about
Long unfolded linkers facilitate membrane protein import through the nuclear pore complex.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBCavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozymeProbing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r)Subpolar addition of new cell wall is directed by DivIVA in mycobacteria.Energetic dissection of Gleevec's selectivity toward human tyrosine kinases.The energy landscape of adenylate kinase during catalysis.Cystathionine β-synthase (CBS) domains 1 and 2 fulfill different roles in ionic strength sensing of the ATP-binding cassette (ABC) transporter OpuA.Kinase dynamics. Using ancient protein kinases to unravel a modern cancer drug's mechanismOptimized co-solute paramagnetic relaxation enhancement for the rapid NMR analysis of a highly fibrillogenic peptide.A minor conformation of a lanthanide tag on adenylate kinase characterized by paramagnetic relaxation dispersion NMR spectroscopy.Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.Comprehensive determination of (3)J (HNHalpha) for unfolded proteins using (13)C'-resolved spin-echo difference spectroscopy.Comprehensive analysis of NMR data using advanced line shape fitting.Conformational Selection in a Protein-Protein Interaction Revealed by Dynamic Pathway Analysis.1H, 13C, and 15N resonance assignments of the phosphorylated enzyme IIB of the mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.Conformational fluctuations affect protein alignment in dilute liquid crystal media.Rescue of conformational dynamics in enzyme catalysis by directed evolution.Dynamics of human protein kinase Aurora A linked to drug selectivityMechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2Protein Surface and Core Dynamics Show Concerted Hydration-Dependent ActivationProbing the Transition State in Enzyme Catalysis by High-Pressure NMR Dynamics
P50
Q27940107-7EAB74EB-1526-4C8C-9BA1-13543D50CECCQ30366264-3B94A3B1-94C1-4596-B3CC-C136ECF65336Q30883065-454184BD-7327-46F8-8574-F59EF1DF0D00Q33740930-6647CFB7-25DB-425C-87C7-A964CFF086ACQ34025409-3DE781E5-0991-49A8-97D1-EBB1A9EB2648Q34703677-90967D23-78B5-436B-90DC-9D58AB0AF2A5Q35054579-163AD8A4-CFF6-4DD3-A5E7-4EB9E526E8D4Q35423594-2606A8F3-0C73-4C0C-B76F-02A62928ECEFQ35509663-CB337CAC-6C1F-4196-B5AF-BACDA1B1B5BBQ41143551-BFCE2736-580E-40BF-9135-61BAC0C4DCF7Q41617844-9D16333F-A447-498D-8715-75F296D678A5Q41962826-BF192D4A-E726-4F8B-9FBF-776F659A149CQ42637099-1F974710-8191-4F1C-9FF5-5829610C6C47Q42695897-23D51B9F-E5F6-47F4-A6ED-8E86EBCFE088Q42872555-B970F58B-6D84-4BC6-8429-7077B1FDA4F6Q45210433-87913D84-B7C1-4017-B9B6-BDF9D404ECFBQ53001088-A790646F-E33F-4B14-8258-8F0E25FC2F00Q55016820-C7646608-9891-4D59-AE61-C28FACC16B06Q56889888-3817E847-B98F-4D8E-99C1-554DC44D10B5Q58097742-BD6023FF-69C5-489C-B864-BDEA9CCEF181Q60228218-5A8E19EF-7BBB-4085-8313-E6FFF0B7675EQ90224651-A786CB37-2516-4972-948F-41DCF2180B3C
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Renee Otten
@ast
Renee Otten
@en
Renee Otten
@es
Renee Otten
@nl
Renee Otten
@sl
type
label
Renee Otten
@ast
Renee Otten
@en
Renee Otten
@es
Renee Otten
@nl
Renee Otten
@sl
prefLabel
Renee Otten
@ast
Renee Otten
@en
Renee Otten
@es
Renee Otten
@nl
Renee Otten
@sl
P106
P21
P31
P496
0000-0001-7342-6131