Protein Folding in the Endoplasmic Reticulum

SignalP 4.0: discriminating signal peptides from transmembrane regions

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Roles of N-Linked Glycans in the Endoplasmic Reticulum

Helenius, A., & Aebi, M. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073752 · Cited by 2,037

Precision Mapping of an In Vivo N-Glycoproteome Reveals Rigid Topological and Sequence Constraints

Zielinska, D. F., Gnad, F., Wiśniewski, J. R., & Mann, M. (2010) · Cell · doi:10.1016/j.cell.2010.04.012 · Cited by 902

Peptide-binding specificity of the molecular chaperone BiP

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GHKL, an emergent ATPase/kinase superfamily

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The human protein disulphide isomerase family: substrate interactions and functional properties

Ellgaard, L., & Ruddock, L. W. (2005) · EMBO reports · doi:10.1038/sj.embor.7400311 · Cited by 755

Protein Folding and Modification in the Mammalian Endoplasmic Reticulum

Braakman, I., & Bulleid, N. J. (2011) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062209-093836 · Cited by 691

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP

Blond-Elguindi, S. (1993) · Cell · doi:10.1016/0092-8674(93)90492-9 · Cited by 645

Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum

Hebert, D. N., Foellmer, B., & Helenius, A. (1995) · Cell · doi:10.1016/0092-8674(95)90395-x · Cited by 552

OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1–SEL1L ubiquitin ligase complex for ERAD

Christianson, J. C., Shaler, T. A., Tyler, R. E., & Kopito, R. R. (2008) · Nature Cell Biology · doi:10.1038/ncb1689 · Cited by 509

Catalysis of protein folding by prolyl isomerase

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The ER function BiP is a master regulator of ER function.

Hendershot, L. M. (2004) · PubMed · Cited by 446

A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody.

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Protein folding and quality control in the endoplasmic reticulum

Kleizen, B., & Braakman, I. (2004) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2004.06.012 · Cited by 439

The surprising complexity of signal sequences

Hegde, R. S., & Bernstein, H. D. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2006.08.004 · Cited by 424

Glucose‐stimulated signaling pathways in biphasic insulin secretion

Straub, S. G., & Sharp, G. W. G. (2002) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.329 · Cited by 421

Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

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Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum.

Braakman, I., Helenius, J., & Helenius, A. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05223.x · Cited by 410

The Structure of Calnexin, an ER Chaperone Involved in Quality Control of Protein Folding

Schrag, J. D., Bergeron, J. J. M., Li, Y., Borisova, S., Hahn, M., Thomas, D. Y., & Cygler, M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00318-5 · Cited by 392

Cotranslational and Posttranslational N-Glycosylation of Polypeptides by Distinct Mammalian OST Isoforms

Ruiz-Canada, C., Kelleher, D. J., & Gilmore, R. (2009) · Cell · doi:10.1016/j.cell.2008.11.047 · Cited by 391

Interaction of the Thiol-Dependent Reductase ERp57 with Nascent Glycoproteins

Oliver, J. D., van der Wal, F. J., Bulleid, N. J., & High, S. (1997) · Science · doi:10.1126/science.275.5296.86 · Cited by 390

Principles of protein folding in the cellular environment

Ellis, R. J., & Hartl, F. U. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)80013-x · Cited by 356

The Lipopolysaccharide-activated Toll-like Receptor (TLR)-4 Induces Synthesis of the Closely Related Receptor TLR-2 in Adipocytes

Lin, Y., Lee, H., Berg, A. H., Lisanti, M. P., Shapiro, L., & Scherer, P. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002137200 · Cited by 355

Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein.

Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.3.761 · Cited by 340

Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57

Zapun, A., Darby, N. J., Tessier, D. C., Michalak, M., Bergeron, J. J. M., & Thomas, D. Y. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.11.6009 · Cited by 335

Chaperone Selection During Glycoprotein Translocation into the Endoplasmic Reticulum

Molinari, M., & Helenius, A. (2000) · Science · doi:10.1126/science.288.5464.331 · Cited by 329

Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein

Earl, P. L., Moss, B., & Doms, R. W. (1991) · Journal of Virology · doi:10.1128/jvi.65.4.2047-2055.1991 · Cited by 327

ERp57 Functions as a Subunit of Specific Complexes Formed with the ER Lectins Calreticulin and Calnexin

Oliver, J. D., Roderick, H. L., Llewellyn, D. H., & High, S. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2573 · Cited by 326

Folding of influenza hemagglutinin in the endoplasmic reticulum.

Braakman, I., Hoover-Litty, H., Wagner, K. R., & Helenius, A. (1991) · The Journal of cell biology · doi:10.1083/jcb.114.3.401 · Cited by 318

Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability

Randow, F., & Seed, B. (2001) · Nature Cell Biology · doi:10.1038/ncb1001-891 · Cited by 316

Getting In and Out from Calnexin/Calreticulin Cycles

Caramelo, J. J., & Parodi, A. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700048200 · Cited by 307

Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes.

Hebert, D. N., Foellmer, B., & Helenius, A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00659.x · Cited by 293

Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

Braakman, I., Helenius, J., & Helenius, A. (1992) · Nature · doi:10.1038/356260a0 · Cited by 287

N-Linked Glycans Direct the Cotranslational Folding Pathway of Influenza Hemagglutinin

Daniels, R., Kurowski, B., Johnson, A. E., & Hebert, D. N. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00821-3 · Cited by 275

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.

Peterson, J. R., Ora, A., Van, P. N., & Helenius, A. (1995) · Molecular Biology of the Cell · doi:10.1091/mbc.6.9.1173 · Cited by 275

The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase.

Sousa, M., & Parodi, A. J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00093.x · Cited by 265

The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags

Hebert, D. N., Garman, S. C., & Molinari, M. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.05.007 · Cited by 264

Synthesis and processing of protein-linked oligosaccharides in vivo.

Hubbard, S. C., & Robbins, P. W. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30049-2 · Cited by 260

The Number and Location of Glycans on Influenza Hemagglutinin Determine Folding and Association with Calnexin and Calreticulin

Hebert, D. N., Zhang, J.-X., Chen, W., Foellmer, B., & Helenius, A. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.3.613 · Cited by 255

Mutations in SIL1 cause Marinesco-Sjögren syndrome, a cerebellar ataxia with cataract and myopathy

Senderek, J., Krieger, M., Stendel, C., Bergmann, C., Moser, M., Breitbach-Faller, N., Rudnik-Schöneborn, S., Blaschek, A., Wolf, N. I., Harting, I., et al. (2005) · Nature Genetics · doi:10.1038/ng1678 · Cited by 252

Scavenger receptor-A mediates gp96/GRP94 and calreticulin internalization by antigen-presenting cells

Berwin, B. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg572 · Cited by 245

Retention of Unassembled Components of Integral Membrane Proteins by Calnexin

Rajagopalan, S., Xu, Y., & Brenner, M. B. (1994) · Science · doi:10.1126/science.8278814 · Cited by 243

The gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperone

Anttonen, A.-K., Mahjneh, I., Hämäläinen, R. H., Lagier-Tourenne, C., Kopra, O., Waris, L., Anttonen, M., Joensuu, T., Kalimo, H., Paetau, A., et al. (2005) · Nature Genetics · doi:10.1038/ng1677 · Cited by 242

Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex.

Lodish, H. F., & Kong, N. (1984) · The Journal of cell biology · doi:10.1083/jcb.98.5.1720 · Cited by 239

The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stability

Hanson, S. R., Culyba, E. K., Hsu, T.-L., Wong, C.-H., Kelly, J. W., & Powers, E. T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810318105 · Cited by 236

Secreted MD-2 is a large polymeric protein that efficiently confers lipopolysaccharide sensitivity to Toll-like receptor 4

Visintin, A., Mazzoni, A., Spitzer, J. A., & Segal, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211445098 · Cited by 230

Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP

Zhao, L., Longo-Guess, C., Harris, B. S., Lee, J.-W., & Ackerman, S. L. (2005) · Nature Genetics · doi:10.1038/ng1620 · Cited by 214

Asparagine-linked Oligosaccharides Protect Lamp-1 and Lamp-2 from Intracellular Proteolysis

Kundra, R., & Kornfeld, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.31039 · Cited by 208

Assembly in vivo of mouse muscle acetylcholine receptor: Identification of an α subunit species that may be an assembly intermediate

Merlie, J. P., & Lindstrom, J. (1983) · Cell · doi:10.1016/0092-8674(83)90531-7 · Cited by 205

The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules.

Vassilakos, A., Cohen-Doyle, M. F., Peterson, P. A., Jackson, M. R., & Williams, D. B. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00493.x · Cited by 201

BAP, a Mammalian BiP-associated Protein, Is a Nucleotide Exchange Factor That Regulates the ATPase Activity of BiP

Chung, K. T., Shen, Y., & Hendershot, L. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208377200 · Cited by 197

Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.

Doms, R. W., Ruusala, A., Machamer, C., Helenius, J., Helenius, A., & Rose, J. K. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.1.89 · Cited by 195

Biochemically Distinct Vesicles from the Endoplasmic Reticulum Fuse to Form Peroxisomes

van der Zand, A., Gent, J., Braakman, I., & Tabak, H. F. (2012) · Cell · doi:10.1016/j.cell.2012.01.054 · Cited by 187

UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates

Caramelo, J. J., Castro, O. A., Alonso, L. G., de Prat-Gay, G., & Parodi, A. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262661199 · Cited by 183

Life and death of a BiP substrate

Otero, J. H., Lizák, B., & Hendershot, L. M. (2010) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2009.12.008 · Cited by 181

The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum

Alder, N. N., Shen, Y., Brodsky, J. L., Hendershot, L. M., & Johnson, A. E. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200409174 · Cited by 172

Large Scale Protein Identification in Intracellular Aquaporin-2 Vesicles from Renal Inner Medullary Collecting Duct

Barile, M., Pisitkun, T., Yu, M.-J., Chou, C.-L., Verbalis, M. J., Shen, R.-F., & Knepper, M. A. (2005) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500049-mcp200 · Cited by 171

GRP94 Is Essential for Mesoderm Induction and Muscle Development Because It Regulates Insulin-like Growth Factor Secretion

Wanderling, S. S., Simen, B. B., Ostrovsky, O., Ahmed, N. T., Vogen, S. M., Gidalevitz, T., & Argon, Y. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0275 · Cited by 164

The Charged Linker Region Is an Important Regulator of Hsp90 Function

Hainzl, O., Lapina, M. C., Buchner, J., & Richter, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031658 · Cited by 162

Coordinated Nonvectorial Folding in a Newly Synthesized Multidomain Protein

Jansens, A., van Duijn, E., & Braakman, I. (2002) · Science · doi:10.1126/science.1078376 · Cited by 161

Interaction of Radicicol with Members of the Heat Shock Protein 90 Family of Molecular Chaperones

Schulte, T. W. (1999) · Molecular Endocrinology · doi:10.1210/me.13.9.1435 · Cited by 161

Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum

Hendriks, G., Koudijs, M. J., van Balkom, B. W. M., Oorschot, V. M. J., Klumperman, J., Deen, P. M. T., & van der Sluijs, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310767200 · Cited by 148

SHEPHERD is the Arabidopsis GRP94 responsible for the formation of functional CLAVATA proteins

Ishiguro, S., Watanabe, Y., Ito, N., Nonaka, H., Takeda, N., Sakai, T., Kanaya, H., & Okada, K. (2002) · The EMBO Journal · doi:10.1093/emboj/21.5.898 · Cited by 145

Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells.

Tatu, U. S., Braakman, I., & Helenius, A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05863.x · Cited by 139

Disulfide Bond Formation in the Mammalian Endoplasmic ReticulumPreprint

Bulleid, N. J. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013219 · Cited by 139

The Endoplasmic Reticulum Glucosyltransferase Recognizes Nearly Native Glycoprotein Folding Intermediates

Caramelo, J. J., Castro, O., Gay, G. D. P., & Parodi, A. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408404200 · Cited by 132

Consequences of ERp57 Deletion on Oxidative Folding of Obligate and Facultative Clients of the Calnexin Cycle

Soldà, T., Garbi, N., Hämmerling, G. J., & Molinari, M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513595200 · Cited by 123

Persistent Glycoprotein Misfolding Activates the Glucosidase II/UGT1-Driven Calnexin Cycle to Delay Aggregation and Loss of Folding Competence

Molinari, M., Galli, C., Vanoni, O., Arnold, S. M., & Kaufman, R. J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.027 · Cited by 121

Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two‐hybrid system

Pollock, S., Kozlov, G., Pelletier, M.-F., Trempe, J., Jansen, G., Sitnikov, D., Bergeron, J. J. M., Gehring, K., Ekiel, I. H., & Thomas, D. Y. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600119 · Cited by 112

Regulation of Protein Compartmentalization Expands the Diversity of Protein Function

Shaffer, K. L., Sharma, A., Snapp, E. L., & Hegde, R. S. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.09.001 · Cited by 110

Folding of HIV‐1 Envelope glycoprotein involves extensive isomerization of disulfide bonds and conformation‐dependent leader peptide cleavage

Land, A., Zonneveld, D., & Braakman, I. (2003) · The FASEB Journal · doi:10.1096/fj.02-0811com · Cited by 104

N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression.

Shakin-Eshleman, S. H., Remaley, A. T., Eshleman, J. R., Wunner, W. H., & Spitalnik, S. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50073-4 · Cited by 101

Structural Basis of Cyclophilin B Binding by the Calnexin/Calreticulin P-domain

Kozlov, G., Bastos‐Aristizabal, S., Määttänen, P., Rosenauer, A., Zheng, F., Killikelly, A. M., Trempe, J., Thomas, D. Y., & Gehring, K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.160101 · Cited by 100

Malectin Participates in a Backup Glycoprotein Quality Control Pathway in the Mammalian ER

Galli, C., Bernasconi, R., Soldà, T., Calanca, V., & Molinari, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016304 · Cited by 98

Intracellular transport of soluble and membrane‐bound glycoproteins: folding, assembly and secretion of anchor‐free influenza hemagglutinin.

Singh, I., Doms, R. W., Wagner, K. R., & Helenius, A. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08155.x · Cited by 96

The Primary Folding Defect and Rescue of ΔF508 CFTR Emerge during Translation of the Mutant Domain

Hoelen, H., Kleizen, B., Schmidt, A., Richardson, J., Charitou, P., Thomas, P., & Braakman, I. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015458 · Cited by 96

Bulk Flow Revisited: Transport of a Soluble Protein in the Secretory Pathway

Thor, F., Gautschi, M., Geiger, R., & Helenius, A. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00989.x · Cited by 95

Folding and assembly of newly synthesized thyroglobulin occurs in a pre-Golgi compartment

Kim, P. S., & Arvan, P. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98913-1 · Cited by 91

Nonprolyl cis peptide bonds in unfolded proteins cause complex folding kinetics.

Pappenberger, G., Aygün, H., Engels, J. W., Reimer, U., Fischer, G. S., & Kiefhaber, T. (2001) · Nature Structural Biology · doi:10.1038/87624 · Cited by 91

Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin

Wada, I., Kai, M., Imai, S., Sakane, F., & Kanoh, H. (1997) · The EMBO Journal · doi:10.1093/emboj/16.17.5420 · Cited by 91

The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase

Schiene‐Fischer, C., Habazettl, J. M., Schmid, F. X., & Fischer, G. S. (2002) · Nature Structural Biology · doi:10.1038/nsb804 · Cited by 89

Insulin Gene Mutations as Cause of Diabetes in Children Negative for Five Type 1 Diabetes Autoantibodies

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Glycosylation Increases Potassium Channel Stability and Surface Expression in Mammalian Cells

Khanna, R., Myers, M. P., Lainé, M., & Papazian, D. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105248200 · Cited by 88

Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport.

Li, Y. X., Bergeron, J. J. M., Luo, L., Ou, W. J., Thomas, D. Y., & Kang, C. Y. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9606 · Cited by 86

Signal sequence insufficiency contributes to neurodegeneration caused by transmembrane prion protein

Rane, N. S., Chakrabarti, O., Feigenbaum, L., & Hegde, R. S. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911115 · Cited by 79

The Chaperone Activity of GRP94 Toward Insulin-like Growth Factor II Is Necessary for the Stress Response to Serum Deprivation

Ostrovsky, O., Ahmed, N. T., & Argon, Y. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-04-0346 · Cited by 78

Human neuropeptide Y signal peptide gain-of-function polymorphism is associated with increased body mass index: possible mode of function

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Radicicol-sensitive Peptide Binding to the N-terminal Portion of GRP94

Vogen, S. M., Gidalevitz, T., Biswas, C., Simen, B. B., Stein, E. M., Gulmen, F., & Argon, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205323200 · Cited by 77

Lectin chaperones help direct the maturation of glycoproteins in the endoplasmic reticulum

Pearse, B. R., & Hebert, D. N. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.10.008 · Cited by 74

Cysteine String Protein Interacts with and Modulates the Maturation of the Cystic Fibrosis Transmembrane Conductance Regulator

Zhang, H., Peters, K. W., Sun, F., Marino, C. R., Lang, J., Burgoyne, R. D., & Frizzell, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111706200 · Cited by 71

The Cotranslational Maturation of the Type I Membrane Glycoprotein Tyrosinase: The Heat Shock Protein 70 System Hands Off to the Lectin-based Chaperone System

Wang, N., Daniels, R., & Hebert, D. N. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-05-0381 · Cited by 68

Oligosaccharide-based Information in Endoplasmic Reticulum Quality Control and Other Biological Systems

Lehrman, M. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.r100002200 · Cited by 68

Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum.

Labriola, C. A., Cazzulo, J. J., & Parodi, A. J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.4.771 · Cited by 66

Insertion of a Chaperone Domain Converts FKBP12 into a Powerful Catalyst of Protein Folding

Knappe, T. A., Eckert, B., Schaarschmidt, P., Scholz, C., & Schmid, F. X. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.02.097 · Cited by 65

Chaperone-Like Functions of High-Mannose Type and Complex-Type N-Glycans and Their Molecular Basis

Jitsuhara, Y., Toyoda, T., Itai, T., & Yamaguchi, H. (2002) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a003290 · Cited by 65

Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control

Maynard, J. C., Pham, T. T., Zheng, T., Jockheck-Clark, A. R., Rankin, H. B., Newgard, C. B., Spana, E. P., & Nicchitta, C. V. (2010) · Developmental Biology · doi:10.1016/j.ydbio.2009.12.023 · Cited by 64

Malectin: A Novel Carbohydrate-binding Protein of the Endoplasmic Reticulum and a Candidate Player in the Early Steps of Protein N-Glycosylation

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Structural Transitions Accompanying the Activation of Peptide Binding to the Endoplasmic Reticulum Hsp90 Chaperone GRP94

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