David B Williams

Summary

Affiliation: University of Toronto
Country: Canada

Publications

  1. ncbi request reprint Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation
    Michael R Leach
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 279:9072-9. 2004
  2. pmc Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    Lori A Rutkevich
    Department of Biochemistry, University of Toronto, Toronto, Canada
    Mol Biol Cell 21:3093-105. 2010
  3. ncbi request reprint Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    David B Williams
    Department of Biochemistry and Immunology, University of Toronto, Toronto, Ontario, Canada, M5S 1A8
    J Cell Sci 119:615-23. 2006
  4. pmc Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
    Breanna S Ireland
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    Mol Biol Cell 19:2413-23. 2008
  5. pmc Structural and functional relationships between the lectin and arm domains of calreticulin
    Cosmin L Pocanschi
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 286:27266-77. 2011
  6. pmc ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity
    Yinan Zhang
    Departments of Biochemistry and Immunology, University of Toronto, Toronto M5S 1A8, Canada
    J Biol Chem 284:10160-73. 2009
  7. pmc Delineation of the lectin site of the molecular chaperone calreticulin
    Sten P Thomson
    Department of Biochemistry, Medical Sciences Building, University of Toronto, Toronto, ON, Canada
    Cell Stress Chaperones 10:242-51. 2005
  8. ncbi request reprint Assembly of MHC class I molecules within the endoplasmic reticulum
    Yinan Zhang
    Departments of Biochemistry and Immunology, University of Toronto Toronto, Ontario, Canada
    Immunol Res 35:151-62. 2006
  9. ncbi request reprint Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    Michael R Leach
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 277:29686-97. 2002
  10. ncbi request reprint Bap29/31 influences the intracellular traffic of MHC class I molecules
    Marie Eve Paquet
    Department of Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Immunol 172:7548-55. 2004

Collaborators

  • Guennadi Kozlov
  • Kalle Gehring
  • Tim Elliott
  • Jing Li
  • Gordon C Shore
  • Biling Wang
  • R A Reithmeier
  • Lori A Rutkevich
  • Yinan Zhang
  • Ulf Brockmeier
  • Achim Brockmeier
  • Breanna S Ireland
  • Marie Eve Paquet
  • Michael R Leach
  • Cosmin L Pocanschi
  • Daniel C Chapman
  • Sian T Patterson
  • Myrna F Cohen-Doyle
  • Sten P Thomson
  • Slim Cherif
  • Jeong Ah Kang
  • Amittha Wickrema
  • Pekka Maattanen
  • Chris Howe
  • Christopher M Howe
  • Monika Niggemann
  • Ehtesham Baig
  • Myrna Cohen-Doyle
  • Claude Monneret
  • David Y Thomas

Detail Information

Publications22

  1. ncbi request reprint Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation
    Michael R Leach
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 279:9072-9. 2004
    ..Thus, at least for class I molecules, the lectin site of calnexin is dispensable for some of its chaperone functions...
  2. pmc Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins
    Lori A Rutkevich
    Department of Biochemistry, University of Toronto, Toronto, Canada
    Mol Biol Cell 21:3093-105. 2010
    ..In contrast, depletion of ERp72 or P5, either alone or in combination with PDI or ERp57 had minimal impact, revealing a narrow substrate specificity for ERp72 and no detectable role for P5 in oxidative protein folding...
  3. ncbi request reprint Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum
    David B Williams
    Department of Biochemistry and Immunology, University of Toronto, Toronto, Ontario, Canada, M5S 1A8
    J Cell Sci 119:615-23. 2006
    ..Furthermore, there is clear evidence that ERp57 participates in glycoprotein biogenesis either alone or in tandem with calnexin and calreticulin...
  4. pmc Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules
    Breanna S Ireland
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    Mol Biol Cell 19:2413-23. 2008
    ....
  5. pmc Structural and functional relationships between the lectin and arm domains of calreticulin
    Cosmin L Pocanschi
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 286:27266-77. 2011
    ..Furthermore, a hydrophobic patch was detected on the arm domain that mediates crystal packing and may contribute to calreticulin chaperone function...
  6. pmc ERp57 does not require interactions with calnexin and calreticulin to promote assembly of class I histocompatibility molecules, and it enhances peptide loading independently of its redox activity
    Yinan Zhang
    Departments of Biochemistry and Immunology, University of Toronto, Toronto M5S 1A8, Canada
    J Biol Chem 284:10160-73. 2009
    ..Thus, ERp57 appears to play a structural rather than catalytic role within the peptide loading complex...
  7. pmc Delineation of the lectin site of the molecular chaperone calreticulin
    Sten P Thomson
    Department of Biochemistry, Medical Sciences Building, University of Toronto, Toronto, ON, Canada
    Cell Stress Chaperones 10:242-51. 2005
    ..This provides the first direct demonstration of the importance of CRT's lectin site in suppressing the aggregation of nonnative glycoproteins...
  8. ncbi request reprint Assembly of MHC class I molecules within the endoplasmic reticulum
    Yinan Zhang
    Departments of Biochemistry and Immunology, University of Toronto Toronto, Ontario, Canada
    Immunol Res 35:151-62. 2006
    ..This review describes our contributions to elucidating the functions of these proteins; the combined effort of many dedicated students and postdoctoral fellows...
  9. ncbi request reprint Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    Michael R Leach
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 277:29686-97. 2002
    ..These findings are integrated into a model that describes the interaction of glycoprotein folding intermediates with calnexin and calreticulin...
  10. ncbi request reprint Bap29/31 influences the intracellular traffic of MHC class I molecules
    Marie Eve Paquet
    Department of Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Immunol 172:7548-55. 2004
    ..Our results are consistent with the view that class I molecules are largely recruited to ER exit sites by Bap29/31, and that Bap29/31 is a cargo receptor for MHC class I molecules...
  11. doi request reprint Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function
    Achim Brockmeier
    Department of Biochemistry and Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 284:3433-44. 2009
    ....
  12. ncbi request reprint Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    Yinan Zhang
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 281:14622-31. 2006
    ..Interestingly, depletion of another thiol oxidoreductase, ERp72, had no detectable effect on class I biogenesis, consistent with a specialized role for ERp57 in this process...
  13. pmc Loss of specific chaperones involved in membrane glycoprotein biosynthesis during the maturation of human erythroid progenitor cells
    Sian T Patterson
    Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    J Biol Chem 284:14547-57. 2009
    ..These results demonstrate that CNX and ERp57 are not required for major glycoprotein biosynthesis during red cell development, in contrast to their role in glycoprotein folding and quality control in other cells...
  14. ncbi request reprint In vitro assays of the functions of calnexin and calreticulin, lectin chaperones of the endoplasmic reticulum
    Breanna S Ireland
    Department of Immunology, University Toronto, Toronto, Ontario, Canada
    Methods Mol Biol 347:331-42. 2006
    ..Furthermore, details are provided of assays that detect ERp57 binding by calnexin and calreticulin, as well as the abilities of these chaperones to suppress the aggregation of non-native protein substrates...
  15. pmc Structural basis of carbohydrate recognition by calreticulin
    Guennadi Kozlov
    Department of Biochemistry, Groupe de recherche axé sur la structure des protéines, McGill University, Montreal, Quebec H3G 0B1, Canada
    J Biol Chem 285:38612-20. 2010
    ..Finally, the structure rationalizes previous mutagenesis of CRT and lays a structural groundwork for future studies of the role of CNX/CRT in diverse biological pathways...
  16. ncbi request reprint In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control
    Marie Eve Paquet
    Department of Biochemistry, University of Toronto, Toronto, Canada M5S 1A8
    Methods 35:338-47. 2005
    ..These systems have been valuable in assessing folding and quality control events in vivo that are influenced by CNX or CRT as well as in characterizing the spectrum of substrates that are recognized by these chaperones...
  17. doi request reprint ER quality control in the biogenesis of MHC class I molecules
    Daniel C Chapman
    Department of Immunology, University of Toronto, Toronto, Ontario, M5S 1A8, Canada
    Semin Cell Dev Biol 21:512-9. 2010
    ..In this review we discuss these processes as well as a number of strategies that viruses have evolved to subvert normal class I assembly within the ER and thereby evade immune recognition by cytotoxic T cells...
  18. doi request reprint Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum
    Lori A Rutkevich
    Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8
    Curr Opin Cell Biol 23:157-66. 2011
    ..We highlight issues related to function and substrate specificity as well as the functional interplay between the two systems...
  19. ncbi request reprint Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum
    Achim Brockmeier
    Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8
    Biochemistry 45:12906-16. 2006
    ..These findings demonstrate that calnexin is a potent molecular chaperone that is capable of suppressing the aggregation of substrates through polypeptide-based interactions under conditions that exist within the ER lumen...
  20. pmc Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum
    Lori A Rutkevich
    Department of Biochemistry, University of Toronto, Toronto, ON, Canada
    Mol Biol Cell 23:2017-27. 2012
    ..In contrast, no involvement of QSOX1 in ER oxidative processes could be detected. These findings establish VKOR as a significant contributor to disulfide bond formation within the ER...
  21. ncbi request reprint Mutant MHC class I molecules define interactions between components of the peptide-loading complex
    Marie Eve Paquet
    Department of Immunology, University of Toronto, Toronto, Ontario M5S 1A8, Canada
    Int Immunol 14:347-58. 2002
    ....
  22. ncbi request reprint Synthesis of a molecular mimic of the Glc1Man9 oligoside as potential inhibitor of calnexin binding to DeltaF508 CFTR protein
    Slim Cherif
    UMR 176 CNRS Institut Curie, Section de Recherche, 26 Rue d Ulm, 75248 Cedex 05, Paris, France
    Bioorg Med Chem Lett 12:1237-40. 2002
    ..Ability of this mimic to inhibit the binding of the natural Glc1Man9GlcNAc oligoside to calnexin has been measured...