Binding of immunophilins to the 90 kDa heat shock protein (hsp90) via a tetratricopeptide repeat domain is a conserved protein interaction in plants.

No abstract is available for this paper.

• Publication year

  1996

• Venue

  Biochemistry

• Publication date

  1996-12-03

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1021/BI9615349PMID 8952474
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Interaction of the progesterone receptor with binding proteins for FK506 and cyclosporin A.

  1995cited by this paper
• The Cyclosporin A-binding Immunophilin CyP-40 and the FK506-binding Immunophilin hsp56 Bind to a Common Site on hsp90 and Exist in Independent Cytosolic Heterocomplexes with the Untransformed Glucocorticoid Receptor (*)

  1995cited by this paper
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  1995cited by this paper
• Evidence that the FK506-binding immunophilin heat shock protein 56 is required for trafficking of the glucocorticoid receptor from the cytoplasm to the nucleus.

  1995cited by this paper
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  1995cited by this paper
• Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes

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  1994cited by this paper
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  1994cited by this paper
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• Proof that hsp70 is required for assembly of the glucocorticoid receptor into a heterocomplex with hsp90.

  1994cited by this paper
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  1994cited by this paper
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  1990cited by this paper
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