World's Best Scientists 2026 revealed!
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Best Scientists
2025
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Biology and Biochemistry
Germany
2026

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Best Scientists

D-Index
189
Citations
134543
World Ranking
443
National Ranking
14

Biology and Biochemistry

D-Index
188
Citations
134536
World Ranking
53
National Ranking
2

Research.com Recognitions

  • 2026 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2025 - Research.com Best Scientists Award
  • 2025 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2023 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2022 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2021 - OSA Fellows Robert Huber Universität zu Lübeck, Germany For outstanding contributions to the development of tunable lasers and imaging techniques, especially Fourier domain mode locking
  • 2003 - Member of the European Academy of Sciences
  • 1999 - Fellow of the Royal Society, United Kingdom
  • 1995 - Member of the National Academy of Sciences
  • 1994 - Fellow, The World Academy of Sciences
  • 1990 - Member of Academia Europaea
  • 1988 - Nobel Prize for the determination of the three-dimensional structure of a photosynthetic reaction centre
  • Member of the European Academy of Sciences and Arts
  • Member of the European Academy of Sciences and Arts
  • Member of the European Academy of Sciences and Arts
  • Member of the European Academy of Sciences and Arts

Overview

Robert Huber is affiliated with the University of Duisburg-Essen in Germany and specializes in research within the fields of Biochemistry, Genetics and Molecular Biology, as well as Medicine. Their work spans subfields including Molecular Biology, Oncology, Organic Chemistry, Materials Chemistry, and Biomedical Engineering.

The primary topics covered in Robert Huber's research include Peptidase Inhibition and Analysis, Chemical Synthesis and Analysis, Genetics and Neurodevelopmental Disorders, Neuropeptides and Animal Physiology, Carbon dioxide utilization in catalysis, Chemical Synthesis and Reactions, and Enzyme Structure and Function.

Their recent papers comprise:

  • A precisely positioned MED12 activation helix stimulates CDK8 kinase activity (2020, Proceedings of the National Academy of Sciences)
  • Activation by substoichiometric inhibition (2020, Proceedings of the National Academy of Sciences)
  • Structural basis for the regulation of nucleosome recognition and HDAC activity by histone deacetylase assemblies (2021, Science Advances)
  • Dipeptidyl peptidase 9 triggers BRCA2 degradation and promotes DNA damage repair (2022, EMBO Reports)
  • Chemoproteomics-Enabled Identification of 4-Oxo-β-Lactams as Inhibitors of Dipeptidyl Peptidases 8 and 9 (2022, Angewandte Chemie International Edition)

Frequent co-authors working alongside Robert Huber include Markus Kaiser, Ruth Geiss-Friedlander, B. Ross, Oguz Bolgi, and Lorenz Fehr.

They have published multiple articles in several scientific venues, notably:

  • Proceedings of the National Academy of Sciences
  • Angewandte Chemie International Edition
  • European Journal of Organic Chemistry
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Angewandte Chemie

Robert Huber's distinctions include:

  • Nobel Prize (1988) for the determination of the three-dimensional structure of a photosynthetic reaction centre
  • Member of Academia Europaea (1990)
  • Fellow, The World Academy of Sciences (1994)
  • Member of the National Academy of Sciences (1995)
  • Fellow of the Royal Society, United Kingdom (1999)
  • Member of the European Academy of Sciences (2003)
  • OSA Fellow (2021) for contributions to tunable lasers and imaging techniques, especially Fourier domain mode locking
  • Member of the European Academy of Sciences and Arts

Best Publications

  • Structure of the protein subunits in the photosynthetic reaction centre of Rhodopseudomonas viridis at 3Å resolution

    Johann Deisenhofer;Otto Epp;Kunio Miki;Robert Huber

  • Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement

    Richard A. Engh;Robert Huber

  • Structure of 20S proteasome from yeast at 2.4 A resolution.

    Michael Groll;Lars Ditzel;Jan Löwe;Daniela Stock

  • X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis

    Johann Deisenhofer;Otto Epp;Kunio Miki;Robert Huber

  • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.

    Jan Löwe;Daniela Stock;Bing Jap;Peter Zwickl

  • Natural protein proteinase inhibitors and their interaction with proteinases

    Wolfram Bode;Robert Huber

  • The complete genome of the hyperthermophilic bacterium Aquifex aeolicus

    Gerard Deckert;Patrick V. Warren;Terry Gaasterland;William G. Young

  • Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins.

    Huber R;Carrell Rw

  • The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment.

    W Bode;I Mayr;U Baumann;R Huber

  • Human α1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function

    Hartmut Loebermann;Ryoji Tokuoka;Johann Deisenhofer;Robert Huber

  • Thermotoga maritima sp. nov. represents a new genus of unique extremely thermophilic eubacteria growing up to 90°C

    Robert Huber;Thomas A. Langworthy;Helmut König;Michael Thomm

  • A gated channel into the proteasome core particle.

    Michael Groll;Monica Bajorek;Alwin Köhler;Luis Moroder

  • The structure of a complex of recombinant hirudin and human alpha-thrombin

    Timothy J. Rydel;K. G. Ravichandran;A. Tulinsky;Wolfram Bode

  • Structural basis of the activation and action of trypsin

    Robert Huber;Wolfram Bode

  • Handbook of metalloproteins

    Albrecht Messerschmidt;R. Huber;Thomas Poulos;Karl Wieghardt

  • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex.

    Peter Sondermann;Robert Huber;Vaughan Oosthuizen;Vaughan Oosthuizen;Uwe Jacob

  • Proteasome from Thermoplasma acidophilum: A threonine protease

    Erika Seemüller;Andrei Lupas;Daniela Stock;Jan Löwe

  • Organic anion-transporting polypeptide B (OATP-B) and its functional comparison with three other OATPs of human liver

    Gerd A. Kullak-Ublick;Manfred G. Ismair;Bruno Stieger;Lukas Landmann

  • The Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors

    M. Marquart;J. Walter;J. Deisenhofer;W. Bode

  • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases.

    W. Bode;R. Engh;D. Musil;U. Thiele

Frequent Co-Authors

Wolfram Bode
Wolfram Bode Max Planck Society
Michael Groll
Michael Groll Technical University of Munich
Karl O. Stetter
Karl O. Stetter University of Regensburg
Richard A. Engh
Richard A. Engh University of Tromsø - The Arctic University of Norway
Luis Moroder
Luis Moroder Max Planck Society
Albrecht Messerschmidt
Albrecht Messerschmidt Max Planck Society
Tim Clausen
Tim Clausen Research Institute of Molecular Pathology
Adelbert Bacher
Adelbert Bacher Technical University of Munich
Hans Brandstetter
Hans Brandstetter University of Salzburg
Maria João Romão
Maria João Romão Universidade Nova de Lisboa

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