Search Results - "Lee, Amy S"
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Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential
Published in Nature reviews. Cancer (01-04-2014)“…Key Points The glucose-regulated proteins (GRPs) GRP78, GRP94, GRP170 and GRP75, are members of the heat shock protein family. They primarily reside in the…”
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Role of the unfolded protein response, GRP78 and GRP94 in organ homeostasis
Published in Journal of cellular physiology (01-07-2015)“…The endoplasmic reticulum (ER) is a cellular organelle where secretory and membrane proteins, as well as lipids, are synthesized and modified. When cells are…”
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GRP78 induction in cancer : Therapeutic and prognostic implications
Published in Cancer research (Chicago, Ill.) (15-04-2007)“…Cancer cells adapt to chronic stress in the tumor microenvironment by inducing the expression of GRP78/BiP, a major endoplasmic reticulum chaperone with…”
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Beyond the endoplasmic reticulum: atypical GRP78 in cell viability, signalling and therapeutic targeting
Published in Biochemical journal (01-03-2011)“…GRP78 (glucose-regulated protein of 78 kDa) is traditionally regarded as a major ER (endoplasmic reticulum) chaperone facilitating protein folding and…”
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ER chaperones in mammalian development and human diseases
Published in FEBS letters (31-07-2007)“…The field of endoplasmic reticulum (ER) stress in mammalian cells has expanded rapidly during the past decade, contributing to understanding of the molecular…”
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The critical role of GRP78 in physiologic and pathologic stress
Published in Current opinion in cell biology (01-04-2011)“…GRP78 is a major endoplasmic reticulum chaperone as well as a master regulator of the unfolded protein response. In addition to playing an essential role in…”
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The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection
Published in The Journal of biological chemistry (01-01-2021)“…The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of the COVID-19 global pandemic, utilizes the host receptor…”
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Peroxisomes Are Signaling Platforms for Antiviral Innate Immunity
Published in Cell (14-05-2010)“…Peroxisomes have long been established to play a central role in regulating various metabolic activities in mammalian cells. These organelles act in concert…”
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eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation
Published in Nature (London) (04-08-2016)“…The initiation protein eIF3d serves as an alternative cap-recognition factor for a subclass of mRNAs, such as c-Jun; the high-resolution structure of the eIF3d…”
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Grp78 Loss in Epithelial Progenitors Reveals an Age-linked Role for Endoplasmic Reticulum Stress in Pulmonary Fibrosis
Published in American journal of respiratory and critical care medicine (15-01-2020)“…Alveolar epithelial cell (AEC) injury and dysregulated repair are implicated in the pathogenesis of pulmonary fibrosis. Endoplasmic reticulum (ER) stress in…”
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The ER chaperone and signaling regulator GRP78/BiP as a monitor of endoplasmic reticulum stress
Published in Methods (San Diego, Calif.) (01-04-2005)“…The multiple implications of ER stress and the unfolded protein response in health and disease highlight the importance of identifying convenient monitoring…”
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The stress-inducible ER chaperone GRP78/BiP is upregulated during SARS-CoV-2 infection and acts as a pro-viral protein
Published in Nature communications (14-11-2022)Get full text
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GRP94 Regulates Circulating Cholesterol Levels through Blockade of PCSK9-Induced LDLR Degradation
Published in Cell reports (Cambridge) (15-12-2015)“…Clearance of circulating low-density lipoprotein cholesterol (LDLc) by hepatic LDL receptors (LDLR) is central for vascular health. Secreted by hepatocytes,…”
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Cell Surface Relocalization of the Endoplasmic Reticulum Chaperone and Unfolded Protein Response Regulator GRP78/BiP
Published in The Journal of biological chemistry (14-05-2010)“…The recent discovery that GRP78/BiP, a typical endoplasmic reticulum (ER) lumenal chaperone, can be expressed on the cell surface, interacting with an…”
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Characterization and Mechanism of Stress-induced Translocation of 78-Kilodalton Glucose-regulated Protein (GRP78) to the Cell Surface
Published in The Journal of biological chemistry (27-03-2015)“…Glucose-regulated protein (GRP78)/BiP, a major chaperone in the endoplasmic reticulum, is recently discovered to be preferably expressed on the surface of…”
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Role of the unfolded protein response regulator GRP78/BiP in development, cancer, and neurological disorders
Published in Antioxidants & redox signaling (01-09-2009)“…GRP78/BiP is a major endoplasmic reticulum (ER) chaperone protein critical for protein quality control of the ER, as well as controlling the activation of the…”
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GRP78/BiP inhibits endoplasmic reticulum BIK and protects human breast cancer cells against estrogen starvation-induced apoptosis
Published in Cancer research (Chicago, Ill.) (15-04-2007)“…The recent development of hormonal therapy that blocks estrogen synthesis represents a major advance in the treatment of estrogen receptor-positive breast…”
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Ortholog of autism candidate gene RBM27 regulates mitoribosomal assembly factor MALS-1 to protect against mitochondrial dysfunction and axon degeneration during neurodevelopment
Published in PLoS biology (31-10-2024)“…Mitochondrial dysfunction is thought to be a key component of neurodevelopmental disorders such as autism, intellectual disability, and attention-deficit…”
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The COOH-Terminal Proline-Rich Region of GRP78 Is a Key Regulator of Its Cell Surface Expression and Viability of Tamoxifen-Resistant Breast Cancer Cells
Published in Neoplasia (New York, N.Y.) (01-08-2019)“…Translocation of 78-kDa glucose-regulated protein (GRP78) from endoplasmic reticulum (ER) to plasma membrane represents a paradigm shift beyond its traditional…”
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The glucose-regulated proteins: stress induction and clinical applications
Published in Trends in Biochemical Sciences (01-08-2001)“…A protective mechanism used by cells to adapt to stress of the endoplasmic reticulum (ER) is the induction of members of the glucose-regulated protein (Grp)…”
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