{"id":89,"date":"2024-02-06T20:49:36","date_gmt":"2024-02-06T20:49:36","guid":{"rendered":"https:\/\/sites.biochem.umass.edu\/hebertlab\/?page_id=89"},"modified":"2025-05-21T15:31:52","modified_gmt":"2025-05-21T15:31:52","slug":"publications","status":"publish","type":"page","link":"https:\/\/sites.biochem.umass.edu\/hebertlab\/publications\/","title":{"rendered":""},"content":{"rendered":"\n<p class=\"has-large-font-size\"><strong>Publications<\/strong><\/p>\n\n\n\n<pre class=\"wp-block-preformatted has-black-color has-very-light-gray-to-cyan-bluish-gray-gradient-background has-text-color has-background has-link-color has-small-font-size wp-elements-01c8a7941e57276b266191a70cef6bbd\" style=\"font-style:normal;font-weight:400;text-decoration:none\">99. <a href=\"https:\/\/www.nature.com\/articles\/s41580-025-00855-y\">Kevin P. Guay, Wen-Chuan Chou, Nathan P. Canniff, Kylie B. Paul &amp; Daniel N. Hebert <br>N-glycan-dependent protein maturation and quality control in the ER.  Nature Reviews Molecular Cell Biology (2025)<\/a><br><br>98. <a href=\"https:\/\/www.cell.com\/ajhg\/fulltext\/S0002-9297(25)00139-9\">Zain Dardas, Laura Harrold, Daniel G. Calame1,Claire G. Salter, Takashi Kikuma, Kevin P. Guay, Bobby G. Ng,Kanae Sano, Ahmad K. Saad1, Haowei Du, Riccardo Sangermano, Sohil G. Patankar, Shalini N. Jhangiani,Semra G\u00fcrsoy, Mohamed S. Abdel-Hamid,Mahmoud K.H. Ahmed, Reza Maroofian, Rauan Kaiyrzhanov, Kamran Salayev, Wendy D. Jones, Ana P\u00e9rez Caballero, Lucy McGavin, Michael Spiller, Miranda Durkie, Nick Wood,Lauren O\u2019Grady, Paula Goldenberg,Ann M. Neumeye, Amber Begtrup,Sherif F. Abdel-Ghafar, Maha S. Zaki, Hilde Van Esch, Jennifer E. Posey, Olivia K. Wenger, Ethan M. Scott, Kinga M. Bujakowska, Richard A. Gibbs, Davut Pehlivan,Dana Marafi1,Joseph S. Leslie, Nishanka Ubeyratna,Jacob Day, Martina Owens, Jessica Settle,Soher Balkhy, Abdullah Tamim, Lama Alabdi, Fowzan S. Alkuraya, Yoichi Takeda, Hudson H. Freeze, Daniel N. Hebert, James R. Lupski1, Andrew H.  Emma L. Baple<br>Bi-allelic UGGT1 variants cause a congenital disorder of glycosylation. AJHG. 2025 April 3;112(4)<\/a><br><br>97. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC11348098\/\">Williams RV, Guay KP, Hurlbut Lesk OA, Clerico EM, Hebert DN, Gierasch LM.<br>Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15. Proc Natl Acad Sci U S A. 2024 Aug 20; 121(34): e2315009121<\/a><br><br>96.<a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/tra.12927\"> Tax, G., K. P. Guay, L. Pantalone, M. Ceci, T. Sold\u00e0, C. J. Hitchman, J. C. Hill, S. Vasiljevi\u0107,<br>A. Lia, C. P. Modenutti, K. R. Straatman, A. Santino, M. Molinari, N. Zitzmann, D. N. Hebert, P. Roversi and M. Trerotola (2024),<br>Rescue of secretion of rare-disease associated misfolded mutant glycoproteins in UGGT1 knock-out<br>mammalian cells. Traffic Jan;25(1):e12927.\u00a0doi: 10.1111\/tra.12927.<\/a><br><br>95. <a href=\"\/\/www.jbc.org\/action\/showPdf?pii=S0021-9258%2823%2902478-X\">Canniff, N.P., J.B. Graham, K.P. Guay, D.A. Lubicki, S.J. Eyles, J.N. Rauch and D.N. Hebert (2023)<br>TTC17 is an endoplasmic reticulum resident TPR- containing adaptor protein, J. Biol. Chem.<br>299(12)105450<\/a><br><br>94. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S109727652300922X\">Guay, K.P., H. Ke, N.P. Canniff, G.T. George, S.J. Eyles, M. Mariappan, J.N. Contessa, A. Gershenson, L.M. Gierasch and D.N. Hebert (2023) ER chaperones use a protein folding and quality control glyco-code,<br>Molecular Cell 83(4524-4537)<\/a><br><br>93. <a href=\"https:\/\/www.cell.com\/iscience\/fulltext\/S2589-0042(23)01996-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS258900422301996X%3Fshowall%3Dtrue\">Guay, K.P., R. Ibba, J.L. Kiappes, S. Vasiljevic, F. Boni, M. De Benedictis, I. Zeni, J.D. Le Cornu, M. Hensen, A.V. Chandran, A.L. Kantsadi, A.T. Caputo, J.I. Blanco Capurro, Y. Bayo, J.C. Hill, K. Hudson, A. Lia, J. Brun, C.P. Modenutti, S.G. Withers, M. Marti, E. Biasini, A. Santino, M. De Rosa, M. Milani, D.N. Hebert, N. Zitzmann and P. Roversi (2023)<br>A quinoline-8-ol sub-millimolar inhibitor of UGGT, the ER glycoprotein folding quality control<br>checkpoint, iScience, 26(10):107919<br><\/a><br>92. <a href=\"https:\/\/link.springer.com\/protocol\/10.1007\/978-1-0716-3605-3_14\">Guay, K.P., H. Ke, L. M. Gierasch, A. Gershenson and D.N. Hebert (2023) Monitoring the <br>secretion and activity of alpha-1 antitrypsin in various mammalian cell types. Methods Mol<br>Biol.143-163<\/a><br><br>91. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/B978012821618700016X?via%3Dihub\">Canniff, N. P., K.P. Guay, and D.N. Hebert (2023) Carbohydrates Direct the Maturation and<br>Trafficking of Glycoproteins in the Secretory Pathway. In: Bradshaw Ralph A., Hart Gerald<br>W. and Stahl Philip D. (eds.) Encyclopedia of Cell Biology, Second Edition, vol. 4, pp. 320-<br>330. Oxford: Elsevier.<\/a><br><br>90. <a href=\"https:\/\/www.embopress.org\/doi\/full\/10.15252\/embj.2022113003#accessDenialLayout\">Guay, K.P., R.V. Williams and D.N. Hebert (2022) Calnexin reveals a sugar-free taste within<br>the lipid bilayer. EMBO J. 41(24):e113003. doi: 10.15252\/embj.2022113003. Epub 2022<br>Nov 15. PMID: 36377534<br><\/a><br>89. <a href=\"https:\/\/www.pnas.org\/doi\/10.1073\/pnas.2206103119?url_ver=Z39.88-2003&amp;rfr_id=ori%3Arid%3Acrossref.org&amp;rfr_dat=cr_pub++0pubmed\">Ke, H., K.P. Guay, T. R. Flotte, L. M. Gierasch, A. Gershenson and D.N. Hebert (2022)<br>Secretion of functional a1-antitrypsin is cell type dependent: implications for intramuscular<br>delivery for gene therapy. Proc. Natl. Acad. Sci. USA 119(31):e2206103119.<br>PMID: 35901208<\/a><br><br>88. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC9185992\/pdf\/nihms-1810492.pdf\">Adams, B. M., N. P. Canniff, K. P. Guay and D. N. Hebert (2021) The role of ER chaperones<br>in protein folding and quality control. Progress in Molecular and Subcellular Biology:<br>Cellular Biology of the Endoplasmic Reticulum Editor Marek Michalak and Louis Agellon.<br>Springer Nature PMID: 34050861<br><\/a><br>87. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7771966\/pdf\/elife-63997.pdf\">Adams, B. M., N. P. Canniff, K. P. Guay, I.S.B. Larsen and D. N. Hebert (2020) Quantitative<br>glycoproteomics reveals substrate selectivity of the ER quality control sensors UGGT1 and<br>UGGT2. eLife e63997. PMID: 33320095 PMCID: PMC7771966<\/a><br><br>86. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7082142\/pdf\/mSphere.00187-20.pdf\">Daniels, R. and D. N. Hebert (2020) In support of simian polyomavirus 40 VP4 as a latter<br>expressed viroporin. mSphere. 5(2) e00187-20. PMID: 32188752<\/a><br><br>85. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7001481\/pdf\/mbc-31-167.pdf\">Graham, J. B., J. C. Sunryd, K. Mathavan, E, Weir, I.S.B. Larsen, A. Halim, H. Clausen, H.<br>Cousin, D. Alfandari, D. N. Hebert (2020) Endoplasmic reticulum transmembrane protein<br>TMTC3 contributes to O-mannosylation of E-cadherin, cellular adherence, and embryonic<br>gastrulation. Molecular Biology of the Cell 31(3):167-183. PMID: 31851597<\/a><br><br>84. <a href=\"\/\/www.jbc.org\/action\/showPdf?pii=S0021-9258%2820%2930816-4\">Adams, B. M., H. Ke, L. M. Gierasch. A. Gershenson and D. N. Hebert (2019) Proper<br>secretion of the serpin antithrombin relies strictly on thiol-dependent quality control, J. Biol.<br>Chem. 294(50):18992-19011. PMID: 31662433<br><\/a><br>83. <a href=\"https:\/\/www.tandfonline.com\/doi\/full\/10.1080\/10409238.2019.1590305?scroll=top&amp;needAccess=true\">Graham, J. B., N. P. Canniff and D. N. Hebert (2019) TPR containing proteins control protein<br>organization and homeostasis in the endoplasmic reticulum. Critical Reviews in Molecular<br>and Cellular Biology 54(2):103-118.<br><\/a><br>82. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC6589386\/pdf\/nihms-1527440.pdf\">Adams, B. M., M. E. Oster and D. N. Hebert (2019) Protein quality control in the<br>endoplasmic reticulum. The Protein Journal 38(3):317-329. PMC6589386<\/a><br><br>81. <a href=\"https:\/\/www.jbc.org\/article\/S0021-9258(20)30947-9\/fulltext\">Lamriben, L., Oster ME, Tamura T, Tian W, Yang Z, Clausen H, and D. N. Hebert (2018)<br>EDEM1's mannosidase-like domain binds ERAD client proteins in a redox-sensitive manner<br>and possesses catalytic activity. J. Biol. Chem. 293(36):13932-13945.<br><\/a><br>80. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2817%2931011-0\">Lamriben, L. and D. N. Hebert (2018) Activating and repressing IRE1 alpha: The Hsp47 and BiP<br>Tug of War, Mol. Cell 69(2):159-160.<br><\/a><br>79. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5906034\/pdf\/nihms956498.pdf\">Krishnan, B., L. Hedstrom, D. N. Hebert, L. M. Gierasch and A. Gershenson, (2018)<br>Expression and purification of active recombinant human Alpha-1 Antitrypsin (AAT) from Escherichia coli. Methods Mol Biol.<br>1639: 195-209.<\/a><br><br>78. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC5743216\/pdf\/nihms896130.pdf\">Braakman, I., L. Lamriben, G. van Zadelhoff and D. N. Hebert (2017) Analysis of disulfide<br>bond formation overview. In Current protocols in protein science, J. E. Coligan, H.L. Ploegh,<br>J. A. Smith, D. W. Speicher and P.T. Wingfield, eds. (Brooklyn, NY: Greene Publ. Assoc. and<br>Wiley-Interscience.<\/a><br><br>77. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2816%2930459-2\">Hebert, D. N., E. M. Clerico and L. M. Gierasch (2016) Division of labor: ER-resident BiP<br>co-chaperones match substrates to fates based on specific binding sequences. Mol. Cell<br>63(5):721-723.<br><\/a><br>76. <a href=\"https:\/\/www.pnas.org\/doi\/10.1073\/pnas.1603386113?url_ver=Z39.88-2003&amp;rfr_id=ori%3Arid%3Acrossref.org&amp;rfr_dat=cr_pub++0pubmed\">Chandrasekhar, K., H. Ke, N. Wang, T. Goodwin, L.M. Gierasch, A. Gershenson, D. N.<br>Hebert (2016) Cellular folding pathway of a metastable serpin. Proc. Natl. Acad. Sci. USA<br>113(23):6484-9.<\/a><br><br>75. <a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/tra.12358\">Lamriben, L., J. B. Graham, B. M. Adams, and D. N. Hebert, (2016) N-glycan based ER<br>molecular chaperone and protein quality control system: the calnexin binding cycle. Traffic.<br>17(4):308-26.<br><\/a><br>74. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1084952115001068?via%3Dihub\">Molinari, M. and D. N. Hebert. (2015) Glycoprotein maturation and quality control,<br>Seminars in Cell and Developmental Biology, 41:70.<br><\/a><br>73. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4474783\/pdf\/nihms652877.pdf\">Tannous, A., G. B. Pisoni, D. N. Hebert and M. Molinari. (2015) N-linked sugar regulated<br>protein folding and quality control in the ER, Seminars in Cell and Developmental Biology,<br>41:79-89.<\/a><br><br>72. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4310732\/pdf\/390.pdf\">Tannous, A., N. Patel, T. Tamura, and D. N. Hebert. (2015) Reglucosylation by UDP-<br>glucose: glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not<br>degradation. Molecular Biology of the Cell, 26(3):390-405.<\/a><br><br>71. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4399817\/pdf\/nihms678828.pdf\">Guiliano, D.B, H. Fussell, I. Lenart, E. Tsao, D. Nesbeth, A. Fletcher, E. C. Campbell, S.<br>Lynch, S. Santos, A. Cameron, G. Towers, P. Kellam, D. N. Hebert, K. Gould, S. J. Powis,<br>and A. N. Antoniou. (2014) EDEM1 targets misfolded HLA-B27 dimers for endoplasmic reticulum associated<br>degradation.<\/a><br><br>70. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4232232\/pdf\/nihms639910.pdf\">Hebert, D. N., L. Lamriben, E. T. Powers and J. W. Kelly. (2014) The intrinsic and extrinsic<br>effects of N-linked glycans on glycoproteostasis. Nature Chemical Biology, 10(11):902-910.<\/a><br><br>69. <a href=\"\/\/www.jbc.org\/action\/showPdf?pii=S0021-9258%2820%2933504-3\">Sunryd, J.C., B. Cheon, J. B. Graham, K. M. Giorda, R. A. Fissore, D. N. Hebert. (2014)<br>TMTC1 and TMTC2 are novel endoplasmic reticulum TPR-containing adapter proteins<br>involved in calcium homeostasis. J. Biol. Chem. 289:16085-16099.<br><\/a><br>68. <a href=\"https:\/\/books.google.com\/books?hl=en&amp;lr=&amp;id=MCpnBAAAQBAJ&amp;oi=fnd&amp;pg=PP5&amp;dq=The+Molecular+Chaperones+Interaction+Networks+in+Protein+Folding+and+Degradation,+Springer+Press&amp;ots=XAvULaWnon&amp;sig=BC2nCmCu_-hC_Xeo_-CUvQOkjUE#v=onepage&amp;q=The%20Molecular%20Chaperones%20Interaction%20Networks%20in%20Protein%20Folding%20and%20Degradation%2C%20Springer%20Press&amp;f=false\">Sunryd, J. C., T. Tannous, L. Lamriben and D. N. Hebert (2014) Chaperones of the ERAD<br>pathway. In W. A. Houry (ed.), The Molecular Chaperones Interaction Networks in Protein<br>Folding and Degradation, Springer Press.<br><\/a><br>67. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3785214\/pdf\/dna.2013.2159.pdf\">Giorda, K. M. and D. N. Hebert (2013) Viroporins customize host cells for efficient viral<br>propagation. DNA &amp; Cell Biol. 2013 Oct;32(10):557-64.<br><\/a><br>66. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4235334\/pdf\/nihms639536.pdf\">Raghava, S., K. M. Giorda, F. B. Romano, A. P. Heuck and D. N. Hebert (2013) SV40 late<br>protein VP4 forms toroidal pores to disrupt membranes for viral release. Biochemistry. 2013<br>Jun 4;52(22):3939-48.<br><\/a><br>65. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3554919\/pdf\/zbc2510.pdf\">Giorda, K. M., S. Raghava, M. W. Zhang and D. N. Hebert (2013) The viroporin activity of<br>the minor structural proteins VP2 and VP3 is required for SV40 propagation. J. Biol. Chem.<br>288(4):2510-2520.<\/a><br><br>64. <a href=\"https:\/\/cshperspectives.cshlp.org\/content\/5\/5\/a013201.long\">Braakman, I. and D. N. Hebert (2013) \u201cProtein folding in the endoplasmic reticulum\u201d, in<br>Ferro-Novick, S, R. Schekman, and T. Rapoport (ed.), Endoplasmic Reticulum Monograph,<br>Cold Spring Harbor Laboratory Press. May 1;5(5):a013201.<\/a><br><br>63. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2812%2900822-2\">Hebert, D.N., K. D. Chandrasekhar and L. M. Gierasch (2012) You have to know when to<br>hold (or unfold) \u2018em\u2026 [Preview] Molecular Cell 48(1):3-4.<br><\/a><br>62. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3459134\/pdf\/main.pdf\">Hebert, D. N. and M. Molinari (2012) Flagging and Docking: dual roles for N-glycans in<br>protein quality control and cellular proteostasis. Trends in Biochemical Sciences<br>37(10):404-410.<br><\/a><br>61. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3374742\/pdf\/2236.pdf\">Hebert, D. N. (2012), An MBoC Favorite: Malectin: a novel carbohydrate-binding protein of<br>the endoplasmic reticulum and a candidate player in the early steps of protein N-<br>glycosylation. Molecular Biology of the Cell 23(12):2236.<\/a><br><br>60. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC3302328\/pdf\/zjv3180.pdf\">Giorda, K. M., S. Raghava and D. N. Hebert (2012) The SV40 late viral protein VP4 disrupts<br>the nuclear envelope for viral release. Journal of Virology, 86(6):3180-92.<\/a><br><br>59. <a href=\"https:\/\/hstalks.com\/t\/2226\/the-erad-network\/?biosci\">Hebert, D. N. (2012), \"The ERAD Network\", in Houry, W. (ed.), Protein Homeostasis, The<br>Biomedical &amp; Life Sciences Collection, Henry Stewart Talks Ltd, London (online at<br>http:\/\/hstalks.com\/?t=BL1423153-Hebert).<br><\/a><br>58. <a href=\"\/\/www.jbc.org\/action\/showPdf?pii=S0021-9258%2819%2948653-5\">Tamura, T., J. H. Cormier and D. N. Hebert (2011) Characterization of the early EDEM1<br>maturation events and their functional implications. J. Biol. Chem., 286(28):24906-15.<\/a><br><br>57. <a href=\"https:\/\/journals.plos.org\/plospathogens\/article?id=10.1371\/journal.ppat.1002116\">Raghava, S., K. M. Giorda, F. B. Romano, A. P. Heuck and D. N. Hebert (2011) The SV40<br>late protein VP4 is a viroporin that forms pores to disrupt membranes viral release, PLoS<br>Pathogens, 7(6):e1002116.<\/a><br><br>56. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC4232234\/pdf\/nihms-639895.pdf\">Tamura, T., J. C. Sunryd and D. N. Hebert (2010) Sorting things out through ER quality<br>control, Molecular Membranes Biology, 27(8):412-427.<\/a><br><br>55. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2878942\/pdf\/JCB_200912105.pdf\">Pearse, B. R., T, Tamura, J. C. Sunryd, G. A. Grabowski, R. J. Kaufman and D. N. Hebert<br>(2010) The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an<br>obligate substrate, prosaposin, Journal of Cell Biology, 189:829-841.<br><\/a><br>54. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1084952109002523?via%3Dihub\">Hebert, D.N., R. Bernasconi and M. Molinari (2010) ERAD substrates: which way out?<br>Seminar in Cell and Developmental Biology, 21:526-532.<\/a><br><br>53.<a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2875293\/pdf\/nihms157659.pdf\"> Pearse, B. R. and D. N. Hebert (2010) Lectin chaperones help direct maturation of<br>glycoproteins in the endoplasmic reticulum, Biochimica et Biophysica Acta, 1803:684-693.<\/a><br><br>52. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2775177\/pdf\/embor2009224.pdf\">Cyr, D. M. and D. N. Hebert (2009) Protein Quality Control: A Meeting on Links Between<br>the Unfolded Protein Response and Disease, EMBO Reports, 10(11):1206-10.<br><\/a><br>51. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2748041\/pdf\/1700-08.pdf\">Jejcic, A., R. Daniels, L. Goobar-Larsson, D. N. Hebert, and A. Vahlne (2009) Small<br>molecule targets Env for ER-associated protein degradation and inhibits HIV-1 propagation.<br>Journal of Virology 83(19):10075-84.<br><\/a><br>50. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2809%2900397-9\">Hebert, D. N. and L. M. Gierasch (2009) The molecular dating game: an antibody heavy<br>chain hangs loose with a chaperone while waiting for its life partner. [Preview] Molecular<br>Cell 34:635-636.<br><\/a><br>49. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2740909\/pdf\/nihms120830.pdf\">Cormier, J. H., T. Tamura and D. N. Hebert (2009) EDEM1 recognition and delivery of<br>misfolded proteins to the SEL1L-containing ERAD complex. Molecular Cell 34:627-633.<\/a><br><br>48. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2590707\/pdf\/33826.pdf\">Wang, N., E. J. Glidden, S. R. Murphy, B. R. Pearse and D. N. Hebert (2008) The<br>cotranslational maturation program for the type II membrane glycoprotein influenza<br>neuraminidase. J. Biol. Chem. 283:33826-33837.<br><\/a><br>47. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S0968-0004%2808%2900103-5\">Tamura, T., J. H. Cormier and D. N. Hebert (2008) Sweet bays of ERAD. Trends in<br>Biochemical Sciences 33:298-300.<\/a><br><br>46. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC2315677\/\">Pearse B. R., L. Gabriel, N. Wang and D. N. Hebert (2008) A cell-based reglucosylation<br>assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein.<br>Journal of Cell Biology 181:309-320.<\/a><br><br>45. <a href=\"https:\/\/journals.physiology.org\/doi\/full\/10.1152\/physrev.00050.2006?rfr_dat=cr_pub++0pubmed&amp;url_ver=Z39.88-2003&amp;rfr_id=ori%3Arid%3Acrossref.org\">Hebert, D. N. and M. Molinari (2007) In and out of the ER: protein folding, quality control<br>and degradation, and related human diseases. Physiology Reviews 87:1377-1408.<br><\/a><br>44. <a href=\"https:\/\/hstalks.com\/t\/98\/glycoprotein-maturation-and-quality-control-in-the\/\">Hebert, D.N. (2007), \"Glycoprotein Maturation and Quality Control in the Endoplasmic<br>Reticulum\", in Michalak, M. (ed.), The Endoplasmic Reticulum: Fundamentals and Role in<br>Disease, The Biomedical &amp; Life Sciences Collection, Henry Stewart Talks Ltd, London<br>(online at http:\/\/www.hstalks.com\/?t=BL0121544-Hebert).<\/a><br><br>43. <a href=\"https:\/\/journals.plos.org\/plospathogens\/article?id=10.1371\/journal.ppat.0030098\">Daniels, R., D. Sadowicz and D. N. Hebert (2007) A very late viral protein triggers the lytic<br>release of SV40. PLoS Pathogens 3:e98, 0928-0938.<\/a><br><br>42. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/S1874604707250115\">Pearse, B. R. and D. N. Hebert (2007) Calnexin, Calreticulin and their associated<br>oxidoreductase ERp57, The Enzymes, Vol. 25, \u201cMolecular Machines involved in Protein<br>Transport across Cellular Membranes\u201d Edited by R. E. Dalbey, C. Koehler and F. Tamanoi<br>for Academic Press\/Elsevier.<\/a><br><br>41. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC1810509\/\">Zuber, C., J. H Cormier, B. Guhl, R. Santimara, D. N. Hebert, and J. Roth (2007) EDEM1<br>reveals a novel quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites.<br>Proc. Natl. Acad. Sci. USA 104:4407-4412.<\/a><br><br>40. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2806%2900742-8\">Daniels, R., N. M. Rusan, P. Wadsworth and D. N. Hebert (2006) SV40 VP2 and VP3<br>insertion into ER membranes is controlled by the capsid protein VP1: Implications for DNA<br>translocation out of the ER. Molecular Cell 24:955-966.<\/a><br><br>39. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2806%2900606-X\">Pearse, B. R. and D. N. Hebert (2006) Co-translocational degradation: utilitarianism in the<br>ER stress response. [Preview] Molecular Cell 23:773-775.<br><\/a><br>38. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC1488938\/pdf\/0347-06.pdf\">Daniels, R., N. M. Rusan, A,-K. Wilbuer, L. C. Norkin, P. Wadsworth and D. N. Hebert<br>(2006) Simian Virus 40 late proteins possess lytic properties capable of permeabilizing cellular<br>membranes Journal of Virology 80:6575-87.<\/a><br><br>37.<a href=\"https:\/\/onlinelibrary.wiley.com\/doi\/epdf\/10.1111\/j.1600-0749.2005.00288.x\"> Wang, N. and D. N. Hebert (2006) Tyrosinase maturation through the mammalian secretory<br>pathway: bringing color to life. Pigment Cell Research 19:3-18.<br><\/a><br>36. <a href=\"\/\/www.cell.com\/action\/showPdf?pii=S1097-2765%2805%2901593-5\">Cormier, J. H., B. R. Pearse and D. N. Hebert (2005) Yos9p: A sweet-toothed bouncer of<br>the secretory pathway. [Preview] Molecular Cell 19:717-719.<\/a><br><br>35. <a href=\"\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC1182312\/pdf\/00163740.pdf\">Wang, N., R. Daniels and D. N. Hebert (2005) The co-translational maturation of the type I<br>membrane glycoprotein tyrosinase: the Hsp70 system hands off to the lectin-based<br>chaperone system. Molecular Biology of the Cell 16:3740-3752.<\/a><br><br>34. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0962892405001327?via%3Dihub\">Hebert, D. N., S. C. Garman and M. Molinari (2005) The glycan code of the endoplasmic<br>reticulum: asparagine-linked carbohydrates as protein maturation and quality control tags.\"<br>Trends in Cell Biology 15:364-370.<br><\/a><br>33. <a href=\"https:\/\/journals.biologists.com\/jcs\/article\/117\/14\/2937\/27652\/Carbohydrates-act-as-sorting-determinants-in-ER\">Svedine, S., T. Wang, R. Halaban and D. N. Hebert (2004) Carbohydrates act as sorting determinants in<br>ER-associated degradation of tyrosinase Journal of Cell Science 117:2937-49.<\/a><br><br>32. <a href=\"https:\/\/link.springer.com\/article\/10.1385\/CBB:41:1:113\">Daniels, R., S. Svedine and D. N. Hebert (2004) N-Linked Carbohydrates Act as Lumenal Maturation<br>and Quality Control Protein Tags Cell Biochemistry and Biophysics 41:113-137.<\/a><br><br>31. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0021925819750765?via%3Dihub\">Francis, E., N. Wang, H. Parag, R. Halaban and D. N. Hebert (2003) Tyrosinase maturation and oligomerization<br>in the endoplasmic reticulum requires a melanocyte-specific<br>factor. J. Biol. Chem. 278: 25607-17.<\/a><br><br>30. <a href=\"https:\/\/www.nature.com\/articles\/nsb0603-412.epdf?sharing_token=MfijIcXwhKYfrCrCtqJMj9RgN0jAjWel9jnR3ZoTv0OsG_xIBQIcPOp_TzP13ugoXQU2ckA5bnCl9Cpd04UAxoxtuiE_YplWAn4h59mk9gMi5JRNalr08f9M6j9vTnUFFmdAhoT_gOJT4tVjpeyeUA%3D%3D\">Hebert, D. N. (2003) Totally Sweet. [book review] Nat. Struct. Biol. 10:412.<br><\/a><br>29. <a href=\"https:\/\/www.nature.com\/articles\/nsb0503-319\">Wang, T. and D. N. Hebert (2003) EDEM, a quality control receptor. [News and Views], Nature Structure Biology 10:319-321.<\/a><br><br>28. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0092867403001107?via%3Dihub\">Schnell, D. J. and D. N. Hebert (2003) Protein translocons: Multi-functional mediators of<br>protein translocation across membranes. Cell 112:491-505.<\/a><br><br>27. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1097276502008213?via%3Dihub\">Daniels, R., B. Kurowski, A. E. Johnson and D. N. Hebert (2003) N-linked glycans direct the<br>co-translational maturation of influenza hemagglutinin. Molecular Cell<br>11:79-90.<\/a><br><br>26. Halaban, R., Hebert, D. N., and Fisher, D. E. (2003) Biology of melanocytes. In: I. M.<br>Freedberg, A. Z. Eisen, K. Wolff, F. K. Austen, L. A. Goldsmith, and S. I. Katz (eds.),<br>Dermatology In General Medicine, 6 th edition, Vol. I, pp. 127-148. New York, NY:<br>McGraw Hill Medical Publishing.<br><br>25. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0021925819608665?via%3Dihub\">Halaban, R., R. Patton, E. Cheng, S. Svedine, E. S. Trombetta, M. Wahl, S. Ariyan and D. N.<br>Hebert (2002) Abnormal acidification of Melanoma cells induces tyrosinase retention in<br>the early secretory pathway. J. Biol. Chem. 277: 14821-14828<\/a>.<br><br>24. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0022202X15417488\">Halaban, R. E. Cheng and D. N. Hebert, (2002) Co-Expression of Wild Type Tyrosinase<br>Enhances Maturation of Temperature-Sensitive Tyrosinase Mutants, J. Invest<br>Dermatology 119:481-488.<\/a><br><br>23. <a href=\"https:\/\/currentprotocols.onlinelibrary.wiley.com\/doi\/10.1002\/0471143030.cb1506s14\">Francis, E., R. Daniels and D. N. Hebert (2002) Analysis of Protein Folding and Oxidation in the Endoplasmic Reticulum In<br>Current Protocols in Cell Biology, J. S. Bonifacino, M. Dasso, J. B. Harford, J. Lippincott- Schwartz,<br>and K.M. Yamada, eds. NY: John Wiley &amp; Sons Inc.<\/a><br><br>22. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0021925819463448?via%3Dihub\">\u00dajv\u00e1ri, A., R. Aron, T. Eisenhaure, E. Cheng, H. Parag, Y. Smicun, R. Halaban and D. N.<br>Hebert (2001) Translation rate of human tyrosinase determines its N-linked glycosylation level. J.<br>Biol. Chem. 276:5924-5931<br><\/a><br>21. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0021925819460699\">Halaban, R., E. Cheng, S. Svedine, R. Aron, and D. N. Hebert, (2001) Proper folding and endoplasmic reticulum<br>to Golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine. J. Biol.<br>Chem. 276:11933-11938.<br><\/a><br>20. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC18529\/\">Halaban, R., S. Svedine, E. Cheng, Y. Smicun, R. Aron and D. N. Hebert (2000)<br>Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative<br>albinism. Proc. Natl. Acad. Sci. USA 97:5889-5894.<\/a><br><br>19. <a href=\"https:\/\/www.nature.com\/articles\/nsb1299_1084\">Hebert, D. N. (1999) Protein unfolding, mitochondria offer a helping hand. Nature Structure<br>Biology 6:1084-1085.<br><\/a><br>18. <a href=\"https:\/\/cdnsciencepub.com\/doi\/10.1139\/o98-077\">Hebert, D. N., J.-X. Zhang and A. Helenius (1998) Protein folding and maturation in a cell- free<br>system. Biochem. and Cell Biol. 76: 867-873.<\/a><br><br>17. <a href=\"https:\/\/rupress.org\/jcb\/article\/139\/3\/613\/757\/The-Number-and-Location-of-Glycans-on-Influenza\">Hebert, D. N., J.-X. Zhang, W. Chen, B. Foellmer and A. Helenius (1997) The number and<br>location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin J. Cell Biol.<br>139:613-623.<\/a><br><br>16. <a href=\"https:\/\/www.pnas.org\/doi\/10.1073\/pnas.94.12.6210\">Halaban, R., E. Chang, Y. Zhang, G. Moellmann, D. Henlon, M. Michalak, V. Setaluri and<br>D.N. Hebert (1997) Aberrant retention of tyrosinase in the endoplasmic reticulum mediates<br>accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of<br>amelanotic melanoma cells, Proc. Natl. Acad. Sci. USA 94: 6210-6215.<\/a><br><br>15. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/pii\/S0962892497010325?via%3Dihub\">Helenius, A., E. S. Trombetta, D.N. Hebert and J.F. Simons (1997) Calnexin, calreticulin and<br>the folding of glycoproteins. Trends Cell Biology 7: 193-200.<\/a><br><br>14. <a href=\"https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC450237\/\">Hebert, D. N., B. Foellmer and A. Helenius (1996) Calnexin and calreticulin promote<br>folding, delay oligomerization and suppress degradation of influenza hemagglutinin in<br>microsomes. EMBO J. 12: 2961-2968.<\/a><br><br>13. <a href=\"https:\/\/scholar.google.com\/citations?view_op=view_citation&amp;hl=en&amp;user=zWVxBkAAAAAJ&amp;cstart=100&amp;pagesize=100&amp;citation_for_view=zWVxBkAAAAAJ:_Qo2XoVZTnwC\">Braakman, I. and D. N. Hebert (1996) Disulfide (-SS-) bond formation overview. In Current<br>protocols in protein science, J. E. Coligan, H.L. Ploegh, J. A. Smith, D. W. Speicher and<br>P.T. Wingfield, eds. (Brooklyn, NY: Greene Publ. Assoc. and Wiley-Interscience.<br><\/a><br>12. <a href=\"https:\/\/www.jbc.org\/article\/S0021-9258(18)46797-X\/fulltext\">Cannon, K.S., D.N. Hebert and A. Helenius (1996) Glycan dependent and independent<br>association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem. 271:<br>14280-14284.<br><\/a><br>11. <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/7736594\/\">Hebert, D. N., B. Foellmer and A. Helenius (1995) Glucose trimming and reglucosylation<br>determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81: 425-<br>433.<\/a><br><br>10. <a href=\"https:\/\/symposium.cshlp.org\/content\/60\/405.long\">Hebert, D.N., J.F. Simons, J.R. Peterson and A. Helenius (1995) Calnexin, calreticulin and<br>BiP\/Kar2p in protein folding. Cold Spring Harbor Symposia on Quantitative Biology, LX<br>405-415.<\/a><br><br>9. <a href=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/bi00030a011\">Zottola, R. J., E. K. Cloherty, P. E. Coderre, A. Hansen, D. N. Hebert and A. Carruthers.<br>(1995) Glucose transporter function is controlled by transporter oligomeric structure: a<br>single, intramolecular disulfide promotes GLUT1 tetramerization. Biochemistry 34:9734-<br>9747.<\/a><br><br>8. <a href=\"\/\/www.jbc.org\/article\/S0021-9258(19)36561-5\/pdf\">Marquardt, T., D. N. Hebert and A. Helenius (1993) Folding of influenza hemagglutinin in<br>isolated endoplasmic reticulum derived microsomes. J. Biol. Chem. 268:19618-19625<br><\/a><br>7. <a href=\"\/\/www.jbc.org\/article\/S0021-9258(18)35912-X\/pdf\">Hebert, D. N. and A. Carruthers (1992) Glucose transporter oligomeric structure determines<br>transporter function: reversible redox-dependent interconversions of tetrameric and dimeric<br>GLUT1. J. Biol. Chem. 267:23829-23838.<br><\/a><br>6. <a href=\"https:\/\/pubs.acs.org\/doi\/epdf\/10.1021\/bi00233a003\">Hebert, D. N. and A. Carruthers (1991) Cholate-solubilized erythrocyte glucose transporters<br>exist as a mixture of homodimers and homotetramers. Biochemistry 30:4654-4658.<\/a><br><br>5. <a href=\"https:\/\/www.sciencedirect.com\/science\/article\/abs\/pii\/095506749190044Y\">Hebert, D. N. and A. Carruthers (1991) Uniporters and antiporters. Curr. Opin. Cell Biol., 3:702-709.<br><\/a><br>4. <a href=\"\/\/www.jbc.org\/article\/S0021-9258(18)54911-5\/pdf\">Pessino, A., D. N. Hebert, C. W. Woon, S. A. Harrison, B. M. Clancy, J. M. Buxton, A.<br>Carruthers and M. P. Czech (1991) Evidence that functional erythrocyte-type glucose<br>transporter are oligomers J. Biol. Chem. 266:20213-20217<\/a>.<br><br>3. <a href=\"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/bi00441a038#\">Helgerson, A. L., D. N. Hebert, S. Naderi and A. Carruthers (1989) Characterization of two<br>independent modes of action of ATP on human erythrocyte sugar transport. Biochemistry<br>28:6410-6417.<\/a><br><br>2. <a href=\"https:\/\/nyaspubs.onlinelibrary.wiley.com\/doi\/abs\/10.1111\/j.1749-6632.1989.tb12490.x?sid=nlm%3Apubmed\">Carruthers, A., A. L. Helgerson, D. N. Hebert, R. E. Tefft, Jr., S. Naderi and D. L. Melchior<br>(1989) Effects of calcium, ATP and lipids on the human erythrocyte sugar transporter. Ann.<br>N.Y. Acad. Sci. 568:52-67.<br><\/a><br>1. <a href=\"\/\/www.jbc.org\/article\/S0021-9258(18)67495-2\/pdf\">Hebert, D. N. and A. Carruthers (1986) Direct evidence for ATP modulation of sugar<br>transport in human erythrocyte ghosts. J. Biol. Chem.  261:10093-10099.<\/a><\/pre>\n","protected":false},"excerpt":{"rendered":"<p>Publications 99. Kevin P. Guay, Wen-Chuan Chou, Nathan P. Canniff, Kylie B. Paul &amp; Daniel N. Hebert N-glycan-dependent protein maturation and quality control in the ER. Nature Reviews Molecular Cell Biology (2025)98. Zain Dardas,&#46;&#46;&#46;<\/p>\n","protected":false},"author":59,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-89","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/pages\/89","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/users\/59"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/comments?post=89"}],"version-history":[{"count":77,"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/pages\/89\/revisions"}],"predecessor-version":[{"id":460,"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/pages\/89\/revisions\/460"}],"wp:attachment":[{"href":"https:\/\/sites.biochem.umass.edu\/hebertlab\/wp-json\/wp\/v2\/media?parent=89"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}