Molecular Chaperones and Protein Quality Control

[1]  Bernd Bukau,et al.  Allosteric regulation of Hsp70 chaperones by a proline switch. , 2006, Molecular cell.

[2]  Peter Walter,et al.  On the mechanism of sensing unfolded protein in the endoplasmic reticulum. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[3]  R. Vabulas,et al.  Protein Synthesis upon Acute Nutrient Restriction Relies on Proteasome Function , 2005, Science.

[4]  Johannes Buchner,et al.  The Yeast Hsp110 Sse1 Functionally Interacts with the Hsp70 Chaperones Ssa and Ssb* , 2005, Journal of Biological Chemistry.

[5]  J. Frydman,et al.  Hsp110 Cooperates with Different Cytosolic HSP70 Systems in a Pathway for de Novo Folding* , 2005, Journal of Biological Chemistry.

[6]  Peter Walter,et al.  Inaugural Article: On the mechanism of sensing unfolded protein in the endoplasmic reticulum , 2005 .

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

[8]  G. Bjørkøy,et al.  p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death , 2005, The Journal of cell biology.

[9]  Tania A. Baker,et al.  Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines , 2005, Nature.

[10]  K. Römisch Endoplasmic reticulum-associated degradation. , 2005, Annual review of cell and developmental biology.

[11]  D. Hebert,et al.  Yos9p: a sweet-toothed bouncer of the secretory pathway. , 2005, Molecular cell.

[12]  Atsushi Iwata,et al.  Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[13]  G. J. Raymond,et al.  The most infectious prion protein particles , 2005, Nature.

[14]  P. Jenö,et al.  The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. , 2005, Proceedings of the National Academy of Sciences of the United States of America.

[15]  K. Furtak,et al.  Loops in the Central Channel of ClpA Chaperone Mediate Protein Binding, Unfolding, and Translocation , 2005, Cell.

[16]  Tania A. Baker,et al.  Asymmetric Interactions of ATP with the AAA+ ClpX6 Unfoldase: Allosteric Control of a Protein Machine , 2005, Cell.

[17]  E. Craig,et al.  The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1 , 2005, Nature Structural &Molecular Biology.

[18]  E. Craig,et al.  Human Mpp11 J Protein: Ribosome-Tethered Molecular Chaperones Are Ubiquitous , 2005, Science.

[19]  Masaaki Komatsu,et al.  Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice , 2005, The Journal of cell biology.

[20]  J. Brodsky,et al.  Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). , 2005, Journal of biochemistry.

[21]  Axel T Brunger,et al.  Nucleotide dependent motion and mechanism of action of p97/VCP. , 2005, Journal of molecular biology.

[22]  Andreas Bracher,et al.  Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. , 2005, Molecular cell.

[23]  E. Bennett,et al.  Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. , 2005, Molecular cell.

[24]  I. Braakman,et al.  Versatility of the Endoplasmic Reticulum Protein Folding Factory , 2005, Critical reviews in biochemistry and molecular biology.

[25]  Takeshi Tokuhisa,et al.  The role of autophagy during the early neonatal starvation period , 2004, Nature.

[26]  Bernd Bukau,et al.  Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB , 2004, Cell.

[27]  Daisuke Oikawa,et al.  A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1 , 2004, The Journal of cell biology.

[28]  Mark R. Segal,et al.  Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death , 2004, Nature.

[29]  Greg L. Hersch,et al.  Sculpting the Proteome with AAA+ Proteases and Disassembly Machines , 2004, Cell.

[30]  D. Gai,et al.  Mechanisms of Conformational Change for a Replicative Hexameric Helicase of SV40 Large Tumor Antigen , 2004, Cell.

[31]  E. Mancini,et al.  Atomic Snapshots of an RNA Packaging Motor Reveal Conformational Changes Linking ATP Hydrolysis to RNA Translocation , 2004, Cell.

[32]  A. Helenius,et al.  Roles of N-linked glycans in the endoplasmic reticulum. , 2004, Annual review of biochemistry.

[33]  Francesco Scaravilli,et al.  Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease , 2004, Nature Genetics.

[34]  D. Ng,et al.  Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control , 2004, The Journal of cell biology.

[35]  Ronald Wetzel,et al.  Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. , 2004, Molecular cell.

[36]  Daniel J Klionsky,et al.  Development by self-digestion: molecular mechanisms and biological functions of autophagy. , 2004, Developmental cell.

[37]  J. Tyson,et al.  Coordinated Activation of Hsp70 Chaperones , 2004, Science.

[38]  I. Wada,et al.  EDEM As an Acceptor of Terminally Misfolded Glycoproteins Released from Calnexin , 2003, Science.

[39]  Maurizio Molinari,et al.  Role of EDEM in the Release of Misfolded Glycoproteins from the Calnexin Cycle , 2003, Science.

[40]  R. Kaufman,et al.  The mammalian unfolded protein response. , 2003, Annual review of biochemistry.

[41]  M. Wiedmann,et al.  The in vivo function of the ribosome-associated Hsp70, Ssz1, does not require its putative peptide-binding domain , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[42]  T. Lithgow,et al.  RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[43]  A. Matouschek,et al.  ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. , 2001, Molecular cell.

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

[45]  L. Gierasch,et al.  Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. , 1999, Journal of molecular biology.

[46]  J Kuriyan,et al.  Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. , 1997, Science.

[47]  K. Römisch Cdc48p is UBX-linked to ER ubiquitin ligases. , 2006, Trends in biochemical sciences.

[48]  R. Kopito,et al.  Impairment of the ubiquitin-proteasome system by protein aggregation. , 2001, Science.