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1. Full Text Tay-Sachs disease mutations in HEXA target the ? chain of hexosaminidase A to endoplasmic reticulum-associated degradation
by Dersh, Devin and Iwamoto, Yuichiro and Argon, Yair
Molecular Biology of the Cell, ISSN 1059-1524, 12/2016, Volume 27, Issue 24, pp. 3813 - 3827
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2. Full Text Quality Control across Compartments-Connecting ERAD with Ribosomal Quality Control
by Argon, Yair and Gidalevitz, Tali
Journal of molecular biology, 11/2018
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3. Full Text GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum
by Marzec, Michal and Eletto, Davide and Argon, Yair
BBA - Molecular Cell Research, ISSN 0167-4889, 03/2012, Volume 1823, Issue 3, pp. 774 - 787
Glucose-regulated protein 94 is the HSP90-like protein in the lumen of the endoplasmic reticulum and therefore it chaperones secreted and membrane proteins. It... 
Glucose-regulated protein 94 | Protein folding | Endoplasmic reticulum | Secretory proteins pathway | ER stress response | TYROSINE PHOSPHORYLATION | PEPTIDE-BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-SURFACE EXPRESSION | STRESS-RESPONSE | ATP-BINDING | CELL BIOLOGY | GLUCOSE-REGULATED PROTEINS | N-TERMINAL DOMAIN | TOLL-LIKE RECEPTORS | MOLECULAR CHAPERONE | SALT-DEPENDENT-LIPASE | Amino Acid Sequence | Animals | Humans | Endoplasmic Reticulum - metabolism | HSP90 Heat-Shock Proteins - metabolism | Molecular Sequence Data | Membrane Proteins - metabolism | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Proteins | Post-translational modification | Heat shock proteins | Quality control | Membrane proteins
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4. Full Text Stressed-Out Endoplasmic Reticulum Inflames the Mitochondria
by Shin, Sunny and Argon, Yair
Immunity, ISSN 1074-7613, 09/2015, Volume 43, Issue 3, pp. 409 - 411
Bacterial infection induces inflammasome activation and release of interleukin-1 (IL-1) cytokines. show that during infection, an endoplasmic reticulum stress... 
THIOREDOXIN-INTERACTING PROTEIN | NLRP3 INFLAMMASOME | IMMUNOLOGY | ER STRESS | CELL-DEATH | Animals | Humans | Inflammasomes - immunology | Mitochondria - immunology | Carrier Proteins - immunology | Endoplasmic Reticulum Stress - immunology | Caspase 2 - immunology | Mitochondrial DNA | Bacterial infections | Proteins | Mitochondria | Transcription factors | Infections | Kinases | Endoplasmic reticulum | Apoptosis
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5. Full Text Quality Control across Compartments—Connecting ERAD with Ribosomal Quality Control
by Argon, Yair and Gidalevitz, Tali
Journal of Molecular Biology, ISSN 0022-2836, 01/2019, Volume 431, Issue 2, pp. 142 - 144
PROTEINS | PATHWAY | STOP | BIOCHEMISTRY & MOLECULAR BIOLOGY
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6. Full Text The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivation
by Ostrovsky, Olga and Ahmed, Noreen T and Argon, Yair
Molecular Biology of the Cell, ISSN 1059-1524, 03/2009, Volume 20, Issue 6, pp. 1845 - 1854
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7. Full Text Orchestration of secretory protein folding by ER chaperones
by Gidalevitz, Tali and Stevens, Fred and Argon, Yair
BBA - Molecular Cell Research, ISSN 0167-4889, 11/2013, Volume 1833, Issue 11, pp. 2410 - 2424
The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The... 
Secretome | Chaperones | Protein folding | Endoplasmic reticulum | DISULFIDE BOND FORMATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | NEWLY SYNTHESIZED PROTEINS | PHOSPHATIDYLSERINE-CONTAINING MEMBRANES | NEMATODE CAENORHABDITIS-ELEGANS | HUMAN CHORIONIC-GONADOTROPIN | VIRUS-G PROTEIN | ENDOPLASMIC-RETICULUM CHAPERONES | MARINESCO-SJOGREN-SYNDROME | CELL BIOLOGY | MHC CLASS-I | NUCLEOTIDE EXCHANGE FACTOR | Molecular Chaperones | Protein Biosynthesis | Animals | Proteins - secretion | Humans | Endoplasmic Reticulum - metabolism | Protein Processing, Post-Translational | Protein Folding | Protein Transport | Enzymes
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8. Full Text Redox controls UPR to control redox
by Eletto, Davide and Chevet, Eric and Argon, Yair and Appenzeller-Herzog, Christian
Journal of Cell Science, ISSN 0021-9533, 2014, Volume 127, Issue 17, pp. 3649 - 3658
In many physiological contexts, intracellular reduction-oxidation (redox) conditions and the unfolded protein response (UPR) are important for the control of... 
Protein disulfide isomerase | Mitochondria | Reactive oxygen species | Endoplasmic reticulum | Endoplasmic reticulum stress | Unfolded protein response | OXIDATIVE STRESS | PROTEIN-DISULFIDE-ISOMERASE | P53-UP-REGULATED MODULATOR | ER-STRESS | THIOREDOXIN-INTERACTING PROTEIN | ENDOPLASMIC-RETICULUM STRESS | CELL-DEATH | CELL BIOLOGY | REACTIVE OXYGEN | INOSITOL 1,4,5-TRISPHOSPHATE RECEPTORS | TRANSMEMBRANE PROTEIN | Animals | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Humans | Endoplasmic Reticulum - metabolism | Mitochondria - metabolism | Unfolded Protein Response - physiology | Endoplasmic Reticulum Stress - physiology
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9. Full Text Protein Disulfide Isomerase A6 Controls the Decay of IRE1α Signaling via Disulfide-Dependent Association
by Eletto, Davide and Eletto, Daniela and Dersh, Devin and Gidalevitz, Tali and Argon, Yair
Molecular Cell, ISSN 1097-2765, 02/2014, Volume 53, Issue 4, pp. 562 - 576
The response to endoplasmic reticulum (ER) stress relies on activation of unfolded protein response (UPR) sensors, and the outcome of the UPR depends on the... 
NF-Y | ACTIVATION | CAENORHABDITIS-ELEGANS | ER STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | UNFOLDED-PROTEIN | IRE1 KINASE | ENDOPLASMIC-RETICULUM STRESS | DIMERIZATION DOMAIN | TRANSCRIPTION FACTOR | SENSOR IRE1-ALPHA | CELL BIOLOGY | Phosphorylation | Cell Proliferation | Protein Disulfide-Isomerases - metabolism | Humans | Caenorhabditis elegans Proteins - metabolism | Endoplasmic Reticulum - metabolism | Molecular Sequence Data | RNA, Messenger - metabolism | Disulfides - chemistry | HEK293 Cells | Oxygen - chemistry | Protein Denaturation | Protein-Serine-Threonine Kinases - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Signal Transduction | Cysteine - chemistry | Protein Folding | Gene Expression Regulation, Enzymologic | Sequence Homology, Amino Acid | Animals | Carrier Proteins - metabolism | Inositol - chemistry | Mice | 3T3 Cells | Caenorhabditis elegans - enzymology
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10. Full Text GRP94 in ER quality control and stress responses
by Eletto, Davide and Dersh, Devin and Argon, Yair
Seminars in Cell and Developmental Biology, ISSN 1084-9521, 2010, Volume 21, Issue 5, pp. 479 - 485
A system of endoplasmic reticulum (ER) chaperones has evolved to optimize the output of properly folded secretory and membrane proteins. An important player in... 
ER chaperone | ERAD | HSP90 | IGF | Calcium | HSP90 MOLECULAR CHAPERONE | PEPTIDE-BINDING | MUSCLE DEVELOPMENT | DEVELOPMENTAL BIOLOGY | ENDOPLASMIC-RETICULUM STRESS | GROWTH-FACTOR-II | CELL BIOLOGY | GLUCOSE-REGULATED PROTEIN | UNFOLDED PROTEIN RESPONSE | MISFOLDED GLYCOPROTEINS | N-TERMINAL DOMAIN | ANTIGEN-PRESENTING CELLS | Animals | Molecular Chaperones - metabolism | Proteins - metabolism | Endoplasmic Reticulum - physiology | Endoplasmic Reticulum - metabolism | Membrane Proteins - metabolism | Protein Processing, Post-Translational | HSP70 Heat-Shock Proteins | Protein Folding | Heat shock proteins | Quality control | Membrane proteins | calcium
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11. Full Text PDIA6 regulates insulin secretion by selectively inhibiting the RIDD activity of IRE1
by Eletto, Daniela and Eletto, Davide and Boyle, Sarah and Argon, Yair
FASEB Journal, ISSN 0892-6638, 02/2016, Volume 30, Issue 2, pp. 653 - 665
Protein disulfide isomerase A6 (PDIA6) interacts with protein kinase RNA-like endoplasmic reticulum kinase (PERK) and inositol requiring enzyme (IRE)-1 and... 
GSIS | β-cell metabolism | Unfolded protein response | SMALL-MOLECULE | ER STRESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | IRE1-ALPHA | DEATH | ENDOPLASMIC-RETICULUM STRESS | PERK | beta-cell metabolism | UNFOLDED-PROTEIN-RESPONSE | CELL BIOLOGY | unfolded protein response | KINASE IRE1 | MESSENGER-RNA | BIOLOGY | PANCREATIC BETA-CELL | Endoribonucleases - genetics | Protein Disulfide-Isomerases - metabolism | eIF-2 Kinase - metabolism | Humans | Actins - metabolism | RNA, Messenger - metabolism | X-Box Binding Protein 1 | Actins - genetics | DNA-Binding Proteins - metabolism | RNA Splicing | Islets of Langerhans - metabolism | Membrane Proteins - metabolism | Insulin Secretion | Protein-Serine-Threonine Kinases - metabolism | eIF-2 Kinase - genetics | Cell Line | Endoribonucleases - metabolism | Membrane Proteins - genetics | RNA, Messenger - genetics | Enzyme Inhibitors - pharmacology | Gene Silencing | Protein-Serine-Threonine Kinases - genetics | Glucose - pharmacology | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Regulatory Factor X Transcription Factors | Transcription Factors - metabolism | Insulin - metabolism | Protein Disulfide-Isomerases - genetics | Animals | Glucose - metabolism | Thapsigargin - pharmacology | Mice | Research Communication
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12. Full Text Tay-Sachs disease mutations in HEXA target the alpha chain of hexosaminidase A to endoplasmic reticulum-associated degradation
by Dersh, D and Iwamoto, Y and Argon, Y
MOLECULAR BIOLOGY OF THE CELL, ISSN 1059-1524, 12/2016, Volume 27, Issue 24, pp. 3813 - 3827
Loss of function of the enzyme beta-hexosaminidase A (HexA) causes the lysosomal storage disorder Tay-Sachs disease (TSD). It has been proposed that mutations... 
ADULT FORM | CRYSTAL-STRUCTURE | GM2 GANGLIOSIDOSIS | HUMAN BETA-HEXOSAMINIDASE | LYSOSOMAL STORAGE DISORDERS | SITE-DIRECTED MUTAGENESIS | PROTEIN-FOLDING DISEASES | SANDHOFF-DISEASE | FIBROBLASTS | PRO-ALPHA | CELL BIOLOGY | Molecular Chaperones - metabolism | beta-N-Acetylhexosaminidases - metabolism | Humans | Endoplasmic Reticulum - metabolism | Protein Transport - physiology | Hexosaminidase A - metabolism | Tay-Sachs Disease - genetics | Lysosomes - metabolism | Hexosaminidase A - biosynthesis | Proteolysis | Endoplasmic Reticulum-Associated Degradation - physiology | HEK293 Cells | Tay-Sachs Disease - metabolism | Hexosaminidase A - genetics | Mutation | Primary Cell Culture | Hexosaminidase A - physiology
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13. Full Text Tyrosine 870 of TLR9 is critical for receptor maturation rather than phosphorylation-dependent ligand-induced signaling
by Biswas, Chhanda and Rao, Sheila and Slade, Katharine and Hyman, David and Dersh, Devin and Mantegazza, Adriana R and Zoltick, Philip W and Marks, Michael S and Argon, Yair and Behrens, Edward M
PLoS ONE, ISSN 1932-6203, 07/2018, Volume 13, Issue 7, p. e0200913
Toll like receptors (TLRs) share a conserved structure comprising the N-terminal ectodomain, a transmembrane segment and a C-terminal cytoplasmic Toll/IL-1... 
PROTEOLYTIC CLEAVAGE | ADAPTER PROTEIN-3 | MASTER CHAPERONE | STRUCTURAL BASIS | TETRACYCLINE RESISTANCE | MULTIDISCIPLINARY SCIENCES | TOLL-LIKE RECEPTORS | GENE-REGULATION | ENDOPLASMIC-RETICULUM | TET REPRESSOR | INNATE IMMUNITY | Tyrosine | Physiological aspects | TLR9 | Cellular signal transduction | Research | Dendritic cells | Pediatrics | Phosphorylation | Laboratories | Trafficking | Egress | Interleukin 1 receptors | Chaperones | Autophagy | Proteins | Signal transduction | Receptors | Interleukin 1 | Toll-like receptors | Bone marrow | Bacteria | Deoxyribonucleic acid--DNA | Assembly | CpG islands | Immune system | Maturation | Rheumatology | Inflammation | TLR4 protein | TLR9 protein | Children & youth | Mutants | Medicine | Pathology | Signaling | Hospitals | Mutagenesis | Microscopy | Quality control | Ligands | Transduction | Endoplasmic reticulum | Protein structure | Deoxyribonucleic acid | DNA
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14. Candidate genes that affect aging through protein homeostasis
by Argon, Yair and Gidalevitz, Tali
Advances in Experimental Medicine and Biology, ISSN 0065-2598, 2015, Volume 847, pp. 45 - 72
Because aging is a multifactorial, pleiotropic process where many interacting mechanisms contribute to the organismal decline, the candidate gene approach... 
MEDICINE, RESEARCH & EXPERIMENTAL | HEAT-SHOCK FACTOR-1 | OXIDATIVE STRESS | HUMAN LONGEVITY | APOLIPOPROTEIN-E | LIFE-SPAN EXTENSION | CAENORHABDITIS-ELEGANS | SIGNALING PATHWAY | BIOLOGY | GENETICS & HEREDITY | C-ELEGANS | ENDOPLASMIC-RETICULUM | GROWTH-FACTOR-I | Somatomedins - physiology | Tumor Suppressor Protein p53 - physiology | Animals | Proteins - metabolism | Aging - genetics | Humans | Sirtuins - physiology | Homeostasis | TOR Serine-Threonine Kinases - physiology | Longevity - genetics | Protein Folding
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15. Full Text An Essential Role for ATP Binding and Hydrolysis in the Chaperone Activity of GRP94 in Cells
by Olga Ostrovsky and Catherine A. Makarewich and Erik L. Snapp and Yair Argon and Peter Cresswell
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2009, Volume 106, Issue 28, pp. 11600 - 11605
Glucose-regulated protein 94 (GRP94) is an endoplasmic reticulum (ER) chaperone for which only few client proteins and no cofactors are known and whose mode of... 
Proteins | Hydrolysis | Cell growth | B lymphocytes | Adenosine triphosphatases | Cell lines | Amino acids | Nucleotides | Viability | Endoplasmic reticulum | Peptide hormones | Protein folding | ACTIVATION | SPECIFICITY | PEPTIDE-BINDING | MULTIDISCIPLINARY SCIENCES | ENDOPLASMIC-RETICULUM HSP90 | IDENTIFICATION | peptide hormones | LIGAND INTERACTIONS | CLIENT PROTEIN | IN-VIVO | N-TERMINAL DOMAIN | MOLECULAR CHAPERONE | protein folding | endoplasmic reticulum | Protein Structure, Tertiary | Cell Line |