Characterization of protein quality control components via dual reporter-containing misfolded cytosolic model substrates.

[1]  Ingo Amm,et al.  Molecular mass as a determinant for nuclear San1‐dependent targeting of misfolded cytosolic proteins to proteasomal degradation , 2016, FEBS letters.

[2]  Ingo Amm,et al.  Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase , 2015, PloS one.

[3]  Ingo Amm,et al.  Quality Control of a Cytoplasmic Protein Complex , 2015, The Journal of Biological Chemistry.

[4]  T. Ravid,et al.  Chaperoning Proteins for Destruction: Diverse Roles of Hsp70 Chaperones and their Co-Chaperones in Targeting Misfolded Proteins to the Proteasome , 2014, Biomolecules.

[5]  D. Fitzpatrick,et al.  Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity , 2014, BMC Genomics.

[6]  Shuai Cheng Li,et al.  Spectral probabilities of top-down tandem mass spectra , 2014, BMC Genomics.

[7]  M. Hochstrasser,et al.  Molecular architecture and assembly of the eukaryotic proteasome. , 2013, Annual review of biochemistry.

[8]  R. Dohmen,et al.  Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins , 2013, Proceedings of the National Academy of Sciences.

[9]  Kevin W Eliceiri,et al.  NIH Image to ImageJ: 25 years of image analysis , 2012, Nature Methods.

[10]  C. Grant,et al.  The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae , 2012, Genetics.

[11]  D. Garza,et al.  Firefly luciferase mutants as sensors of proteome stress , 2011, Nature Methods.

[12]  J. Frydman,et al.  Cellular strategies of protein quality control. , 2011, Cold Spring Harbor perspectives in biology.

[13]  Nadinath B. Nillegoda,et al.  Ubr1 and Ubr2 Function in a Quality Control Pathway for Degradation of Unfolded Cytosolic Proteins , 2010, Molecular biology of the cell.

[14]  R. Hampton,et al.  Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1 , 2009, Proceedings of the National Academy of Sciences.

[15]  F. Hartl,et al.  Converging concepts of protein folding in vitro and in vivo , 2009, Nature Structural &Molecular Biology.

[16]  D. Wolf,et al.  Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1 , 2008, FEBS letters.

[17]  P. Coffino,et al.  The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. , 2006, Molecular biology of the cell.

[18]  J. Frydman,et al.  Folding and Quality Control of the VHL Tumor Suppressor Proceed through Distinct Chaperone Pathways , 2005, Cell.

[19]  M. D. Temple,et al.  Complex cellular responses to reactive oxygen species. , 2005, Trends in cell biology.

[20]  D. Wolf,et al.  A genome‐wide screen identifies Yos9p as essential for ER‐associated degradation of glycoproteins , 2004, FEBS letters.

[21]  D. Wolf,et al.  A genomic screen identifies Dsk2p and Rad23p as essential components of ER‐associated degradation , 2004, EMBO reports.

[22]  V. Iyer,et al.  Genome-Wide Analysis of the Biology of Stress Responses through Heat Shock Transcription Factor , 2004, Molecular and Cellular Biology.

[23]  M. Karp,et al.  One‐step measurement of firefly luciferase activity in yeast , 2003, Yeast.

[24]  Alexander Varshavsky,et al.  The ubiquitin system. , 1998, Annual review of biochemistry.

[25]  S. Lindquist,et al.  Hsp104, Hsp70, and Hsp40 A Novel Chaperone System that Rescues Previously Aggregated Proteins , 1998, Cell.

[26]  D. Wolf,et al.  ER Degradation of a Misfolded Luminal Protein by the Cytosolic Ubiquitin-Proteasome Pathway , 1996, Science.

[27]  A. Marchler-Bauer,et al.  The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are required for transcriptional induction through the stress response element (STRE). , 1996, The EMBO journal.

[28]  R. Schekman,et al.  Selective Uptake of Cytosolic, Peroxisomal, and Plasma Membrane Proteins into the Yeast Lysosome for Degradation (*) , 1996, The Journal of Biological Chemistry.

[29]  M. Knop,et al.  Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. , 1996, The EMBO journal.

[30]  Gerald R. Fink,et al.  Guide to yeast genetics and molecular biology , 1993 .

[31]  S Subramani,et al.  A conserved tripeptide sorts proteins to peroxisomes , 1989, The Journal of cell biology.

[32]  M. Werner-Washburne,et al.  Yeast Hsp70 RNA levels vary in response to the physiological status of the cell , 1989, Journal of bacteriology.

[33]  R. Sikorski,et al.  A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. , 1989, Genetics.

[34]  E. Craig,et al.  Transcriptional regulation of an hsp70 heat shock gene in the yeast Saccharomyces cerevisiae , 1987, Molecular and cellular biology.

[35]  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.

[36]  Thomas Sommer,et al.  Protein quality control and elimination of protein waste: the role of the ubiquitin-proteasome system. , 2014, Biochimica et biophysica acta.

[37]  D. Wolf,et al.  Use of CPY and its derivatives to study protein quality control in various cell compartments. , 2012, Methods in molecular biology.

[38]  S. Wickner,et al.  Hsp104 and ClpB: protein disaggregating machines. , 2009, Trends in biochemical sciences.

[39]  D. Wolf,et al.  Yeast genomics in the elucidation of endoplasmic reticulum (ER) quality control and associated protein degradation (ERQD). , 2005, Methods in enzymology.

[40]  M. Deluca,et al.  Firefly luciferase. , 1976, Advances in enzymology and related areas of molecular biology.