About: Malene Jensen

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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	Jensen, Malene Jensen, Malene Jensen, Malene
alternative label	Ringkjobing-Jensen, Malene
preferred label	Jensen, Malene
name	Malene Jensen
Language	http://lexvo.org/id/iso639-3/und
Given name	Malene
familyName	Jensen
gender	female
ORCID iD	0000-0003-0419-2196
Scopus ID	35579443800
is sameAs of	Jensen, Malene Jensen, Malene
is Thesis advisor of	http://www.sudoc.fr/193066750/id http://www.sudoc.fr/274961903/id http://www.sudoc.fr/277265274/id
is Praeses of	http://www.sudoc.fr/252250192/id
is Author of	Structure of Nipah virus unassembled nucleoprotein in complex with its viral chaperone. Ensemble Structure of the Highly Flexible Complex Formed between Vesicular Stomatitis Virus Unassembled Nucleoprotein and its Phosphoprotein Chaperone. Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics Structure and Functions of Microtubule Associated Proteins Tau and MAP2c: Similarities and Differences Large-Scale Conformational Dynamics Control H5N1 Influenza Polymerase PB2 Binding to Importin alpha Intrinsic disorder within the erythrocyte binding-like proteins from Plasmodium falciparum. Ensemble Calculation for Intrinsically Disordered Proteins Using NMR Parameters. Targeting the disordered C terminus of PTP1B with an allosteric inhibitor. Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein. Structural dynamics of the C-terminal X domain of Nipah and Hendra viruses controls the attachment to the C-terminal tail of the nucleocapsid protein Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly Insights into the Structure and Dynamics of Measles Virus Nucleocapsids by (1)H-detected Solid-state NMR. On the Origin of NMR Dipolar Waves in Transient Helical Elements of Partially Folded Proteins Elucidating binding mechanisms and dynamics of intrinsically disordered protein complexes using NMR spectroscopy Intrinsically disordered proteins implicated in paramyxoviral replication machinery. Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage A Unified Description of Intrinsically Disordered Protein Dynamics under Physiological Conditions Using NMR Spectroscopy Structural basis of the bacteriophage TP901-1 CI repressor dimerization and interaction with DNA Mouse Rif1 is a regulatory subunit of protein phosphatase 1 (PP1). Experimental studies of binding of intrinsically disordered proteins to their partners Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1 Structure, dynamics and phase separation of measles virus RNA replication machinery A General Method for Determining the Electron Self-ExchangeRates of Blue Copper Proteins by Longitudinal NMRRelaxation Deciphering the Dynamic Interaction Profile of an Intrinsically Disordered Protein by NMR Exchange Spectroscopy Quantitative Description of Backbone Conformational Sampling of Unfolded Proteins at Amino Acid Resolution from NMR Residual Dipolar Couplings Visualizing protein breathing motions associated with aromatic ring flipping Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex Assembly and cryo-EM structures of RNA-specific measles virus nucleocapsids provide mechanistic insight into paramyxoviral replication Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A Metal−Protein Interactions: Structure Information from Ni2+-InducedPseudocontact Shifts in a Native Nonmetalloprotein Solution Structure of a Conformationally Restricted Fully Active Derivative of the Human Relaxin-like Factor An ultraweak interaction in the intrinsically disordered replication machinery is essential for measles virus function Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment Identification of Dynamic Modes in an Intrinsically Disordered Protein Using Temperature-Dependent NMR Relaxation. Structural analysis of the complex between influenza B nucleoprotein and human importin-α Small-angle X-ray scattering- and nuclear magnetic resonance-derived conformational ensemble of the highly flexible antitoxin PaaA2. A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin. Characterizing Protein-Protein Interactions Using Solution NMR Spectroscopy. Metal Binding Sites in Proteins: Identification and Characterization byParamagnetic NMR Relaxation Structure of the tetramerization domain of measles virus phosphoprotein. Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus Visualizing the molecular recognition trajectory of an intrinsically disordered protein using multinuclear relaxation dispersion NMR Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase Quantitative Conformational Analysis of Partially Folded Proteins from Residual Dipolar Couplings: Application to the Molecular Recognition Element of Sendai Virus Nucleoprotein Atomic resolution description of the interaction between the nucleoprotein and phosphoprotein of Hendra virus. Structural Characterization of the SMRT Corepressor Interacting with Histone Deacetylase 7. Self-Assembly of Measles Virus Nucleocapsid-like Particles: Kinetics and RNA Sequence-Dependence. Structural and dynamics studies of a truncated variant of CI repressor from bacteriophage TP901-1 Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments Adenosine-dependent activation mechanism of prodrugs targeting an aminoacyl-tRNA synthetase https://hal.archives-ouvertes.fr/hal-04717912#id https://hal.archives-ouvertes.fr/hal-04782007#id PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins
is primary topic of	http://www.idref.fr/057318565
is Translator of	http://www.sudoc.fr/003778037/id
is Opponent of	http://www.sudoc.fr/199586241/id http://www.sudoc.fr/194282481/id
is Thesis referee of	http://www.sudoc.fr/198705794/id http://www.sudoc.fr/202413411/id http://www.sudoc.fr/241058732/id http://www.sudoc.fr/241346452/id http://www.sudoc.fr/226649563/id http://www.sudoc.fr/257276610/id http://www.sudoc.fr/26943271X/id http://www.sudoc.fr/242148557/id http://www.sudoc.fr/276062531/id

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