Identification of an endoplasmic reticulum proteostasis modulator that enhances insulin production in pancreatic β cells.

[1]  R. L. Wiseman,et al.  Small molecule strategies to harness the unfolded protein response: where do we go from here? , 2020, The Journal of Biological Chemistry.

[2]  H. Kosako,et al.  Cell-based HTS identifies a chemical chaperone for preventing ER protein aggregation and proteotoxicity , 2019, eLife.

[3]  P. Arvan,et al.  Cells Deploy a Two-Pronged Strategy to Rectify Misfolded Proinsulin Aggregates. , 2019, Molecular cell.

[4]  M. van Lith,et al.  ERp18 regulates activation of ATF6α during unfolded protein response , 2019, The EMBO journal.

[5]  R. Kaufman,et al.  Proinsulin misfolding is an early event in the progression to type 2 diabetes , 2019, eLife.

[6]  D. Scheuner,et al.  PDIA1/P4HB is required for efficient proinsulin maturation and ß cell health in response to diet induced obesity , 2019, eLife.

[7]  J. Vilo,et al.  g:Profiler: a web server for functional enrichment analysis and conversions of gene lists (2019 update) , 2019, Nucleic Acids Res..

[8]  P. Arvan,et al.  Endoplasmic Reticulum Chaperone Glucose-Regulated Protein 94 Is Essential for Proinsulin Handling , 2019, Diabetes.

[9]  L. Hendershot,et al.  The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends , 2018, The Journal of Biological Chemistry.

[10]  Laura M. Geffert,et al.  Clickable photoaffinity ligands for the human serotonin transporter based on the selective serotonin reuptake inhibitor (S)-citalopram. , 2018, Bioorganic & medicinal chemistry letters.

[11]  C. Hetz,et al.  ER Proteostasis Control of Neuronal Physiology and Synaptic Function , 2018, Trends in Neurosciences.

[12]  C. Kalodimos,et al.  Oligomerization of a molecular chaperone modulates its activity , 2018, eLife.

[13]  J. Miyazaki,et al.  IRE1–XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells , 2018, The Journal of cell biology.

[14]  P. Arvan,et al.  Misfolded proinsulin in the endoplasmic reticulum during development of beta cell failure in diabetes , 2018, Annals of the New York Academy of Sciences.

[15]  J. Reinstein,et al.  Bap (Sil1) regulates the molecular chaperone BiP by coupling release of nucleotide and substrate , 2018, Nature Structural & Molecular Biology.

[16]  A. Zhuravleva,et al.  Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation , 2017, eLife.

[17]  R. Kaufman,et al.  Physiological/pathological ramifications of transcription factors in the unfolded protein response , 2017, Genes & development.

[18]  Y. Li,et al.  Discovery of a Benzamide Derivative That Protects Pancreatic β-Cells against Endoplasmic Reticulum Stress. , 2017, Journal of medicinal chemistry.

[19]  D. Ron,et al.  Paradoxical Sensitivity to an Integrated Stress Response Blocking Mutation in Vanishing White Matter Cells , 2016, PloS one.

[20]  Max A. Horlbeck,et al.  Compact and highly active next-generation libraries for CRISPR-mediated gene repression and activation , 2016, eLife.

[21]  D. Ron,et al.  AMPylation matches BiP activity to client protein load in the endoplasmic reticulum , 2015, eLife.

[22]  D. Ron,et al.  Skeletal muscle–specific eukaryotic translation initiation factor 2α phosphorylation controls amino acid metabolism and fibroblast growth factor 21–mediated non–cell-autonomous energy metabolism , 2015, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[23]  L. Hendershot,et al.  Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker , 2015, eLife.

[24]  N. Volkmann,et al.  The IRE1α/XBP1s Pathway Is Essential for the Glucose Response and Protection of β Cells , 2015, PLoS biology.

[25]  A. Yalçin,et al.  Phenotypic assays identify azoramide as a small-molecule modulator of the unfolded protein response with antidiabetic activity , 2015, Science Translational Medicine.

[26]  Matthias J. Feige,et al.  BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions. , 2015, Journal of molecular biology.

[27]  M. Katze,et al.  Antioxidants Complement the Requirement for Protein Chaperone Function to Maintain β-Cell Function and Glucose Homeostasis , 2015, Diabetes.

[28]  J. Miyazaki,et al.  γ-Oryzanol protects pancreatic β-cells against endoplasmic reticulum stress in male mice. , 2015, Endocrinology.

[29]  Max A. Horlbeck,et al.  Genome-Scale CRISPR-Mediated Control of Gene Repression and Activation , 2014, Cell.

[30]  Dustin J Maly,et al.  Allosteric Inhibition of the IRE1α RNase Preserves Cell Viability and Function during Endoplasmic Reticulum Stress , 2014, Cell.

[31]  Neville E. Sanjana,et al.  Improved vectors and genome-wide libraries for CRISPR screening , 2014, Nature Methods.

[32]  Joseph E Chambers,et al.  Endoplasmic reticulum stress in malignancy. , 2014, Cancer cell.

[33]  A. Ittner,et al.  The nucleotide exchange factor SIL1 is required for glucose-stimulated insulin secretion from mouse pancreatic beta cells in vivo , 2014, Diabetologia.

[34]  P. Froguel,et al.  Role of the Unfolded Protein Response in β Cell Compensation and Failure during Diabetes , 2014, Journal of diabetes research.

[35]  T. Gidalevitz,et al.  Protein disulfide isomerase A6 controls the decay of IRE1α signaling via disulfide-dependent association. , 2014, Molecular cell.

[36]  R. Kaufman,et al.  Endoplasmic reticulum stress and type 2 diabetes. , 2012, Annual review of biochemistry.

[37]  P. Walter,et al.  The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation , 2011, Science.

[38]  F. Urano,et al.  Endoplasmic reticulum stress and pancreatic β-cell death , 2011, Trends in Endocrinology & Metabolism.

[39]  L. Glimcher,et al.  Dual and opposing roles of the unfolded protein response regulated by IRE1α and XBP1 in proinsulin processing and insulin secretion , 2011, Proceedings of the National Academy of Sciences.

[40]  G. Lewis,et al.  Sodium Phenylbutyrate, a Drug With Known Capacity to Reduce Endoplasmic Reticulum Stress, Partially Alleviates Lipid-Induced Insulin Resistance and β-Cell Dysfunction in Humans , 2011, Diabetes.

[41]  Matthias J. Feige,et al.  Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions , 2011, Nature Structural &Molecular Biology.

[42]  T. Hartley,et al.  Endoplasmic reticulum stress response in an INS-1 pancreatic β-cell line with inducible expression of a folding-deficient proinsulin , 2010, BMC Cell Biology.

[43]  C. Seidel,et al.  The conformational dynamics of the mitochondrial Hsp70 chaperone. , 2010, Molecular cell.

[44]  D. Ron,et al.  ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis , 2010, The Journal of Cell Biology.

[45]  G. Hotamışlıgil Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease , 2010, Cell.

[46]  D. Eizirik,et al.  ER Stress in Pancreatic β Cells: The Thin Red Line Between Adaptation and Failure , 2010, Science Signaling.

[47]  A. Volchuk,et al.  GRP78, but Not Protein-disulfide Isomerase, Partially Reverses Hyperglycemia-induced Inhibition of Insulin Synthesis and Secretion in Pancreatic β-Cells* , 2009, Journal of Biological Chemistry.

[48]  Kun Wook Chung,et al.  Loss of autophagy diminishes pancreatic beta cell mass and function with resultant hyperglycemia. , 2008, Cell metabolism.

[49]  Masaaki Komatsu,et al.  Autophagy is important in islet homeostasis and compensatory increase of beta cell mass in response to high-fat diet. , 2008, Cell metabolism.

[50]  J. Brodsky,et al.  The activities and function of molecular chaperones in the endoplasmic reticulum. , 2007, Seminars in cell & developmental biology.

[51]  Barbara C. McGrath,et al.  PERK EIF2AK3 control of pancreatic beta cell differentiation and proliferation is required for postnatal glucose homeostasis. , 2006, Cell metabolism.

[52]  K. Mori,et al.  Role of Disulfide Bridges Formed in the Luminal Domain of ATF6 in Sensing Endoplasmic Reticulum Stress , 2006, Molecular and Cellular Biology.

[53]  E. Yilmaz,et al.  Chemical Chaperones Reduce ER Stress and Restore Glucose Homeostasis in a Mouse Model of Type 2 Diabetes , 2006, Science.

[54]  C. Mathews,et al.  Proteasome Inhibition Alters Glucose-stimulated (Pro)insulin Secretion and Turnover in Pancreatic β-Cells* , 2005, Journal of Biological Chemistry.

[55]  P. Arvan,et al.  Proinsulin Disulfide Maturation and Misfolding in the Endoplasmic Reticulum* , 2005, Journal of Biological Chemistry.

[56]  D. Ron,et al.  CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. , 2004, Genes & development.

[57]  H. Patzelt,et al.  Functional Dissection of Escherichia coli Trigger Factor: Unraveling the Function of Individual Domains , 2004, Journal of bacteriology.

[58]  K. Mori,et al.  The endoplasmic reticulum stress response is stimulated through the continuous activation of transcription factors ATF6 and XBP1 in Ins2+/Akita pancreatic β cells , 2004 .

[59]  D. Scheuner,et al.  Cytoprotection by pre‐emptive conditional phosphorylation of translation initiation factor 2 , 2004, The EMBO journal.

[60]  Masataka Mori,et al.  Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes. , 2002, The Journal of clinical investigation.

[61]  K. Mori,et al.  XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor , 2001, Cell.

[62]  D. Ron,et al.  Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival. , 2001, Molecular cell.

[63]  J. Miyazaki,et al.  Insulin secretion and differential gene expression in glucose-responsive and -unresponsive MIN6 sublines. , 2000, American journal of physiology. Endocrinology and metabolism.

[64]  Pierre Fafournoux,et al.  Amino Acids Control Mammalian Gene Transcription: Activating Transcription Factor 2 Is Essential for the Amino Acid Responsiveness of the CHOP Promoter , 2000, Molecular and Cellular Biology.

[65]  K. Mori Tripartite Management of Unfolded Proteins in the Endoplasmic Reticulum , 2000, Cell.

[66]  Y. Tanabe,et al.  Practical and efficient methods for sulfonylation of alcohols using Ts(Ms)Cl/Et3N and catalytic Me3H·HCl as combined base: Promising alternative to traditional pyridine , 1999 .

[67]  Hiderou Yoshida,et al.  Identification of the cis-Acting Endoplasmic Reticulum Stress Response Element Responsible for Transcriptional Induction of Mammalian Glucose-regulated Proteins , 1998, The Journal of Biological Chemistry.

[68]  C. Kalodimos,et al.  Supplementary Materials for Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone , 2014 .

[69]  Danhong Lu,et al.  A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse. , 1999, The Journal of clinical investigation.