Krishnan, B., L. Hedstrom, D. N. Hebert, L. M. Gierasch, and A. Gershenson, (2016) Expression and purification of active recombinant human a1-antitrypsin. Methods Mol Biol. in press


Chandrasekhar K., H. Ke, N. Wang, T. Goodwin, L.M. Gierasch, A. Gershenson, D. N. Hebert (2016) Cellular folding pathway of a metastable serpin. Proc. Natl. Acad. Sci. USA 113(23):6484-9


Lamriben L, Graham JB, Adams BM, Hebert DN. N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle. Traffic. 2016 Apr;17(4):308-26


Tannous A, Pisoni GB, Hebert DN, Molinari M. N-linked sugar-regulated protein folding and quality control in the ER. Semin Cell Dev Biol. 2015 May;41:79-89


Tannous A, Patel N, Tamura T, Hebert DN. Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation. Mol Biol Cell. 2015 Feb 1;26(3):390-405


Hebert, D. N., L. Lamriben, E. T. Powers and J. W. Kelly. The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis. Nature Chemical Biology, Nat Chem Biol. 2014 Nov;10(11):902-910


Guiliano, D.B, H. Fussell, I. Lenart, E. Tsao, D. Nesbeth, A. Fletcher, E. C. Campbell, S. Lynch, S. Santos, A. Cameron, G. Towers, P. Kellam, D. N. Hebert, K. Gould, S. J. Powis, and A. N. Antoniou. HLA-B27 dimers preferentially interact with EDEM1 and are targeted for degradation by an HRD1-dependent pathway. Arthritis Rheumatol. 2014 Nov;66(11):2976-88


Sunryd, J. C., T. Tannous, L. Lamriben and D. N. Hebert. Chaperones of the ERAD pathway. In W. A. Houry (ed.), The Molecular Chaperones Interaction Networks in Protein Folding and Degradation, Springer Press


Sunryd JC, Cheon B, Graham JB, Giorda KM, Fissore RA, Hebert DN. TMTC1 and TMTC2 are novel endoplasmic reticulum TPR-containing adapter proteins involved in calcium homeostasis. J Biol Chem. 2014 Jun 6;289(23):16085-16099


Giorda KM, Hebert DN. Viroporins customize host cells for efficient viral propagation. DNA Cell Biol. 2013 Oct;32(10):557-64.


Raghava S, Giorda KM, Romano FB, Heuck AP, Hebert DN. SV40 late protein VP4 forms toroidal pores to disrupt membranes for viral release. Biochemistry. 2013 Jun 4;52(22):3939-48.


Braakman I, Hebert DN. Protein folding in the endoplasmic reticulum. Cold Spring Harb Perspect Biol. 2013 May 1;5(5):a013201.


Giorda KM, Raghava S, Zhang MW, Hebert DN. The viroporin activity of the minor structural proteins VP2 and VP3 is required for SV40 propagation. J Biol Chem. 2013 Jan 25;288(4):2510-20.

  Hebert DN, Chandrasekhar KD, Gierasch LM. You got to know when to hold (or unfold) 'em….Mol Cell. 2012 Oct 12;48(1):3-4.

Hebert, D. N. and M. Molinari (2012) Flagging and Docking: dual roles for N-glycans in protein quality control and cellular proteostasis. Trends in Biochemical Sciences in press


Braakman, I. and D. N. Hebert (2012) “Protein folding in the endoplasmic reticulum”, in Ferro-Novick, S, R. Schekman, and T. Rapoport (ed.), Endoplasmic Reticulum Monograph, Cold Spring Harbor Laboratory Press, in press


Hebert, D. N. (2012), "The ERAD Network", in Houry, W. (ed.), Protein Homeostasis, The Biomedical & Life Sciences Collection, Henry Stewart Talks Ltd, London (online at http://hstalks.com/?t=BL1423153-Hebert)


Hebert, D. N. (2012), An MBoC Favorite: Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Molecular Biology of the Cell 23(12):2236.


Giorda KM, Raghava S, Hebert DN. The Simian virus 40 late viral protein VP4 disrupts the nuclear envelope for viral release. J Virol. 2012 Mar;86(6):3180-92.


Raghava S, Giorda KM, Romano FB, Heuck AP, Hebert D. The SV40 Late Protein VP4 Is a Viroporin that Forms Pores to Disrupt Membranes for Viral Release. PLoS Pathog. 2011 Jun;7(6):e1002116. Epub 2011 Jun 30.


Tamura T, Cormier JH, Hebert DN. Characterization of early EDEM1 maturation events and their functional implications. Biol Chem. 2011 Jul 15;286(28):24906-15

  Tamura T, Sunryd JC, Hebert DN. Sorting things out through endoplasmic reticulum quality control. Mol Membr Biol. 2010 Nov;27(8):412-27
  Pearse BR, Tamura T, Sunryd JC, Grabowski GA, Kaufman RJ, Hebert DN. The role of UDP-Glc:glycoprotein glucosyltransferase1 in the maturation of an obligate substrate prosaposin. J Cell Biol. 2010 May 31;189(5):829-41.
  Hebert DN, Bernasconi R, Molinari M. ERAD substrates: which way out? Semin Cell Dev Biol. 2010 Jul;21(5):526-32. Epub 2009 Dec 22.
  Pearse BR, Hebert DN. Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum. Biochim Biophys Acta. 2010 Jun;1803(6):684-693.
  Cyr DM, Hebert DN. Protein quality control--linking the unfolded protein response to disease. Conference on 'From Unfolded Proteins in the Endoplasmic Reticulum to Disease'. EMBO Rep. 2009 Nov;10(11):1206-10.
  A. Jejcic, R. Daniels, L. Goobar-Larsson, D.N. Hebert, A.Vahlne. Small molecule targets Env for ER-associated protein degradation and inhibits HIV-1 propagation. J Virol. 2009 Oct;83(19):10075-84.
  D.N. Hebert , L.M. Gierasch. The molecular dating game: an antibody heavy chain hangs loose with a chaperone while waiting for its life partner. Molecular Cell. 2009 Jun 26;34(6):635-6.
  J. H. Cormier , Tamura T., J.C, Sunryd, D.N. Hebert. EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex. Molecular Cell. 2009 Jun 12;34(5):627-33.
  Wang, N., E.J. Glidden, S.R. Murphy, B.R. Pearse, and D.N. Hebert. The co-translational maturation program for the type II membrane glycopotein influenza neuraminidase. J Biol Chem., 2008. 283(49):33826-37.
  Tamura, T., J.H. Cormier, and D.N. Hebert. Sweet Bays of ERAD. Trends Biochem Sci. 2008. Jul;33(7):298-300.
  Pearse, B.R., L. Gabriel, N. Wang, and D.N. Hebert. A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein. J Cell Biol., 2008. 181: 309-320.
  Hebert, D.N. and M. Molinari. (2007). In and out of the ER: protein folding, quality control and degradation, and related human diseases. Physiology Reviews. 87(4): p. 1377-1408.
  Hebert, D.N. (2007). Glycoprotein maturation and quality control in the endoplasmic reticulum. [Audio Lecture]. Henry Stewart talks lecture series on the Endoplasmic Reticulum: Fundamentals and role in disease. London, UK. Series editor M. Michalak.
  Pearse, B. R. and D. N. Hebert. (2007). Calnexin, Calreticulin and their associated oxidoreductase ERp57. The Enzymes, Vol. 25, Molecular Machines involved in Protein Transport across Cellular Membranes, Edited by R. E. Dalbey, C. Koehler and F. Tamanoi for Academic Press/Elsevier. August 2007.
  Daniels, R., D. Sadowicz., and D.N. Hebert, A Very Late Viral Protein Triggers the Lytic Release of SV40. PLOS Pathogens, 2007. 3(7)
  Zuber, C.*, J.H. Cormier*, B. Guhl, R. Santimaria, D.N. Hebert, and J. Roth, EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc. Natl. Acad. Sci. USA, 2007. 104(11): p. 4407-12.
  Daniels, R., N.M. Rusan, P. Wadsworth, and D.N. Hebert, SV40 VP2 and VP3 Insertion into ER Membranes Is Controlled by the Capsid Protein VP1: Implications for DNA Translocation out of the ER. Molecular Cell, 2006. 24(6): p. 955-66.
  Pearse, B.R. and D.N. Hebert, Cotranslocational degradation: utilitarianism in the ER stress response. Molecular Cell, 2006. 23(6): p. 773-5.
Daniels, R., N.M. Rusan, A.K. Wilbuer, L.C. Norkin, P. Wadsworth, and D.N. Hebert, Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes. J Virol, 2006. 80(13): p. 6575-87.
Wang, N. and D.N. Hebert. Tyrosinase maturation through the mammalian secretory pathway: bringing color to life. Pigment Cell Res, 2006. 19(1): p. 3-18.
Wang, N., R. Daniels, and D.N. Hebert, The cotranslational maturation of the type I membrane glycoprotein tyrosinase: the heat shock protein 70 system hands off to the lectin-based chaperone system. Mol Biol Cell, 2005. 16(8): p. 3740-52.
Hebert, D.N., S.C. Garman, and M. Molinari, The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol, 2005. 15(7): p. 364-70.
Cormier, J.H., B.R. Pearse, and D.N. Hebert, Yos9p: a sweet-toothed bouncer of the secretory pathway. Molecular Cell, 2005. 19(6): p. 717-9.
Svedine, S., T. Wang, R. Halaban, and D.N. Hebert, Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase. J Cell Sci, 2004. 117(Pt 14): p. 2937-49.
Daniels, R., S. Svedine, and D.N. Hebert, N-linked carbohydrates act as lumenal maturation and quality control protein tags. Cell Biochem Biophys, 2004. 41(1): p. 113-38.
Daniels, R., B. Kurowski, A.E. Johnson, and D.N. Hebert, N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Molecular Cell, 2003. 11(1): p. 79-90.
Francis, E., N. Wang, H. Parag, R. Halaban, and D.N. Hebert, Tyrosinase maturation and oligomerization in the endoplasmic reticulum require a melanocyte-specific factor. J Biol Chem, 2003. 278(28): p. 25607-17.
Wang, T. and D.N. Hebert, EDEM an ER quality control receptor. Nat Struct Biol, 2003. 10(5): p. 319-21.
Schnell, D.J. and D.N. Hebert, Protein translocons: multifunctional mediators of protein translocation across membranes. Cell, 2003. 112(4): p. 491-505.
Hebert, D. N. 2003. Totally Sweet. [book review] Nat. Struct. Biol. 10 (6):412

Halaban, R., Hebert, D. N., and Fisher, D. E. (2003) Biology of melanocytes. In: I. M. Freedberg, A. Z. Eisen, K. Wolff, F. K. Austen, L. A. Goldsmith, and S. I. Katz (eds.), Dermatology In General Medicine, 6 th edition, Vol. I, pp. 127-148. New York , NY : McGraw Hill Medical Publishing.

Halaban, R., R.S. Patton, E. Cheng, S. Svedine, E.S. Trombetta, M.L. Wahl, S. Ariyan, and D.N. Hebert, Abnormal acidification of melanoma cells induces tyrosinase retention in the early secretory pathway. J Biol Chem, 2002. 277(17): p. 14821-8.
Halaban, R., E. Cheng, and D.N. Hebert, Coexpression of wild-type tyrosinase enhances maturation of temperature-sensitive tyrosinase mutants. J Invest Dermatol, 2002. 119(2): p. 481-8.
Francis, E., R. Daniels and D. N. Hebert. (2002). Analysis of protein folding in vivo . In Current Protocols in Cell Biology, J. S. Bonifacino, M. Dasso, J. B. Harford, J. Lippincott-Schwartz, and K.M. Yamada, eds. NY: John Wiley & Sons Inc.
Ujvari, A., R. Aron, T. Eisenhaure, E. Cheng, H.A. Parag, Y. Smicun, R. Halaban, and D.N. Hebert, Translation rate of human tyrosinase determines its N-linked glycosylation level. J Biol Chem, 2001. 276(8): p. 5924-31.
Halaban, R., E. Cheng, S. Svedine, R. Aron, and D.N. Hebert, Proper folding and endoplasmic reticulum to golgi transport of tyrosinase are induced by its substrates, DOPA and tyrosine. J Biol Chem, 2001. 276(15): p. 11933-8.
Halaban, R., S. Svedine, E. Cheng, Y. Smicun, R. Aron, and D.N. Hebert, Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism. Proc Natl Acad Sci U S A, 2000. 97(11): p. 5889-94.
Hebert, D.N., Protein unfolding: mitochondria offer a helping hand. Nat Struct Biol, 1999. 6(12): p. 1084-5.
Hebert, D.N., J.X. Zhang, and A. Helenius, Protein folding and maturation in a cell-free system. Biochem Cell Biol, 1998. 76(5): p. 867-73.
Halaban, R., E. Cheng, Y. Zhang, G. Moellmann, D. Hanlon, M. Michalak, V. Setaluri, and D.N. Hebert, Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci U S A, 1997. 94(12): p. 6210-5.
Hebert, D.N., J.X. Zhang, W. Chen, B. Foellmer, and A. Helenius, The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J Cell Biol, 1997. 139(3): p. 613-23.
  Helenius, A., E. S. Trombetta, D.N. Hebert and J.F. Simons, Calnexin, calreticulin and the folding of glycoproteins. Trends Cell Biology, 1997. (7): p. 193-200.
Cannon, K.S., D.N. Hebert, and A. Helenius, Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin. J Biol Chem, 1996. 271(24): p. 14280-4.
Hebert, D.N., B. Foellmer, and A. Helenius, Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. Embo J, 1996. 15(12): p. 2961-8.

Braakman, I. and D. N. Hebert (1996). Disulfide (-SS-) bond formation overview. In Current protocols in protein science, J. E. Coligan, H.L. Ploegh, J. A. Smith, D. W. Speicher and P.T. Wingfield, eds. (Brooklyn, NY: Greene Publ. Assoc. and Wiley-Interscience.

Hebert, D.N., J.F. Simons, J.R. Peterson, and A. Helenius, Calnexin, calreticulin, and Bip/Kar2p in protein folding. Cold Spring Harb Symp Quant Biol, 1995. 60: p. 405-15.
Hebert, D.N., B. Foellmer, and A. Helenius, Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell, 1995. 81(3): p. 425-33.