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October 1, 1990Proceedings of the National Academy of SciencesOpen Access

Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.

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Authors

TLThomas LübbenLeibniz-Institut für Werkstofforientierte Technologien - IWTAGA.A. GatenbyUniversity of YorkGDGail K. DonaldsonXenon Pharmaceuticals (Canada)

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Lübben et al. (1990) studied this question.

synapsesocial.com/papers/6a7d413bab1caed3bf749b5ahttps://doi.org/10.1073/pnas.87.19.7683
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Also Consider

Synapse has enriched 2 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Function of the Maize Mitochondrial Chaperonin hsp60: Specific Association between hsp60 and Newly Synthesized F1-ATPase Alpha Subunits1990 · 17 citations
  2. 2Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent1990 · 383 citations