Mechanism of substrate unfolding and translocation by the regulatory particle of the proteasome from Methanocaldococcus jannaschii.

[1]  D. Finley,et al.  Recognition and processing of ubiquitin-protein conjugates by the proteasome. , 2009, Annual review of biochemistry.

[2]  Yigong Shi,et al.  Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. , 2009, Molecular cell.

[3]  D. Kraut,et al.  How to pick a protein and pull at it , 2008, Nature Structural &Molecular Biology.

[4]  Tania A. Baker,et al.  Pore loops of the AAA+ ClpX machine grip substrates to drive translocation and unfolding , 2008, Nature Structural &Molecular Biology.

[5]  M. Glickman,et al.  The central unit within the 19S regulatory particle of the proteasome , 2008, Nature Structural &Molecular Biology.

[6]  Andreas Martin,et al.  Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. , 2008, Molecular cell.

[7]  A. Matouschek,et al.  Protein targeting to ATP-dependent proteases. , 2008, Current opinion in structural biology.

[8]  A. Horwitz,et al.  ATP-induced Structural Transitions in PAN, the Proteasome-regulatory ATPase Complex in Archaea* , 2007, Journal of Biological Chemistry.

[9]  Andreas Martin,et al.  Distinct static and dynamic interactions control ATPase-peptidase communication in a AAA+ protease. , 2007, Molecular cell.

[10]  T. Gillette,et al.  Proteasomes: Machines for All Reasons , 2007, Cell.

[11]  A. Goldberg Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. , 2007, Biochemical Society transactions.

[12]  A. Goldberg,et al.  Docking of the Proteasomal ATPases ’ C-termini in the 20 S Proteasomes alpha Ring Opens the Gate for Substrate Entry , 2007 .

[13]  A. Goldberg,et al.  Proteasomes and their associated ATPases: a destructive combination. , 2006, Journal of structural biology.

[14]  Thomas Walz,et al.  ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins. , 2005, Molecular cell.

[15]  R. Huber,et al.  Molecular Machines for Protein Degradation , 2005, Chembiochem : a European journal of chemical biology.

[16]  C. Hill,et al.  THE 1.9 ANGSTROM STRUCTURE OF A PROTEASOME-11S ACTIVATOR COMPLEX AND IMPLICATIONS FOR THE PROTEASOME-PAN/PA700 INTERACTIONS , 2005 .

[17]  Michael Knop,et al.  A versatile toolbox for PCR‐based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes , 2004, Yeast.

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

[19]  D. Mckay,et al.  Kinetics of protein substrate degradation by HslUV. , 2004, Journal of structural biology.

[20]  Robert E. Cohen,et al.  Proteasomes and their kin: proteases in the machine age , 2004, Nature Reviews Molecular Cell Biology.

[21]  Attila Nagy,et al.  Thermal stability of chemically denatured green fluorescent protein (GFP): A preliminary study , 2004 .

[22]  Deborah S Wuttke,et al.  Nucleic acid recognition by OB-fold proteins. , 2003, Annual review of biophysics and biomolecular structure.

[23]  V. Agrawal,et al.  OB-fold: growing bigger with functional consistency. , 2003, Current protein & peptide science.

[24]  C. Gross,et al.  Lack of a robust unfoldase activity confers a unique level of substrate specificity to the universal AAA protease FtsH. , 2003, Molecular cell.

[25]  A. Goldberg,et al.  ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. , 2003, Molecular cell.

[26]  V. Arcus OB-fold domains: a snapshot of the evolution of sequence, structure and function. , 2002, Current opinion in structural biology.

[27]  T. Mizushima,et al.  The structure of the mammalian 20S proteasome at 2.75 A resolution. , 2002, Structure.

[28]  T. Mizushima,et al.  Structure determination of the constitutive 20S proteasome from bovine liver at 2.75 A resolution. , 2002, Journal of biochemistry.

[29]  A. Goldberg,et al.  Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. , 2001, Molecular cell.

[30]  A. Goldberg,et al.  PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone , 2000, Nature Cell Biology.

[31]  H. Aldrich,et al.  Biochemical and Physical Properties of the Methanococcus jannaschii 20S Proteasome and PAN, a Homolog of the ATPase (Rpt) Subunits of the Eucaryal 26S Proteasome , 2000, Journal of bacteriology.

[32]  A. Goldberg,et al.  An Archaebacterial ATPase, Homologous to ATPases in the Eukaryotic 26 S Proteasome, Activates Protein Breakdown by 20 S Proteasomes* , 1999, The Journal of Biological Chemistry.

[33]  A. Horwich,et al.  Global unfolding of a substrate protein by the Hsp100 chaperone ClpA , 1999, Nature.

[34]  K. Siegers,et al.  Epitope tagging of yeast genes using a PCR‐based strategy: more tags and improved practical routines , 1999, Yeast.

[35]  R. Sauer,et al.  The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. , 1998, Genes & development.

[36]  R. Huber,et al.  Structure of 20S proteasome from yeast at 2.4Å resolution , 1997, Nature.

[37]  A. Varshavsky,et al.  The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses , 1987, Cell.

[38]  G. Fink,et al.  Methods in yeast genetics , 1979 .

[39]  Shreedhar Gadge,et al.  THE MOLECULAR STRUCTURE OF GREEN FLUORESCENT PROTEIN , 2022 .