Cited by 186

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone

Liu, Bei, Yang, Yi, Qiu, Zhijuan, Staron, Matthew, Hong, Feng, Li, Yi, Wu, Shuang, Li, Yunfeng, Hao, Bing, Bona, Robert, Han, David, Li, Zihai·2010·Nature Communications

Verifying this paper

8 of 9 steps done · this page updates itself — you can leave and come back

  1. Registry recordVerified
  2. Full textFetching the open-access text — a few minutes for a paper we haven’t read before
  3. Reference listNot fetched yet
  4. Reference checkNot run yet for this paper
  5. StatisticsNeeds the full text
  6. ClaimsNeeds the full text
  7. Cited sourcesNeeds claims to check
  8. Self-checkNeeds the full text
  9. VerificationFindings verified

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 · 10.1038/ncomms1070

Cites

3 of 3 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

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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

Flagged first, then by citations

Research works printed but not linked: 47

  1. Kampinga, H. H. et al. Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones 14, 105–111 (2009). · DOI
  2. Chen, B., Piel, W. H., Gui, L., Bruford, E. & Monteiro, A. The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86, 627–637 (2005). · DOI
  3. Li, Z. & Srivastava, P. K. Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation. EMBO J. 12, 3143–3151 (1993). · DOI
  4. Frey, S., Leskovar, A., Reinstein, J. & Buchner, J. The ATPase cycle of the endoplasmic chaperone Grp94. J. Biol. Chem. 282, 35612–35620 (2007). · DOI
  5. Dollins, D. E., Warren, J. J., Immormino, R. M. & Gewirth, D. T. Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones. Mol. Cell. 28, 41–56 (2007). · DOI
  6. Yang, Y. & Li, Z. Roles of heat shock protein gp96 in the ER quality control: redundant or unique function? Mol. Cells 20, 173–182 (2005). · DOI
  7. Zhao, R. et al. Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone. Cell 120, 715–727 (2005). · DOI · Paper page
  8. Pearl, L. H. & Prodromou, C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271–294 (2006). · DOI · Paper page
  9. Yang, Y. et al. Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages. Immunity 26, 215–226 (2007). · DOI · Paper page
  10. Randow, F. & Seed, B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat. Cell. Biol. 3, 891–896 (2001). · DOI · Paper page
  11. Liu, B. & Li, Z. Endoplasmic reticulum HSP90b1 (gp96, grp94) optimizes B-cell function via chaperoning integrin and TLR but not immunoglobulin. Blood 112, 1223–1230 (2008). · DOI · Paper page
  12. Staron, M. et al. gp96, an endoplasmic reticulum master chaperone for integrins and Toll-like receptors, selectively regulates early T and B lymphopoiesis. Blood 115, 2380–2390 (2010). · DOI · Paper page
  13. Richter, K., Reinstein, J. & Buchner, J. A Grp on the Hsp90 mechanism. Mol. Cell. 28, 177–179 (2007). · DOI
  14. Medzhitov, R. Toll-like receptors and innate immunity. Nat. Rev. Immunol. 1, 135–145 (2001). · DOI · Paper page
  15. Kim, Y. M., Brinkmann, M. M., Paquet, M. E. & Ploegh, H. L. UNC93B1 delivers nucleotide-sensing toll-like receptors to endolysosomes. Nature 452, 234–238 (2008). · DOI · Paper page
  16. Ewald, S. E. et al. The ectodomain of Toll-like receptor 9 is cleaved to generate a functional receptor. Nature 456, 658–662 (2008). · DOI
  17. Park, B. et al. Proteolytic cleavage in an endolysosomal compartment is required for activation of Toll-like receptor 9. Nat. Immunol. 9, 1407–1414 (2008). · DOI
  18. Latz, E. et al. TLR9 signals after translocating from the ER to CpG DNA in the lysosome. Nat. Immunol. 5, 190–198 (2004). · DOI
  19. Haas, T. et al. The DNA sugar backbone 2′ deoxyribose determines toll-like receptor 9 activation. Immunity 28, 315–323 (2008). · DOI
  20. Latz, E. et al. Ligand-induced conformational changes allosterically activate Toll-like receptor 9. Nat. Immunol. 8, 772–779 (2007). · DOI
  21. Matsumoto, M. et al. Subcellular localization of Toll-like receptor 3 in human dendritic cells. J. Immunol. 171, 3154–3162 (2003). · DOI
  22. Yamamoto, M. et al. Role of adaptor TRIF in the MyD88-independent toll-like receptor signaling pathway. Science 301, 640–643 (2003). · DOI
  23. Takahashi, K. et al. A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is required for TLR-dependent immune responses. J. Exp. Med. 204, 2963–2976 (2007). · DOI
  24. Hirate, Y. & Okamoto, H. Canopy1, a novel regulator of FGF signaling around the midbrain-hindbrain boundary in zebrafish. Curr. Biol. 16, 421–427 (2006). · DOI
  25. Ahn, V. E., Faull, K. F., Whitelegge, J. P., Fluharty, A. L. & Prive, G. G. Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proc. Natl Acad. Sci. USA 100, 38–43 (2003). · DOI
  26. Wakabayashi, Y. et al. A protein associated with toll-like receptor 4 (PRAT4A) regulates cell surface expression of TLR4. J. Immunol. 177, 1772–1779 (2006). · DOI
  27. Pichlmair, A. & Reis e Sousa, C. Innate recognition of viruses. Immunity 27, 370–383 (2007). · DOI
  28. Meylan, E. & Tschopp, J. Toll-like receptors and RNA helicases: two parallel ways to trigger antiviral responses. Mol. Cell. 22, 561–569 (2006). · DOI
  29. Kiyokawa, T. et al. A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors. Int. Immunol. 20, 1407–1415 (2008). · DOI
  30. Barton, G. M., Kagan, J. C. & Medzhitov, R. Intracellular localization of Toll-like receptor 9 prevents recognition of self DNA but facilitates access to viral DNA. Nat. Immunol. 7, 49–56 (2006). · DOI
  31. Nishiya, T. & DeFranco, A.L. Ligand-regulated chimeric receptor approach reveals distinctive subcellular localization and signaling properties of the Toll-like receptors. J. Biol. Chem. 279, 19008–19017 (2004). · DOI
  32. Nishiya, T., Kajita, E., Miwa, S. & Defranco, A. L. TLR3 and TLR7 are targeted to the same intracellular compartments by distinct regulatory elements. J. Biol. Chem. 280, 37107–37117 (2005). · DOI
  33. Zheng, H., Dai, J., Stoilova, D. & Li, Z. Cell surface targeting of heat shock protein gp96 induces dendritic cell maturation and antitumor immunity. J. Immunol. 167, 6731–6735 (2001). · DOI
  34. Liu, B. et al. Cell surface expression of an endoplasmic reticulum resident heat shock protein gp96 triggers MyD88-dependent systemic autoimmune diseases. Proc. Natl Acad. Sci. USA 100, 15824–15829 (2003). · DOI
  35. Trombetta, E.S. & Parodi, A.J. Quality control and protein folding in the secretory pathway. Annu. Rev. Cell. Dev. Biol. 19, 649–676 (2003). · DOI
  36. Young, J. C., Moarefi, I. & Hartl, F. U. Hsp90: a specialized but essential protein-folding tool. J. Cell. Biol. 154, 267–273 (2001). · DOI
  37. Krukenberg, K. A., Bottcher, U. M., Southworth, D. R. & Agard, D. A. Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide. Protein Sci. 18, 1815–1827 (2009). · DOI
  38. Ostrovsky, O., Makarewich, C.A., Snapp, E.L. & Argon, Y. An essential role for ATP binding and hydrolysis in the chaperone activity of GRP94 in cells. Proc. Natl Acad Sci. USA 106, 11600–11605 (2009). · DOI
  39. Zhang, W. et al. Biochemical and structural studies of the interaction of Cdc37 with Hsp90. J. Mol. Biol. 340, 891–907 (2004). · DOI
  40. Roe, S. M. et al. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116, 87–98 (2004). · DOI
  41. Barral, J. M., Hutagalung, A. H., Brinker, A., Hartl, F. U. & Epstein, H. F. Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science 295, 669–671 (2002). · DOI
  42. Sun, J. et al. Structural and functional analyses of the human Toll-like receptor 3. Role of glycosylation. J. Biol. Chem. 281, 11144–11151 (2006). · DOI
  43. Meunier, L., Usherwood, Y. K., Chung, K. T. & Hendershot, L. M. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell. 13, 4456–4469 (2002). · DOI
  44. Vandenbroeck, K., Martens, E. & Alloza, I. Multi-chaperone complexes regulate the folding of interferon-gamma in the endoplasmic reticulum. Cytokine 33, 264–273 (2006). · DOI
  45. Sepulveda, F. E. et al. Critical role for asparagine endopeptidase in endocytic Toll-like receptor signaling in dendritic cells. Immunity 31, 737–748 (2009). · DOI
  46. Cyr, J. L. & Heinen, C. D. Hereditary cancer-associated missense mutations in hMSH6 uncouple ATP hydrolysis from DNA mismatch binding. J. Biol. Chem. 283, 31641–31648 (2008). · DOI
  47. Wu, L. et al. Global survey of human T leukemic cells by integrating proteomics and transcriptomics profiling. Mol. Cell. Proteomics 6, 1343–1353 (2007). · DOI

Cited by

Sorted by citations

Metadata

Authors
Liu, B., Yang, Y., Qiu, Z., Staron, M., Hong, F., Li, Y., Wu, S., Li, Y., Hao, B., Bona, R., Han, D., & Li, Z.
Venue
Nature Communications
Published
2010-09-21
Volume
1
Issue
1
ISSN
2041-1723
Cited by
186
References
3
Language
en
Update notices
erratum (2012-01-31)

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