about
Biophysical characterisation of fibulin-5 proteins associated with diseaseStructure and interdomain interactions of a hybrid domain: a disulphide-rich module of the fibrillin/LTBP superfamily of matrix proteinsA refined solution structure of hen lysozyme determined using residual dipolar coupling dataA camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozymePlasticity of the TSG-6 HA-binding loop and mobility in the TSG-6-HA complex revealed by NMR and X-ray crystallographyA conserved face of the Jagged/Serrate DSL domain is involved in Notch trans-activation and cis-inhibitionOxidation State-dependent Protein-Protein Interactions in Disulfide CascadesStructure of the Fibrillin-1 N-Terminal Domains Suggests that Heparan Sulfate Regulates the Early Stages of Microfibril AssemblyAn Extended Active-site Motif Controls the Reactivity of the Thioredoxin FoldStructure of the terminal PCP domain of the non-ribosomal peptide synthetase in teicoplanin biosynthesisConsequences of inducing intrinsic disorder in a high-affinity protein-protein interactionAnalysis of the solution structure of human interleukin-4 determined by heteronuclear three-dimensional nuclear magnetic resonance techniquesProbing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometryResidual dipolar couplings: are multiple independent alignments always possible?Water mediation is essential to nucleation of β-turn formation in peptide folding motifs.(15)N NMR relaxation data reveal significant chemical exchange broadening in the alpha-domain of human alpha-lactalbumin.Asparagine and glutamine side-chain conformation in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings.Iain D Campbell 1941-2014.Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins.Molecular basis for Jagged-1/Serrate ligand recognition by the Notch receptorHeteronuclear NMR investigations of dynamic regions of intact Escherichia coli ribosomesCharacterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy¹H, ¹³C and ¹⁵N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment.¹H, ¹³C and ¹⁵N assignments of the four N-terminal domains of human fibrillin-1.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.The human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7.Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies.Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.(1)H, (13)C and (15)N assignments of EGF domains 8-11 of human Notch-1.Secondary structure and topology of human interleukin 4 in solution.(1)H, (13)C and (15)N resonance assignments for the response regulator CheY3 from Rhodobacter sphaeroides.The N-Terminal Region of Fibrillin-1 Mediates a Bipartite Interaction with LTBP1.Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.NMR spectroscopic and bioinformatic analyses of the LTBP1 C-terminus reveal a highly dynamic domain organisation.Pressure-induced unfolding of the molten globule of all-Ala alpha-lactalbumin.Characterization of the unfolded state of bovine alpha-lactalbumin and comparison with unfolded states of homologous proteins.Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.Mouse N-acetyltransferase type 2, the homologue of human N-acetyltransferase type 1.1H, 13C and 15N resonance assignments for the oxidized and reduced states of the N-terminal domain of DsbD from Escherichia coli.The dynamics of lysozyme from bacteriophage lambda in solution probed by NMR and MD simulations.
P50
Q24337314-6C165DFB-9D5A-4CE0-A7C0-273572473B5BQ24654634-AB7B6610-B008-479B-AFB2-F60E9E07D313Q27630831-87B55FD2-784C-496B-85EB-0EEFADD775F3Q27641839-EEBA2942-60A9-46F6-BB1B-15D5516AB214Q27646300-92A1AAFD-993B-4542-A885-BCBF0FB7DBC7Q27651367-3BAF68EA-B921-41F4-B681-EA4DA85D7870Q27667688-FA69390C-7A73-4E0C-B1F0-091874DC3DECQ27679940-A552F265-28A7-4F2A-A2CD-D627CAD15564Q27681479-E807F2A6-41AF-4A08-B7DC-9C89138BEB1FQ27697457-2FA2AE46-B463-4C8D-8B85-9CD5B2B17505Q27700163-A5DA7AC9-E728-4751-8E72-ED72B7D9AEBCQ27731268-DED5A466-6253-4A54-BE3F-B47F6F2B2873Q28214226-3008A7CD-52A9-45C9-8980-F8A97900FDB7Q30397881-2EC9DB62-E02A-49BA-97D7-6AA89B632B2BQ30678312-F5B37F68-E752-4DE2-84F2-05C1D4B698C0Q33421000-39841341-F152-43AB-B479-42536D4CF6E6Q34401020-C09A38A8-D0B5-4564-AA22-4020A0B18E6CQ34418958-59201A8B-7AC5-4267-8542-7708D8E2B42FQ35850729-01D563CB-FD5D-49AB-B4E7-EA3BC0D77584Q36666270-379F6B4C-BCA7-4D53-8C37-E7F3AF34BDDCQ37284885-BA78215A-FFDF-4C88-B387-19915AB9D33CQ38272161-C5D81B26-9F91-46B9-8FAA-4CE2A7201A16Q38284286-D51A8DAB-946D-413C-9707-41EAD14DC9F2Q38284297-404CBDAC-CFD6-4F38-8420-24D9D4BE466FQ39729538-870489E9-090E-450A-BBA5-9938867F1C20Q39805609-6E14F293-DCAE-41AA-8384-293CABFEFB09Q39903567-05D7CAAF-D227-4D53-AD04-E0866A2F658AQ40282249-85360215-96DA-4EEF-BAD5-919A6C2025F3Q40991119-DAE3EBC8-855A-4CC4-BB4D-B629DF3D96BBQ41168558-673E7792-A48B-4A8A-8D9E-65CB97B6319CQ41200407-53529BE2-6C60-4584-BBCD-D2D4F9976313Q41312162-CF32722E-168C-405B-821E-E31DF2EBA2C2Q41518456-A6D72B63-111D-4838-85AE-DA7356BE8235Q41784001-719F61B7-93BE-4663-A919-2F5E891D66DFQ41813101-95D6CC98-3D54-4B64-904D-8FAF5F7AC825Q41887041-889EC77E-CE89-46B7-8890-FFE159E3070AQ41905582-F4C5E8D6-5D52-4C1E-89AA-63E951473273Q41949567-F0FDCAA4-C1B3-4E5C-9182-16A875A6D690Q42027426-75C739EC-74E7-482F-9220-8AE293CCAE18Q42288089-E9EF58D4-08A6-4452-A5CA-C70820D7F559
P50
description
hulumtuese
@sq
researcher
@en
ricercatrice
@it
wetenschapper
@nl
հետազոտող
@hy
name
Christina Redfield
@ast
Christina Redfield
@en
Christina Redfield
@es
Christina Redfield
@nl
Christina Redfield
@sl
type
label
Christina Redfield
@ast
Christina Redfield
@en
Christina Redfield
@es
Christina Redfield
@nl
Christina Redfield
@sl
prefLabel
Christina Redfield
@ast
Christina Redfield
@en
Christina Redfield
@es
Christina Redfield
@nl
Christina Redfield
@sl
P214
P244
P106
P21
P214
P244
P31
P496
0000-0001-7297-7708
P734
P735
P7859
lccn-n88642608