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F. Ulrich Hartl

F. Ulrich Hartl

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Biology and Biochemistry
Germany
2026

D-Index & Metrics

Biology and Biochemistry

D-Index
139
Citations
84965
World Ranking
281
National Ranking
20

Research.com Recognitions

  • 2026 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2025 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2023 - Research.com Biology and Biochemistry in Germany Leader Award
  • 2011 - Member of the National Academy of Sciences
  • 2009 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 2000 - Fellow of the American Academy of Arts and Sciences

Overview

F. Ulrich Hartl is affiliated with the Max Planck Society in Germany and has contributed extensively to the fields of Biochemistry, Genetics, and Molecular Biology, with a particular focus on Molecular Biology. Their research covers several subfields including Materials Chemistry, Neurology, Cell Biology, and Cellular and Molecular Neuroscience.

The topics central to their work include heat shock proteins research, protein structure and dynamics, mitochondrial function and pathology, enzyme structure and function, endoplasmic reticulum stress and disease, genetic neurodegenerative diseases, and prion diseases and protein misfolding.

Their recent publications include:

  • Recent advances in understanding catalysis of protein folding by molecular chaperones (2020), published in FEBS Letters
  • Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein (2020), published in Nature Communications
  • High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2 (2020), published in Biochemical and Biophysical Research Communications
  • In situ architecture of neuronal α-Synuclein inclusions (2021), published in Nature Communications
  • The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends (2021), published in Nature Communications

Frequent co-authors in their research work include:

  • Mark S. Hipp
  • Andreas Bracher
  • Victoria A. Trinkaus
  • Manajit Hayer-Hartl
  • Patricia Yuste-Checa

They have published extensively in several scientific venues, with the most frequent publication outlets being:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Nature Communications
  • Molecular Cell
  • SSRN Electronic Journal
  • Nature Structural & Molecular Biology

F. Ulrich Hartl has received several recognitions during their career, including:

  • Member of the National Academy of Sciences (2011)
  • Fellow of the American Association for the Advancement of Science (AAAS) (2009)
  • Fellow of the American Academy of Arts and Sciences (2000)

Best Publications

  • Molecular chaperones in cellular protein folding.

    Hartl Fu

  • Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein

    F. Ulrich Hartl;Manajit Hayer-Hartl

  • Molecular chaperones in protein folding and proteostasis

    F. Ulrich Hartl;Andreas Bracher;Manajit Hayer-Hartl

  • Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent

    C E Stebbins;A A Russo;C Schneider;N Rosen

  • Molecular Chaperone Functions in Protein Folding and Proteostasis

    Yujin E. Kim;Mark S. Hipp;Andreas Bracher;Manajit Hayer-Hartl

  • Structure of TPR Domain–Peptide Complexes: Critical Elements in the Assembly of the Hsp70–Hsp90 Multichaperone Machine

    Clemens Scheufler;Achim Brinker;Gleb Bourenkov;Stefano Pegoraro

  • Converging concepts of protein folding in vitro and in vivo

    F Ulrich Hartl;Manajit Hayer-Hartl

  • Pathways of chaperone-mediated protein folding in the cytosol

    Jason C. Young;Vishwas R. Agashe;Katja Siegers;F. Ulrich Hartl

  • In vivo aspects of protein folding and quality control

    David Balchin;Manajit Hayer-Hartl;F. Ulrich Hartl

  • Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria.

    Ming Yuan Cheng;Franz-Ulrich Hartl;Jörg Martin;Robert A. Pollock

  • The proteostasis network and its decline in ageing.

    Mark S. Hipp;Prasad Kasturi;F. Ulrich Hartl

  • Hsp90: a specialized but essential protein-folding tool

    Jason C. Young;Ismail Moarefi;F. Ulrich Hartl

  • Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

    J Martin;T Langer;R Boteva;A Schramel

  • Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

    Jason C. Young;Nicholas J. Hoogenraad;F.Ulrich Hartl

  • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis.

    Joachim Ostermann;Arthur Horwich;Walter Neupert;Franz-Ulrich Hartl

  • Hsp70 and Hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils

    Paul J. Muchowski;Gregor Schaffar;Annie Sittler;Erich E. Wanker

  • The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.

    Franz-Ulrich Hartl;Stewart Lecker;Elmar Schiebel;Joseph P. Hendrick

  • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

    H. Schröder;T. Langer;F.U. Hartl;B. Bukau

  • Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

    Michael J. Kerner;Dean J. Naylor;Yasushi Ishihama;Tobias Maier

  • MOLECULAR CHAPERONES IN CELLULAR PROTEIN FOLDING

    Jörg Martin;F.‐Ulrich Hartl

Frequent Co-Authors

Manajit Hayer-Hartl
Manajit Hayer-Hartl Max Planck Society
Andreas Bracher
Andreas Bracher Max Planck Society
Matthias Mann
Matthias Mann Max Planck Institute of Biochemistry
Wolfgang Baumeister
Wolfgang Baumeister Max Planck Society
Konstanze F. Winklhofer
Konstanze F. Winklhofer Ruhr University Bochum
Jörg Tatzelt
Jörg Tatzelt Ruhr University Bochum
Walter Neupert
Walter Neupert Max Planck Institute of Biochemistry
Costa Georgopoulos
Costa Georgopoulos University of Utah
Hans A. Kretzschmar
Hans A. Kretzschmar Ludwig-Maximilians-Universität München
Alan N. Houghton
Alan N. Houghton Memorial Sloan Kettering Cancer Center

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