Cited by 197Endoplasmic Reticulum Stress and DiseaseIon Channels and ReceptorsRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 124 of the 124 references it cites were found in a registry or an index.

Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

Brostrom, Margaret A, Brostrom, Charles O·2003·Cell Calcium

Open this paper in CoChat — free account

Abstract

The endoplasmic reticulum (ER) possesses the structural and functional features expected of an organelle that supports the integration and coordination of major cellular processes. Ca(2+) sequestered within the ER sustains lumenal protein processing while providing a reservoir of the cation to support stimulus-response coupling in the cytosol. Release of ER Ca(2+) sufficient to impair protein processing promotes ER stress and signals the "unfolded protein response" (UPR). The association of the UPR with an acute suppression of mRNA translational initiation and a longer term up-regulation of ER chaperones and partial translational recovery is discussed. Regulatory sites in mRNA translation and the mechanisms responsible for the early and later phases of the UPR are reviewed. The regulatory significance of GRP78/BiP, a multifunctional, broad-specificity ER chaperone, in the coordination of ER protein processing with mRNA translation during acute and chronic ER stress is addressed. The relationship of ER stress to protein misfolding in the cytoplasm is examined. Translational alterations in embryonic cardiomyocytes during treatments with various Ca(2+)-mobilizing, growth-promoting stimuli are described. The importance of ER Ca(2+) stores, ER chaperones, and cytosolic-free Ca(2+) in translational control and growth promotion by these stimuli is assessed. Some perspectives are provided regarding Ca(2+) as an integrating factor in the generation or diversion of metabolic energy. Circumstances impacting upon cellular adaptability during exposure to growth stimuli or during stressful conditions that require rapid adjustments in ATP for continued viability are considered.

Integrity signals

Registry

Crossref · 10.1016/s0143-4160(03)00127-1

Cites

124 of 124 references verified0 citation errors · 0 not checkable

Statistics

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

Claims the paper makes

This paper’s full text isn’t openly available, 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?

The versatility and universality of calcium signalling
Berridge, M. J., Lipp, P., & Bootman, M. D. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036035 · Cited by 5,701
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
Regulated Translation Initiation Controls Stress-Induced Gene Expression in Mammalian Cells
Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. K. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,335
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
IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
Calfon, M. A., Zeng, H., Urano, F., Till, J. H., Hubbard, S. R., Harding, H. P., Clark, S. G., & Ron, D. (2002) · Nature · doi:10.1038/415092a · Cited by 2,907
Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,871
Intracellular Functions of N-Linked Glycans
Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405
Perk is essential for translational regulation and cell survival during the unfolded protein response
Harding, H. P., Zhang, Y., Bertolotti, A., Zeng, H., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80330-5 · Cited by 2,021
Regulation of translation initiation by FRAP/mTOR
Gingras, A.-C., Raught, B., & Sonenberg, N. (2001) · Genes & Development · doi:10.1101/gad.887201 · Cited by 1,545
ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals
Shen, J., Chen, X., Hendershot, L. M., & Prywes, R. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00203-4 · Cited by 1,461
Invited Review: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance
Kregel, K. C. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01267.2001 · Cited by 1,450
Feedback Inhibition of the Unfolded Protein Response by GADD34-Mediated Dephosphorylation of eIF2α
Novoa, I., Zeng, H., Harding, H. P., & Ron, D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.1011 · Cited by 1,434
Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis
Scheuner, D. L., Song, B., McEwen, E. L., Liu, C., Laybutt, D. R., Gillespie, P. J., Saunders, T. L., Bonner‐Weir, S., & Kaufman, R. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00265-9 · Cited by 1,355
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,184
Proteinase-activated Receptors
Macfarlane, S. R., Seatter, M. J., Kanke, T., Hunter, G. D., & Plevin, R. J. (2006) · Springer eBooks · doi:10.1007/3-540-29832-0_1335 · Cited by 1,137
Ryanodine Receptor Calcium Release Channels
Fill, M., & Copello, J. A. (2002) · Physiological Reviews · doi:10.1152/physrev.00013.2002 · Cited by 1,096
IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein responsePreprint
Lee, K., Tirasophon, W., Shen, X., Michalak, M., Prywes, R., Okada, T., Yoshida, H., Mori, K., & Kaufman, R. J. (2002) · Genes & Development · doi:10.1101/gad.964702 · Cited by 1,085
The glucose-regulated proteins: stress induction and clinical applications
Lee, A. S. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01908-9 · Cited by 1,033
Roles of the heat shock transcription factors in regulation of the heat shock response and beyond
Pirkkala, L., NYKÄNEN, P., & Sistonen, L. (2001) · The FASEB Journal · doi:10.1096/fj00-0294rev · Cited by 996
Transcriptional and Translational Control in the Mammalian Unfolded Protein Response
Harding, H. P., Calfon, M. A., Urano, F., Novoa, I., & Ron, D. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.011402.160624 · Cited by 918
The Transmembrane Kinase Ire1p Is a Site-Specific Endonuclease That Initiates mRNA Splicing in the Unfolded Protein Response
Sidrauski, C., & Walter, P. (1997) · Cell · doi:10.1016/s0092-8674(00)80369-4 · Cited by 904
Regulation of mitochondrial ATP synthesis by calcium: Evidence for a long-term metabolic priming
Jouaville, L. S., Pinton, P., Bastianutto, C., Rutter, G. A., & Rizzuto, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13807 · Cited by 831
PKR; a sentinel kinase for cellular stress
Williams, B. R. (1999) · Oncogene · doi:10.1038/sj.onc.1203127 · Cited by 820
Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals
Patil, C., & Walter, P. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00219-2 · Cited by 779
Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
Kedersha, N., & Anderson, P. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300963 · Cited by 741
Gene-Specific Regulation by General Translation Factors
Dever, T. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00642-6 · Cited by 730
KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene
Rose, M. D., Misra, L. M., & Vogel, J. P. (1989) · Cell · doi:10.1016/0092-8674(89)90058-5 · Cited by 689
Protein Glucosylation and Its Role in Protein Folding
Parodi, A. J. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.69 · Cited by 659
Evidence That Ternary Complex (eIF2-GTP-tRNA i Met )–Deficient Preinitiation Complexes Are Core Constituents of Mammalian Stress Granules
Kedersha, N., Chen, S., Farny, N. G., Li, W., Miller, I. J., Stahl, J., & Anderson, P. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-05-0221 · Cited by 624
Contributions of mitochondria to animal physiology: from homeostatic sensor to calcium signalling and cell death
Duchen, M. R. (1999) · The Journal of Physiology · doi:10.1111/j.1469-7793.1999.001aa.x · Cited by 610
The PERK Eukaryotic Initiation Factor 2α Kinase Is Required for the Development of the Skeletal System, Postnatal Growth, and the Function and Viability of the Pancreas
Zhang, P., McGrath, B. C., Li, S., Frank, A. T., Zambito, F., Reinert, J., GANNON, M. A., Ma, K., McNaughton, K., & Cavener, D. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.11.3864-3874.2002 · Cited by 604
The Translocon: A Dynamic Gateway at the ER Membrane
Johnson, A. E., & van Waes, M. A. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.799 · Cited by 601
Heat shock factors and the control of the stress response
SANTORO, M. G. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00299-3 · Cited by 587
How the protease thrombin talks to cells
Coughlin, S. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11023 · Cited by 581
Role and regulation of the ER chaperone BiP
Gething, M.-J. H. (1999) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1999.0318 · Cited by 557
Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
Okada, T., Yoshida, H., Akazawa, R., Negishi, M., & Mori, K. (2002) · Biochemical Journal · doi:10.1042/bj20020391 · Cited by 539
The endoplasmic reticulum Ca2+ store: a view from the lumen
Meldolesi, J., & Pozzan, T. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01143-2 · Cited by 528
Mechanisms of capacitative calcium entry
Putney, J. W., Broad, L. M., Braun, F.-J., Lièvremont, J.-P., & Bird, G. S. J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.12.2223 · Cited by 524
Regulation of peptide‐chain elongation in mammalian cells
Browne, G. J., & Proud, C. G. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03290.x · Cited by 473
Complexes containing activating transcription factor (ATF)/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT/enhancer-binding protein (C/EBP)‒ATF composite site to regulate Gadd153 expression during the stress response
Fawcett, T. W., Martindale, J. L., Guyton, K. Z., Hai, T., & Holbrook, N. J. (1999) · Biochemical Journal · doi:10.1042/bj3390135 · Cited by 470
Endoplasmic reticulum of animal cells and its organization into structural and functional domains
Baumann, O., & Walz, B. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)05004-5 · Cited by 465
International Union of Pharmacology. XXVIII. Proteinase-Activated Receptors
Hollenberg, M. D., & Compton, S. J. (2002) · Pharmacological Reviews · doi:10.1124/pr.54.2.203 · Cited by 441
The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones.
Morimoto, R. I., Kline, M. P., Bimston, D. N., & Cotto, J. J. (1997) · PubMed · Cited by 435
Ligand-independent Dimerization Activates the Stress Response Kinases IRE1 and PERK in the Lumen of the Endoplasmic Reticulum
Liu, C. Y., Schröder, M., & Kaufman, R. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004454200 · Cited by 421
The Regulation of Skeletal Muscle Phosphorylase Kinase by Ca2+
Brostrom, C. O., Hunkeler, F. L., & Krebs, E. G. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77175-0 · Cited by 418
Self-citation
Regulation of mammalian translation factors by nutrients
Proud, C. G. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03292.x · Cited by 388
ER quality control: towards an understanding at the molecular level
Ellgaard, L., & Helenius, A. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00233-7 · Cited by 388
Modelling of simple and complex calcium oscillations
Schuster, S., Marhl, M., & Höfer, T. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02720.x · Cited by 386
Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58 IPK
Yan, W., Frank, C. L., Korth, M. J., Sopher, B. L., Novoa, I., Ron, D., & Katze, M. G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252341799 · Cited by 385
Stressful initiations
Anderson, P., & Kedersha, N. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.16.3227 · Cited by 383
Control of eukaryotic protein synthesis by upstream open reading frames in the 5′-untranslated region of an mRNA
Meijer, H. A., & Thomas, A. A. M. (2002) · Biochemical Journal · doi:10.1042/bj20011706 · Cited by 323
Invited Review: Role of insulin in translational control of protein synthesis in skeletal muscle by amino acids or exercise
Kimball, S. R., Farrell, P. A., & Jefferson, L. S. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00221.2002 · Cited by 304
Mammalian stress granules represent sites of accumulation of stalled translation initiation complexes
Kimball, S. R., Horetsky, R. L., Ron, D., Jefferson, L. S., & Harding, H. P. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00314.2002 · Cited by 291
Regulation of Translational Initiation during Cellular Responses to Stress
Brostrom, C. O., & Brostrom, M. A. (1997) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60034-3 · Cited by 278
Self-citation
Overexpression of Calreticulin Increases Intracellular Ca2+ Storage and Decreases Store-operated Ca2+ Influx
Mery, L., Mesaeli, N., Michalak, M., Opas, M., Lew, D. P., & Krause, K. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9332 · Cited by 271
Dimerization and Release of Molecular Chaperone Inhibition Facilitate Activation of Eukaryotic Initiation Factor-2 Kinase in Response to Endoplasmic Reticulum Stress
Ma, K., Vattem, K. M., & Wek, R. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200903200 · Cited by 268
Calcium, a signaling molecule in the endoplasmic reticulum?
Corbett, E. F., & Michalak, M. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01588-7 · Cited by 265
Endoplasmic reticulum dysfunction – a common denominator for cell injury in acute and degenerative diseases of the brain?
Paschen, W., & Frandsen, A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00623.x · Cited by 239
Molecular Pathways of Protein Synthesis Inhibition during Brain Reperfusion: Implications for Neuronal Survival or Death
DeGracia, D. J., Kumar, R., Owen, C. R., Krause, G. S., & White, B. C. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200202000-00001 · Cited by 233
Translational control: the cancer connection
Clemens, M. J., & Bommer, U. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(98)00127-7 · Cited by 220
Initiation Factor eIF2α Phosphorylation in Stress Responses and Apoptosis
Clemens, M. J. (2001) · Progress in molecular and subcellular biology · doi:10.1007/978-3-662-09889-9_3 · Cited by 216
Coordinate regulation of translation by the PI 3-kinase and mTOR pathways
Martin, K. A., & Blenis, J. (2002) · Advances in cancer research · doi:10.1016/s0065-230x(02)86001-8 · Cited by 204
Regulation of Internal Ribosomal Entry Site-mediated Translation by Phosphorylation of the Translation Initiation Factor eIF2α
Fernandez, J., Yaman, İ., Sarnow, P., Snider, M. D., & Hatzoglou, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201052200 · Cited by 196
Interconversion of three differentially modified and assembled forms of BiP.
Freiden, P. J., Gaut, J. R., & Hendershot, L. M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05028.x · Cited by 180
The endoplasmic reticulum and calcium storage
Koch, G. L. E. (1990) · BioEssays · doi:10.1002/bies.950121105 · Cited by 179
Modular Structure of PACT: Distinct Domains for Binding and Activating PKR
Peters, G. A., Hartmann, R., Qin, J., & Sen, G. C. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.6.1908-1920.2001 · Cited by 178
The Chaperone Protein BiP Binds to a Mutant Prion Protein and Mediates Its Degradation by the Proteasome
Jin, T., Gu, Y., Zanusso, G., Sy, M., Kumar, A., Cohen, M. L., Gambetti, P. L., & Singh, N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005543200 · Cited by 173
Protein folding in the ER
Stevens, F. J., & Argon, Y. (1999) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.1999.0315 · Cited by 170
Calcium signalling: a historical account, recent developments and future perspectives
Brini, M., & Carafoli, E. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000698 · Cited by 169
Pancreatic eukaryotic initiation factor-2α kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress
Sood, R., Porter, A. C., Kun, M. A., Quilliam, L. A., & Wek, R. C. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3460281 · Cited by 165
New aspects of calcium signaling in skeletal muscle cells: implications in Duchenne muscular dystrophy
Gailly, P. L. (2002) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/s1570-9639(02)00442-9 · Cited by 146
Translation of glucose-regulated protein 78/immunoglobulin heavy-chain binding protein mRNA is increased in poliovirus-infected cells at a time when cap-dependent translation of cellular mRNAs is inhibited.
Sarnow, P. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.15.5795 · Cited by 139
PROTEINASE-ACTIVATED RECEPTORS
Chambers, R. C. (2006) · Elsevier eBooks · doi:10.1016/b0-12-370879-6/00321-5 · Cited by 136
Inhibition of Translational Initiation by Activators of the Glucose-regulated Stress Protein and Heat Shock Protein Stress Response Systems
Brostrom, C. O., Prostko, C. R., Kaufman, R. J., & Brostrom, M. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.40.24995 · Cited by 129
Self-citation
BiP is feed-back regulated by control of protein translation efficiency
Gülow, K., Bienert, D., & Haas, I. G. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.11.2443 · Cited by 123
Ca2+oscillations, gradients, and homeostasis in vascular smooth muscle
Lee, C., Poburko, D., Kuo, K., Seow, C. Y., & van Breemen, C. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01035.2001 · Cited by 120
Endoplasmic Reticulum (ER)-associated Degradation of Misfolded N-Linked Glycoproteins Is Suppressed upon Inhibition of ER Mannosidase I
Tokunaga, F., Brostrom, C. O., Koide, T., & Arvan, P. R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001073200 · Cited by 119
Self-citation
Pancreatic eukaryotic initiation factor-2α kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress
Sood, R., Porter, A. C., Ma, K., et al. (2000) · Biochemical Journal · doi:10.1042/bj3460281 · Cited by 116
Molecules in focus Thrombin
Goldsack, N., Chambers, R. C., Dabbagh, K., & Laurent, G. J. (1998) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(98)00011-9 · Cited by 113
Organizational Diversity among Distinct Glycoprotein Endoplasmic Reticulum-associated Degradation Programs
Cabral, C. M., Liu, Y., Moremen, K. W., & Sifers, R. N. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-02-0068 · Cited by 109
Translational regulation in cell stress and apoptosis. Roles of the eIF4E binding proteins
Clemens, M. J. (2001) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2001.tb00157.x · Cited by 103
Uptake of Calcium by Mitochondria: Transport and Possible Function
Gunter, T. E., & Gunter, K. K. (2001) · IUBMB Life · doi:10.1080/15216540152846000 · Cited by 96
Thrombin as a Regulator of Inflammation and Reparative Processes in Tissues
Strukova, S. M. (2001) · Biochemistry (Moscow) · doi:10.1023/a:1002869310180 · Cited by 96
Regulation of Eukaryotic Initiation Factor eIF2B
Proud, C. G. (2001) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-56688-2_4 · Cited by 91
BiP Binding Keeps ATF6 at Bay
Sommer, T., & Jarosch, E. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00210-1 · Cited by 90
Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
Fassio, A., & Sitia, R. (2002) · Histochemistry and Cell Biology · doi:10.1007/s00418-001-0364-0 · Cited by 89
The Dynamic Role of GRP78/BiP in the Coordination of mRNA Translation with Protein Processing
Laitusis, A. L., Brostrom, M. A., & Brostrom, C. O. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.1.486 · Cited by 86
Self-citation
Calcium and mitosis
Whitaker, M., & Larman, M. G. (2001) · Seminars in Cell and Developmental Biology · doi:10.1006/scdb.2000.0217 · Cited by 83
Loss of Kinase Activity in a Patient With Wolcott-Rallison Syndrome Caused By a Novel Mutation in the EIF2AK3 Gene
Biason‐Lauber, A., Lang‐Muritano, M., Vaccaro, T., & Schoenle, E. J. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2301 · Cited by 72
Phas proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation
Lawrence, J. C., Fadden, P., Haystead, T., & Lin, T.-A. (1997) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(96)00016-7 · Cited by 69
Inhibition of Translational Initiation in Eukaryotic Cells by Calcium Ionophore
Brostrom, C. O., Chin, K., Wong, W. L., Cade, C., & Brostrom, M. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94235-3 · Cited by 64
Self-citation
Accommodation of protein synthesis to chronic deprivation of intracellular sequestered calcium. A putative role for GRP78
Brostrom, M. A., Cade, C., Prostko, C. R., Gmitter, D., & Brostrom, C. O. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30536-7 · Cited by 58
Self-citation
Translational control of gene expression: Role of IRESs and consequences for cell transformation and angiogenesis
Prats, A., & Prats, H. (2002) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(02)72075-8 · Cited by 53
Probing for Membrane Domains in the Endoplasmic Reticulum: Retention and Degradation of Unassembled MHC Class I Molecules
Spiliotis, E. T., Pentcheva, T., & Edidin, M. A. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-07-0322 · Cited by 51
Signal transduction mechanisms in the regulation of protein synthesis
Morley, S. (1994) · Molecular Biology Reports · doi:10.1007/bf00986964 · Cited by 48
Calcium ion activation of rabbit liver alpha 1,2-mannosidase.
Schutzbach, J. S., & Forsee, W. T. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39835-7 · Cited by 47
The Direct Binding of the Catalytic Subunit of Protein Phosphatase 1 to the PKR Protein Kinase Is Necessary but Not Sufficient for Inactivation and Disruption of Enzyme Dimer Formation
Tan, S., Tareen, S. U., Melville, M. W., Blakely, C. M., & Katze, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205109200 · Cited by 47
Regulation of protein synthesis in isolated hepatocytes by calcium-mobilizing hormones.
Brostrom, C. O., Bocckino, S. B., Brostrom, M. A., & Galuska, E. M. (1986) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10098-9 · Cited by 44
Self-citation
ATP-Dependent Dissociation of Non-Disulfide-Linked Aggregates of Coagulation Factor VIII Is a Rate-Limiting Step for Secretion
Tagliavacca, L., Wang, Q., & Kaufman, R. J. (2000) · Biochemistry · doi:10.1021/bi991896r · Cited by 40
ADP-ribosylation of the molecular chaperone GRP78/BiP
Ledford, B. E., & Leno, G. H. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf00928456 · Cited by 40
Thrombin Receptor Actions in Neonatal Rat Ventricular Myocytes
Jiang, T., Kuznetsov, V., Pak, E. S., Zhang, H., Robinson, R. B., & Steinberg, S. F. (1996) · Circulation Research · doi:10.1161/01.res.78.4.553 · Cited by 40
Regulation of the Endoplasmic Reticulum Calcium Storage During the Unfolded Protein Response—Significance in Tissue Ischemia?
Treiman, M. (2002) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(01)00147-5 · Cited by 40
Vasopressin-induced hypertrophy in H9c2 heart-derived myocytes
Brostrom, M. A., Reilly, B., Wilson, F. J., & Brostrom, C. O. (2000) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00037-6 · Cited by 39
Self-citation
Regulation of Protein Synthesis in Ventricular Myocytes by Vasopressin
Reilly, B., Brostrom, M. A., & Brostrom, C. O. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3747 · Cited by 38
Self-citation
The Thrombin Receptor Is Present in Myoblasts and Its Expression Is Repressed upon Fusion
Suidan, H. S., Niclou, S. P., Dreessen, J., Beltraminelli, N., & Monard, D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.29162 · Cited by 37
Does protein phosphorylation play a role in translational control by eukaryotic aminoacyl-tRNA synthetases?
Clemens, M. J. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90153-3 · Cited by 36
Endoplasmic Reticulum Stress Causes Thyroglobulin Retention in this Organelle and Triggers Activation of Nuclear Factor-κB Via Tumor Necrosis Factor Receptor-Associated Factor 2
Leonardi, A., Vito, P., Mauro, C., Pacifico, F., Ulianich, L., Consiglio, E., Formisano, S., & Jeso, B. D. (2002) · Endocrinology · doi:10.1210/endo.143.6.8825 · Cited by 35
P58IPK, a novel cochaperone containing tetratricopeptide repeats and a J-domain with oncogenic potential
Melville, M. W., Katze, M. G., & Tan, S. L. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000692 · Cited by 33
Analysis of the endoplasmic reticular Ca2+ requirement for α1-antitrypsin processing and transport competence
COOPER, G. R., Brostrom, C. O., & Brostrom, M. A. (1997) · Biochemical Journal · doi:10.1042/bj3250601 · Cited by 27
Self-citation
The importance of trimming reactions on asparagine-linked oligosaccharides for protein quality control
Roth, J., Zuber, C., Guhl, B., Fan, J., & Ziak, M. (2002) · Histochemistry and Cell Biology · doi:10.1007/s00418-001-0365-z · Cited by 27
Regulation of protein synthesis in intact rat liver by calcium mobilizing agents
Chin, K., Cade, C., Brostrom, M. A., & Brostrom, C. O. (1988) · International Journal of Biochemistry · doi:10.1016/0020-711x(88)90236-4 · Cited by 27
Self-citation
Signal Transduction of Arginine Vasopressin-Induced Arachidonic Acid Release in H9c2 Cardiac Myoblasts: Role of Ca 2+ and the Protein Kinase C-Dependent Activation of p42 Mitogen-Activated Protein Kinase 1
Chen, W., & Chen, C. (1999) · Endocrinology · doi:10.1210/endo.140.4.6654 · Cited by 26
Stimulation of GRP78 gene transcription by phorbol ester and cAMP in GH3 pituitary cells. The accommodation of protein synthesis to chronic deprivation of intracellular sequestered calcium.
Prostko, C. R., Brostrom, M. A., Galuska, E. M., & Brostrom, C. O. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55061-4 · Cited by 24
Self-citation
ATP Is Required for Correct Folding and Disulfide Bond Formation of Rotavirus VP7
Mirazimi, A., & Svensson, L. (2000) · Journal of Virology · doi:10.1128/jvi.74.17.8048-8052.2000 · Cited by 23
Regulated expression of GRP78 during vasopressin‐induced hypertrophy of heart‐derived myocytes
Brostrom, M. A., Mourad, F., & Brostrom, C. O. (2001) · Journal of Cellular Biochemistry · doi:10.1002/jcb.1219 · Cited by 23
Self-citation
The Thrombin Receptor Elevates Intracellular Calcium in Adult Rat Ventricular Myocytes
Jiang, T., Danilo, P., & Steinberg, S. F. (1998) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0779 · Cited by 22
Translational suppression by Ca2+ ionophores: Reversibility and roles of Ca2+ mobilization, Ca2+ influx, and nucleotide depletion
Gmitter, D., Brostrom, C. O., & Brostrom, M. A. (1996) · Cell Biology and Toxicology · doi:10.1007/bf00143360 · Cited by 18
Self-citation
Insulin, Phorbol Ester and Serum Regulate the Elongation Phase of Protein Synthesis
Traugh, J. A. (2001) · Progress in molecular and subcellular biology · doi:10.1007/978-3-642-56688-2_2 · Cited by 17
An Examination of the Role of Increased Cytosolic Free Ca2+Concentrations in the Inhibition of mRNA Translation
Laitusis, A. L., Brostrom, C. O., Ryazanov, A. G., & Brostrom, M. A. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0712 · Cited by 17
Self-citation
Receptors linked to polyphosphoinositide hydrolysis stimulate Ca2+ extrusion by a phospholipase C-independent mechanism
Broad, L. M., Cannon, T. R., Short, A. D., & Taylor, C. W. (1999) · Biochemical Journal · doi:10.1042/bj3420199 · Cited by 14
PDGF-BB-induced DNA synthesis is delayed by angiotensin II in vascular smooth muscle cells
Dahlfors, G., Chen, Y., Wasteson, M., & Arnqvist, H. J. (1998) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.1998.274.5.h1742 · Cited by 13
Functional receptor for platelet‐derived growth factor in rat embryonic heart‐derived myocytes: Role of sequestered Ca2+ stores in receptor signaling and antagonism by arginine vasopressin
Brostrom, M. A., Meiners, S. A., & Brostrom, C. O. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10085 · Cited by 11
Self-citation
Ca2+ dynamics of thrombin-stimulated rat heart-derived embryonic myocytes: relationship to protein synthesis and cell growth
Brostrom, M. A., Pan, Z., Meiners, S. A., Drumm, C., Ahmed, I., & Brostrom, C. O. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(03)00132-8 · Cited by 6
Self-citation

Sorted by citations

Mitochondria Supply Membranes for Autophagosome Biogenesis during Starvation
Hailey, D. W., Rambold, A. S., Satpute‐Krishnan, P., Mitra, K., Sougrat, R., Kim, P. K., & Lippincott‐Schwartz, J. (2010) · Cell · doi:10.1016/j.cell.2010.04.009 · Cited by 1,491
Physiology and Pathophysiology of the Calcium Store in the Endoplasmic Reticulum of Neurons
Verkhratsky, A. (2004) · Physiological Reviews · doi:10.1152/physrev.00004.2004 · Cited by 718
The Endoplasmic Reticulum: Folding, Calcium Homeostasis, Signaling, and Redox Control
Görlach, A., Klappa, P., & Kietzmann, T. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1391 · Cited by 627
Evidence of Placental Translation Inhibition and Endoplasmic Reticulum Stress in the Etiology of Human Intrauterine Growth Restriction
Yung, H.-W., Calabrese, S., Hynx, D., Hemmings, B. A., Cetin, I., Charnock-Jones, D. S., & Burton, G. J. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.071193 · Cited by 388
Biology of Endoplasmic Reticulum Stress in the Heart
Groenendyk, J., Sreenivasaiah, P. K., Kim, D. H., Agellon, L. B., & Michalak, M. (2010) · Circulation Research · doi:10.1161/circresaha.110.227033 · Cited by 319

See all 197

Authors: Brostrom, M. A., & Brostrom, C. O.
Corresponding author: Brostrom, Margaret A
Venue: Cell Calcium
Publisher: Elsevier BV
Published: 2003-10
Volume: 34
Issue: 4-5
Pages: 345-363
ISSN: 0143-4160 (ISSN-L)
DOI: 10.1016/s0143-4160(03)00127-1
OpenAlex: W2038563918
Cited by: 197
References: 124
Citations by year: 2026: 3 · 2025: 5 · 2024: 4 · 2023: 3 · 2022: 5 · 2021: 6 · 2020: 8 · 2019: 12 · 2018: 5 · 2017: 16 · 2016: 5 · 2015: 9 · 2014: 10 · 2013: 12 · 2012: 13
FWCI: 0.48
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell Calcium (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: endoplasmic reticulum calcium, ER calcium stores, unfolded protein response, endoplasmic reticulum stress, protein synthesis regulation, translational regulation, GRP78, ER chaperones, cytosolic free calcium, protein misfolding, embryonic cardiomyocytes, cell growth, ATP metabolism, mRNA translation regulation
MeSH terms: Endoplasmic Reticulum Chaperone BiP, Adenosine Triphosphate, Animals, Calcium, Carrier Proteins, Cell Division, Endoplasmic Reticulum, Gene Expression Regulation, Heat-Shock Proteins, Hormones, Humans, Hypertrophy, Models, Biological, Protein Processing, Post-Translational, Sarcoplasmic Reticulum, Protein Biosynthesis, Vasopressins, Eukaryotic Initiation Factor-2, Molecular Chaperones, Calcium Signaling, Myocytes, Cardiac

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

Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

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