Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control

Quality control in the endoplasmic reticulum

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Setting the Standards: Quality Control in the Secretory Pathway

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INHIBITORS OF THE BIOSYNTHESIS AND PROCESSING OF N-LINKED OLIGOSACCHARIDE CHAINS

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MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING

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Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport

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Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

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Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP

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Quality control in the secretory pathway

Hammond, C., & Helenius, A. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80009-3 · Cited by 672 · see citing works

Protein Glucosylation and Its Role in Protein Folding

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How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.

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Calreticulin Is Essential for Cardiac Development

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Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation

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Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle

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EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin

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The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins

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

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

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Chaperone Selection During Glycoprotein Translocation into the Endoplasmic Reticulum

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

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Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

Molinari, M., & Helenius, A. (1999) · Nature · doi:10.1038/47062 · Cited by 320 · see citing works

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 320 · see citing works

Folding of VSV G Protein: Sequential Interaction with BiP and Calnexin

Hammond, C., & Helenius, A. (1994) · Science · doi:10.1126/science.7939687 · Cited by 319 · see citing works

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 294 · see citing works

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

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

Changes in Endoplasmic Reticulum Luminal Environment Affect Cell Sensitivity to Apoptosis

Nakamura, K., Bossy‐Wetzel, E., Burns, K., Fadel, M. P., Lozyk, M. D., Goping, I. S., Opas, M., Bleackley, R. C., Green, D. R., & Michalak, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.4.731 · Cited by 286 · see citing works

Definition of the Lectin-like Properties of the Molecular Chaperone, Calreticulin, and Demonstration of Its Copurification with Endomannosidase from Rat Liver Golgi

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

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

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Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin

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Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells

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

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

Assembly and Antigen-Presenting Function of MHC Class I Molecules in Cells Lacking the ER Chaperone Calreticulin

Gao, B., Adhikari, R., Howarth, M. R., Nakamura, K., Gold, M. C., Hill, A. B., Knee, R., Michalak, M., & Elliott, T. J. (2002) · Immunity · doi:10.1016/s1074-7613(01)00260-6 · Cited by 246 · see citing works

Modulation of amplitude and direction ofin vivo immune responses by co-administration of cytokine gene expression cassettes with DNA immunogens

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Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER

Molinari, M., Galli, C., Piccaluga, V., Pieren, M., & Paganetti, P. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200204122 · Cited by 232 · see citing works

Calcium is required for folding of newly made subunits of the asialoglycoprotein receptor within the endoplasmic reticulum.

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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. E., et al. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.1.89 · Cited by 197 · see citing works

Quality Control in the Secretory Pathway: The Role of Calreticulin, Calnexin and BiP in the Retention of Glycoproteins with C-Terminal Truncations

Zhang, J., Braakman, I., Matlack, K. E. S., & Helenius, A. (1997) · Molecular Biology of the Cell · doi:10.1091/mbc.8.10.1943 · Cited by 190 · see citing works

Lectin control of protein folding and sorting in the secretory pathway

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Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity

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Stage-specific assays for coated pit formation and coated vesicle budding in vitro.

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Quality control in the endoplasmic reticulum: folding and misfolding of vesicular stomatitis virus G protein in cells and in vitro.

de Silva, A. M., Balch, W. E., & Helenius, A. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.111.3.857 · Cited by 151 · see citing works

A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation.

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Differential Interaction of Coagulation Factor VIII and Factor V with Protein Chaperones Calnexin and Calreticulin

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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 · see citing works

Calreticulin Interacts with Newly Synthesized Human Immunodeficiency Virus Type 1 Envelope Glycoprotein, Suggesting a Chaperone Function Similar to That of Calnexin

Otteken, A., & Moss, B. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.1.97 · Cited by 136 · see citing works

Natural killing target antigens as inducers of interferon: studies with an immunoselected, natural killing-resistant human T lymphoblastoid cell line.

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N-butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1/V2 region of gp120

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Functional Relationship between Calreticulin, Calnexin, and the Endoplasmic Reticulum Luminal Domain of Calnexin

Danilczyk, U. G., Cohen-Doyle, M. F., & Williams, D. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.13089 · Cited by 109 · see citing works

MHC class I expression and transport in a calnexin-deficient cell line

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Inhibition of Glucose Trimming with Castanospermine Reduces Calnexin Association and Promotes Proteasome Degradation of the α-Subunit of the Nicotinic Acetylcholine Receptor

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Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment.

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Tyrosinase Folding and Copper Loading in Vivo: A Crucial Role for Calnexin and α-Glucosidase II

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Calnexin Deficiency and Endoplasmic Reticulum Stress-Induced Apoptosis

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Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin–class I–TAP complexes

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Setting the Standards

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The Related Molecular Chaperones Calnexin and Calreticulin Differentially Associate with Nascent T Cell Antigen Receptor Proteins within the Endoplasmic Reticulum

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Characterization of endomannosidase inhibitors and evaluation of their effect on N-linked oligosaccharide processing during glycoprotein biosynthesis

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A chaperone with a sweet tooth

Hammond, C., & Helenius, A. (1993) · Current Biology · doi:10.1016/0960-9822(93)90226-e · Cited by 58 · see citing works

BiP-binding Sequences in HIV gp160

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Intermediates in the Assembly and Degradation of Class I Major Histocompatibility Complex (MHC) Molecules Probed with Free Heavy Chain–specific Monoclonal Antibodies

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Compromised calnexin function in calreticulin-deficient cells

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The role of calnexin in NK-target cell interaction

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T Cell Receptor Assembly and Expression in the Absence of Calnexin

Gardner, T. G., Franklin, R. A., Robinson, P. J., Pederson, N. E., Howe, C. J., & Kearse, K. P. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1804 · Cited by 11 · see citing works

A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex

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ER‐to‐lysosome‐associated degradation of proteasome‐resistant ATZ polymers occurs via receptor‐mediated vesicular transport

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More Than One Glycan Is Needed for ER Glucosidase II to Allow Entry of Glycoproteins into the Calnexin/Calreticulin Cycle

Deprez, P., Gautschi, M., & Helenius, A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.05.029 · Cited by 141 · see citing works

Narrow mutational signatures drive acquisition of multidrug resistance in the fungal pathogen Candida glabrata

Ksiezopolska, E., Schikora-Tamarit, M. À., Beyer, R., Nunez-Rodriguez, J. C., Schüller, C., & Gabaldón, T. (2021) · Current Biology · doi:10.1016/j.cub.2021.09.084 · Cited by 107 · see citing works

Cooperation between ER stress and calcineurin signaling contributes to the maintenance of cell wall integrity in Candida glabrata

Tanaka, Y., Sasaki, M., Ito, F., Aoyama, T., Sato-Okamoto, M., Takahashi-Nakaguchi, A., Chibana, H., & Shibata, N. (2018) · Fungal Biology · doi:10.1016/j.funbio.2017.09.007 · Cited by 13 · see citing works

Endoplasmic reticulum quality control and congenital pathology

Michalak, M. (2005) · Journal of Applied Biomedicine · doi:10.32725/jab.2005.021

Functional Relationship between Calreticulin, Calnexin, and the Endoplasmic Reticulum Luminal Domain of Calnexin

Danilczyk, U. G., Cohen-Doyle, M. F., & Williams, D. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.13089 · Cited by 109 · see citing works

Alternative chaperone machinery may compensate for calreticulin/calnexin deficiency in Caenorhabditis elegans

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The Use of Calnexin and Calreticulin by Cellular and Viral Glycoproteins

Pieren, M., Galli, C., Denzel, A., & Molinari, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501020200 · Cited by 72 · see citing works

Calnexin /Calreticulin Cycle and Glycoprotein ER-Associated Degradation

Sheng-li, L. (2004) · Foreign Medical Sciences