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Heinz-Jürgen Steinhoff

Researcher at University of Osnabrück

Publications -  152
Citations -  6027

Heinz-Jürgen Steinhoff is an academic researcher from University of Osnabrück. The author has contributed to research in topics: Spin label & Site-directed spin labeling. The author has an hindex of 43, co-authored 151 publications receiving 5642 citations. Previous affiliations of Heinz-Jürgen Steinhoff include University College London & Max Planck Society.

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Global hairpin folding of tau in solution.

TL;DR: The data indicate that tau retains some global folding even in its "natively unfolded" state, combined with the high flexibility of the chain.
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Nitrite reductase activity of myoglobin regulates respiration and cellular viability in myocardial ischemia-reperfusion injury.

TL;DR: Testing the central role of myoglobin as a functional nitrite reductase that regulates hypoxic NO• generation, controls cellular respiration, and therefore confirms a cytoprotective response to cardiac ischemia-reperfusion (I/R) injury finds that myoglobin is responsible for nitrite-dependent NO•generation and cardiomyocyte protein iron-nitrosylation.
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Spin labeling EPR

TL;DR: Continuous wave EPR spectra analyses and pulse EPR techniques are reviewed with special emphasis on applications to the sensory rhodopsin–transducer complex mediating the photophobic response of the halophilic archaeum Natronomonas pharaonis and the photosynthetic reaction center from Rhodobacter sphaeroides R26.
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Structural insights into the early steps of receptor—transducer signal transfer in archaeal phototaxis

TL;DR: Electron paramagnetic resonance‐based inter‐residue distance measurements between site‐directed spin‐labelled sites of sensory rhodopsin II and its transducer NpHtrII from Natronobacterium pharaonis revealed a 2:2 complex with 2‐fold symmetry.
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Determination of interspin distances between spin labels attached to insulin: comparison of electron paramagnetic resonance data with the X-ray structure

TL;DR: The study of interspin distances between attached spin labels can be applied to obtain structural information on proteins under conditions where other methods like two-dimensional nuclear magnetic resonance spectroscopy or x-ray crystallography are not applicable.