The substrate translocation channel of the proteasome.

[1]  C. Hill,et al.  Structural basis for the activation of 20S proteasomes by 11S regulators , 2000, Nature.

[2]  R. Huber,et al.  A gated channel into the proteasome core particle , 2000, Nature Structural Biology.

[3]  H. Holzhütter,et al.  Evidence for the Existence of a Non-catalytic Modifier Site of Peptide Hydrolysis by the 20 S Proteasome* , 2000, The Journal of Biological Chemistry.

[4]  A. Lupas,et al.  Structure and mechanism of ATP-dependent proteases. , 1999, Current opinion in chemical biology.

[5]  R. Huber,et al.  The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[6]  A. Goldberg,et al.  Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. , 1999, Molecular cell.

[7]  C. Slaughter,et al.  The Proteasome, a Novel Protease Regulated by Multiple Mechanisms* , 1999, The Journal of Biological Chemistry.

[8]  W Baumeister,et al.  Proteasomes and other self-compartmentalizing proteases in prokaryotes. , 1999, Trends in microbiology.

[9]  Robert Huber,et al.  Contribution of Proteasomal β-Subunits to the Cleavage of Peptide Substrates Analyzed with Yeast Mutants* , 1998, The Journal of Biological Chemistry.

[10]  W. Baumeister,et al.  A Subcomplex of the Proteasome Regulatory Particle Required for Ubiquitin-Conjugate Degradation and Related to the COP9-Signalosome and eIF3 , 1998, Cell.

[11]  M. Glickman,et al.  Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome , 1998, The EMBO journal.

[12]  R. Huber,et al.  Conformational constraints for protein self-cleavage in the proteasome. , 1998, Journal of molecular biology.

[13]  A. R. Khan,et al.  Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes , 1998, Protein science : a publication of the Protein Society.

[14]  M. Hochstrasser,et al.  Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

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

[16]  P. Kloetzel,et al.  Analysis of mammalian 20S proteasome biogenesis: the maturation of beta‐subunits is an ordered two‐step mechanism involving autocatalysis. , 1996, The EMBO journal.

[17]  M. Hochstrasser,et al.  Autocatalytic Subunit Processing Couples Active Site Formation in the 20S Proteasome to Completion of Assembly , 1996, Cell.

[18]  R. Huber,et al.  Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. , 1995, Science.

[19]  M. Rechsteiner,et al.  Activation of the multicatalytic protease. The 11 S regulator and 20 S ATPase complexes contain distinct 30-kilodalton subunits. , 1994, The Journal of biological chemistry.

[20]  C. Slaughter,et al.  Identification, purification, and characterization of a high molecular weight, ATP-dependent activator (PA700) of the 20 S proteasome. , 1994, The Journal of biological chemistry.

[21]  A. Varshavsky,et al.  In vivo half-life of a protein is a function of its amino-terminal residue. , 1986, Science.

[22]  M. Rechsteiner,et al.  The proteasome activator 11 S REG (PA28) and class I antigen presentation. , 2000, The Biochemical journal.

[23]  W. Baumeister,et al.  The 26S proteasome: a molecular machine designed for controlled proteolysis. , 1999, Annual review of biochemistry.