about
Signaling and Adaptation Modulate the Dynamics of the Photosensoric Complex of Natronomonas pharaonisHydrogen bonding of nitroxide spin labels in membrane proteins.Effects of solubilization on the structure and function of the sensory rhodopsin II/transducer complex.Conformational changes of the betaine transporter BetP from Corynebacterium glutamicum studied by pulse EPR spectroscopy.Phosphorylation of a membrane curvature-sensing motif switches function of the HOPS subunit Vps41 in membrane tethering.Simulation vs. reality: a comparison of in silico distance predictions with DEER and FRET measurementsMolecular mechanisms of gene regulation studied by site-directed spin labeling.The archaeal sensory rhodopsin II/transducer complex: a model for transmembrane signal transfer.Sensory rhodopsin II and bacteriorhodopsin: light activated helix F movement.Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction.A comparative electron paramagnetic resonance study of the nucleotide-binding domains' catalytic cycle in the assembled maltose ATP-binding cassette importer.Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimerSpin labeling EPR.Transmembrane signal transduction in archaeal phototaxis: the sensory rhodopsin II-transducer complex studied by electron paramagnetic resonance spectroscopy.Ligand-induced conformational capture of a synthetic tetracycline riboswitch revealed by pulse EPR.Ferredoxin:NADP(H) Oxidoreductase Abundance and Location Influences Redox Poise and Stress Tolerance.In vivo EPR on spin labeled colicin A reveals an oligomeric assembly of the pore-forming domain in E. coli membranes.A structure-based simulation approach for electron paramagnetic resonance spectra using molecular and stochastic dynamics simulations.Assessing oligomerization of membrane proteins by four-pulse DEER: pH-dependent dimerization of NhaA Na+/H+ antiporter of E. coli.Nitrite regulates hypoxic vasodilation via myoglobin-dependent nitric oxide generation.Interconversion between bound and free conformations of LexA orchestrates the bacterial SOS response.ATP-dependent Conformational Changes Trigger Substrate Capture and Release by an ECF-type Biotin TransporterTemperature-dependent equilibrium between the open and closed conformation of the p66 subunit of HIV-1 reverse transcriptase revealed by site-directed spin labelling.Molecular details of Bax activation, oligomerization, and membrane insertion.Clustering and dynamics of phototransducer signaling domains revealed by site-directed spin labeling electron paramagnetic resonance on SRII/HtrII in membranes and nanodiscs.Salt-driven equilibrium between two conformations in the HAMP domain from Natronomonas pharaonis: the language of signal transfer?Microtubule binding and trapping at the tip of neurites regulate tau motion in living neurons.The attachment affinity of hemoglobin toward silver-containing bioactive glass functionalized with glutaraldehyde.A commonly used spin label: S-(2,2,5,5-tetramethyl-1-oxyl-delta3-pyrrolin-3-ylmethyl) methanethiosulfonate.Prevention of peroxidation of cardiolipin liposomes by quinol-based antioxidants.Acidic pH-induced membrane insertion of colicin A into E. coli natural lipids probed by site-directed spin labeling.Interaction of alpha-crystallin with spin-labeled peptides.Light-induced movement of the transmembrane helix B in channelrhodopsin-2.Conformational changes of the histidine ATP-binding cassette transporter studied by double electron-electron resonance spectroscopy.Structure and dynamics of spin-labeled insulin entrapped in a silica matrix by the sol-gel method.Orientation selective DEER measurements on vinculin tail at X-band frequencies reveal spin label orientations.A simple method for determination of rotational correlation times and separation of rotational and polarity effects from EPR spectra of spin-labeled biomolecules in a wide correlation time range.Extracellular loop 4 of the proline transporter PutP controls the periplasmic entrance to ligand binding sites.Topology of the amphipathic helices of the colicin A pore-forming domain in E. coli lipid membranes studied by pulse EPR.Two-Dimensional Trap for Ultrasensitive Quantification of Transient Protein Interactions.
P50
Q28551022-992011D4-E513-4F30-9F59-2D9AF1C0E0BCQ30833328-9EFCB74C-C3DC-4857-9AFA-A1E8B71FBC1CQ33231544-27DF06CA-DD73-4B91-9B88-4B2EC9CB2C83Q34066245-8EE64567-32C6-4737-9C34-A1F105886B40Q34317009-EDE5163B-1B80-4310-8516-EE777294E847Q34326170-21008C9F-0568-4AA5-8952-962185DEFEFBQ35073586-3D882BBD-F624-412F-84B7-9329044E5AD9Q35757339-41881C56-3AD6-4CBC-934C-084DA1313D40Q35788168-E2196053-DF09-44CD-9019-D217DA461E7AQ35954764-CC976E74-DFEA-4450-82A3-F43BE701DE0FQ36856323-F82D8441-FD10-4E65-9699-1A0463164BFEQ37285226-8F88CA84-FC4A-4769-818B-13552D65AF71Q37591402-D85DE233-6D2E-40B9-95D9-3A9A221DA4B9Q37891534-C1CA5FFB-F3E1-48C3-8C3C-AAF1F873EC73Q38339171-37B4622A-40F6-4D4A-BDE1-94BB19613583Q39383654-CC53EC24-C848-4B37-B583-D3E66F3AD34DQ41541111-8B5085DD-AE5E-4A15-B88A-13F5F21D51F5Q41809810-7868F0CF-14E2-4FEB-B6AF-00A4B0915F0FQ41867016-6A79556B-B3F3-477E-A1C7-7B21F8A29535Q41886769-915014C0-FF95-4609-9199-2B049A63F441Q42186310-D4202497-DD5D-4E9C-A380-9A85732B54D2Q42350077-08273D72-44E1-4842-94FF-793A03F1E54BQ42632779-2DB2DAA4-7ACC-460D-9C3A-F1F52DD784A2Q42910802-2A2B1797-FA63-45A5-B11C-F40E3FBE19CDQ43023585-6A4DFC65-72B2-4BD5-8708-E4C271B96FC9Q43155965-F3F08A68-DEF2-4D09-BD66-5BF0A50D8B31Q43278561-5CBB8203-AB3A-4F34-B0D9-932F9CD331B5Q43791072-69583B0D-AFFD-4297-B815-09B4122CA076Q46260861-4125195A-1CF2-4AF9-BC90-721C92A429DBQ46797392-99FA6AD8-83DA-4596-8505-20185B5CB902Q46913016-E2D4D5CC-5777-422C-B8F0-2CADC266A628Q46915672-96EE12EC-DAB8-494A-853D-B90ED6C13B44Q47916031-1B30A688-4BE7-4BAB-8251-4F7823DDE2C8Q50001325-8B143B3A-102F-4A12-9D70-9A8C890A1E02Q50863289-34E7D757-4158-4F9E-A987-C5A18E4B21A4Q51435605-56A85CA2-A316-4327-8411-B01CF1407ED3Q52548829-427C511D-04CD-4748-87BD-DE2E6B23EEE9Q54290342-77581DA0-87B0-4FF3-B6BC-08F63223E9FFQ54401047-8187EC03-4589-4DEB-BD83-C065DF680DBCQ55044032-480217E5-1EFC-461E-A047-A0D16F708FF4
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Heinz-Jürgen Steinhoff
@ast
Heinz-Jürgen Steinhoff
@br
Heinz-Jürgen Steinhoff
@co
Heinz-Jürgen Steinhoff
@cs
Heinz-Jürgen Steinhoff
@da
Heinz-Jürgen Steinhoff
@de
Heinz-Jürgen Steinhoff
@en
Heinz-Jürgen Steinhoff
@es
Heinz-Jürgen Steinhoff
@fr
Heinz-Jürgen Steinhoff
@id
type
label
Heinz-Jürgen Steinhoff
@ast
Heinz-Jürgen Steinhoff
@br
Heinz-Jürgen Steinhoff
@co
Heinz-Jürgen Steinhoff
@cs
Heinz-Jürgen Steinhoff
@da
Heinz-Jürgen Steinhoff
@de
Heinz-Jürgen Steinhoff
@en
Heinz-Jürgen Steinhoff
@es
Heinz-Jürgen Steinhoff
@fr
Heinz-Jürgen Steinhoff
@id
altLabel
Heinz-Juergen Steinhoff
@en
prefLabel
Heinz-Jürgen Steinhoff
@ast
Heinz-Jürgen Steinhoff
@br
Heinz-Jürgen Steinhoff
@co
Heinz-Jürgen Steinhoff
@cs
Heinz-Jürgen Steinhoff
@da
Heinz-Jürgen Steinhoff
@de
Heinz-Jürgen Steinhoff
@en
Heinz-Jürgen Steinhoff
@es
Heinz-Jürgen Steinhoff
@fr
Heinz-Jürgen Steinhoff
@id
P106
P21
P31
P496
0000-0002-5888-0157