Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.

[1]  R. Morimoto,et al.  Proteotoxic stress and ageing triggers the loss of redox homeostasis across cellular compartments , 2015, The EMBO journal.

[2]  K. Mikoshiba,et al.  ERp44 Exerts Redox-Dependent Control of Blood Pressure at the ER. , 2015, Molecular cell.

[3]  A. Mitra,et al.  Regulation and Quality Control of Adiponectin Assembly by Endoplasmic Reticulum Chaperone ERp44* , 2015, The Journal of Biological Chemistry.

[4]  R. Sitia,et al.  Proteostasis and "redoxtasis" in the secretory pathway: Tales of tails from ERp44 and immunoglobulins. , 2015, Free radical biology & medicine.

[5]  A. Gramolini,et al.  Endoplasmic Reticulum Resident Protein 44 (ERp44) Deficiency in Mice and Zebrafish Leads to Cardiac Developmental and Functional Defects , 2014, Journal of the American Heart Association.

[6]  M. Degano,et al.  Progressive quality control of secretory proteins in the early secretory compartment by ERp44 , 2014, Journal of Cell Science.

[7]  P. van der Harst,et al.  Circulating peroxiredoxin 4 and type 2 diabetes risk: the Prevention of Renal and Vascular Endstage Disease (PREVEND) study , 2014, Diabetologia.

[8]  H. Yamaguchi,et al.  Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family. , 2014, Structure.

[9]  J. D. Watson Type 2 diabetes as a redox disease , 2014, The Lancet.

[10]  T. Natsume,et al.  Dynamic Regulation of Ero1α and Peroxiredoxin 4 Localization in the Secretory Pathway* , 2013, The Journal of Biological Chemistry.

[11]  M. Hagiwara,et al.  Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding , 2013, Scientific Reports.

[12]  A. Fornili,et al.  A pH-Regulated Quality Control Cycle for Surveillance of Secretory Protein Assembly , 2013, Molecular cell.

[13]  W. Gong,et al.  Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase. , 2013, Antioxidants & redox signaling.

[14]  Cong-Zhao Zhou,et al.  Structural Snapshots of Yeast Alkyl Hydroperoxide Reductase Ahp1 Peroxiredoxin Reveal a Novel Two-cysteine Mechanism of Electron Transfer to Eliminate Reactive Oxygen Species* , 2012, The Journal of Biological Chemistry.

[15]  G. Miller,et al.  The Role of ERp44 in Maturation of Serotonin Transporter Protein* , 2012, The Journal of Biological Chemistry.

[16]  J. Schulte Peroxiredoxin 4: a multifunctional biomarker worthy of further exploration , 2011, BMC medicine.

[17]  K. Fritz-Wolf,et al.  Crystal structure of the human thioredoxin reductase-thioredoxin complex. , 2011, Nature communications.

[18]  Owen Johnson,et al.  iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM , 2011, Acta crystallographica. Section D, Biological crystallography.

[19]  D. Ron,et al.  Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. , 2010, Molecular cell.

[20]  N. Bulleid,et al.  Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum , 2010, The EMBO journal.

[21]  N. Bulleid,et al.  Peroxiredoxin IV protects cells from oxidative stress by removing H2O2 produced during disulphide formation , 2010, Journal of Cell Science.

[22]  Lei Wang,et al.  Domain a’ of protein disulfide isomerase plays key role in inhibiting α-synuclein fibril formation , 2010, Cell Stress and Chaperones.

[23]  P. Emsley,et al.  Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.

[24]  Randy J. Read,et al.  Acta Crystallographica Section D Biological , 2003 .

[25]  Yi Liang,et al.  Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase. , 2009, The Journal of biological chemistry.

[26]  A. Ballabio,et al.  Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. , 2008, Human molecular genetics.

[27]  M. Degano,et al.  Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy‐terminal tail , 2008, EMBO reports.

[28]  N. Bulleid,et al.  Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. , 2008, The Biochemical journal.

[29]  T. Dierks,et al.  ERp44 Mediates a Thiol-independent Retention of Formylglycine-generating Enzyme in the Endoplasmic Reticulum* , 2008, Journal of Biological Chemistry.

[30]  S. Masciarelli,et al.  Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis , 2007, The EMBO journal.

[31]  Randy J. Read,et al.  Phaser crystallographic software , 2007, Journal of applied crystallography.

[32]  P. Scherer,et al.  Secretion of the Adipocyte-Specific Secretory Protein Adiponectin Critically Depends on Thiol-Mediated Protein Retention , 2007, Molecular and Cellular Biology.

[33]  Satoshi Murakami,et al.  Crystal Structure of the DsbB-DsbA Complex Reveals a Mechanism of Disulfide Bond Generation , 2006, Cell.

[34]  L. Ruddock,et al.  pH dependence of the peptide thiol-disulfide oxidase activity of six members of the human protein disulfide isomerase family. , 2006, Antioxidants & redox signaling.

[35]  R. Sitia,et al.  Dynamic retention of Ero1α and Ero1β in the endoplasmic reticulum by interactions with PDI and ERp44 , 2006 .

[36]  K. Vandenbroeck,et al.  Celecoxib Inhibits Interleukin-12 αβ and β2 Folding and Secretion by a Novel COX2-Independent Mechanism Involving Chaperones of the Endoplasmic Reticulum , 2006, Molecular Pharmacology.

[37]  Yuan Shi,et al.  Annular Arrangement and Collaborative Actions of Four Domains of Protein-disulfide Isomerase , 2006, Journal of Biological Chemistry.

[38]  K. Mikoshiba,et al.  Subtype-Specific and ER Lumenal Environment-Dependent Regulation of Inositol 1,4,5-Trisphosphate Receptor Type 1 by ERp44 , 2005, Cell.

[39]  S. Camerini,et al.  Thiol‐mediated protein retention in the endoplasmic reticulum: the role of ERp44 , 2003, The EMBO journal.

[40]  M. Alessio,et al.  ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family , 2002, The EMBO journal.

[41]  N Taniguchi,et al.  Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions. , 2000, Journal of biochemistry.

[42]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[43]  F. Sun,et al.  Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4. , 2012, The Biochemical journal.

[44]  P. Evans,et al.  Scaling and assessment of data quality. , 2006, Acta crystallographica. Section D, Biological crystallography.