World's Best Scientists 2026 revealed!

D-Index & Metrics

Biology and Biochemistry

D-Index
85
Citations
33471
World Ranking
3093
National Ranking
235

Research.com Recognitions

  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Fellow of The Academy of Medical Sciences, United Kingdom
  • Fellow of The Academy of Medical Sciences, United Kingdom

Overview

What is he best known for?

The fields of study he is best known for:

  • Gene
  • Enzyme
  • Amino acid

Mathias Gautel spends much of his time researching Titin, Obscurin, Biophysics, Actinin, alpha 2 and Myosin. His Titin study combines topics from a wide range of disciplines, such as Crystallography and Protein kinase domain. Mathias Gautel interconnects Telethonin and Skeletal muscle in the investigation of issues within Obscurin.

His research integrates issues of Protein structure, Spectrin repeat, Spectrin and Actin in his study of Biophysics. His Actinin, alpha 2 research is multidisciplinary, incorporating perspectives in Myomesin, Immunoglobulin domain, Pathology, Molecular biology and Myotilin. Mathias Gautel has begun a study into Myosin, looking into Biochemistry and Cell biology.

His most cited work include:

  • Guidelines for the use and interpretation of assays for monitoring autophagy (3242 citations)
  • Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM (2436 citations)
  • The Kinase Domain of Titin Controls Muscle Gene Expression and Protein Turnover (480 citations)

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

Mathias Gautel focuses on Titin, Cell biology, Biophysics, Myosin and Sarcomere. His study connects Crystallography and Titin. His research in Biophysics intersects with topics in Protein structure, α actinin and Calcium.

Mathias Gautel works mostly in the field of Myosin, limiting it down to topics relating to Actin and, in certain cases, Actinin, as a part of the same area of interest. His work carried out in the field of Sarcomere brings together such families of science as Protein filament, Myofibril and Anatomy, Skeletal muscle. As a member of one scientific family, Mathias Gautel mostly works in the field of Obscurin, focusing on Molecular biology and, on occasion, Gene isoform.

He most often published in these fields:

  • Titin (51.56%)
  • Cell biology (33.85%)
  • Biophysics (31.25%)

What were the highlights of his more recent work (between 2013-2021)?

  • Titin (51.56%)
  • Cell biology (33.85%)
  • Biophysics (31.25%)

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

Titin, Cell biology, Biophysics, Sarcomere and Genetics are his primary areas of study. His study in Obscurin and Telethonin is carried out as part of his studies in Titin. His Obscurin research includes elements of Myomesin and Immunoglobulin domain.

His work in Cell biology addresses issues such as Protein kinase domain, which are connected to fields such as Plasma protein binding, Drosophila Protein, DNA-binding protein, Molecular biology and Ankyrin repeat. His Biophysics research includes themes of Cardiac muscle, Calcium, α actinin, Protein filament and Actin. His studies deal with areas such as Anatomy, Skeletal muscle, Pathology, A protein and Myosin as well as Sarcomere.

Between 2013 and 2021, his most popular works were:

  • The sarcomeric cytoskeleton: from molecules to motion. (110 citations)
  • The Structure and Regulation of Human Muscle α-Actinin (109 citations)
  • Recessive TTN truncating mutations define novel forms of core myopathy with heart disease (103 citations)

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

  • Gene
  • Enzyme
  • Amino acid

The scientist’s investigation covers issues in Titin, Cell biology, Myosin, Obscurin and Actin. A large part of his Titin studies is devoted to Telethonin. His Cell biology research is multidisciplinary, incorporating elements of Actinin and Biochemistry.

His Myosin study incorporates themes from Genetically modified mouse, Sarcomere and Mitochondrion. His studies in Obscurin integrate themes in fields like Crystallography, Myomesin and Immunoglobulin domain. His Actin research focuses on Biophysics and how it relates to Protein filament and Sarcomere organization.

Best Publications

  • Guidelines for the use and interpretation of assays for monitoring autophagy

    Daniel J. Klionsky;Fabio C. Abdalla;Hagai Abeliovich;Robert T. Abraham

  • Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM

    Matthias Rief;Mathias Gautel;Filipp Oesterhelt;Julio M. Fernandez

  • Transcriptional mechanisms regulating skeletal muscle differentiation, growth and homeostasis

    Thomas Braun;Mathias Gautel

  • The Kinase Domain of Titin Controls Muscle Gene Expression and Protein Turnover

    Stephan Lange;Fengqing Xiang;Andrey Yakovenko;Anna Vihola

  • Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy.

    Bonne G;Bercovici J;Cruaud C

  • Structural basis for activation of the titin kinase domain during myofibrillogenesis

    O. Mayans;P. F. M. Van Der Ven;M. Wilm;A. Mues

  • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?

    M. Gautel;O. Zuffardi;A. Freiburg;S. Labeit

  • Towards a molecular understanding of titin.

    S. Labeit;M. Gautel;A. Lakey;J. Trinick

  • Mechanoenzymatics of titin kinase

    Elias M. Puchner;Alexander Alexandrovich;Ay Lin Kho;Ulf Hensen

  • Obscurin, a giant sarcomeric Rho guanine nucleotide exchange factor protein involved in sarcomere assembly

    Paul Young;Elisabeth Ehler;Mathias Gautel

  • The spectrin repeat: a structural platform for cytoskeletal protein assemblies.

    Kristina Djinovic-Carugo;Mathias Gautel;Jari Ylänne;Paul Young

  • A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy.

    Alexandra Freiburg;Mathias Gautel

  • Molecular Basis for Cross-Linking of Actin Filaments: Structure of the α-Actinin Rod

    Kristina Djinović-Carugo;Paul Young;Mathias Gautel;Matti Saraste

  • Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of α-actinin

    Paul Young;Charles Ferguson;Sonia Bañuelos;Mathias Gautel

  • Mutations in beta-myosin S2 that cause familial hypertrophic cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin-binding protein-C.

    Mathias Gruen;Mathias Gautel

  • Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin

    Wolfgang M.J. Obermann;Mathias Gautel;Klaus Weber;Dieter O. Fürst;Dieter O. Fürst

  • Myosin Binding Protein C, a Phosphorylation-Dependent Force Regulator in Muscle That Controls the Attachment of Myosin Heads by Its Interaction With Myosin S2

    Gudrun Kunst;Kai R. Kress;Mathias Gruen;Dietmar Uttenweiler

  • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure

    Wolfgang A. Linke;Diane E. Rudy;Thomas Centner;Mathias Gautel

  • A regular pattern of two types of 100-residue motif in the sequence of titin.

    S. Labeit;D. P. Barlow;M. Gautel;T. Gibson

  • Minireview The spectrin repeat: a structural platform for cytoskeletal protein assemblies

    Kristina Djinovic-Carugo;Mathias Gautel;Jari Yla;Paul Young

Frequent Co-Authors

Dieter O. Fürst
Dieter O. Fürst University of Bonn
Matthias Wilmanns
Matthias Wilmanns Universität Hamburg
Hermann E. Gaub
Hermann E. Gaub Ludwig-Maximilians-Universität München
Siegfried Labeit
Siegfried Labeit European Bioinformatics Institute
Caroline Sewry
Caroline Sewry University College London
Francesco Muntoni
Francesco Muntoni University College London
Dmitri I. Svergun
Dmitri I. Svergun European Bioinformatics Institute
Elisabeth Ehler
Elisabeth Ehler King's College London
Klaus Weber
Klaus Weber Max Planck Society
Bjarne Udd
Bjarne Udd University of Helsinki

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