World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
54
Citations
11107
World Ranking
15579
National Ranking
1097

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • DNA

His primary areas of investigation include Biochemistry, Proteases, Cell biology, Protease and PDZ domain. Biochemistry is closely attributed to Biophysics in his work. His work carried out in the field of Proteases brings together such families of science as Heat shock protein, HTRA1, Protein folding, Protein structure and Serine Protease HTRA1.

His Heat shock protein research is multidisciplinary, incorporating elements of JUNQ and IPOD and Chaperone. In Cell biology, Michael Ehrmann works on issues like Protein quality, which are connected to Cell fate determination. His PDZ domain research incorporates elements of Cell envelope, Crystal structure and Function.

His most cited work include:

  • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. (674 citations)
  • The HtrA Family of Proteases: Implications for Protein Composition and Cell Fate (535 citations)
  • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine (354 citations)

What are the main themes of his work throughout his whole career to date?

Michael Ehrmann mainly focuses on Biochemistry, Protease, Cell biology, Proteases and Protein folding. His is involved in several facets of Biochemistry study, as is seen by his studies on PDZ domain, Periplasmic space, Escherichia coli, Allosteric regulation and Proteolysis. His work deals with themes such as HTRA1, Chaperone and Peptide, which intersect with Protease.

His Cell biology research includes elements of Mutation and Cell fate determination. His Proteases study integrates concerns from other disciplines, such as Serine protease, Serine Protease HTRA1, Serine and Heat shock protein. His studies deal with areas such as Protein structure, Plasma protein binding, Biophysics and Function as well as Protein folding.

He most often published in these fields:

  • Biochemistry (65.47%)
  • Protease (44.60%)
  • Cell biology (38.85%)

What were the highlights of his more recent work (between 2016-2021)?

  • Cell biology (38.85%)
  • Computational biology (7.19%)
  • Proteomics (7.19%)

In recent papers he was focusing on the following fields of study:

Michael Ehrmann mainly investigates Cell biology, Computational biology, Proteomics, Serine protease and Binding site. When carried out as part of a general Cell biology research project, his work on Notch signaling pathway is frequently linked to work in Tube formation, therefore connecting diverse disciplines of study. His work on Serine Protease Inhibitors as part of general Serine protease research is frequently linked to Non covalent, bridging the gap between disciplines.

Biochemistry and Protease are the subject areas of his Serine Protease Inhibitors study. His Biochemistry study frequently links to adjacent areas such as Dynamic light scattering. His Proteases research focuses on Allosteric regulation and how it connects with Protein structure, Bacterial outer membrane and Chaperone.

Between 2016 and 2021, his most popular works were:

  • VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy. (115 citations)
  • Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions (42 citations)
  • Tailored protein encapsulation into a DNA host using geometrically organized supramolecular interactions (42 citations)

In his most recent research, the most cited papers focused on:

  • Gene
  • Enzyme
  • DNA

His primary scientific interests are in Binding site, Cell biology, Serine protease, Molecular probe and Nanotechnology. Michael Ehrmann combines subjects such as Intrinsically disordered proteins and Electrospray ionization, Ion-mobility spectrometry, Mass spectrometry with his study of Binding site. Michael Ehrmann works in the field of Cell biology, focusing on Protein degradation in particular.

The Serine protease study combines topics in areas such as Chemical biology, Mode of action, Computational biology, Drug discovery and Peptide synthesis. His study in Molecular probe is interdisciplinary in nature, drawing from both Supramolecular chemistry, A-DNA, Molecular recognition and Intermolecular force. His research in Autophagy intersects with topics in Mutation, Deubiquitinating enzyme and Lysosome.

Best Publications

  • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

    Christoph Spiess;Alexandra Beil;Michael Ehrmann

  • The HtrA Family of Proteases: Implications for Protein Composition and Cell Fate

    Tim Clausen;Christopher Southan;Michael Ehrmann

  • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine

    Tobias Krojer;Marta Garrido-Franco;Robert Huber;Michael Ehrmann

  • HTRA proteases: regulated proteolysis in protein quality control

    Tim Clausen;Markus Kaiser;Robert Huber;Michael Ehrmann;Michael Ehrmann

  • Structural basis for the regulated protease and chaperone function of DegP

    Tobias Krojer;Justyna Sawa;Eva Schäfer;Helen R. Saibil

  • Lysine-Specific Molecular Tweezers Are Broad-Spectrum Inhibitors of Assembly and Toxicity of Amyloid Proteins

    Sharmistha Sinha;Dahabada H. J. Lopes;Zhenming Du;Eric S. Pang

  • Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease.

    Corinna Wilken;Karina Kitzing;Robert Kurzbauer;Michael Ehrmann

  • The role of human HtrA1 in arthritic disease.

    Sandra Grau;Peter J. Richards;Briedgeen Kerr;Clare Elizabeth Hughes

  • VCP/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy.

    Chrisovalantis Papadopoulos;Philipp Kirchner;Monika Bug;Daniel Grum

  • Proteolysis as a Regulatory Mechanism

    Michael Ehrmann;Tim Clausen

  • Implications of the serine protease HtrA1 in amyloid precursor protein processing

    Sandra Grau;Alfonso Baldi;Rossana Bussani;Xiaodan Tian

  • Periplasmic glycerophosphodiester phosphodiesterase of Escherichia coli, a new enzyme of the glp regulon.

    T J Larson;M Ehrmann;W Boos

  • Peptide Functionalized Polydiacetylene Liposomes Act as a Fluorescent Turn-On Sensor for Bacterial Lipopolysaccharide

    Junchen Wu;Adam Zawistowski;Michael Ehrmann;Tao Yi

  • Protein Quality Control in the Bacterial Periplasm

    Melisa Merdanovic;Tim Clausen;Markus Kaiser;Robert Huber

  • Genetic analysis of membrane protein topology by a sandwich gene fusion approach.

    Michael Ehrmann;Dana Boyd;Jonathan Beckwith

  • Serine protease HtrA1 modulates chemotherapy-induced cytotoxicity

    Jeremy Chien;Giovanni Aletti;Alfonso Baldi;Vincenzo Catalano

  • The ABC maltose transporter

    Michael Ehrmann;Rainer Ehrle;Eckhard Hofmann;Winfried Boos

  • Cerebral small vessel disease-related protease HtrA1 processes latent TGF-β binding protein 1 and facilitates TGF-β signaling

    Nathalie Beaufort;Eva Scharrer;Elisabeth Kremmer;Vanda Lux

  • Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins.

    Tobias Krojer;Karen Pangerl;Juliane Kurt;Justyna Sawa

  • The HtrA Family of Proteases: Implications for Protein Composition and Cell Fate: Implications for Protein Composition and Cell Fate

    Michael Ehrmann;Tim Clausen;Chris Southan

Frequent Co-Authors

Markus Kaiser
Markus Kaiser University of Duisburg-Essen
Tim Clausen
Tim Clausen Research Institute of Molecular Pathology
Robert Huber
Robert Huber University of Duisburg-Essen
Winfried Boos
Winfried Boos University of Konstanz
Alfonso Baldi
Alfonso Baldi University of Campania "Luigi Vanvitelli"
Dana Boyd
Dana Boyd Harvard University
Gal Bitan
Gal Bitan University of California, Los Angeles
Frank-Gerrit Klärner
Frank-Gerrit Klärner University of Duisburg-Essen
Thomas Schrader
Thomas Schrader University of Duisburg-Essen
Jon Beckwith
Jon Beckwith Harvard University

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