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From chaperone +‎ -ome (suffix indicating the complete whole of a class of substances for a species or an individual), coined by American biochemist Xiaodong Wang and his collaborators in a November 2006 article in Cell: see the quotation.



chaperome (plural chaperomes)

  1. (biochemistry) All the proteins called chaperones that assist in the folding of misfolded proteins in an organism, and other functions. [from 2006]
    • 2006 November 17, Xiaodong Wang [et al.], “Hsp90 Cochaperone Aha1 Downregulation Rescues Misfolding of CFTR in Cystic Fibrosis”, in Cell[1], volume 127, number 4, Cambridge, Mass.: Cell Press, DOI:10.1016/j.cell.2006.09.043, ISSN 0092-8674, OCLC 960911191, archived from the original on 29 August 2020, page 813, column 1:
      The availability of chaperones and cochaperones for folding of cargo will be sensitive to the globalcellular pool that we now define as the chaperome, a general term to define the unique steady-state composition of chaperones and their regulators in a given cell type. It is well established that the chaperome can be altered by multiple signaling pathways to accommodate cellular stress and misfolding load.
    • 2011, Andreas Wyttenbach; Shmma Quraishe; Joanne Bailey; Vincent O’Connor, “Molecular Chaperones in the Mammalian Brain: Regional Distribution, Cellular Compartmentalization and Synaptic Interactions”, in Andreas Wyttenbach and Vincent O’Connor, editors, Folding for the Synapse, New York, N.Y.; Dordrecht: Springer, DOI:10.1007/978-1-4419-7061-9, →ISBN, part III (Chaperone Modalities and Homeostatic Mechanisms in the Synaptic Compartment), page 124:
      To date data exist to describe the organ-specific distribution and function of many chaperones, but less is known about their cell-type specificity and how this changes in response to different stressors. A systems view on the entire "chaperome" would be essential to understand chaperone function under basal and stress conditions.
    • 2020, Swathi Merugu [et al.], “Chemical Probes and Methods for Single-cell Detection and Quantification of Epichaperones in Hematologic Malignancies”, in David M. Chenoweth, editor, Chemical Tools for Imaging, Manipulating, and Tracking Biological Systems: Diverse Methods for Optical Imaging and Conjugation (Methods in Enzymology; 639), Cambridge, Mass.; San Diego, Calif.: Academic Press, →ISBN, ISSN 0076-6879, section 2.4 (Epichaperome Probes), page 294:
      The nature of the epichaperome, therefore, which presents as stable, multi-partner complexes affected by strong interactions as opposed to other cellular forms of chaperomes present in dynamic complexes of weak interactions, provide opportunities for its detection through small molecules [...].
    • 2020, Kun Wang; Yu Shang; Fei Dou, “Brain Aging: Hsp90 and Neurodegenerative Diseases”, in Zhao Wang, editor, Aging and Aging-related Diseases: Mechanisms and Interventions (Advances in Experimental Medicine and Biology; 1086), Singapore: Springer Nature Singapore, DOI:10.1007/978-981-13-1117-8, →ISBN, ISSN 0065-2598, page 96:
      In another study, Brehme et al. have examined the chaperome in C. elegans and human. They find that chaperome expression is dramatically affected in human brain aging. At the same time, chaperome dynamics are associated with aging and neurodegenerative diseases.
    • 2020, Pengrong Yan; Tai Wang; Monica L. Guzman; Radu I. Peter; Gabriela Chiosis, “Chaperome Networks – Redundancy and Implications for Cancer Treatment”, in Marc Laurence Mendillo, David Pincus, and Ruth Scherz-Shouval, editors, HSF1 and Molecular Chaperones in Biology and Cancer (Advances in Experimental Medicine and Biology; 1243), Cham, Switzerland: Springer Nature, DOI:10.1007/978-3-030-40204-4, →ISBN, ISSN 0065-2598, part II (Function), section 6.3 (Chaperome Network Redundancy), page 90, column 2:
      Redundancy in the chaperome networks is evidenced in a number of large-scale investigations where individual chaperomes were either genetically deleted or pharmacologically inhibited.

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