About: Nathalie Declerck

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An Entity of Type : foaf:Person, within Data Space : data.idref.fr associated with source document(s)

Attributes	Values
type	Person
sameAs	Declerck, Nathalie Declerck, Nathalie Declerck, Nathalie
preferred label	Declerck, Nathalie
name	Nathalie Declerck
dbpedia-owl:citizenship	http://sws.geonames.org/3017382/
Language	http://lexvo.org/id/iso639-3/eng http://lexvo.org/id/iso639-3/fra
Given name	Nathalie
familyName	Declerck
has biographical i...tion (Deprecated)	Directeur de recherche au Centre de biochimie structurale, INSERM /CNRS (en 2011).Rapporteur d'une thèse de doctorat de : Structure, fonction et ingénierie des protéines, Université Paris-Sud, Châtenay-Malabry (en 2011)
gender	female
ORCID iD	0000-0003-1551-1607
is sameAs of	Declerck, Nathalie Declerck, Nathalie Declerck, Nathalie
is Thesis advisor of	http://www.sudoc.fr/233333371/id
is Author of	Fructose-1,6-bisphosphate acts both as an inducer and as a structural cofactor of the central glycolytic genes repressor (CggR). A part toolbox to tune genetic expression in Bacillus subtilis Hyperthermostable variants of a highly thermostable alpha-amylase Structural mechanism of signal transduction between the RNA-binding domain and the PTS-regulation domain of the LicT antiterminator. Interactions in Gene Expression Networks Studied by Two-Photon Fluorescence Fluctuation Spectroscopy Regulation of trypsin activity by Cu2+ chelation of the substrate binding site Mutation of recombinant catalytic subunit alpha of the protein kinase CK2 that affects catalytic efficiency and specificity https://hal.archives-ouvertes.fr/hal-02359578#id Competitive folding of RNA structures at a termination-antitermination site Refined solution structure and backbone dynamics of 15N-labeled C12A-p8MTCP1 studied by NMR relaxation Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY https://hal.archives-ouvertes.fr/hal-01569011#id RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT Novel substrate specificity engineered in the arabinose binding protein Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY Dimer stabilization upon activation of the transcriptional antiterminator LicT 1 1Edited by T. Richmond Fructose-1,6-bisphosphate Acts Both as an Inducer and as a Structural Cofactor ofthe Central Glycolytic Genes Repressor (CggR) Characterization of the CcpN repressor by FCCS and other biophysical approaches. High pressure activation of the Mrr restriction endonuclease in <em>Escherichia coli</em> involves tetramer dissociation Integration, amplification and expression of the Bacillus licheniformis alpha-amylase gene in Bacillus subtilis chromosome Two types of transcriptional repression in living cells of [i]Bacillus subtilis[/i] characterized by number and brightness analysis Quantitative High-Resolution Imaging of Live Microbial Cells at High Hydrostatic Pressure Probing structural determinants specifying high thermostability in Bacillus licheniformis alpha-amylase Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. Structure Structural insights into the allosteric activation of the LicT antiterminator by PTS- mediated phosphorylation Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50°C temperature range Rapid determination of protein solubility and stability conditions for NMR studies using incomplete factorial design Activation of Bacillus licheniformis alpha-amylase through a disorder-order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad Novel substrate specificity engineered in the arabinose binding protein Impact of the lysine-188 and aspartic acid-189 inversion on activity of trypsin Intrinsic disorder in Viral Proteins Genome-Linked: experimental and predictive analyses Structural insights into the regulation of bacterial signalling proteins containing PRDs Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides A phospho-sugar binding domain homologous to NagB enzymes regulates the activity of the central glycolytic genes repressor. Absolute quantification of gene expression in individual bacterial cells using two-photon fluctuation microscopy A natural variant of Bacillus licheniformis alpha-amylase isolated from flour mill wastewaters sheds light on the origin of high thermostability. Overlapping reading frames at the LYS5 locus in the yeast Yarrowia lipolytica Hyperthermostable mutants of Bacillus licheniformis alpha-amylase : multiple amino acid replacements and molecular modelling Hyperthermostable mutants of Bacillus licheniformis α-amylase: multiple amino acid replacements and molecular modelling Inducer-modulated cooperative binding of the tetrameric CggR repressor to operator DNA. Molecular basis for group-specific activation of the virulence regulator PlcR by PapR heptapeptides. Reconciling molecular regulatory mechanisms with noise patterns of bacterial metabolic promoters in induced and repressed states An oligomeric switch controls the Mrr-induced SOS response in E. coli NMR chemical shift assignment of a constitutively active fragment of the antitermination protein LicT Resolving the activation mechanism of the D99N antiterminator LicT protein Use of amber suppressors to investigate the thermostability of Bacillus licheniformis alpha-amylase Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator Structure of PlcR: Insights into virulence regulation and evolution of quorum sensing in Gram-positive bacteria Prevention of cross-talk in conserved regulatory systems: identification of specificity determinants in RNA-binding anti-termination proteins of the BglG family RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT Dimer stabilization upon activation of the transcriptional antiterminator LicT Hyperthermostable mutants of Bacillus licheniformis alfa-amylase : thermodynamic studies and structural interpretation Activation of Bacillus licheniformis alpha-amylase through a disorder order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
is primary topic of	http://www.idref.fr/157061299
is Opponent of	http://www.sudoc.fr/255717059/id
is Thesis referee of	http://www.sudoc.fr/157845516/id http://www.sudoc.fr/240774833/id

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