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Martin Engelhard

Martin Engelhard

D-Index & Metrics

Chemistry

D-Index
59
Citations
10225
World Ranking
10351
National Ranking
753

Overview

Martin Engelhard is affiliated with the Max Planck Society in Germany. Their research primarily focuses on neuroscience, with specific attention to cellular and molecular neuroscience. Engelhard's work spans several interrelated fields, including spectroscopy, molecular biology, plant science, and atomic and molecular physics and optics.

Engelhard's research explores multiple scientific topics, notably photoreceptor and optogenetics research, neuroscience and neuropharmacology, mass spectrometry techniques and applications, photosynthetic processes and mechanisms, the effects of light on plants, spectroscopy and quantum chemical studies, and molecular spectroscopy and chirality.

Frequent coauthors in Engelhard's publications include:

  • Valentin Gordeliy
  • Ernst Bamberg
  • Kirill Kovalev
  • Ivan Gushchin
  • Alexey Alekseev

The main venues for Engelhard's publications are:

  • RWTH Publications (RWTH Aachen)
  • Zenodo (CERN European Organization for Nuclear Research)
  • Nature Structural & Molecular Biology
  • Scientific Reports
  • Nature Communications

Among recent significant papers authored or co-authored by Engelhard are:

  • "True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins," 2022, Nature Structural & Molecular Biology
  • "Molecular model of a sensor of two-component signaling system," 2021, Scientific Reports
  • "Structural insights into light-driven anion pumping in cyanobacteria," 2022, Nature Communications
  • "Molecular Biology of Microbial Rhodopsins," 2022, Methods in Molecular Biology
  • "New structural insights in chloroplast F1FO-ATP synthases," 2020, RWTH Publications (RWTH Aachen)

Best Publications

  • Molecular basis of transmembrane signalling by sensory rhodopsin II–transducer complex

    Valentin I. Gordeliy;Jörg Labahn;Rouslan Moukhametzianov;Rouslan Efremov

  • A new synthetic route to tert-butyloxycarbonylaminoacyl-4-(oxymethyl)phenylacetamidomethyl-resin, an improved support for solid-phase peptide synthesis

    Alexander R. Mitchell;Stephen B. H. Kent;Martin Engelhard;R. B. Merrifield

  • Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation of static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane

    Engelhard M;Gerwert K;Hess B;Kreutz W

  • Bioenergetics of the Archaea

    Günter Schäfer;Martin Engelhard;Volker Müller

  • Proteorhodopsin is a light-driven proton pump with variable vectoriality.

    Thomas Friedrich;Sven Geibel;Rolf Kalmbach;Igor Chizhov

  • Secondary Structure, Dynamics, and Topology of a Seven‐Helix Receptor in Native Membranes, Studied by Solid‐State NMR Spectroscopy

    Manuel Etzkorn;Swetlana Martell;Ovidiu C. Andronesi;Karsten Seidel

  • Development of the signal in sensory rhodopsin and its transfer to the cognate transducer.

    Rouslan Moukhametzianov;Johann P. Klare;Rouslan Efremov;Christian Baeken

  • Spectrally silent transitions in the bacteriorhodopsin photocycle.

    I. Chizhov;D.S. Chernavskii;M. Engelhard;K.H. Mueller

  • Structural insights into the early steps of receptor—transducer signal transfer in archaeal phototaxis

    Ansgar-A. Wegener;Johann P. Klare;Martin Engelhard;Heinz-Jürgen Steinhoff

  • The photophobic receptor from Natronobacterium pharaonis: temperature and pH dependencies of the photocycle of sensory rhodopsin II

    Igor Chizhov;Georg Schmies;Ralf Seidel;Jens R. Sydor

  • Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II.

    Ansgar-A Wegener;Igor Chizhov;Martin Engelhard;Heinz-Jürgen Steinhoff

  • Functional Cell-free Synthesis of a Seven Helix Membrane Protein: In situ Insertion of Bacteriorhodopsin into Liposomes

    Rolf Kalmbach;Igor Chizhov;Miria C. Schumacher;Thomas Friedrich

  • Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation.

    Gu¨nther Metz;Friedrich Siebert;Martin Engelhard

  • Transient kinetic studies on the interaction of ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex

    Jens R. Sydor;Martin Engelhard;Alfred Wittinghofer;Roger S. Goody

  • Purification of histidine tagged bacteriorhodopsin, pharaonis halorhodopsin and pharaonis sensory rhodopsin II functionally expressed in Escherichia coli

    Ilja P Hohenfeld;Ansgar A Wegener;Martin Engelhard

  • Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy.

    X. Jiang;E. Zaitseva;M. Schmidt;F. Siebert

  • The primary structure of sensory rhodopsin II: a member of an additional retinal protein subgroup is coexpressed with its transducer, the halobacterial transducer of rhodopsin II.

    Ralf Seidel;Birgit Scharf;Mathias Gautel;Karl Kleine

  • The archaeal sensory rhodopsin II/transducer complex: a model for transmembrane signal transfer

    Johann P Klare;Valentin I Gordeliy;Jörg Labahn;Georg Büldt

  • Microbial rhodopsins: scaffolds for ion pumps, channels, and sensors.

    Johann P. Klare;Igor Chizhov;Martin Engelhard

  • Blue halorhodopsin from Natronobacterium pharaonis: wavelength regulation by anions.

    Birgit Scharf;Martin Engelhard

Frequent Co-Authors

Friedrich Siebert
Friedrich Siebert University of Freiburg
Heinz-Jürgen Steinhoff
Heinz-Jürgen Steinhoff Osnabrück University
Roger S. Goody
Roger S. Goody Max Planck Society
Benno Hess
Benno Hess Max Planck Society
Dieter Oesterhelt
Dieter Oesterhelt Max Planck Society
Ernst Bamberg
Ernst Bamberg Max Planck Society
Jörg Tatzelt
Jörg Tatzelt Ruhr University Bochum
Konstanze F. Winklhofer
Konstanze F. Winklhofer Ruhr University Bochum
Peter Hildebrandt
Peter Hildebrandt Technical University of Berlin
Stephen B. H. Kent
Stephen B. H. Kent University of Chicago

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