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Manajit Hayer-Hartl

Manajit Hayer-Hartl

D-Index & Metrics

Biology and Biochemistry

D-Index
61
Citations
27735
World Ranking
11093
National Ranking
795

Research.com Recognitions

  • 2018 - German National Academy of Sciences Leopoldina - Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften Biochemistry and Biophysics
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)
  • Member of the European Molecular Biology Organization (EMBO)

Overview

Manajit Hayer-Hartl is affiliated with the Max Planck Society in Germany. Their research primarily focuses on biochemistry, genetics, and molecular biology with a significant emphasis on molecular biology as a subfield. The scientist's work covers key topics such as photosynthetic processes and mechanisms, heat shock proteins research, enzyme structure and function, ATP synthase and ATPases research, protein structure and dynamics, mitochondrial function and pathology, and RNA and protein synthesis mechanisms.

Their frequent publication venues include:

  • Trends in Biochemical Sciences
  • FEBS Letters
  • Cell
  • bioRxiv (Cold Spring Harbor Laboratory)
  • SSRN Electronic Journal

Among recent papers authored or co-authored by Manajit Hayer-Hartl are:

  • "Recent advances in understanding catalysis of protein folding by molecular chaperones," 2020, FEBS Letters
  • "Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein," 2020, Nature Communications
  • "Chaperone Machineries of Rubisco - The Most Abundant Enzyme," 2020, Trends in Biochemical Sciences
  • "Dual Functions of a Rubisco Activase in Metabolic Repair and Recruitment to Carboxysomes," 2020, Cell
  • "Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis," 2021, Nature Structural & Molecular Biology

Frequent co-authors of Manajit Hayer-Hartl include:

  • F. Ulrich Hartl
  • Huping Wang
  • Andreas Bracher
  • David Balchin
  • Mirkko Flecken

In recognition of their contributions to the field, Manajit Hayer-Hartl has received awards such as election to the German National Academy of Sciences Leopoldina in 2018 for achievements in biochemistry and biophysics. They are also a member of the European Molecular Biology Organization (EMBO).

Best Publications

  • 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

  • Molecular Chaperone Functions in Protein Folding and Proteostasis

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

  • Converging concepts of protein folding in vitro and in vivo

    F Ulrich Hartl;Manajit Hayer-Hartl

  • In vivo aspects of protein folding and quality control

    David Balchin;Manajit Hayer-Hartl;F. 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

  • Amyloid-like Aggregates Sequester Numerous Metastable Proteins with Essential Cellular Functions

    Heidi Olzscha;Sonya M. Schermann;Andreas C. Woerner;Stefan Pinkert

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

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

  • Crystal Structure of the Nucleotide Exchange Factor GrpE Bound to the ATPase Domain of the Molecular Chaperone DnaK

    Celia J. Harrison;Celia J. Harrison;Manajit Hayer-Hartl;Manajit Hayer-Hartl;Maurizio Di Liberto;Maurizio Di Liberto;F.-Ulrich Hartl;F.-Ulrich Hartl

  • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington’s disease

    Annie Sittler;Rudi Lurz;Gerhild Lueder;Josef Priller

  • Cellular toxicity of polyglutamine expansion proteins: Mechanism of transcription factor deactivation

    Gregor Schaffar;Peter Breuer;Raina Boteva;Christian Behrends

  • Protein Folding in the Cytoplasm and the Heat Shock Response

    R. M. Vabulas;S. Raychaudhuri;M. Hayer-Hartl;F. U. Hartl

  • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone.

    Sae-Hun Park;Yury Kukushkin;Rajat Gupta;Taotao Chen

  • DnaK functions as a central hub in the E. coli chaperone network

    Giulia Calloni;Taotao Chen;Sonya M. Schermann;Hung-chun Chang

  • The GroEL–GroES Chaperonin Machine: A Nano-Cage for Protein Folding

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

  • Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding

    A. Brinker;G. Pfeifer;M.J. Kerner;D.J. Naylor

  • Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein

    Yun-Chi Tang;Hung-Chun Chang;Annette Roeben;Dirk Wischnewski

  • Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity

    H. Sakahira;P. Breuer;M. K. Hayer-Hartl;F. U. Hartl

  • Function of Trigger Factor and DnaK in Multidomain Protein Folding: Increase in Yield at the Expense of Folding Speed

    Vishwas R. Agashe;Suranjana Guha;Hung Chun Chang;Pierre Genevaux

  • Failure of RQC machinery causes protein aggregation and proteotoxic stress

    Young-Jun Choe;Sae-Hun Park;Timm Hassemer;Roman Körner

Frequent Co-Authors

Andreas Bracher
Andreas Bracher Max Planck Society
F. Ulrich Hartl
F. Ulrich Hartl Max Planck Society
Costa Georgopoulos
Costa Georgopoulos University of Utah
Don C. Lamb
Don C. Lamb Ludwig-Maximilians-Universität München
Frank Weber
Frank Weber HEMAP AG
Matthias Mann
Matthias Mann Max Planck Institute of Biochemistry
John R. Engen
John R. Engen Northeastern University
Erich E. Wanker
Erich E. Wanker Max Delbrück Center for Molecular Medicine
Gian Gaetano Tartaglia
Gian Gaetano Tartaglia Italian Institute of Technology
Hans Lehrach
Hans Lehrach Max Planck Society

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