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Hidden Agenda - The Involvement of Endoplasmic Reticulum Stress and Unfolded Protein Response in Inflammation-Induced Muscle Wasting

Kny, M., & Fielitz, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.878755 · Cited by 48

The Role of the Hypoxia-Related Unfolded Protein Response (UPR) in the Tumor Microenvironment

Bartoszewska, S., Collawn, J. F., & Bartoszewski, R. (2022) · Cancers · doi:10.3390/cancers14194870 · Cited by 43

The mTOR Signaling Pathway Interacts with the ER Stress Response and the Unfolded Protein Response in Cancer

Mafi, S., Ahmadi, E., Meehan, E. V., Chiari, C. C., Mansoori, B., Sadeghi, H., Milani, S., Jafarinia, M., Taeb, S., Bashmagh, B. M., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3032 · Cited by 43

Cardioprotection in ischaemia–reperfusion injury: novel mechanisms and clinical translation

Altamirano, F. J., Wang, Z. V., & Hill, J. A. (2015) · The Journal of Physiology · doi:10.1113/jp270953 · Cited by 43

Apoptosis induction associated with the ER stress response through up-regulation of JNK in HeLa cells by gambogic acid

Krajarng, A., Imoto, M., Tashiro, E., Fujimaki, T., Shinjo, S., & Watanapokasin, R. Y. (2015) · BMC Complementary and Alternative Medicine · doi:10.1186/s12906-015-0544-4 · Cited by 43

Alternative splicing alterations of Ca 2+ handling genes are associated with Ca 2+ signal dysregulation in myotonic dystrophy type 1 ( DM 1) and type 2 ( DM 2) myotubes

Santoro, M., Piacentini, R., Masciullo, M., Bianchi, M. L. E., Modoni, A., Podda, M. V., Ricci, E., Silvestri, G., & Grassi, C. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12076 · Cited by 43

The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation

Słomińska-Wojewódzka, M., & Sandvig, K. (2015) · Molecules · doi:10.3390/molecules20069816 · Cited by 46

AKT-mTOR signaling modulates the dynamics of IRE1 RNAse activity by regulating ER-mitochondria contacts

Sánchez‐Álvarez, M., del Pozo, M. Á., & Bakal, C. (2017) · Scientific Reports · doi:10.1038/s41598-017-16662-1 · Cited by 47

Melatonin Protects Against Neuronal Apoptosis via Suppression of the ATF6/CHOP Pathway in a Rat Model of Intracerebral Hemorrhage

Xu, W., Lu, X., Zheng, J., Li, T., Gao, L., Lenahan, C., Shao, A., Zhang, J., & Yu, J. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00638 · Cited by 43

Etoposide‐resistant HT‐29 human colon carcinoma cells during glucose deprivation are sensitive to piericidin A, a GRP78 down‐regulator

Hwang, J., Kim, J., Cha, M., Ryoo, I., Choo, S., Cho, S., Tsukumo, Y., Tomida, A., Shin‐ya, K., Hwang, Y., et al. (2007) · Journal of Cellular Physiology · doi:10.1002/jcp.21308 · Cited by 43

A Serine Protease Inhibitor Prevents Endoplasmic Reticulum Stress-induced Cleavage but Not Transport of the Membrane-bound Transcription Factor ATF6

Okada, T., Haze, K., Nadanaka, S., Yoshida, H., Seidah, N. G., Hirano, Y., Sato, R., Negishi, M., & Mori, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300923200 · Cited by 213

Dependence of Site-2 Protease Cleavage of ATF6 on Prior Site-1 Protease Digestion Is Determined by the Size of the Luminal Domain of ATF6

Shen, J., & Prywes, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408466200 · Cited by 149

ER stress signaling by regulated proteolysis of ATF6

Shen, J., & Prywes, R. (2005) · Methods · doi:10.1016/j.ymeth.2004.10.011 · Cited by 120

Role of Disulfide Bridges Formed in the Luminal Domain of ATF6 in Sensing Endoplasmic Reticulum Stress

Nadanaka, S., Okada, T., Yoshida, H., & Mori, K. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00408-06 · Cited by 268

Analysis of ATF6 Activation in Site-2 Protease-deficient Chinese Hamster Ovary Cells

Nadanaka, S., Yoshida, H., Sato, R., & Mori, K. (2006) · Cell Structure and Function · doi:10.1247/csf.06015 · Cited by 30