Chaperone Diagram - Search
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  1. Nature
    https://www.nature.com/articles/s41467-021-22369-9

    The landscape of molecular chaperones across human tissues …

    • The sensitivity of the protein-folding environment to chaperone disruption can be highly tissue-specific. Yet, the organization of the chaperone system across physiological human tissues has received little at… See more

    Introduction

    Chaperones are highly conserved molecular machines that control cellular protein homeostasis (proteostasis). Across species, they promote de novo protein folding and … See more

    Nature
    Results

    Chaperones are ubiquitously and highly expressed across human tissues
    We … See more

    Nature
    Discussion

    Chaperones are basic components of all living organisms, and are thus commonly regarded as house-keeping genes1. But, are all folding environments similar to each other? In a … See more

    Nature
    Methods

    Curation of an integrated list of human chaperones
    We compiled a curated list of 195 known human chaperone, co-chaperone, and folding enz… See more

    Nature
    Code availability

    Data of chaperones analyzed in the study are available as Supplementary Data 1. Data of tissues analyzed in the study appear in Supplementary Data 2. Data of disease-as… See more

    Nature
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    Table of Contents
    Introduction
    Results
    Discussion
    Methods
    Code availability
     

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  2. Studies of Chaperone Diagram
    National Center for Biotechnology Information
    The landscape of molecular chaperones across human tissues reveals a layered architecture of core and variable chaperones
    Chaperones are highly conserved molecular machines that control cellular protein homeostasis (proteostasis). Across species, they promote de novo protein folding and protein maturation1, protein translocation2, protein-complexes assembly and disassembly3, protein disaggregation and refolding4, and p...
    Author: Netta Shemes…
    Published: 2021
    Publication: Nat Com…
    National Center for Biotechnology Information
    Redefining Molecular Chaperones as Chaotropes
    Molecular chaperones are the key instruments of bacterial protein homeostasis. Chaperones not only facilitate folding of client proteins, but also transport them, prevent their aggregation, dissolve aggregates and resolve misfolded states. Despite this seemingly large variety, single chaperones can ...
    Author: Jakub Macoše…
    Published: 2021
    Publication: Front Mol …
    ResearchGate
    Molecular Chaperones: Structure-Function Relationship and their Role in Protein Folding
    During heat shock conditions a plethora of proteins are found to play a role in maintaining cellular homeostasis. They play diverse roles from folding of non-native proteins to the proteasomal degradation of harmful aggregates. A few out of these heat shock proteins (Hsp) help in the folding of non-...
    Published: 2018/05/02
    DOI: 10.1007/978-3-31…
    PubMed
    General Structural and Functional Features of Molecular Chaperones
    Molecular chaperones are a group of structurally diverse and highly conserved ubiquitous proteins. They play crucial roles in facilitating the correct folding of proteins in vivo by preventing protein aggregation or facilitating the appropriate folding and assembly of proteins. Heat shock proteins f...
    Author: Adrienne Lesle…
    Published: 2021
    Keywords: Hsp110; Hs…
    ScienceDirect
    Review Unfolding the role of chaperones and chaperonins in human disease
    Molecular chaperones comprise several highly conserved families of related proteins, many of which are also heat shock proteins. Chaperone proteins are crucial for the maintenance of native protein conformation and recent research has demonstrated several mechanisms where defective chaperone protein...
    Published: 2001/09/01
    Cited By: 0
    Keywords: chaperone …
    National Center for Biotechnology Information
    A History of Molecular Chaperone Structures in the Protein Data Bank
    Thirty years ago a class of proteins was found to prevent the aggregation of Rubisco. These proteins’ ability to prevent unwanted associations led to their being called chaperones. These chaperone proteins also increased in expression as a response to heat shock, hence their label as heat shock prot...
    Author: Neil Andrew D…
    Published: 2019/12
    Publication: Int J Mol …
    National Center for Biotechnology Information
    Visualizing chaperone-assisted protein folding
    Challenges in determining the structures of heterogeneous and dynamic protein complexes have greatly hampered past efforts to obtain a mechanistic understanding of many important biological processes. One such process is chaperone-assisted protein folding, where obtaining structural ensembles of cha...
    Author: Scott Horowitz…
    Published: 2016/07
    DOI: 10.1038/nsmb.3237
     
  3. The New England Journal of Medicine
    https://www.nejm.org/doi/full/10.1056/NEJMra050111

    Sick Chaperones, Cellular Stress, and Disease | NEJM

     
  4. Wikipedia
    https://en.wikipedia.org/wiki/Chaperone_(protein)

    Chaperone (protein) - Wikipedia

  5. National Center for Biotechnology Information
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8042005

    The landscape of molecular chaperones across human tissues …

  6. National Center for Biotechnology Information
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8237284

    Redefining Molecular Chaperones as Chaotropes - PMC

  7. PDB-101
    https://pdb101.rcsb.org/motm/32

    Molecule of the Month: Chaperones - RCSB: PDB-101

    WEBMolecule of the Month: Chaperones. Chaperones help new proteins fold into their proper shape. Protein chaperonin GroEL-GroES. Download high quality TIFF image. As you can see when looking through the many …

  8. Royal Society of Chemistry
    https://books.rsc.org/books/edited-volume/…

    Biophysics of Molecular Chaperones - Royal Society …

    WEBNov 1, 2023 — Molecular chaperones are critical to control protein quality in all living cells. Understanding chaperone function at the atomic level, and in particular its mode of interaction with client proteins, is crucial to …

  9. Cell Press
    https://www.cell.com/trends/genetics/fullte…

    Unfolding the role of chaperones and chaperonins in …

    WEBSep 1, 2001 — A chaperone is a protein that selectively recognizes and binds to the exposed hydrophobic surfaces of a non-native protein in a noncovalent interaction in order to inhibit irreversible aggregation.

  10. Nature
    https://www.nature.com/articles/nature10317

    Molecular chaperones in protein folding and proteostasis

  11. embopress.org
    https://www.embopress.org/doi/full/10.1038/msb.2009.26

    An atlas of chaperone–protein interactions in

  12. Nature
    https://www.nature.com/articles/nrm3658

    Chaperone machines for protein folding, unfolding and …

    WEBSep 12, 2013 — The major chaperone systems of the cell, namely heat shock protein 60 (HSP60), HSP70, HSP90 and HSP100, use the energy of ATP binding and hydrolysis to carry out their actions, which include...

  13. frontiersin.org
    https://www.frontiersin.org/journals/molecular...

    Redefining Molecular Chaperones as Chaotropes - Frontiers

  14. Springer
    https://link.springer.com/chapter/10.1007/978-3-030-78397-6_2

    General Structural and Functional Features of Molecular …

  15. ResearchGate
    https://www.researchgate.net/publication/…

    (PDF) Molecular Chaperones: Structure-Function …

    WEBMay 2, 2018 — An overview of the conformational cycle of HSP90: Several co-chaperones and ATP mediate the transition between the early, intermediate and late stages of substrate-bound HSP90 (Copyright...

  16. Science | AAAS
    https://www.science.org/doi/10.1126/science.1068408

    Molecular Chaperones in the Cytosol: from Nascent Chain to …

  17. Springer
    https://link.springer.com/chapter/10.1007/978-94-007-4667-1_2

    Chaperones: General Characteristics and Classifications

  18. PubMed
    https://pubmed.ncbi.nlm.nih.gov/34569020

    General Structural and Functional Features of Molecular …

  19. iBiology
    https://www.ibiology.org/cell-biology/chaperone

    Chaperone-assisted protein folding I: Chaperonins - iBiology

  20. National Center for Biotechnology Information
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940948

    A History of Molecular Chaperone Structures in the Protein Data …

  21. ScienceDirect
    https://www.sciencedirect.com/science/article/pii/S0168952501024131

    Unfolding the role of chaperones and chaperonins in human disease

  22. Pearson
    https://www.pearson.com/.../chaperone-proteins

    Biochemistry - Online Tutor, Practice Problems & Exam Prep

  23. nih.gov
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2568879

    Molecular chaperones and photoreceptor function - PMC

  24. National Center for Biotechnology Information
    https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2776907

    Q&A: What are pharmacological chaperones and why are they …