The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites. - Test2 - elhamkhani - TriplyDB

The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.

The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.

http://www.wikidata.org/entity/Q33187465

about

Computational Approaches for the Discovery of Human Proteasome Inhibitors: An Overview Proteomics in Traditional Chinese Medicine with an Emphasis on Alzheimer's Disease The 26S proteasome is a multifaceted target for anti-cancer therapies Molecular mechanisms of bortezomib resistant adenocarcinoma cells Heat shock proteins in neurodegenerative disorders and aging The origin of proteasome-inhibitor resistant HLA class I peptidomes: a study with HLA-A*68:01 Proteasome activator enhances survival of Huntington's disease neuronal model cells The proteasome and intracellular redox status: implications for apoptotic regulation in lens epithelial cells.Colorectal cancer and NF-κB signaling pathway Combination of novel proteasome inhibitor NPI-0052 and lenalidomide trigger in vitro and in vivo synergistic cytotoxicity in multiple myeloma.Antileukemic activity and mechanism of drug resistance to the marine Salinispora tropica proteasome inhibitor salinosporamide A (Marizomib).Modelling proteasome and proteasome regulator activities.Similar intracellular peptide profile of TAP1/β2 microglobulin double-knockout mice and C57BL/6 wild-type mice as revealed by peptidomic analysis.Molecular characterization and expressional affirmation of the beta proteasome subunit cluster in rock bream immune defense.Apigenin manipulates the ubiquitin-proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells.Proteasome regulator marizomib (NPI-0052) exhibits prolonged inhibition, attenuated efflux, and greater cytotoxicity than its reversible analogs Multicolor monitoring of the proteasome's catalytic signature.Identification of Novel Proteasome Inhibitors from an Enaminone Library.Generation of major histocompatibility complex class I antigens: functional interplay between proteasomes and TPPII.Quantitative time-resolved analysis reveals intricate, differential regulation of standard- and immuno-proteasomes Interferon-gamma, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing.Highbrow proteasome in high-throughput technology.The T210M Substitution in the HLA-a*02:01 gp100 Epitope Strongly Affects Overall Proteasomal Cleavage Site Usage and Antigen Processing.Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma Synergistic anti-myeloma activity of the proteasome inhibitor marizomib and the IMiD immunomodulatory drug pomalidomide.Regulation of translation is required for dendritic cell function and survival during activation.Tungsten Toxicity in Plants A novel class of intrinsic proteasome inhibitory gene transfer peptides.What happened to plant caspases?The roles of the proteasome pathway in signal transduction and neurodegenerative diseases.Targeted inhibition of the immunoproteasome is a potent strategy against models of multiple myeloma that overcomes resistance to conventional drugs and nonspecific proteasome inhibitors Assessing the role of immuno-proteasomes in a mouse model of familial ALS The immunoproteasome as a target in hematologic malignancies.A novel membrane fusion-mediated plant immunity against bacterial pathogens.Proteasome activators.Two vacuole-mediated defense strategies in plants.Synthesis and pharmacology of proteasome inhibitors.Harnessing proteasome dynamics and allostery in drug design.Protease signaling in animal and plant-regulated cell death.Methylene Blue Inhibits Caspases by Oxidation of the Catalytic Cysteine.

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P2860

The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.

http://www.wikidata.org/entity/Q33187465

description

2003 nî lūn-bûn

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2003 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի հունիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

The caspase-like sites of prot ...... s with the trypsin-like sites.

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The caspase-like sites of prot ...... s with the trypsin-like sites.

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type

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The caspase-like sites of prot ...... s with the trypsin-like sites.

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The caspase-like sites of prot ...... s with the trypsin-like sites.

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The caspase-like sites of prot ...... s with the trypsin-like sites.

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The caspase-like sites of prot ...... s with the trypsin-like sites.

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P1433

Journal of Biological Chemistry

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The caspase-like sites of prot ...... ns with the trypsin-like sites

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P2093

Alexei F Kisselev

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Alfred L Goldberg

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Erin Peterson

http://www.w3.org/2001/XMLSchema#string

Herman S Overkleeft

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Hidde L Ploegh

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Margarita Garcia-Calvo

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Nancy A Thornberry

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P2860

26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide.

A gated channel into the proteasome core particle

Structural basis for the activation of 20S proteasomes by 11S regulators

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

Structure of 20S proteasome from yeast at 2.4 A resolution

A combinatorial approach for determining protease specificities: application to interleukin-1beta converting enzyme (ICE)

Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation.

The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release.

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

A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes

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35869-35877

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10.1074/JBC.M303725200

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P433

38

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P478

278

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Michael W Pennington

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2003-06-18T00:00:00Z

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6950319

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12815064

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P921

allosteric inhibitor