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Collect. Czech. Chem. Commun. 1999, 64, 717-725

Chaperone-Like Activity of Human Haptoglobin: Similarity with α-Crystallin

Zdeněk Pavlíček* and Rüdiger Ettrich

Department of Physical and Macromolecular Chemistry, Charles University, 128 40 Prague 2, Czech Republic

Crossref Cited-by Linking

  • Geraghty Nicholas J., Satapathy Sandeep, Wilson Mark R.: The Emerging Roles of Extracellular Chaperones in Complement Regulation. Cells 2022, 11, 3907. <>
  • Naryzny S. N., Legina O. K.: Haptoglobin as a Biomarker. Biochem. Moscow Suppl. Ser. B 2021, 15, 184. <>
  • Naryzhny S.N., Legina O.K.: Haptoglobin as a biomarker. BIOMED KHIM 2021, 67, 105. <>
  • Wyatt Amy R., Yerbury Justin J., Ecroyd Heath, Wilson Mark R.: Extracellular Chaperones and Proteostasis. Annu. Rev. Biochem. 2013, 82, 295. <>
  • Wyatt Amy R., Yerbury Justin J., Dabbs Rebecca A., Wilson Mark R.: Roles of Extracellular Chaperones in Amyloidosis. Journal of Molecular Biology 2012, 421, 499. <>
  • Yerbury Justin J., Kumita Janet R., Meehan Sarah, Dobson Christopher M., Wilson Mark R.: α2-Macroglobulin and Haptoglobin Suppress Amyloid Formation by Interacting with Prefibrillar Protein Species. Journal of Biological Chemistry 2009, 284, 4246. <>
  • Wilson Mark R., Yerbury Justin J., Poon Stephen: Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity. Mol. BioSyst. 2008, 4, 42. <>
  • Ettrich R., Brandt W., Kopecký V., Baumruk V., Hofbauerová K., Pavlícek Z.: Study of Chaperone-Like Activity of Human Haptoglobin: Conformational Changes under Heat Shock Conditions and Localization of Interaction Sites. Biological Chemistry 2002, 383. <>