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PERK Utilizes Intrinsic Lipid Kinase Activity To Generate Phosphatidic Acid, Mediate Akt Activation, and Promote Adipocyte Differentiation

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1992.tb05426.xopenalex-snapshot

Phosphatidylinositol 3′‐kinase is activated by association with IRS‐1 during insulin stimulation.

inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06289.xopenalex-snapshot

PI 3‐kinase: structural and functional analysis of intersubunit interactions.

inferredcites →https://doi.org/10.1016/j.abb.2004.09.032openalex-snapshot

The iSH2 domain of PI 3-kinase is a rigid tether for p110 and not a conformational switch

inferredcites →https://doi.org/10.1016/j.plipres.2009.06.001openalex-snapshot

Mammalian phosphoinositide kinases and phosphatases

inferredcites →https://doi.org/10.1016/j.semcancer.2008.11.010openalex-snapshot

Is Akt the “Warburg kinase”?—Akt-energy metabolism interactions and oncogenesis

inferredcites →https://doi.org/10.1016/s0005-2760(97)00105-7openalex-snapshot

Phosphatidylinositol synthase from mammalian tissues

inferredcites →https://doi.org/10.1016/s0009-3084(99)00019-5openalex-snapshot

Pathways for phosphoinositide synthesis

inferredcites →https://doi.org/10.1016/s0021-9258(18)92935-2openalex-snapshot

De novo synthesis of diacylglycerol from glucose. A new pathway of signal transduction in human neutrophils stimulated during phagocytosis of beta-glucan particles

inferredcites →https://doi.org/10.1016/s0021-9258(18)98375-4openalex-snapshot

Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85-kDa subunit

inferredcites →https://doi.org/10.1016/s0021-9258(19)61473-0openalex-snapshot

Activation of ATF6 and an ATF6 DNA Binding Site by the Endoplasmic Reticulum Stress Response

inferredcites →https://doi.org/10.1016/s0898-6568(01)00158-9openalex-snapshot

Phosphoinositides : key players in cell signalling, in time and space

inferredcites →https://doi.org/10.1016/s1097-2765(01)00265-9openalex-snapshot

Translational Control Is Required for the Unfolded Protein Response and In Vivo Glucose Homeostasis

inferredcites →https://doi.org/10.1023/a:1006102411439openalex-snapshot

De‐regulation of GRP stress protein expression in human breast cancer cell lines

inferredcites →https://doi.org/10.1023/a:1006332011207openalex-snapshot

Overexpression of the glucose-regulated stress gene GRP78 in malignant but not benign human breast lesions

inferredcites →https://doi.org/10.1038/16729openalex-snapshot

Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

inferredcites →https://doi.org/10.1038/ncb1592openalex-snapshot

The lymphocyte function-associated antigen-1 receptor costimulates plasma membrane Ras via phospholipase D2

inferredcites →https://doi.org/10.1038/ncb1594openalex-snapshot

Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos

inferredcites →https://doi.org/10.1038/nm.2099openalex-snapshot

The regulatory subunits of PI3K, p85α and p85β, interact with XBP-1 and increase its nuclear translocation

inferredcites →https://doi.org/10.1038/nm.2121openalex-snapshot

A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box–binding protein-1 to modulate the unfolded protein response

inferredcites →https://doi.org/10.1038/nrc2842openalex-snapshot

Phosphoinositide signalling in cancer: beyond PI3K and PTEN

inferredcites →https://doi.org/10.1038/nrg1879openalex-snapshot

The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism

inferredcites →https://doi.org/10.1038/onc.2008.428openalex-snapshot

PERK-dependent regulation of IAP translation during ER stress

inferredcites →https://doi.org/10.1038/onc.2010.153openalex-snapshot

PERK promotes cancer cell proliferation and tumor growth by limiting oxidative DNA damage

inferredcites →https://doi.org/10.1038/sj.emboj.7600777openalex-snapshot

ER stress‐regulated translation increases tolerance to extreme hypoxia and promotes tumor growth

inferredcites →https://doi.org/10.1042/bj20071040openalex-snapshot

Diacylglycerol kinases: at the hub of cell signalling

inferredcites →https://doi.org/10.1042/bj2320485openalex-snapshot

Regulation of the translocation of phosphatidate phosphohydrolase between the cytosol and the endoplasmic reticulum of rat liver. Effects of unsaturated fatty acids, spermine, nucleotides, albumin and chlorpromazine

inferredcites →https://doi.org/10.1073/pnas.0607899103openalex-snapshot

The p110α isoform of PI3K is essential for proper growth factor signaling and oncogenic transformation

inferredcites →https://doi.org/10.1073/pnas.0800939105openalex-snapshot

ATF6α-Rheb-mTOR signaling promotes survival of dormant tumor cells in vivo

inferredcites →https://doi.org/10.1073/pnas.0808517105openalex-snapshot

PERK-dependent regulation of lipogenesis during mouse mammary gland development and adipocyte differentiation

inferredcites →https://doi.org/10.1073/pnas.1110730109openalex-snapshot

Glycerolipid signals alter mTOR complex 2 (mTORC2) to diminish insulin signaling

inferredcites →https://doi.org/10.1073/pnas.83.18.6785openalex-snapshot

Rapid formation of diacylglycerol from phosphatidylcholine: a pathway for generation of a second messenger.

inferredcites →https://doi.org/10.1074/jbc.274.2.1131openalex-snapshot

Phospholipase D and Its Product, Phosphatidic Acid, Mediate Agonist-dependent Raf-1 Translocation to the Plasma Membrane and the Activation of the Mitogen-activated Protein Kinase Pathway

inferredcites →https://doi.org/10.1074/jbc.m110.153007openalex-snapshot

Heterogeneity of Phosphatidic Acid Levels and Distribution at the Plasma Membrane in Living Cells as Visualized by a Förster Resonance Energy Transfer (FRET) Biosensor

inferredcites →https://doi.org/10.1074/jbc.m110.168575openalex-snapshot

PKCδ Is Activated in a Dietary Model of Steatohepatitis and Regulates Endoplasmic Reticulum Stress and Cell Death

inferredcites →https://doi.org/10.1074/jbc.m407700200openalex-snapshot

Critical Role of Endogenous Akt/IAPs and MEK1/ERK Pathways in Counteracting Endoplasmic Reticulum Stress-induced Cell Death

inferredcites →https://doi.org/10.1074/jbc.m412296200openalex-snapshot

Modulation of the Mammalian Target of Rapamycin Pathway by Diacylglycerol Kinase-produced Phosphatidic Acid

inferredcites →https://doi.org/10.1083/jcb.200406136openalex-snapshot

XBP1

inferredcites →https://doi.org/10.1091/mbc.01-12-0584openalex-snapshot

Akt Maintains Cell Size and Survival by Increasing mTOR-dependent Nutrient Uptake

inferredcites →https://doi.org/10.1091/mbc.10.11.3787openalex-snapshot

Mammalian Transcription Factor ATF6 Is Synthesized as a Transmembrane Protein and Activated by Proteolysis in Response to Endoplasmic Reticulum Stress

inferredcites →https://doi.org/10.1091/mbc.e06-07-0593openalex-snapshot

Cytokine Stimulation Promotes Glucose Uptake via Phosphatidylinositol-3 Kinase/Akt Regulation of Glut1 Activity and Trafficking

inferredcites →https://doi.org/10.1091/mbc.e07-01-0053openalex-snapshot

A Novel Function of eIF2α Kinases as Inducers of the Phosphoinositide-3 Kinase Signaling Pathway

inferredcites →https://doi.org/10.1093/emboj/17.19.5708openalex-snapshot

Cloning of mammalian Ire1 reveals diversity in the ER stress responses

inferredcites →https://doi.org/10.1101/gad.12.12.1812openalex-snapshot

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

inferredcites →https://doi.org/10.1101/gad.889901openalex-snapshot

Inhibition of early apoptotic events by Akt/PKB is dependent on the first committed step of glycolysis and mitochondrial hexokinase

inferredcites →https://doi.org/10.1126/science.1066015openalex-snapshot

Phosphatidic Acid-Mediated Mitogenic Activation of mTOR Signaling

inferredcites →https://doi.org/10.1126/science.1158042openalex-snapshot

Regulation of Hepatic Lipogenesis by the Transcription Factor XBP1

inferredcites →https://doi.org/10.1128/mcb.00782-08openalex-snapshot

Regulation of mTORC1 and mTORC2 Complex Assembly by Phosphatidic Acid: Competition with Rapamycin

inferredcites →https://doi.org/10.1128/mcb.01145-06openalex-snapshot

Perk-Dependent Translational Regulation Promotes Tumor Cell Adaptation and Angiogenesis in Response to Hypoxic Stress

inferredcites →https://doi.org/10.1128/mcb.18.12.7499openalex-snapshot

Identification and Characterization of Pancreatic Eukaryotic Initiation Factor 2 α-Subunit Kinase, PEK, Involved in Translational Control

inferredcites →https://doi.org/10.1128/mcb.20.14.5096-5106.2000openalex-snapshot

ATF6 as a Transcription Activator of the Endoplasmic Reticulum Stress Element: Thapsigargin Stress-Induced Changes and Synergistic Interactions with NF-Y and YY1

inferredcites →https://doi.org/10.1128/mcb.23.20.7198-7209.2003openalex-snapshot

Nrf2 Is a Direct PERK Substrate and Effector of PERK-Dependent Cell Survival

inferredcites →https://doi.org/10.1128/mcb.25.7.2593-2606.2005openalex-snapshot

Role of Phosphoinositide 3-Kinase Regulatory Isoforms in Development and Actin Rearrangement

inferredcites →https://doi.org/10.1158/0008-5472.can-03-2904openalex-snapshot

Akt Stimulates Aerobic Glycolysis in Cancer Cells

inferredcites →https://doi.org/10.1194/jlr.r800049-jlr200openalex-snapshot

Membrane phospholipid synthesis and endoplasmic reticulum function

inferredcites →https://doi.org/10.1385/1-59259-377-1:127openalex-snapshot

Measuring Insulin-Stimulated Phosphatidyl-Inositol 3-Kinase Activity

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4639349openalex-extracted

Protein-Rich Foods, Sea Foods, and Gut Microbiota Amplify Immune Responses in Chronic Diseases and Cancers – Targeting Perk as a Novel Therapeutic Strategy for Cancer

inferred← citeshttps://doi.org/10.1002/glia.24525openalex-snapshot

Oligodendrocyte‐selective deletion of the eIF2α kinase Perk/Eif2ak3 limits functional recovery after spinal cord injury

inferred← citeshttps://doi.org/10.1002/jcp.25336openalex-snapshot

PERK Integrates Oncogenic Signaling and Cell Survival During Cancer Development

inferred← citeshttps://doi.org/10.1002/pro.70703openalex-snapshot

Mitochondrial membrane remodeling in stress adaptation: Lipid control of organelle quality

inferred← citeshttps://doi.org/10.1007/978-3-030-37297-2_8openalex-snapshot

Role of Endoplasmic Reticulum ER Stress-Induced Cell Death Mechanisms

inferred← citeshttps://doi.org/10.1007/978-3-031-63657-8_7openalex-snapshot

Protein Kinases in Obesity, and the Kinase-Targeted Therapy

inferred← citeshttps://doi.org/10.1007/978-3-319-48382-5_5openalex-snapshot

Human Protein Kinases and Obesity

inferred← citeshttps://doi.org/10.1007/s00018-021-03849-zopenalex-snapshot

ER residential chaperone GRP78 unconventionally relocalizes to the cell surface via endosomal transport

inferred← citeshttps://doi.org/10.1007/s00262-020-02740-3openalex-snapshot

Stress relief for cancer immunotherapy: implications for the ER stress response in tumor immunity

inferred← citeshttps://doi.org/10.1007/s12035-022-02826-2openalex-snapshot

Lipid Dyshomeostasis and Inherited Cerebellar Ataxia

inferred← citeshttps://doi.org/10.1007/s12192-018-0905-2openalex-snapshot

Effect of the unfolded protein response on ER protein export: a potential new mechanism to relieve ER stress

inferred← citeshttps://doi.org/10.1007/s12250-019-00107-2openalex-snapshot

Prion Protein Protects Cancer Cells against Endoplasmic Reticulum Stress Induced Apoptosis

inferred← citeshttps://doi.org/10.1016/b978-0-12-822481-6.00012-8openalex-snapshot

Endoplasmic reticulum stress-induced cell death mechanism

inferred← citeshttps://doi.org/10.1016/j.bbadis.2020.165799openalex-snapshot

Regulation of the cerebrovascular smooth muscle cell phenotype by mitochondrial oxidative injury and endoplasmic reticulum stress in simulated microgravity rats via the PERK-eIF2α-ATF4-CHOP pathway

inferred← citeshttps://doi.org/10.1016/j.bbagen.2018.12.009openalex-snapshot

M(en)TORship lessons on life and death by the integrated stress response

inferred← citeshttps://doi.org/10.1016/j.bbagrm.2014.12.007openalex-snapshot

Roles of the translation initiation factor eIF2α serine 51 phosphorylation in cancer formation and treatment

inferred← citeshttps://doi.org/10.1016/j.bbalip.2024.159515openalex-snapshot

The lipid side of unfolded protein response

inferred← citeshttps://doi.org/10.1016/j.biocel.2024.106598openalex-snapshot

Endoplasmic reticulum: Monitoring and maintaining protein and membrane homeostasis in the endoplasmic reticulum by the unfolded protein response

inferred← citeshttps://doi.org/10.1016/j.cell.2024.09.029openalex-snapshot

Structural basis of respiratory complex adaptation to cold temperatures

inferred← citeshttps://doi.org/10.1016/j.celrep.2013.09.046openalex-snapshot

Xbp1-Independent Ire1 Signaling Is Required for Photoreceptor Differentiation and Rhabdomere Morphogenesis in Drosophila

inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2015.07.012openalex-snapshot

Redox modulation of adipocyte differentiation: hypothesis of “Redox Chain” and novel insights into intervention of adipogenesis and obesity

inferred← citeshttps://doi.org/10.1016/j.isci.2021.103448openalex-snapshot

Integrated stress response regulates GDF15 secretion from adipocytes, preferentially suppresses appetite for a high-fat diet and improves obesity

inferred← citeshttps://doi.org/10.1016/j.lfs.2018.11.041openalex-snapshot

Emerging role of Unfolded Protein Response (UPR) mediated proteotoxic apoptosis in diabetes

inferred← citeshttps://doi.org/10.1016/j.mce.2017.05.027openalex-snapshot

ER stress and cancer: The FOXO forkhead transcription factor link

inferred← citeshttps://doi.org/10.1016/j.molcel.2015.06.020openalex-snapshot

ERK2 Mediates Metabolic Stress Response to Regulate Cell Fate

inferred← citeshttps://doi.org/10.1016/j.molcel.2017.01.020openalex-snapshot

The ER Stress Sensor PERK Coordinates ER-Plasma Membrane Contact Site Formation through Interaction with Filamin-A and F-Actin Remodeling

inferred← citeshttps://doi.org/10.1016/j.pharmthera.2024.108604openalex-snapshot

Protein-rich foods, sea foods, and gut microbiota amplify immune responses in chronic diseases and cancers – Targeting PERK as a novel therapeutic strategy for chronic inflammatory diseases, neurodegenerative disorders, and cancer

inferred← citeshttps://doi.org/10.1016/j.phrs.2026.108374openalex-snapshot

Endoplasmic reticulum stress-driven inflammatory mediators in metabolic disorders: From molecular mechanisms to targeted therapies

inferred← citeshttps://doi.org/10.1016/j.semcancer.2015.03.010openalex-snapshot

The PERKs of damage-associated molecular patterns mediating cancer immunogenicity: From sensor to the plasma membrane and beyond

inferred← citeshttps://doi.org/10.1016/j.semcancer.2018.01.011openalex-snapshot

Homeostatic interplay between FoxO proteins and ER proteostasis in cancer and other diseases

inferred← citeshttps://doi.org/10.1016/j.tem.2013.02.003openalex-snapshot

Phosphatidic acid and lipid-sensing by mTOR

inferred← citeshttps://doi.org/10.1016/j.tem.2015.05.007openalex-snapshot

Targeting endoplasmic reticulum stress in insulin resistance

inferred← citeshttps://doi.org/10.1016/j.trecan.2022.06.006openalex-snapshot

Decoding endoplasmic reticulum stress signals in cancer cells and antitumor immunity

inferred← citeshttps://doi.org/10.1016/j.yexcr.2018.12.009openalex-snapshot

PERK is essential for proliferation of intestinal stem cells in mice

inferred← citeshttps://doi.org/10.1038/cddis.2017.369openalex-snapshot

PDI is an essential redox-sensitive activator of PERK during the unfolded protein response (UPR)

inferred← citeshttps://doi.org/10.1038/nature17041openalex-snapshot

Protein misfolding in the endoplasmic reticulum as a conduit to human disease

inferred← citeshttps://doi.org/10.1038/ncomms11422openalex-snapshot

miR-216b regulation of c-Jun mediates GADD153/CHOP-dependent apoptosis

inferred← citeshttps://doi.org/10.1038/nrc3800openalex-snapshot

The impact of the endoplasmic reticulum protein-folding environment on cancer development

inferred← citeshttps://doi.org/10.1038/onc.2012.439openalex-snapshot

Anti-tumorigenic effects of Type 1 interferon are subdued by integrated stress responses

inferred← citeshttps://doi.org/10.1038/onc.2015.178openalex-snapshot

Tumor progression and the different faces of the PERK kinase

inferred← citeshttps://doi.org/10.1038/s41388-019-0890-7openalex-snapshot

Regulation of PERK expression by FOXO3: a vulnerability of drug-resistant cancer cells

inferred← citeshttps://doi.org/10.1038/s41392-025-02439-wopenalex-snapshot

Navigating the landscape of protein folding and proteostasis: from molecular chaperones to therapeutic innovations

inferred← citeshttps://doi.org/10.1038/s41467-019-08908-5openalex-snapshot

Ufbp1 promotes plasma cell development and ER expansion by modulating distinct branches of UPR

inferred← citeshttps://doi.org/10.1038/s41556-024-01555-zopenalex-snapshot

Chaperone-mediated insertion of mitochondrial import receptor TOM70 protects against diet-induced obesity

inferred← citeshttps://doi.org/10.1038/s41568-020-00312-2openalex-snapshot

Endoplasmic reticulum stress signals in the tumour and its microenvironment

inferred← citeshttps://doi.org/10.1038/s44319-023-00027-zopenalex-snapshot

UBXN1 maintains ER proteostasis and represses UPR activation by modulating translation

inferred← citeshttps://doi.org/10.1038/srep09065openalex-snapshot

PERK silence inhibits glioma cell growth under low glucose stress by blockage of p-AKT and subsequent HK2's mitochondria translocation

inferred← citeshttps://doi.org/10.1073/pnas.2214957119openalex-snapshot

Selective involvement of UGGT variant: UGGT2 in protecting mouse embryonic fibroblasts from saturated lipid-induced ER stress

inferred← citeshttps://doi.org/10.1073/pnas.2517552122openalex-snapshot

Drug repurposing screen identifies an HRI activating compound that promotes adaptive mitochondrial remodeling in MFN2-deficient cells

inferred← citeshttps://doi.org/10.1074/jbc.m113.543215openalex-snapshot

Translational Control during Endoplasmic Reticulum Stress beyond Phosphorylation of the Translation Initiation Factor eIF2α

inferred← citeshttps://doi.org/10.1074/jbc.m114.551069openalex-snapshot

The Nuclear Receptor Peroxisome Proliferator-activated Receptor-β/δ (PPARβ/δ) Promotes Oncogene-induced Cellular Senescence through Repression of Endoplasmic Reticulum Stress

inferred← citeshttps://doi.org/10.1074/jbc.r114.566091openalex-snapshot

Phospholipase D and the Maintenance of Phosphatidic Acid Levels for Regulation of Mammalian Target of Rapamycin (mTOR)

inferred← citeshttps://doi.org/10.1074/jbc.ra118.002124openalex-snapshot

Hairy and enhancer of split 1 (HES1) protects cells from endoplasmic reticulum stress–induced apoptosis through repression of

inferred← citeshttps://doi.org/10.1091/mbc.e15-02-0074openalex-snapshot

Ire1-mediated decay in mammalian cells relies on mRNA sequence, structure, and translational status

inferred← citeshttps://doi.org/10.1091/mbc.e23-11-0419openalex-snapshot

Baseline unfolded protein response signaling adjusts the timing of the mammalian cell cycle

inferred← citeshttps://doi.org/10.1093/sleep/zsy186openalex-snapshot

Identifying and validating blood mRNA biomarkers for acute and chronic insufficient sleep in humans: a machine learning approach

inferred← citeshttps://doi.org/10.1101/2025.10.08.681090openalex-snapshot

PERK inhibition rewires translational and CMGC protein kinase networks into an antiviral state

inferred← citeshttps://doi.org/10.1101/gad.201731.112openalex-snapshot

ER stress potentiates insulin resistance through PERK-mediated FOXO phosphorylation

inferred← citeshttps://doi.org/10.1111/cpr.13011openalex-snapshot

PERK signaling pathway in bone metabolism: Friend or foe?

inferred← citeshttps://doi.org/10.1126/scisignal.2004373openalex-snapshot

The ζ Isoform of Diacylglycerol Kinase Plays a Predominant Role in Regulatory T Cell Development and TCR-Mediated Ras Signaling

inferred← citeshttps://doi.org/10.1126/scisignal.aac4380openalex-snapshot

ATF4 induction through an atypical integrated stress response to ONC201 triggers p53-independent apoptosis in hematological malignancies

inferred← citeshttps://doi.org/10.1128/mbio.00167-21openalex-snapshot

Human Cytomegalovirus Uses a Host Stress Response To Balance the Elongation of Saturated/Monounsaturated and Polyunsaturated Very-Long-Chain Fatty Acids

inferred← citeshttps://doi.org/10.1134/s000629792209005xopenalex-snapshot

The Role of Endoplasmic Reticulum Stress in Differentiation of Cells of Mesenchymal Origin

inferred← citeshttps://doi.org/10.1152/ajpheart.00682.2022openalex-snapshot

mTORC1 inhibition impairs activation of the unfolded protein response and induces cell death during ER stress in cardiomyocytes

inferred← citeshttps://doi.org/10.1155/2019/1608787openalex-snapshot

The Best for the Most Important: Maintaining a Pristine Proteome in Stem and Progenitor Cells

inferred← citeshttps://doi.org/10.1158/2159-8290.cd-14-1490openalex-snapshot

Endoplasmic Reticulum Stress–Activated Cell Reprogramming in Oncogenesis

inferred← citeshttps://doi.org/10.1158/2159-8290.cd-18-0348openalex-snapshot

ER Translocation of the MAPK Pathway Drives Therapy Resistance in BRAF-Mutant Melanoma

inferred← citeshttps://doi.org/10.1159/000475915openalex-snapshot

Roles of the Exogenous H2S-Mediated SR-A Signaling Pathway in Renal Ischemia/ Reperfusion Injury in Regulating Endoplasmic Reticulum Stress-Induced Autophagy in a Rat Model

inferred← citeshttps://doi.org/10.1177/2515256418770512openalex-snapshot

The Unfolded Protein Response and Membrane Contact Sites: Tethering as a Matter of Life and Death?

inferred← citeshttps://doi.org/10.1182/blood.2020007975openalex-snapshot

ER-associated degradation preserves hematopoietic stem cell quiescence and self-renewal by restricting mTOR activity

inferred← citeshttps://doi.org/10.1182/blood.2024027846openalex-snapshot

PERK signaling maintains hematopoietic stem cell pool integrity under endoplasmic reticulum stress by promoting proliferation

inferred← citeshttps://doi.org/10.1186/s12943-026-02674-xopenalex-snapshot

Endoplasmic reticulum stress in antitumor immunity and immunotherapy resistance: mechanisms and therapeutic implications

inferred← citeshttps://doi.org/10.1186/s12986-017-0166-6openalex-snapshot

Phosphatidic acid: biosynthesis, pharmacokinetics, mechanisms of action and effect on strength and body composition in resistance-trained individuals

inferred← citeshttps://doi.org/10.1186/s13041-016-0268-5openalex-snapshot

PERK regulates Gq protein-coupled intracellular Ca2+ dynamics in primary cortical neurons

inferred← citeshttps://doi.org/10.1242/jcs.221218openalex-snapshot

Gli2 modulates cell cycle re-entry through autophagy-mediated regulation of the length of primary cilia

inferred← citeshttps://doi.org/10.12688/f1000research.12138.1openalex-snapshot

Recent insights into PERK-dependent signaling from the stressed endoplasmic reticulum

inferred← citeshttps://doi.org/10.1371/journal.pgen.1006518openalex-snapshot

PERK Is a Haploinsufficient Tumor Suppressor: Gene Dose Determines Tumor-Suppressive Versus Tumor Promoting Properties of PERK in Melanoma

inferred← citeshttps://doi.org/10.1371/journal.ppat.1003266openalex-snapshot

PKR-Like Endoplasmic Reticulum Kinase Is Necessary for Lipogenic Activation during HCMV Infection

inferred← citeshttps://doi.org/10.14218/erhm.2018.00003openalex-snapshot

The Role of Endoplasmic Reticulum Stress in the Development of Fibrosis in Crohn’s Disease

inferred← citeshttps://doi.org/10.15252/embj.2023113908openalex-snapshot

PERK signaling promotes mitochondrial elongation by remodeling membrane phosphatidic acid

inferred← citeshttps://doi.org/10.1530/ec-20-0608openalex-snapshot

Androgens impair β-cell function in a mouse model of polycystic ovary syndrome by activating endoplasmic reticulum stress

inferred← citeshttps://doi.org/10.1530/joe-17-0497openalex-snapshot

Attenuation of PERK enhances glucose-stimulated insulin secretion in islets

inferred← citeshttps://doi.org/10.18632/oncotarget.15469openalex-snapshot

mTOR inhibitors activate PERK signaling and favor viability of gastrointestinal neuroendocrine cell lines

inferred← citeshttps://doi.org/10.21203/rs.3.rs-4831443/v1openalex-snapshot

A chaperone-assisted mechanism of outer mitochondrial membrane TOM70 insertion protective against diet-induced obesity

inferred← citeshttps://doi.org/10.2174/1566524016666160523143937openalex-snapshot

The Role of the PERK/eIF2α/ATF4/CHOP Signaling Pathway in Tumor Progression During Endoplasmic Reticulum Stress

inferred← citeshttps://doi.org/10.2217/fon.13.49openalex-snapshot

Control of Oncogenesis by eIF2α Phosphorylation: Implications in PTEN and PI3K–Akt Signaling and Tumor Treatment

inferred← citeshttps://doi.org/10.3109/10715762.2012.760198openalex-snapshot

Protective effect of quercetin on lead-induced oxidative stress and endoplasmic reticulum stress in rat liver via the IRE1/JNK and PI3K/Akt pathway

inferred← citeshttps://doi.org/10.3389/fcell.2020.00675openalex-snapshot

Sticking With It: ER-PM Membrane Contact Sites as a Coordinating Nexus for Regulating Lipids and Proteins at the Cell Cortex

inferred← citeshttps://doi.org/10.3389/fcell.2022.867341openalex-snapshot

The ER-Mitochondria Interface as a Dynamic Hub for T Cell Efficacy in Solid Tumors

inferred← citeshttps://doi.org/10.3389/fcell.2022.988014openalex-snapshot

ER-mitochondria contact sites; a multifaceted factory for Ca2+ signaling and lipid transport

inferred← citeshttps://doi.org/10.3389/fcell.2023.1271141openalex-snapshot

Signaling plasticity in the integrated stress response

inferred← citeshttps://doi.org/10.3389/fendo.2020.580879openalex-snapshot

Mitochondrial Dynamics in the Brain Are Associated With Feeding, Glucose Homeostasis, and Whole-Body Metabolism

inferred← citeshttps://doi.org/10.3389/fmolb.2024.1356500openalex-snapshot

Navigating the landscape of mitochondrial-ER communication in health and disease

inferred← citeshttps://doi.org/10.3389/fonc.2017.00174openalex-snapshot

Mitochondria-Associated Membranes As Networking Platforms and Regulators of Cancer Cell Fate

inferred← citeshttps://doi.org/10.3389/fphar.2020.00737openalex-snapshot

CCT020312 Inhibits Triple-Negative Breast Cancer Through PERK Pathway-Mediated G1 Phase Cell Cycle Arrest and Apoptosis

inferred← citeshttps://doi.org/10.3390/antiox11091845openalex-snapshot

The Impact of Oxidative Stress and AKT Pathway on Cancer Cell Functions and Its Application to Natural Products

inferred← citeshttps://doi.org/10.3390/biology13121074openalex-snapshot

Combined Association of Plasma Metabolites with Body Mass Index and Physical Activity Level

inferred← citeshttps://doi.org/10.3390/biom15020248openalex-snapshot

PERK-Olating Through Cancer: A Brew of Cellular Decisions

inferred← citeshttps://doi.org/10.3390/biomedicines9020156openalex-snapshot

The Structure, Activation and Signaling of IRE1 and Its Role in Determining Cell Fate

inferred← citeshttps://doi.org/10.3390/cancers12092385openalex-snapshot

Proteotoxic Stress and Cell Death in Cancer Cells

inferred← citeshttps://doi.org/10.3390/cancers17223639openalex-snapshot

The Unfolded Protein Response—Novel Mechanisms, Challenges, and Key Considerations for Therapeutic Intervention

inferred← citeshttps://doi.org/10.3390/cells9030540openalex-snapshot

Translational Regulations in Response to Endoplasmic Reticulum Stress in Cancers

inferred← citeshttps://doi.org/10.3390/ijms20184354openalex-snapshot

Dual role of Endoplasmic Reticulum Stress-Mediated Unfolded Protein Response Signaling Pathway in Carcinogenesis

inferred← citeshttps://doi.org/10.3390/molecules25030599openalex-snapshot

Baicalein Alleviates Liver Oxidative Stress and Apoptosis Induced by High-Level Glucose through the Activation of the PERK/Nrf2 Signaling Pathway

inferred← citeshttps://doi.org/10.3390/nu15245082openalex-snapshot

Endoplasmic Reticulum Stress and Its Impact on Adipogenesis: Molecular Mechanisms Implicated

inferred← citeshttps://doi.org/10.3390/nu6010124openalex-snapshot

Non-Alcoholic Steatohepatitis and Hepatocellular Carcinoma: Implications for Lycopene Intervention

inferred← citeshttps://doi.org/10.3390/pharmaceutics15082051openalex-snapshot

Inhibition of Protein Aggregation and Endoplasmic Reticulum Stress as a Targeted Therapy for α-Synucleinopathy

inferred← citeshttps://doi.org/10.3892/mmr.2016.5867openalex-snapshot

Post-translational modifications of FOXO family proteins

inferred← citeshttps://doi.org/10.4161/cbt.29274openalex-snapshot

Generation and characterization of an analog-sensitive PERK allele

inferred← citeshttps://doi.org/10.4161/cl.27732openalex-snapshot

Novel effects of Brefeldin A (BFA) in signaling through the insulin receptor (IR) pathway and regulating FoxO1-mediated transcription

inferred← citeshttps://doi.org/10.70675/0eeb3943z19c5z46a0z925ez8a79ca99ba3eopenalex-snapshot

Implication de l’acide phosphatidique dans le trafic membranaire : rôle et régulation de la phospholipase D au cours de la phagocytose et de l’exocytose régulée

inferred← citeshttps://doi.org/10.70675/a7f68586zb194z4f22z9adbz62a1d34b7bc0openalex-snapshot

Stress du réticulum endoplasmique dans les leucémies aiguës myéloïdes : rôle et régulation du facteur de transcription XBP1

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