery of hydrogen bonds in DNA and a re-evaluation of the 1948 Creeth two-chain model for its structureThe gelatinase biosynthesis-activating pheromone binds and stabilises the FsrB membrane protein in Enterococcus faecalis quorum sensingThe antibiotic vancomycin induces complexation and aggregation of gastrointestinal and submaxillary mucins
P50
Q26747190-F44F5200-4E0B-4F83-8908-8BFC4250784BQ26996573-1F8543AD-ED58-48E9-A36D-D2500278194EQ27642600-33115882-DA30-41B3-A20A-BB36E3FE7464Q27643628-0BD05AEF-DF5A-4BFF-BF8B-9A6D502C690AQ36556118-5575AB17-B498-4093-81FF-72640AB08A22Q36839157-2D97ED58-3283-4420-967E-3D03A94CE7F6Q38647740-0B2095C1-8F66-492C-BD31-37A2DC45FE17Q39955867-76C717FD-1E2D-4568-8865-24D77E9B0BDEQ40210054-2DFCA505-49E4-43B8-8297-6A3450809787Q42079847-ABD32FEA-9939-4DEC-B1CE-C7515073B38DQ42292297-998583BE-618B-4A0E-9618-BAB2ACF7AF6FQ42605624-41936657-33B3-4CA6-AC26-B7DCC7D7912CQ42631193-12E3A09C-D15A-468E-865D-03DF64FBAAE8Q42679308-67E3A2D4-868E-46D0-AA4C-A22184439E73Q43790421-9CB9659A-7552-4AC3-9ECE-D9DFA1740F38Q44038187-3B0EEAD8-B61A-4D0D-A3DA-632DA2F375F7Q44103205-076FD830-B8D1-4165-8BDE-142F37E9AC8EQ44663709-5AC5B10F-929D-4868-8EB9-7F1361C63679Q46128069-441FB0A1-7DEB-4B40-897C-016E2F5768B5Q46374884-A0B24724-F858-4D1B-B4FE-E6D1F5C1DBC6Q52360303-2159DC07-8BFE-44E0-A635-CFE8724163DEQ52845261-4F9B865D-F54A-4CF9-B177-21BE7454C6F0Q52855793-817870E4-EB47-497B-A7BB-21895FE820CBQ52860302-6784F064-B0C0-43EA-8D44-38C211FD0C24Q52863980-3F0FE1D5-E60C-4C48-BAD8-E7FE0457CAB5Q54651421-6074E8AC-1BFF-436D-B9E4-92B571822F07Q56837033-2D141DB6-0465-4A20-AC45-B955CB782DEFQ56837036-4D97D69C-25B2-41EC-B4AF-1586F2C9F07AQ56837043-DFEBCDBD-AF41-4131-90DF-92016B633BB0Q56837044-D1DFD6BD-C299-4816-BD9A-E5635613A484Q57137922-2859BB65-F9F5-4AAD-B5E4-8AA3C06C2C9FQ58760526-D458C2A9-6461-405E-84C4-7EE4751D6C3BQ90623317-E968B918-5CA3-4E09-8C67-B13B4F75197BQ92860386-B2F08634-E50A-4482-BBF2-B33CE237563C
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Mary K Phillips-Jones
@ast
Mary K Phillips-Jones
@en
Mary K Phillips-Jones
@es
Mary K Phillips-Jones
@nl
Mary K Phillips-Jones
@sl
type
label
Mary K Phillips-Jones
@ast
Mary K Phillips-Jones
@en
Mary K Phillips-Jones
@es
Mary K Phillips-Jones
@nl
Mary K Phillips-Jones
@sl
prefLabel
Mary K Phillips-Jones
@ast
Mary K Phillips-Jones
@en
Mary K Phillips-Jones
@es
Mary K Phillips-Jones
@nl
Mary K Phillips-Jones
@sl
P106
P1153
6603912932
P21
P31
P496
0000-0002-0362-4690