Blocking nuclear export of HSPA8 after heat shock stress severely alters cell survival

[1]  S. Muller,et al.  Assessing Autophagy in Mouse Models and Patients with Systemic Autoimmune Diseases , 2017, Cells.

[2]  G. Chiosis,et al.  Chemical Tools to Investigate Mechanisms Associated with HSP90 and HSP70 in Disease. , 2016, Cell chemical biology.

[3]  S. Ha,et al.  A small molecule inhibitor for ATPase activity of Hsp70 and Hsc70 enhances the immune response to protein antigens , 2015, Scientific Reports.

[4]  A. Cuervo,et al.  Modulation of deregulated chaperone-mediated autophagy by a phosphopeptide , 2015, Autophagy.

[5]  J. Blum,et al.  Macronutrient Deprivation Modulates Antigen Trafficking and Immune Recognition through HSC70 Accessibility , 2015, The Journal of Immunology.

[6]  F. Stricher,et al.  HSPA8/HSC70 chaperone protein , 2013, Autophagy.

[7]  E. Otsuji,et al.  Connexin43 Functions as a Novel Interacting Partner of Heat Shock Cognate Protein 70 , 2013, Scientific Reports.

[8]  T. Kodama,et al.  Mouse Model of Lymph Node Metastasis via Afferent Lymphatic Vessels for Development of Imaging Modalities , 2013, PloS one.

[9]  O. Demidov,et al.  Inhibition of HSP70: a challenging anti-cancer strategy. , 2012, Cancer letters.

[10]  Tuoen Liu,et al.  Comprehensive review on the HSC70 functions, interactions with related molecules and involvement in clinical diseases and therapeutic potential. , 2012, Pharmacology & therapeutics.

[11]  J. Gómez-Reino,et al.  Lupuzor/P140 peptide in patients with systemic lupus erythematosus: a randomised, double-blind, placebo-controlled phase IIb clinical trial , 2012, Annals of the rheumatic diseases.

[12]  T. He,et al.  Heat Shock Cognate 70 Regulates the Translocation and Angiogenic Function of Nucleolin , 2012, Arteriosclerosis, thrombosis, and vascular biology.

[13]  S. Muller,et al.  Peptide-based approaches to treat lupus and other autoimmune diseases. , 2012, Journal of autoimmunity.

[14]  K. Nagata,et al.  Oxidative stress caused by a low concentration of hydrogen peroxide induces senescence-like changes in mouse gingival fibroblasts , 2012, International journal of molecular medicine.

[15]  Andrea Ballabio,et al.  TFEB Links Autophagy to Lysosomal Biogenesis , 2011, Science.

[16]  S. Muller,et al.  Extended Report , 2022 .

[17]  U. Stochaj,et al.  Nucleolar Targeting of the Chaperone Hsc70 Is Regulated by Stress, Cell Signaling, and a Composite Targeting Signal Which Is Controlled by Autoinhibition* , 2010, The Journal of Biological Chemistry.

[18]  T. Nakao,et al.  Heat Shock Cognate Protein 70 Is Essential for Akt Signaling in Endothelial Function , 2010, Arteriosclerosis, thrombosis, and vascular biology.

[19]  Alain Van Dorsselaer,et al.  The Spliceosomal Phosphopeptide P140 Controls the Lupus Disease by Interacting with the HSC70 Protein and via a Mechanism Mediated by γδ T Cells , 2009, PloS one.

[20]  M. Drysdale,et al.  Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design. , 2009, Journal of medicinal chemistry.

[21]  A. Cuervo,et al.  The Chaperone-Mediated Autophagy Receptor Organizes in Dynamic Protein Complexes at the Lysosomal Membrane , 2008, Molecular and Cellular Biology.

[22]  M. Jäättelä,et al.  The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions , 2007, FEBS letters.

[23]  R. Sousa,et al.  Structural basis of interdomain communication in the Hsc70 chaperone. , 2005, Molecular cell.

[24]  N. Imamoto,et al.  The 70-kD heat shock cognate protein (hsc70) facilitates the nuclear export of the import receptors , 2005, The Journal of cell biology.

[25]  U. Stochaj,et al.  Stress inhibits nucleocytoplasmic shuttling of heat shock protein hsc70. , 2005, American journal of physiology. Cell physiology.

[26]  F. Tsukahara,et al.  Identification of Novel Nuclear Export and Nuclear Localization-related Signals in Human Heat Shock Cognate Protein 70* , 2004, Journal of Biological Chemistry.

[27]  C. Hunt,et al.  Indomethacin and ibuprofen induce Hsc70 nuclear localization and activation of the heat shock response in HeLa cells. , 2004, Biochemical and biophysical research communications.

[28]  J. Miyazaki,et al.  Antagonist of monocyte chemoattractant protein 1 ameliorates the initiation and progression of lupus nephritis and renal vasculitis in MRL/lpr mice. , 2003, Arthritis and rheumatism.

[29]  J. Swenberg,et al.  Micromolar concentrations of hydrogen peroxide induce oxidative DNA lesions more efficiently than millimolar concentrations in mammalian cells. , 2003, Nucleic acids research.

[30]  A. Emili,et al.  Hsc70 Regulates Accumulation of Cyclin D1 and Cyclin D1-Dependent Protein Kinase , 2003, Molecular and Cellular Biology.

[31]  M. Patarroyo,et al.  T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MRL/lpr mice , 2003 .

[32]  P. Srivastava.  Roles of heat-shock proteins in innate and adaptive immunity , 2002, Nature Reviews Immunology.

[33]  K. R. Ely,et al.  The carboxyl-terminal lobe of Hsc70 ATPase domain is sufficient for binding to BAG1. , 2001, Biochemical and Biophysical Research Communications - BBRC.

[34]  U. Stochaj,et al.  Heat‐induced nuclear accumulation of hsc70 proteins is regulated by phosphorylation and inhibited in confluent cells , 2001, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[35]  T. Rabilloud,et al.  A comparison between Sypro Ruby and ruthenium II tris (bathophenanthroline disulfonate) as fluorescent stains for protein detection in gels , 2001, Proteomics.

[36]  Holger Sondermann,et al.  Structure of a Bag/Hsc70 Complex: Convergent Functional Evolution of Hsp70 Nucleotide Exchange Factors , 2001, Science.

[37]  B. Stockinger,et al.  The HSC73 molecular chaperone: involvement in MHC class II antigen presentation. , 1999, Journal of immunology.

[38]  Shinichi Aizawa,et al.  Heat shock induces transient p53-dependent cell cycle arrest at G1/S , 1997, Oncogene.

[39]  A. Ciechanover,et al.  Ubiquitin-dependent Degradation of Certain Protein Substrates in Vitro Requires the Molecular Chaperone Hsc70* , 1997, The Journal of Biological Chemistry.

[40]  M. Ladjimi,et al.  The COOH-terminal Peptide Binding Domain Is Essential for Self-association of the Molecular Chaperone HSC70* , 1997, The Journal of Biological Chemistry.

[41]  C. Feldherr,et al.  Evidence for the existence of a novel mechanism for the nuclear import of Hsc70. , 1996, Experimental cell research.

[42]  A. Cuervo,et al.  A Receptor for the Selective Uptake and Degradation of Proteins by Lysosomes , 1996, Science.

[43]  I. Auger,et al.  HLA–DR4 and HLA–DR10 motifs that carry susceptibility to rheumatoid arthritis bind 70–kD heat shock proteins , 1996, Nature Medicine.

[44]  P. Sansoni,et al.  New insights suggesting a possible role of a heat shock protein 70-kD family-related protein in antigen processing/presentation phenomenon in humans , 1993 .

[45]  M. Miyagi,et al.  Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins , 1992, The Journal of cell biology.

[46]  R. Mandell,et al.  Identification of two HSP70-related Xenopus oocyte proteins that are capable of recycling across the nuclear envelope , 1990, The Journal of cell biology.

[47]  K. Flaherty,et al.  Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein , 1990, Nature.

[48]  L. Kedes,et al.  Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein , 1985, Molecular and cellular biology.

[49]  H. Kampinga,et al.  Computational analysis of the human HSPH/HSPA/DNAJ family and cloning of a human HSPH/HSPA/DNAJ expression library , 2008, Cell Stress and Chaperones.

[50]  M. Patarroyo,et al.  T cell recognition and therapeutic effect of a phosphorylated synthetic peptide of the 70K snRNP protein administered in MR/lpr mice. , 2003, European journal of immunology.

[51]  P. Sansoni,et al.  New insights suggesting a possible role of a heat shock protein 70-kD family-related protein in antigen processing/presentation phenomenon in humans. , 1993, Blood.