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David B. Williams - Publications

Affiliations: 
University of Toronto University of Toronto, Toronto, ON, Canada 
Area:
Protein chaperones in the ER, MHC processing, calnexin
Website:
http://biochem17.med.utoronto.ca/~david_williams/lab/Home.html
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53 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2018 Rapp CL, Li J, Badior KE, Williams DB, Casey JR, Reithmeier RAF. Role of N-glycosylation in the expression of human SLC26A2 and A3 anion transport membrane glycoproteins. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. PMID 30462520 DOI: 10.1139/Bcb-2018-0139  0.348
2016 Lum R, Ahmad S, Hong SJ, Chapman DC, Kozlov G, Williams DB. Contributions of the lectin and polypeptide-binding sites of calreticulin to its chaperone functions in vitro and in cells. The Journal of Biological Chemistry. PMID 27413183 DOI: 10.1074/Jbc.M116.746321  0.411
2016 Stocki P, Sawicki M, Mays CE, Hong SJ, Chapman DC, Westaway D, Williams DB. Inhibition of the FKBP family of peptidyl prolyl isomerases induces abortive translocation and degradation of the cellular prion protein. Molecular Biology of the Cell. PMID 26764098 DOI: 10.1091/Mbc.E15-10-0729  0.327
2015 Chapman DC, Stocki P, Williams DB. Cyclophilin C Participates in the US2-Mediated Degradation of Major Histocompatibility Complex Class I Molecules. Plos One. 10: e0145458. PMID 26691022 DOI: 10.1371/Journal.Pone.0145458  0.356
2015 Gold L, Williams D, Groenendyk J, Michalak M, Eggleton P. Unfolding the complexities of ER chaperones in health and disease: report on the 11th international calreticulin workshop. Cell Stress & Chaperones. 20: 875-83. PMID 26395641 DOI: 10.1007/S12192-015-0638-4  0.367
2014 Stocki P, Chapman DC, Beach LA, Williams DB. Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis. The Journal of Biological Chemistry. 289: 23086-96. PMID 24990953 DOI: 10.1074/Jbc.M114.570911  0.436
2012 Rutkevich LA, Williams DB. Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum. Molecular Biology of the Cell. 23: 2017-27. PMID 22496424 DOI: 10.1091/Mbc.E12-02-0102  0.73
2011 Rutkevich LA, Williams DB. Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum. Current Opinion in Cell Biology. 23: 157-66. PMID 21094034 DOI: 10.1016/J.Ceb.2010.10.011  0.741
2010 Rutkevich LA, Cohen-Doyle MF, Brockmeier U, Williams DB. Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Molecular Biology of the Cell. 21: 3093-105. PMID 20660153 DOI: 10.1091/Mbc.E10-04-0356  0.74
2010 Chapman DC, Williams DB. ER quality control in the biogenesis of MHC class I molecules. Seminars in Cell & Developmental Biology. 21: 512-9. PMID 20044014 DOI: 10.1016/J.Semcdb.2009.12.013  0.366
2009 Watts JC, Huo H, Bai Y, Ehsani S, Jeon AH, Won AH, Shi T, Daude N, Lau A, Young R, Xu L, Carlson GA, Williams D, Westaway D, Schmitt-Ulms G. Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones. Plos Pathogens. 5: e1000608. PMID 19798432 DOI: 10.1371/Journal.Ppat.1000608  0.393
2009 Donaldson JG, Williams DB. Intracellular assembly and trafficking of MHC class I molecules. Traffic (Copenhagen, Denmark). 10: 1745-52. PMID 19761542 DOI: 10.1111/J.1600-0854.2009.00979.X  0.345
2009 Patterson ST, Li J, Kang JA, Wickrema A, Williams DB, Reithmeier RA. Loss of specific chaperones involved in membrane glycoprotein biosynthesis during the maturation of human erythroid progenitor cells. The Journal of Biological Chemistry. 284: 14547-57. PMID 19258325 DOI: 10.1074/Jbc.M809076200  0.312
2008 Ireland BS, Brockmeier U, Howe CM, Elliott T, Williams DB. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules. Molecular Biology of the Cell. 19: 2413-23. PMID 18337472 DOI: 10.1091/Mbc.E07-10-1055  0.442
2006 Ireland BS, Niggemann M, Williams DB. In vitro assays of the functions of calnexin and calreticulin, lectin chaperones of the endoplasmic reticulum. Methods in Molecular Biology (Clifton, N.J.). 347: 331-42. PMID 17072021 DOI: 10.1385/1-59745-167-3:331  0.451
2006 Zhang Y, Williams DB. Assembly of MHC class I molecules within the endoplasmic reticulum. Immunologic Research. 35: 151-62. PMID 17003517 DOI: 10.1385/Ir:35:1:151  0.375
2006 Williams DB. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. Journal of Cell Science. 119: 615-23. PMID 16467570 DOI: 10.1242/Jcs.02856  0.434
2005 Thomson SP, Williams DB. Delineation of the lectin site of the molecular chaperone calreticulin. Cell Stress & Chaperones. 10: 242-51. PMID 16184769 DOI: 10.1379/Csc-126.1  0.402
2005 Paquet ME, Leach MR, Williams DB. In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control. Methods (San Diego, Calif.). 35: 338-47. PMID 15804605 DOI: 10.1016/J.Ymeth.2004.10.005  0.784
2004 Paquet ME, Cohen-Doyle M, Shore GC, Williams DB. Bap29/31 influences the intracellular traffic of MHC class I molecules. Journal of Immunology (Baltimore, Md. : 1950). 172: 7548-55. PMID 15187134 DOI: 10.4049/Jimmunol.172.12.7548  0.591
2004 Leach MR, Williams DB. Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation. The Journal of Biological Chemistry. 279: 9072-9. PMID 14699098 DOI: 10.1074/Jbc.M310788200  0.709
2002 Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. The Journal of Biological Chemistry. 277: 29686-97. PMID 12052826 DOI: 10.1074/jbc.M202405200  0.68
2002 Cherif S, Leach MR, Williams DB, Monneret C. Synthesis of a molecular mimic of the Glc1Man9 oligoside as potential inhibitor of calnexin binding to DeltaF508 CFTR protein. Bioorganic & Medicinal Chemistry Letters. 12: 1237-40. PMID 11965361 DOI: 10.1016/S0960-894X(02)00151-8  0.72
2002 Paquet ME, Williams DB. Mutant MHC class I molecules define interactions between components of the peptide-loading complex. International Immunology. 14: 347-58. PMID 11934871 DOI: 10.1093/Intimm/14.4.347  0.593
2001 Stronge VS, Saito Y, Ihara Y, Williams DB. Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates. The Journal of Biological Chemistry. 276: 39779-87. PMID 11514579 DOI: 10.1074/Jbc.M107091200  0.453
2001 Danilczyk UG, Williams DB. The Lectin Chaperone Calnexin Utilizes Polypeptide-based Interactions to Associate with Many of Its Substrates in Vivo Journal of Biological Chemistry. 276: 25532-25540. PMID 11337494 DOI: 10.1074/Jbc.M100270200  0.444
2000 Danilczyk UG, Cohen-Doyle MF, Williams DB. Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin Journal of Biological Chemistry. 275: 13089-13097. PMID 10777614 DOI: 10.1074/Jbc.275.17.13089  0.462
2000 Leach M, Williams D. Mapping of the lectin, ERp57-binding and chaperone sites of calnexin and calreticulin Biochemical Society Transactions. 28: A463-A463. DOI: 10.1042/Bst028A463  0.648
2000 Paquet M, Williams DB. Interactions between components of the MHC I peptide loading complex Biochemical Society Transactions. 28: A447-A447. DOI: 10.1042/Bst028A447B  0.526
1999 Saito Y, Ihara Y, Leach MR, Cohen-Doyle MF, Williams DB. Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. The Embo Journal. 18: 6718-29. PMID 10581245 DOI: 10.1093/Emboj/18.23.6718  0.733
1999 Ihara Y, Cohen-Doyle MF, Saito Y, Williams DB. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Molecular Cell. 4: 331-41. PMID 10518214 DOI: 10.1016/S1097-2765(00)80335-4  0.467
1998 Vassilakos A, Michalak M, Lehrman MA, Williams DB. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin Biochemistry. 37: 3480-3490. PMID 9521669 DOI: 10.1021/Bi972465G  0.368
1996 Kim JH, Lingwood CA, Williams DB, Furuya W, Manolson MF, Grinstein S. Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor Journal of Cell Biology. 134: 1387-1399. PMID 8830769 DOI: 10.1083/Jcb.134.6.1387  0.5
1996 Suh WK, Mitchell EK, Yang Y, Peterson PA, Waneck GL, Williams DB. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains Journal of Experimental Medicine. 184: 337-348. PMID 8760787 DOI: 10.1084/Jem.184.2.337  0.348
1996 Vassilakos A, Cohen-Doyle MF, Peterson PA, Jackson MR, Williams DB. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules Embo Journal. 15: 1495-1506. PMID 8612572 DOI: 10.1002/J.1460-2075.1996.Tb00493.X  0.393
1996 Williams DB, Vassilakos A, Suh WK. Peptide presentation by MHC class I molecules Trends in Cell Biology. 6: 267-273. DOI: 10.1016/0962-8924(96)10020-9  0.313
1995 Ware FE, Vassilakos A, Peterson PA, Jackson MR, Lehrman MA, Williams DB. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. The Journal of Biological Chemistry. 270: 4697-704. PMID 7876241 DOI: 10.1074/Jbc.270.9.4697  0.414
1995 Williams DB, Watts TH. Molecular chaperones in antigen presentation Current Opinion in Immunology. 7: 77-84. PMID 7772285 DOI: 10.1016/0952-7915(95)80032-8  0.414
1995 Williams DB. The Merck Frosst Award Lecture 1994/La conference Merck Frosst 1994. Calnexin: a molecular chaperone with a taste for carbohydrate Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 73: 123-132. PMID 7576485 DOI: 10.1139/O95-015  0.497
1995 Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing Cell. 83: 129-135. PMID 7553864 DOI: 10.1016/0092-8674(95)90241-4  0.405
1995 Williams DB. Calnexin leads glycoproteins into the fold Glycoconjugate Journal. 12: iii-iv. PMID 7496128 DOI: 10.1007/Bf00731315  0.344
1994 Jackson MR, Cohen-Doyle MF, Peterson PA, Williams DB. Regulation of MHC Class I transport by the molecular chaperone, calnexin (p88, IP90) Science. 263: 384-387. PMID 8278813 DOI: 10.1126/Science.8278813  0.318
1994 Bergeron JJ, Brenner MB, Thomas DY, Williams DB. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends in Biochemical Sciences. 19: 124-8. PMID 8203019 DOI: 10.1016/0968-0004(94)90205-4  0.408
1994 Suh WK, Cohen-Doyle MF, Fruh K, Wang K, Peterson PA, Williams DB. Interaction of MHC class I molecules with the transporter associated with antigen processing Science. 264: 1322-1326. PMID 8191286 DOI: 10.1126/Science.8191286  0.327
1992 Degen E, Cohen-Doyle MF, Williams DB. Efficient dissociation of the p88 chaperone from major histocompatibility complex class I molecules requires both β2-microglobulin and peptide Journal of Experimental Medicine. 175: 1653-1661. PMID 1588286 DOI: 10.1084/Jem.175.6.1653  0.333
1991 Christinck ER, Luscher MA, Barber BH, Williams DB. Peptide binding to class I MHC on living cells and quantitation of complexes required for CTL lysis Nature. 352: 67-70. PMID 2062379 DOI: 10.1038/352067A0  0.317
1991 Degen E, Williams DB. Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules Journal of Cell Biology. 112: 1099-1115. PMID 1999467 DOI: 10.1083/Jcb.112.6.1099  0.397
1991 Nguyen TH, Law DTS, Williams DB. Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae Proceedings of the National Academy of Sciences of the United States of America. 88: 1565-1569. PMID 1996357 DOI: 10.1073/Pnas.88.4.1565  0.459
1990 Nicholson RC, Williams DB, Moran LA. An essential member of the HSP70 gene family of Saccharomyces cerevisiae is homologous to immunoglobulin heavy chain binding protein Proceedings of the National Academy of Sciences of the United States of America. 87: 1159-1163. PMID 2105497 DOI: 10.1073/Pnas.87.3.1159  0.353
1989 Degen E, Laferte S, Elliott BE, Williams DB. Different Class I antigen oligosaccharides on a murine tumor and a lectin-resistant variant are not responsible for the differential recognition of the tumors by CTL International Journal of Cancer. 43: 828-836. PMID 2497074 DOI: 10.1002/Ijc.2910430515  0.305
1985 Williams DB, Swiedler SJ, Hart GW. Intracellular transport of membrane glycoproteins: two closely related histocompatibility antigens differ in their rates of transit to the cell surface. The Journal of Cell Biology. 101: 725-34. PMID 3928633 DOI: 10.1083/Jcb.101.3.725  0.509
1984 Williams DB, Lennarz WJ. Control of asparagine-linked oligosaccharide chain processing: studies on bovine pancreatic ribonuclease B. An in vitro system for the processing of exogenous glycoproteins. The Journal of Biological Chemistry. 259: 5105-14. PMID 6425284  0.618
1982 Schachter H, Williams D. Biosynthesis of mucus glycoproteins. Advances in Experimental Medicine and Biology. 144: 3-28. PMID 7044062 DOI: 10.1007/978-1-4615-9254-9_1  0.301
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