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. June 4. in press.
  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, 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.