Student or educator? Sign up with your school email and get 6 months of Pro free.
CoChat
Sign Up
Cited by 229

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23.

Open access
Johnson, J.L., Toft, D.O.·1994·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)31487-4
Open this paper in CoChat — free account

Abstract

In the absence of hormone, the avian progesterone receptor exists in a large multiprotein complex that is inactive but able to bind and respond to progestins. This inactive complex can be reconstituted in vitro by incubation of receptor monomer in rabbit reticulocyte lysate in the presence of ATP and magnesium. This results in receptor binding to the two heat shock proteins, hsp90 and hsp70, the FK506 binding-proteins, FKBP54 and FKBP52, the cyclosporin A-binding protein, cyclophilin-40, and the recently characterized protein p23. Immune isolation of p23 from rabbit reticulocyte lysate in the absence of receptor reveals an ATP-dependent complex containing the major proteins associated with steroid receptors. Depletion of p23 from lysate prevents the assembly of progesterone receptor complexes, and the addition of purified p23 restores this activity, indicating that the p23 protein complex is an essential precursor to the formation of progesterone receptor complexes.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/s0021-9258(17)31487-4

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 6 references

Research works printed but not linked: 44

  1. Smith, 1993, J. Biol. Chem., 268, 18365, 10.1016/S0021-9258(17)46853-0 · DOI
  2. Smith, 1993, J. Biol. Chem., 268, 24270, 10.1016/S0021-9258(20)80520-1 · DOI
  3. Peattie, 1992, Proc. Natl. Acad. Sci. U. S. A., 89, 10974, 10.1073/pnas.89.22.10974 · DOI · Paper page
  4. Tai, 1992, Science, 256, 1315, 10.1126/science.1376003 · DOI · Paper page
  5. Lebeau, 1992, J. Biol. Chem., 267, 4281, 10.1016/S0021-9258(18)42827-X · DOI · Paper page
  6. Kieffer, 1992, J. Biol. Chem., 267, 5503, 10.1016/S0021-9258(18)42795-0 · DOI
  7. Kieffer, 1993, J. Biol. Chem., 268, 12303, 10.1016/S0021-9258(18)31389-9 · DOI
  8. Ratajczak, 1993, J. Biol. Chem., 268, 13187, 10.1016/S0021-9258(19)38636-3 · DOI · Paper page
  9. Kunz, 1993, Trends Biochem. Sci., 18, 334, 10.1016/0968-0004(93)90069-Y · DOI · Paper page
  10. Smith, 1992, J. Biol. Chem., 267, 1350, 10.1016/S0021-9258(18)48438-4 · DOI · Paper page
  11. Johnson, 1994, Mol. Cell. Biol., 14, 1956
  12. Sullivan, 1986, Endocrinology, 119, 1549, 10.1210/endo-119-4-1549 · DOI · Paper page
  13. Smith, 1993, Mol. Cell. Biol., 13, 869
  14. Riehl, 1985, Biochemistry, 24, 6586, 10.1021/bi00344a042 · DOI · Paper page
  15. Sullivan, 1985, Biochemistry, 24, 4214, 10.1021/bi00336a060 · DOI
  16. Laemrali, 1970, Nature, 227, 680, 10.1038/227680a0 · DOI · Paper page
  17. O'Farrell, 1975, J. Biol. Chem., 250, 4007, 10.1016/S0021-9258(19)41496-8 · DOI · Paper page
  18. Kost, 1989, Mol. Cell. Biol., 9, 3829
  19. Sanchez, 1990, Biochemistry, 29, 5145, 10.1021/bi00473a021 · DOI · Paper page
  20. Ruff, 1992, J. Biol. Chem., 267, 21285, 10.1016/S0021-9258(19)36603-7 · DOI
  21. Perdew, 1991, J. Biol. Chem., 266, 6708, 10.1016/S0021-9258(20)89556-8 · DOI · Paper page
  22. Renoir, 1990, J. Biol. Chem., 265, 10740, 10.1016/S0021-9258(18)87009-0 · DOI · Paper page
  23. Nadeau, 1993, J. Biol. Chem., 268, 1479, 10.1016/S0021-9258(18)54100-4 · DOI · Paper page
  24. Czar, 1994, J. Biol. Chem., 269, 11155, 10.1016/S0021-9258(19)78104-6 · DOI
  25. Hendrick, 1993, Annu. Rev. Biochem., 62, 349, 10.1146/annurev.bi.62.070193.002025 · DOI · Paper page
  26. Csermely, 1991, J. Biol. Chem., 266, 4943, 10.1016/S0021-9258(19)67740-9 · DOI
  27. Nygard, 1991, J. Biol. Chem., 266, 16425, 10.1016/S0021-9258(18)55316-3 · DOI
  28. Nadeau, 1992, Prot. Sci., 1, 970, 10.1002/pro.5560010802 · DOI
  29. Wiech, 1992, Nature, 358, 169, 10.1038/358169a0 · DOI · Paper page
  30. Shaknovich, 1992, Mol. Cell. Biol., 12, 5059
  31. Alnemri, 1993, Proc. Natl. Acad. Sci. U. S. A., 90, 6839, 10.1073/pnas.90.14.6839 · DOI
  32. Bihan, 1993, Biochem. Biophys. Res. Commun., 195, 600, 10.1006/bbrc.1993.2088 · DOI
  33. Whitelaw, 1991, J. Biol. Chem., 266, 16436, 10.1016/S0021-9258(18)55318-7 · DOI
  34. Hutchison, 1993, Biochemistry, 32, 3953, 10.1021/bi00066a015 · DOI
  35. Bresnick, 1989, J. Biol. Chem., 264, 4992, 10.1016/S0021-9258(18)83689-4 · DOI · Paper page
  36. Scherrer, 1990, J. Biol. Chem., 265, 21397, 10.1016/S0021-9258(18)45746-8 · DOI · Paper page
  37. Hutchinson, 1994, J. Biol. Chem., 269, 5043, 10.1016/S0021-9258(17)37651-2 · DOI · Paper page
  38. Smith, 1993, Mol. Endocrinol., 7, 1418
  39. Tai, 1993, Biochemistry, 32, 8842, 10.1021/bi00085a015 · DOI
  40. Miyata, 1992, J. Biol. Chem., 267, 7042, 10.1016/S0021-9258(19)50533-6 · DOI · Paper page
  41. Matts, 1989, J. Biol. Chem., 264, 15542, 10.1016/S0021-9258(19)84864-0 · DOI
  42. Rose, 1989, J. Biol. Chem., 264, 6239, 10.1016/S0021-9258(18)83339-7 · DOI
  43. Brugge, 1986, Curr. Topics Microbiol. Immunol., 123, 1
  44. Stancato, 1993, J. Biol. Chem., 268, 21711, 10.1016/S0021-9258(20)80600-0 · DOI · Paper page

Cited by

See all 229

Metadata

Authors
Johnson, J. L., & Toft, D. O.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-10
Volume
269
Issue
40
Pages
24989-24993
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(17)31487-4
OpenAlex
W116814209
Cited by
229
References
6
FWCI
5.27
Type
journal article
Language
en
Open access
hybrid
Licence

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. https://app.cochat.ai/papers/10.1016/s0021-9258(17)31487-4
The paper
Johnson, J. L., & Toft, D. O. (1994). A novel chaperone complex for steroid receptors involving heat shock proteins, immunophilins, and p23. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)31487-4

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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.