Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes. - Test2 - elhamkhani - TriplyDB

Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes.

Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes.

http://www.wikidata.org/entity/Q40940981

about

The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses The ubiquitin-proteasome pathway and proteasome inhibitors How an inhibitor of the HIV-I protease modulates proteasome activity.Subunit specific inhibitors of proteasomes and their potential for immunomodulation Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes.Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors LMP2-specific inhibitors: chemical genetic tools for proteasome biology.Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes.Human Tumor Antigens and Cancer Immunotherapy.Differential intra-proteasome interactions involving standard and immunosubunits.

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P2860

Mutational analysis of subunit i beta2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes.

http://www.wikidata.org/entity/Q40940981

description

1999 nî lūn-bûn

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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1999年论文

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1999年论文

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name

Mutational analysis of subunit ...... ast and mammalian proteasomes.

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Mutational analysis of subunit ...... ast and mammalian proteasomes.

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Mutational analysis of subunit ...... ast and mammalian proteasomes.

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Mutational analysis of subunit ...... east and mammalian proteasomes

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B Braun

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M Schmidt

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P M Kloetzel

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S Kral

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S Standera

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U Salzmann

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P2860

Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma

Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes

Structure of 20S proteasome from yeast at 2.4 A resolution

The ubiquitin system

The active sites of the eukaryotic 20 S proteasome and their involvement in subunit precursor processing.

Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digests of enolase 1.

Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants.

Effects of interferon gamma and major histocompatibility complex-encoded subunits on peptidase activities of human multicatalytic proteases.

Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits

The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20S proteasome.

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1-2

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