Cited by 152Endoplasmic Reticulum Stress and DiseaseHeat shock proteins researchIon Channels and Receptors

The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.

Protein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response

Zhang, K., Kaufman, R.J.·2005·Handbook of Experimental Pharmacology

Open this paper in CoChat — free account

Abstract

In all eukaryotic cells, the endoplasmic reticulum (ER) is an intracellular organelle where folding and assembly occurs for proteins destined to the extracellular space, plasma membrane, and the exo/endocytic compartments (Kaufman 1999). As a protein-folding compartment, the ER is exquisitely sensitive to alterations in homeostasis, and provides stringent quality control systems to ensure that only correctly folded proteins transit to the Golgi and unfolded or misfolded proteins are retained and ultimately degraded. A number of biochemical and physiological stimuli, such as perturbation in calcium homeostasis or redox status, elevated secretory protein synthesis, expression of misfolded proteins, sugar/glucose deprivation, altered glycosylation, and overloading of cholesterol can disrupt ER homeostasis, impose stress to the ER, and subsequently lead to accumulation of unfolded or misfolded proteins in the ER lumen. The ER has evolved highly specific signaling pathways called the unfolded protein response (UPR) to cope with the accumulation of unfolded or misfolded proteins. Elucidation of the molecular mechanisms by which accumulation of unfolded proteins in the ER transmits a signal to the cytoplasm and nucleus has led to major new insights into the diverse cellular and physiological processes that are regulated by the UPR. This chapter summarizes how cells respond to the accumulation of unfolded proteins in the cell and the relevance of these signaling pathways to human physiology and disease.

Integrity signals

Registry

Crossref · 10.1007/3-540-29717-0_3

Cites

105 of 105 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
Protein folding in the cell
Gething, M.-J. H., & Sambrook, J. (1992) · Nature · doi:10.1038/355033a0 · Cited by 4,158
XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes
Özcan, U., Cao, Q., Yilmaz, E., Lee, A.-H., Iwakoshi, N. N., Özdelen, E., Tuncman, G., Görgün, C., Glimcher, L. H., & Hotamisligil, G. S. (2004) · Science · doi:10.1126/science.1103160 · Cited by 3,844
An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress
Harding, H. P., Zhang, Y., Zeng, H., Novoa, I., Lu, P. D., Calfon, M. A., Sadri, N., Yun, C., Popko, B., Paules, R. S., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00105-9 · Cited by 3,336
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
Harding, H. P., Zhang, Y., & Ron, D. (1999) · Nature · doi:10.1038/16729 · Cited by 3,310
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A., & Yuan, J. (2000) · Nature · doi:10.1038/47513 · Cited by 3,292
Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.
Urano, F., Wang, X.-Z., Bertolotti, A., Zhang, Y.-H., Chung, P., Harding, H., & Ron, D. (2000) · Science · doi:10.1126/science.287.5453.664 · Cited by 3,081

Flagged first, then by citations

Show all 105 references

Research works printed but not linked: 1

Morishima N, Nakanishi K, Takenouchi H, Shibata T, Yasuhiko Y (2002) An ER stress-specific caspase cascade in apoptosis: cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 3:3

Sorted by citations

Items 101–152 of 152

Biochemical and biophysical characterization of a novel plant protein disulfide isomerase
Gruber, C. W., Čemažar, M., Mechler, Á., Martin, L. L., & Craik, D. J. (2008) · Biopolymers · doi:10.1002/bip.21113 · Cited by 16
Decreased functional expression of Grp78 and Grp94 inhibits proliferation and attenuates apoptosis in a human gastric cancer cell line in vitro
Zhang, X., Zhang, L., Wang, S., Wu, D., & Yang, W.-L. (2014) · Oncology Letters · doi:10.3892/ol.2014.2831 · Cited by 15
Mitochondrial regulation by c-Myc and hypoxia-inducible factor-1α controls sensitivity to econazole
Yu, Y., Niapour, M., Zhang, Y., & Berger, S. A. (2008) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-07-2050 · Cited by 16
Oxidative Stress in the Aging Process: Fundamental Aspects and New Insights
del Valle, L. G., Hernández, R. G., Roche, L. D., & Fernández, O. (2015) · ACS symposium series · doi:10.1021/bk-2015-1200.ch006 · Cited by 15
Bitter orange peel extract induces endoplasmic reticulum-mediated autophagy in human hepatoma cells
Lu, K., Lee, H.-Y., Chu, Y., Ho, C., & Sheen, L. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.06.006 · Cited by 14
Activation of oxygen-responsive pathways are associated with altered protein metabolism in Arctic char exposed to hypoxia
Cassidy, A. A., & Lamarre, S. G. (2019) · Journal of Experimental Biology · doi:10.1242/jeb.203901 · Cited by 14
Polyribosome and ribonucleoprotein complex redistribution of mRNA induced by GnRH involves both EIF2AK3 and MAPK signaling
Minh‐Ha, T., Kim, T., He, F., Dave, H., Intriago, R. E., Astorga, U. A., Jain, S., & Lawson, M. A. (2013) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2013.10.007 · Cited by 13
Elevation of the unfolded protein response increases RANKL expression
Iyer, S. V., Melendez-Suchi, C., Han, L., Baldini, G., Almeida, M., & Jilka, R. L. (2020) · FASEB BioAdvances · doi:10.1096/fba.2019-00032 · Cited by 13
Melatonin treatment combined with treadmill exercise accelerates muscular adaptation through early inhibition of CHOP ‐mediated autophagy in the gastrocnemius of rats with intra‐articular collagenase‐induced knee laxity
Hong, Y., Kim, J., Jin, Y., Lee, S., Park, K., Lee, Y., Chang, K., & Hong, Y. (2013) · Journal of Pineal Research · doi:10.1111/jpi.12110 · Cited by 12
La3+ binds to BiP/GRP78 and induces unfolded protein response in HepG2 cells
Shen, C., Li, Z., Yang, X., & Wang, K. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.07.014 · Cited by 12
Role of the endoplasmic reticulum in the search for early biomarkers of meat quality
González‐Blanco, L., Sierra, V., Diñeiro, Y., Coto‐Montes, A. M., & Oliván, M. (2023) · Meat Science · doi:10.1016/j.meatsci.2023.109224 · Cited by 11
Beta-Cell Function and Failure in Type 2 Diabetes
Popa, S. G., & Mot, M. (2013) · InTech eBooks · doi:10.5772/56467 · Cited by 15
Novel genetic factors involved in resistance to B acillus thuringiensis in P lutella xylostella
Ayra‐Pardo, C., Raymond, B., Gulzar, A., Rodríguez–Cabrera, L., Morán, I., Crickmore, N., & Wright, D. J. (2015) · Insect Molecular Biology · doi:10.1111/imb.12186 · Cited by 10
Extracting Modulation Transfer Function of the Visual System from Contrast Sensitivity Function in External Noise
Lu, Z., Hou, F., & Huang, C. (2013) · Journal of Vision · doi:10.1167/13.9.1268 · Cited by 10
Methylglyoxal stimulates endoplasmic reticulum stress in vascular smooth muscle cells
Kırça, M., & Yeşilkaya, A. (2021) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2021.1918167 · Cited by 10
2-Deoxy-d-glucose as a potential drug against fusogenic viruses including HIV
Parris, G. E. (2007) · Medical Hypotheses · doi:10.1016/j.mehy.2007.08.021 · Cited by 9
A novel double carbonyl analog of curcumin induces the apoptosis of human lung cancer H460 cells via the activation of the endoplasmic reticulum stress signaling pathway
Ye, H., Wei, X., Wang, Z., Zhang, S., Ren, J., Yao, S., Shi, L., Yang, L., Qiu, P., Wu, J., et al. (2016) · Oncology Reports · doi:10.3892/or.2016.4911 · Cited by 9
Endoplasmic reticulum may not be involved in the lead‐induced apoptosis in PC 12 cells in vitro
Xu, J., Ji, L., & Xu, L. (2009) · Environmental Toxicology · doi:10.1002/tox.20474 · Cited by 8
Nitric Oxide and Protein Disulfide Isomerase Explain the Complexities of Unfolded Protein Response Following Intra-hippocampal Aβ Injection
Khodagholi, F., Digaleh, H., Motamedi, F., Foolad, F., & Shaerzadeh, F. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0271-x · Cited by 8
Systems Biology of the Endoplasmic Reticulum Stress Response
Caruso, M.-E., & Chevet, É. (2007) · Springer eBooks · doi:10.1007/978-1-4020-5943-8_13 · Cited by 8
Keystone meeting summary: ‘Adipogenesis, obesity, and inflammation’ and ‘Diabetes mellitus and the control of cellular energy metabolism, ’ January 21–26, 2006, Vancouver, Canada: Figure 1.Preprint
Corvera, S., Burkart, A., Kim, J.-Y., Christianson, J., Wang, Z., & Scherer, P. E. (2006) · Genes & Development · doi:10.1101/gad.1447506 · Cited by 8
Effect of Denervation on XBP1 in Skeletal Muscle and the Neuromuscular Junction
Walter, L. A., Blake, L. P., Gallot, Y. S., Arends, C. J., Sozio, R. S., Onifer, S. M., & Bohnert, K. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010169 · Cited by 7
Inhibition of Endoplasmic Reticulum Stress and Atherosclerosis by 2-Aminopurine in Apolipoprotein E-Deficient Mice
Zhou, L., Yang, D., Wu, D. F., Guo, Z. M., Okoro, E. U., & Yang, H. C. (2013) · ISRN Pharmacology · doi:10.1155/2013/847310 · Cited by 7
Gallotannin attenuates 2‑deoxy‑D‑glucose‑induced dedifferentiation and endoplasmic reticulum stress through inhibition of inositol‑requiring enzyme 1 downstream p38 kinase pathway in chondrocytes
Kim, S. Y., Han, Y., Yu, S., & Kim, S. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10773 · Cited by 5
ER-Associated Degradation of Membrane Proteins in Yeast
de Thozée, C. P., & Ghislain, M. (2006) · The Scientific World JOURNAL · doi:10.1100/tsw.2006.191 · Cited by 5
Leveraging bioanalytical characterization of fractionated monoclonal antibody pools to identify aggregation‐prone and less filterable proteoforms during virus filtration
Isu, S., Vinskus, L., Silva, D., Cunningham, K. M., Elich, T., Greenhalgh, P., Sokolnicki, A., & Raghunath, B. (2024) · Biotechnology Progress · doi:10.1002/btpr.3451 · Cited by 4
Pro-Inflammatory and Pro-Apoptotic Effects of the Non-Protein Amino Acid L-Azetidine-2-Carboxylic Acid in BV2 Microglial Cells
Piper, J. A., Jansen, M. I., Broome, S. T., Rodgers, K. J., Musumeci, G., & Castorina, A. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44100308 · Cited by 4
Multiple Gene Expression in Cell-Free Protein Synthesis Systems for Reconstructing Bacteriophages and Metabolic Pathways
Purkayastha, A., Iyappan, K., & Kang, T. J. (2022) · Microorganisms · doi:10.3390/microorganisms10122477 · Cited by 4
2-Aminopurine Inhibits Lipid Accumulation Induced by Apolipoprotein E-Deficient Lipoprotein in Macrophages: Potential Role of Eukaryotic Initiation Factor-2α Phosphorylation in Foam Cell Formation
Wu, D., Yang, H., Zhao, Y., Sharan, C., Goodwin, J. S., Zhou, L., Guo, Y., & Guo, Z. (2008) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.107.134833 · Cited by 4
Stressors and Stress Responses in Cystic Fibrosis
Bebok, Z., & Fu, L. (2018) · Endoplasmic Reticulum Stress in Diseases · doi:10.1515/ersc-2018-0002 · Cited by 3
Assessment of the Neuroprotective Potential of Glucose-Regulated Heat Shock Protein in a Model of Parkinson’s Disease in Rats
Ekimova, I. V., Пази, М. Б., & Плаксина, Д. В. (2019) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-019-00877-y · Cited by 3
Inhibitors of Aβ42-induced endoplasmic reticular unfolded protein response (UPRER), in yeast, also rescue yeast cells from Aβ42-mediated apoptosis
Derf, A., Mudududdla, R., Bharate, S. B., & Chaudhuri, B. (2018) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2018.11.029 · Cited by 2
Endoplasmic reticulum stress in nonalcoholic fatty liver disease
Foufelle, F., & Ferré, P. (2015) · Wiley eBooks · doi:10.1002/9781118663387.ch10 · Cited by 1
Synergistic Molecular Strategies for Targeting the Unfolded Protein Response in Cancer Therapy
Muradyan, O., Tahir, M., & Sarafian, V. S. (2026) · Pharmaceuticals · doi:10.3390/ph19060941 · Cited by 1
The Role of Hypoxia-Induced Factors
Schipani, E., & Khatri, R. (2010) · Springer eBooks · doi:10.1007/978-1-84882-822-3_7 · Cited by 1
Glucose-6-phosphatase-α participates in dopaminergic differentiation
Chen, J., Ting, W., Zhou, X., Tang, C., & Gao, D. (2017) · Neurological Research · doi:10.1080/01616412.2017.1348681 · Cited by 1
The cell in shock
Morales, M. M., & Petrs‐Silva, H. (2007) · Springer eBooks · doi:10.1007/978-88-470-0571-6_18
STUDIES OF FACTORS AFFECTING INTRACELLULAR TOXICITY OF THE SCA7 DISEASE PROTEIN ATAXIN - 7 : FOCUS ON ATAXIN-7 DEGRADATION AND OXIDATIVE STRESS
Yu, X. (2011) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Unravelling Molecular and Cellular Disease Mechanisms in Infantile Neuronal Ceroid Lipofuscinosis (INCL)
Ahtiainen, L. (2007) · STM:n Hallinnonalan avoin julkaisuarkisto (Julkari)
A Brief Introduction to the Eukaryotic Cell Stress Proteins
Henderson, B. E. (2013) · Heat shock proteins · doi:10.1007/978-94-007-6787-4_2
Translational control during viral infection, investigating the role of severe acute respiratory syndrome non-structural protein 1 and enterovirus 71 internal ribosome entry site.
Leteane, M. M. (2015) · Surrey Research Insight Open Access (The University of Surrey)
Characterisation of cytosolic prion protein-mediated putative cytotoxicity in neuronal cell lines
Mehlhase, J. (2007) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt)
A Dissertation entitled The Impact of FoxO1 on Skeletal Muscle Protein Synthesis
Potter, R. A., & McLoughlin, T. J. (2014)
Molecular Mechanisms Associated with Canine Cyclic Hematopoiesis
Meng, R. (2008)
Novel insights into hyperthermia’s therapeutic effectiveness in treating malignant melanoma
Mantso, T. (2018)
Altering the solubility of recombinant proteins through modification of surface features
Carballo‐Amador, M. A. (2015) · Research Explorer (The University of Manchester)
The regulation of skeletal muscle contractile function by Selenoprotein S.
Addinsall, A. B. (2018) · Own your potential (DEAKIN)
Dynamics of BCL-2 family of proteins in early pancreatic progenitors and β-cells
Loo, L. S. W. (2020) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/142359
Functional redox compartmentation of GSH in the yeast Saccharomyces cerevisiae
Igbaria, A. (2011) · theses.fr (ABES) · doi:10.70675/56d36c2az169az44c0za714zb7198e0b245e
Les effets cellulaires des inhibiteurs de la protéase virale utilisés en thérapie anti-VIH sur le muscle strié squelettique humain.
Mercier, O. (2010) · theses.fr (ABES) · doi:10.70675/45632f96zc2adz4b7azbdfcza75ab5bdd7a5
Paraoxonase 2 as a target for aging-related diseases
Kim, H., Kang, Y. J., Lee, J. H., Lee, H. M., Park, H. S., & Nam, C. (2026) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.25.354
Hepatic ultrastructural and transcriptomic responses of rainbow trout (Oncorhynchus mykiss) to heat stress, hypoxia, and combined heat and hypoxia
刘梦群, Zeng, C., Wang, Q., Zhao, Z., Wen, H., Li, Y., & Qi, X. (2026) · Aquaculture · doi:10.1016/j.aquaculture.2026.744473

Authors: Zhang, K., & Kaufman, R. J.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Kaufman, R.J.
ORCID: Zhang, K.
Kaufman, R.J.
Venue: Handbook of Experimental Pharmacology
Publisher: Springer-Verlag
Published: 2005-12-28
Issue: 172
Pages: 69-91
DOI: 10.1007/3-540-29717-0_3
OpenAlex: W136234913
Cited by: 152
References: 105
Citations by year: 2026: 3 · 2024: 3 · 2023: 2 · 2022: 7 · 2021: 4 · 2020: 3 · 2019: 7 · 2018: 6 · 2017: 5 · 2016: 4 · 2015: 11 · 2014: 7 · 2013: 16 · 2012: 6
FWCI: 24.70
Type: book chapter
Language: en
Open access: closed
Locations: Springer eBooks (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (DK42394)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Keywords: endoplasmic reticulum, unfolded protein response, protein folding, endoplasmic reticulum stress, ER homeostasis, misfolded proteins, calcium homeostasis, redox state, secretory protein synthesis, glucose deprivation, glycosylation
MeSH terms: Animals, Cell Differentiation, Diabetes Mellitus, Endoplasmic Reticulum, Glucose, Humans, Nervous System Diseases, Proteins, Transcription, Genetic, Protein Biosynthesis, Apoptosis, Protein Folding

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Protein Folding in the Endoplasmic Reticulum and the Unfolded Protein Response

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks