Search Results - "Kisselev, A F"

The Ubiquitin Ligase Activity in the DDB2 and CSA Complexes Is Differentially Regulated by the COP9 Signalosome in Response to DNA Damage by Groisman, Regina, Polanowska, Jolanta, Kuraoka, Isao, Sawada, Jun-ichi, Saijo, Masafumi, Drapkin, Ronny, Kisselev, Alexei F., Tanaka, Kiyoji, Nakatani, Yoshihiro

“…Nucleotide excision repair (NER) is a major cellular defense against the carcinogenic effects of ultraviolet light from the sun. Mutational inactivation of NER…”
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The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation by Kisselev, A F, Akopian, T N, Woo, K M, Goldberg, A L

“…Knowledge about the sizes of peptides generated by proteasomes during protein degradation is essential to fully understand their degradative mechanisms and the…”
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Proteasome inhibitors: from research tools to drug candidates by Kisselev, Alexei F., Goldberg, Alfred L.

“…The 26S proteasome is a 2.4 MDa multifunctional ATP-dependent proteolytic complex, which degrades the majority of cellular polypeptides by an unusual enzyme…”
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26S proteasomes and immunoproteasomes produce mainly N‐extended versions of an antigenic peptide by Cascio, Paolo, Hilton, Craig, Kisselev, Alexei F., Rock, Kenneth L., Goldberg, Alfred L.

“…Protein degradation by proteasomes is the source of most antigenic peptides presented on MHC class I molecules. To determine whether proteasomes generate these…”
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Proteasome Active Sites Allosterically Regulate Each Other, Suggesting a Cyclical Bite-Chew Mechanism for Protein Breakdown by Kisselev, Alexei F, Akopian, Tatos N, Castillo, Vanesa, Goldberg, Alfred L

“…In eukaryotes, the 20S proteasome contains two chymotrypsin-like, two trypsin-like, and two active sites shown here to have caspase-like specificity. We report…”
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A post-ubiquitination role for MDM2 and hHR23A in the p53 degradation pathway by BRIGNONE, Chrystelle, BRADLEY, Kathleen E, KISSELEV, Alexei F, GROSSMAN, Steven R

“…Abrogation of ubiquitin/proteasome-dependent turnover of p53 is critical for its activation. UbL-UBA proteins, including human homolog of Rad23 (hHR23)…”
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Range of Sizes of Peptide Products Generated during Degradation of Different Proteins by Archaeal Proteasomes by Kisselev, Alexei F., Akopian, Tatos N., Goldberg, Alfred L.

“…The 20 S proteasome processively degrades cell proteins to peptides. Information on the sizes and nature of these products is essential for understanding the…”
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Why Does Threonine, and Not Serine, Function as the Active Site Nucleophile in Proteasomes? by Kisselev, Alexei F., Songyang, Zhou, Goldberg, Alfred L.

“…Proteasomes belong to the N-terminal nucleophile group of amidases and function through a novel proteolytic mechanism, in which the hydroxyl group of the…”
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Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome from Thermoplasma acidophilum by Akopian, Tatos N., Kisselev, Alexei F., Goldberg, Alfred L.

“…Although the structure of the 20 S proteasome from Thermoplasma acidophilum has been elucidated, its enzymatic properties have not been explored in depth…”
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New insights into the mechanisms and importance of the proteasome in intracellular protein degradation by Goldberg, A L, Akopian, T N, Kisselev, A F, Lee, D H, Rohrwild, M

“…Recent studies of the 20S proteasome from Thermoplasma acidophilum have uncovered some fundamental new properties of its catalytic mechanism. Unlike…”
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The novel  2-selective proteasome inhibitor LU-102 synergizes with bortezomib and carfilzomib to overcome proteasome inhibitor resistance of myeloma cells by Kraus, M., Bader, J., Geurink, P. P., Weyburne, E. S., Mirabella, A. C., Silzle, T., Shabaneh, T. B., van der Linden, W. A., de Bruin, G., Haile, S. R., van Rooden, E., Appenzeller, C., Li, N., Kisselev, A. F., Overkleeft, H., Driessen, C.

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Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates by Kisselev, Alexei F, Goldberg, Alfred L

“…Eukaryotic proteasomes have three different types of active sites: two chymotrypsin-like, two trypsin-like, and two caspase-like (also termed PGPH) sites that…”
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Importance of the Different Proteolytic Sites of the Proteasome and the Efficacy of Inhibitors Varies with the Protein Substrate by Kisselev, Alexei F., Callard, Alice, Goldberg, Alfred L.

“…The relative importance of the different proteolytic sites in mammalian proteasomes in protein degradation has not been studied systematically. Nevertheless,…”
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Cleavage of the complement system C3 component by HIV-1 proteinase by Kisselev, A F, Mentele, R, von der Helm, K

“…The C3 factor of the complement system and its C3b fragment are cleaved in vitro by the proteinase of the human immunodeficiency virus, type 1 (HIV PR). The…”
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Protein degradation by the proteasome and dissection of its in vivo importance with synthetic inhibitors by Goldberg, A L, Akopian, T N, Kisselev, A F, Lee, D H

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Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic β-subunits by Kessler, Benedikt M, Tortorella, Domenico, Altun, Mikael, Kisselev, Alexei F, Fiebiger, Edda, Hekking, Brian G, Ploegh, Hidde L, Overkleeft, Herman S

“…Background: The 26S proteasome is responsible for most cytosolic proteolysis, and is an important protease in major histocompatibility complex class I-mediated…”
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Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings by Kisselev, Alexei F, Kaganovich, Daniel, Goldberg, Alfred L

“…The eukaryotic 20 S proteasome contains the following 6 active sites: 2 chymotrypsin-like, 2 trypsin-like, and 2 caspase-like. We previously showed that…”
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The Caspase-like Sites of Proteasomes, Their Substrate Specificity, New Inhibitors and Substrates, and Allosteric Interactions with the Trypsin-like Sites by Kisselev, Alexei F., Garcia-Calvo, Margarita, Overkleeft, Herman S., Peterson, Erin, Pennington, Michael W., Ploegh, Hidde L., Thornberry, Nancy A., Goldberg, Alfred L.

“…Proteasomes are the primary sites for protein degradation in mammalian cells. Each proteasome particle contains two chymotrypsin-like, two trypsin-like, and…”
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Human immunodeficiency virus type 1 proteinase is rapidly and efficiently inactivated in human plasma by alpha 2-macroglobulin by Kisselev, A F, von der Helm, K

“…Human plasma impairs the activity of the human immunodeficiency virus (HIV-1) proteinase to cleave the HIV-1 gag-polyprotein precursor. The inhibition is due…”
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