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Cited by 538

The DOI matches its Crossref record; 269 of the 269 references it cites were found in a registry or an index.

α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network

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Narberhaus, Franz·2002·Microbiology and Molecular Biology Reviews

Abstract

SUMMARY: α-Crystallins were originally recognized as proteins contributing to the transparency of the mammalian eye lens. Subsequently, they have been found in many, but not all, members of the Archaea, Bacteria, and Eucarya. Most members of the diverse α-crystallin family have four common structural and functional features: (i) a small monomeric molecular mass between 12 and 43 kDa; (ii) the formation of large oligomeric complexes; (iii) the presence of a moderately conserved central region, the so-called α-crystallin domain; and (iv) molecular chaperone activity. Since α-crystallins are induced by a temperature upshift in many organisms, they are often referred to as small heat shock proteins (sHsps) or, more accurately, α-Hsps. α-Crystallins are integrated into a highly flexible and synergistic multichaperone network evolved to secure protein quality control in the cell. Their chaperone activity is limited to the binding of unfolding intermediates in order to protect them from irreversible aggregation. Productive release and refolding of captured proteins into the native state requires close cooperation with other cellular chaperones. In addition, α-Hsps seem to play an important role in membrane stabilization. The review compiles information on the abundance, sequence conservation, regulation, structure, and function of α-Hsps with an emphasis on the microbial members of this chaperone family.

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Metadata

Authors
Narberhaus, F.
Venue
Microbiology and Molecular Biology Reviews
Published
2002-03
Volume
66
Issue
1
Pages
64-93
ISSN
  • 1092-2172 (ISSN-L)
  • 1098-5557
OpenAlex
W2164060511
Cited by
538
References
269
FWCI
2.06
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network. https://app.cochat.ai/papers/10.1128/mmbr.66.1.64-93.2002
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Narberhaus, F. (2002). α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone Network. Microbiology and Molecular Biology Reviews. https://doi.org/10.1128/mmbr.66.1.64-93.2002

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.