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Pierre Goloubinoff

Pierre Goloubinoff

D-Index & Metrics

Biology and Biochemistry

D-Index
63
Citations
17487
World Ranking
10073
National Ranking
176

Overview

Pierre Goloubinoff is affiliated with the University of Lausanne in Switzerland. The primary field of their research spans Biochemistry, Genetics and Molecular Biology, with a focus on Molecular Biology, Plant Science, Cell Biology, Materials Chemistry, and Immunology.

The topics that their work covers include:

  • Heat shock proteins research
  • Protein Structure and Dynamics
  • Endoplasmic Reticulum Stress and Disease
  • Enzyme Structure and Function
  • Toxin Mechanisms and Immunotoxins
  • Photosynthetic Processes and Mechanisms
  • Plant Stress Responses and Tolerance

Recent publications authored or co-authored by Pierre Goloubinoff include:

  • How do plants feel the heat and survive?, 2022, Trends in Biochemical Sciences
  • On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life, 2021, Proceedings of the National Academy of Sciences
  • Quantitative proteomic analysis to capture the role of heat-accumulated proteins in moss plant acquired thermotolerance, 2020, Plant Cell & Environment
  • A fluorescent multi-domain protein reveals the unfolding mechanism of Hsp70, 2022, Nature Chemical Biology
  • Repair or Degrade: the Thermodynamic Dilemma of Cellular Protein Quality-Control, 2021, Frontiers in Molecular Biosciences

The scientist frequently publishes in the following venues:

  • bioRxiv (Cold Spring Harbor Laboratory)
  • Cell Stress and Chaperones
  • Trends in Biochemical Sciences
  • Nature Chemical Biology
  • Frontiers in Molecular Biosciences

Frequent co-authors collaborating with Pierre Goloubinoff include:

  • Mathieu E. Rebeaud
  • Bruno Fauvet
  • Paolo De Los Rios
  • Satyam Tiwari
  • Anthony Guihur

Best Publications

  • How do plants feel the heat

    Ron Mittler;Andrija Finka;Pierre Goloubinoff

  • GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli.

    Pierre Goloubinoff;Anthony A. Gatenby;George H. Lorimer

  • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP

    Pierre Goloubinoff;John T. Christeller;Anthony A. Gatenby;George H. Lorimer

  • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

    Pierre Goloubinoff;Axel Mogk;Anat Peres Ben Zvi;Toshifumi Tomoyasu

  • Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB

    Axel Mogk;Toshifumi Tomoyasu;Pierre Goloubinoff;Stefan Rüdiger

  • Chemical Chaperones Regulate Molecular Chaperones in Vitro and in Cells under Combined Salt and Heat Stresses

    Sophia Diamant;Noa Eliahu;David Rosenthal;Pierre Goloubinoff;Pierre Goloubinoff

  • Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent.

    Paul V. Viitanen;Thomas H. Lubben;Janet Reed;Pierre Goloubinoff

  • The Small Heat-shock Protein IbpB from Escherichia coli Stabilizes Stress-denatured Proteins for Subsequent Refolding by a Multichaperone Network*

    Lea Veinger;Sophia Diamant;Johannes Buchner;Pierre Goloubinoff

  • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol.

    Toshifumi Tomoyasu;Axel Mogk;Hanno Langen;Pierre Goloubinoff

  • The Heat Shock Response in Moss Plants Is Regulated by Specific Calcium-Permeable Channels in the Plasma Membrane

    Younousse Saidi;Younousse Saidi;Andrija Finka;Maude Muriset;Zohar Bromberg

  • Plasma Membrane Cyclic Nucleotide Gated Calcium Channels Control Land Plant Thermal Sensing and Acquired Thermotolerance

    Andrija Finka;America Farinia Henriquez Cuendet;Frans J.M. Maathuis;Younousse Saidi;Younousse Saidi

  • Review: Mechanisms of Disaggregation and Refolding of Stable Protein Aggregates by Molecular Chaperones

    Anat Peres Ben-Zvi;Pierre Goloubinoff

  • Synechocystis HSP17 is an amphitropic protein that stabilizes heat-stressed membranes and binds denatured proteins for subsequent chaperone-mediated refolding.

    Zsolt Török;Pierre Goloubinoff;Ibolya Horváth;Nelly M. Tsvetkova

  • Molecular and biochemical mechanisms associated with dormancy and drought tolerance in the desert legume Retama raetam

    Lilach Pnueli;Elza Hallak-Herr;Mira Rozenberg;Mira Cohen

  • Heat perception and signalling in plants: a tortuous path to thermotolerance.

    Younousse Saidi;Andrija Finka;Pierre Goloubinoff

  • Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling

    Paolo De Los Rios;Anat Ben-Zvi;Olga Slutsky;Abdussalam Azem

  • Size-dependent Disaggregation of Stable Protein Aggregates by the DnaK Chaperone Machinery

    Sophia Diamant;Anat Peres Ben-Zvi;Bernd Bukau;Pierre A Goloubinoff

  • Heavy metal ions are potent inhibitors of protein folding

    Sandeep K. Sharma;Pierre Goloubinoff;Philipp Christen

  • The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase

    Sandeep K Sharma;Paolo De Los Rios;Philipp Christen;Ariel Lustig

  • Evidence for a lipochaperonin: Association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions

    Zsolt Török;Ibolya Horváth;Pierre Goloubinoff;Eszter Kovács

Frequent Co-Authors

László Vígh
László Vígh Hungarian Academy of Sciences
Philipp Christen
Philipp Christen University of Zurich
Marvin Edelman
Marvin Edelman Weizmann Institute of Science
George H. Lorimer
George H. Lorimer University of Maryland, College Park
Bernd Bukau
Bernd Bukau Heidelberg University
Yoram Weiss
Yoram Weiss Tel Aviv University
Elizabeth Vierling
Elizabeth Vierling University of Massachusetts Amherst
Dan S. Tawfik
Dan S. Tawfik Weizmann Institute of Science
Ron Mittler
Ron Mittler University of Missouri
Axel Mogk
Axel Mogk Heidelberg University

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