Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules

[1]  H. Kawasaki,et al.  Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate neurite formation: a novel catalytic activity in proteasome. , 1993, Biochemical and biophysical research communications.

[2]  A. Goldberg,et al.  Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. , 1993, Nature.

[3]  D. Finley,et al.  MHC-linked LMP gene products specifically alter peptidase activities of the proteasome , 1993, Nature.

[4]  A. Goldberg,et al.  A role for the ubiquitin-dependent proteolytic pathway in MHC class l-restricted antigen presentation , 1993, Nature.

[5]  R. Schimke,et al.  In vivo inhibition of cyclin B degradation and induction of cell-cycle arrest in mammalian cells by the neutral cysteine protease inhibitor N-acetylleucylleucylnorleucinal. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[6]  A. Rivett.  Proteasomes: multicatalytic proteinase complexes. , 1993, The Biochemical journal.

[7]  M. Rechsteiner,et al.  The multicatalytic and 26 S proteases. , 1993, The Journal of biological chemistry.

[8]  J. Trowsdale,et al.  The transporters associated with antigen presentation. , 1993, Seminars in cell biology.

[9]  R. Germain,et al.  The biochemistry and cell biology of antigen processing and presentation. , 1993, Annual review of immunology.

[10]  P. Cresswell,et al.  Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I molecules , 1992, Nature.

[11]  M. Orłowski,et al.  Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. , 1992, Biochemistry.

[12]  S. Jentsch,et al.  In vivo function of the proteasome in the ubiquitin pathway. , 1992, The EMBO journal.

[13]  A. Goldberg,et al.  Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle. , 1992, The American journal of physiology.

[14]  A. Goldberg,et al.  Proteolysis, proteasomes and antigen presentation , 1992, Nature.

[15]  A. Ciechanover,et al.  The ubiquitin system for protein degradation. , 1992, Annual review of biochemistry.

[16]  J. Monaco,et al.  A molecular model of MHC class-I-restricted antigen processing. , 1992, Immunology today.

[17]  A. Goldberg.  The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. , 1992, European journal of biochemistry.

[18]  K. Tanaka,et al.  Improved method for preparation of ubiquitin‐ligated lysozyme as substrate of ATP‐dependent proteolysis , 1991, FEBS letters.

[19]  E. Gilboa,et al.  A frameshift mutation at the NH2 terminus of the nucleoprotein gene does not affect generation of cytotoxic T lymphocyte epitopes. , 1991, Journal of immunology.

[20]  A. Hershko,et al.  Methylated ubiquitin inhibits cyclin degradation in clam embryo extracts. , 1991, The Journal of biological chemistry.

[21]  K. Tanaka,et al.  ATP‐dependent reversible association of proteasomes with multiple protein components to form 26S complexes that degrade ubiquitinated proteins in human HL‐60 cells , 1991, FEBS letters.

[22]  K. Rock,et al.  Dissociation of β 2-microglobulin leads to the accumulation of a substantial pool of inactive class I MHC heavy chains on the cell surface , 1991, Cell.

[23]  A. Ciechanover,et al.  The ubiquitin-activating enzyme, E1, is required for stress-induced lysosomal degradation of cellular proteins. , 1991, The Journal of biological chemistry.

[24]  M. Orłowski,et al.  The multicatalytic proteinase complex, a major extralysosomal proteolytic system. , 1990, Biochemistry.

[25]  K. Rock,et al.  Generation of class I MHC-restricted T-T hybridomas. , 1990, Journal of immunology.

[26]  T. Elliott,et al.  Assembly of MHC class I molecules analyzed in vitro , 1990, Cell.

[27]  A. Goldberg,et al.  The proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins. , 1990, The Journal of biological chemistry.

[28]  M. Smith,et al.  The conformational flexibility of class I H-2 molecules as revealed by anti-peptide antibodies specific for intracytoplasmic determinants: differential reactivity of beta 2-microglobulin "bound" and "free" H-2Kb heavy chains. , 1990, Molecular immunology.

[29]  S. Jentsch,et al.  Ubiquitin‐conjugating enzymes UBC4 and UBC5 mediate selective degradation of short‐lived and abnormal proteins. , 1990, The EMBO journal.

[30]  N. Katunuma,et al.  Inhibitory effect of di- and tripeptidyl aldehydes on calpains and cathepsins. , 1990, Journal of enzyme inhibition.

[31]  M. Bevan,et al.  Introduction of soluble protein into the class I pathway of antigen processing and presentation , 1988, Cell.

[32]  J. Dice.  Molecular determinants of protein half‐lives in eukaryotic cells , 1987, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[33]  M. Gething,et al.  Antigen Presentation Pathways to Class I and Class II MHC‐Restricted T Lymphocytes , 1987, Immunological reviews.

[34]  M. Rechsteiner,et al.  Ubiquitin-mediated pathways for intracellular proteolysis. , 1987, Annual review of cell biology.

[35]  H. Ljunggren,et al.  Selective rejection of H–2-deficient lymphoma variants suggests alternative immune defence strategy , 1986, Nature.

[36]  A. Goldberg,et al.  The ATP dependence of the degradation of short- and long-lived proteins in growing fibroblasts. , 1985, The Journal of biological chemistry.

[37]  A. Ciechanover,et al.  Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85 , 1984, Cell.

[38]  K. Rock,et al.  Inhibition of antigen-specific T lymphocyte activation by structurally related Ir gene-controlled polymers. Evidence of specific competition for accessory cell antigen presentation , 1983, The Journal of experimental medicine.

[39]  P. Marrack,et al.  Antigen presentation by Ia+ B cell hybridomas to H-2-restricted T cell hybridomas. , 1982, Proceedings of the National Academy of Sciences of the United States of America.

[40]  C. Janeway,et al.  Cooperative interaction of B lymphocytes with antigen-specific helper T lymphocytes is MHC restricted , 1981, Nature.

[41]  K. Ozato,et al.  Monoclonal antibodies to mouse MHC antigens. III. Hybridoma antibodies reacting to antigens of the H-2b haplotype reveal genetic control of isotype expression. , 1981, Journal of immunology.

[42]  A. Goldberg,et al.  Intracellular protein degradation in mammalian and bacterial cells. , 1974, Annual review of biochemistry.