A. Kisselev

发表

The Sizes of Peptides Generated from Protein by Mammalian 26 and 20 S Proteasomes

A. Goldberg, T. Akopian, A. Kisselev, 1999, The Journal of Biological Chemistry.

S. Tevosian, A. Kisselev, 2011, Cancer biology & therapy.

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

A. Goldberg, P. Cascio, K. Rock, 2001, The EMBO journal.

CSA-dependent degradation of CSB by the ubiquitin-proteasome pathway establishes a link between complementation factors of the Cockayne syndrome.

A. Harel-Bellan, Y. Nakatani, I. Kuraoka, 2006, Genes & development.

A cell-permeable inhibitor and activity-based probe for the caspase-like activity of the proteasome.

H. Overkleeft, G. A. van der Marel, B. Kessler, 2007, Bioorganic & medicinal chemistry letters.

Importance of the Different Proteolytic Sites of the Proteasome and the Efficacy of Inhibitors Varies with the Protein Substrate*

A. Goldberg, A. Kisselev, A. Callard, 2006, Journal of Biological Chemistry.

The Caspase-like Sites of Proteasomes, Their Substrate Specificity, New Inhibitors and Substrates, and Allosteric Interactions with the Trypsin-like Sites*

A. Goldberg, H. Overkleeft, H. Ploegh, 2003, Journal of Biological Chemistry.

Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic beta-subunits.

H. Ploegh, E. Fiebiger, D. Tortorella, 2001, Chemistry & biology.

Subunit specific inhibitors of proteasomes and their potential for immunomodulation.

A. Kisselev, M. Groettrup, 2014, Current opinion in chemical biology.

Binding of Hydrophobic Peptides to Several Non-catalytic Sites Promotes Peptide Hydrolysis by All Active Sites of 20 S Proteasomes

A. Goldberg, A. Kisselev, D. Kaganovich, 2002, The Journal of Biological Chemistry.

A post-ubiquitination role for MDM2 and hHR23A in the p53 degradation pathway

S. Grossman, A. Kisselev, C. Brignone, 2004, Oncogene.

New insights into the mechanisms and importance of the proteasome in intracellular protein degradation.

A. Goldberg, T. Akopian, A. Kisselev, 1997, Biological chemistry.

Incorporation of fluorinated phenylalanine generates highly specific inhibitor of proteasome's chymotrypsin-like sites.

H. Overkleeft, G. A. van der Marel, B. Florea, 2010, Journal of medicinal chemistry.

Discovery of a potent and highly β1 specific proteasome inhibitor from a focused library of urea-containing peptide vinyl sulfones and peptide epoxyketones.

H. Overkleeft, G. A. van der Marel, M. Kaiser, 2012, Organic & biomolecular chemistry.

Nature of Pharmacophore Influences Active Site Specificity of Proteasome Inhibitors*

H. Overkleeft, B. Florea, M. Screen, 2010, The Journal of Biological Chemistry.

UV-dependent phosphorylation of COP9/signalosome in UV-induced apoptosis.

A. Harel-Bellan, S. Gerber, R. Groisman, 2016, Oncology reports.

Why the Structure but Not the Activity of the Immunoproteasome Subunit Low Molecular Mass Polypeptide 2 Rescues Antigen Presentation

M. Przybylski, A. Kisselev, M. Groettrup, 2012, The Journal of Immunology.

Specific cell-permeable inhibitor of proteasome trypsin-like sites selectively sensitizes myeloma cells to bortezomib and carfilzomib.

D. Filippov, H. Overkleeft, B. Florea, 2011, Chemistry & biology.

LPS-Induced Formation of Immunoproteasomes: TNF-α and Nitric Oxide Production are Regulated by Altered Composition of Proteasome-Active Sites

C. Papasian, A. Qureshi, D. Morrison, 2011, Cell Biochemistry and Biophysics.

Incorporation of non-natural amino acids improves cell permeability and potency of specific inhibitors of proteasome trypsin-like sites.

G. A. van der Marel, M. Groll, B. Florea, 2013, Journal of medicinal chemistry.

Certain Pairs of Ubiquitin-conjugating Enzymes (E2s) and Ubiquitin-Protein Ligases (E3s) Synthesize Nondegradable Forked Ubiquitin Chains Containing All Possible Isopeptide Linkages*

Steven P Gygi, S. Gygi, A. Goldberg, 2007, Journal of Biological Chemistry.

An inhibitor of proteasome β2 sites sensitizes myeloma cells to immunoproteasome inhibitors.

P. Richardson, C. Mitsiades, B. Florea, 2018, Blood advances.

Cell-line-specific high background in the Proteasome-Glo assay of proteasome trypsin-like activity.

H. Overkleeft, A. Kisselev, Owen M. Wilkins, 2014, Analytical biochemistry.

Molecular Basis of Differential Sensitivity of Myeloma Cells to Clinically Relevant Bolus Treatment with Bortezomib

A. Eastman, M. Screen, A. Kisselev, 2013, PloS one.

A panel of subunit-selective activity-based proteasome probes.

H. Overkleeft, G. A. van der Marel, B. Florea, 2010, Organic & biomolecular chemistry.

Multiple BH3 Mimetics Antagonize Antiapoptotic MCL1 Protein by Inducing the Endoplasmic Reticulum Stress Response and Up-regulating BH3-only Protein NOXA*

A. Eastman, D. Bates, B. Salerni, 2011, The Journal of Biological Chemistry.

Activity of immunoproteasome inhibitor ONX-0914 in acute lymphoblastic leukemia expressing MLL–AF4 fusion protein

M. Israel, S. Fiering, A. Kisselev, 2021, Scientific Reports.

Inhibition of the proteasome β 2 site sensitizes triple-negative breast cancer cells to β 5 inhibitors through a mechanism involving Nrf1 suppression

A. Goldberg, D. Michael, Zhe Sha, 2017 .

Joining the army of proteasome inhibitors.

A. Kisselev, 2008, Chemistry & biology.

A clinically relevant pulse treatment generates a bortezomib-resistant myeloma cell line that lacks proteasome mutations and is sensitive to Bcl-2 inhibitor venetoclax

A. Kisselev, Sondra Downey-Kopyscinski, Sriraja Srinivasa, 2022, Scientific Reports.

The novel β2-selective proteasome inhibitor LU-102 synergizes with bortezomib and carfilzomib to overcome proteasome inhibitor resistance of myeloma cells

S. Haile, A. Kisselev, T. Silzle, 2015, Haematologica.

The novel β2-selective proteasome inhibitor LU-102 decreases phosphorylation of I kappa B and induces highly synergistic cytotoxicity in combination with ibrutinib in multiple myeloma cells

A. Kisselev, Nora Liu, J. Kraus, 2015, Cancer Chemotherapy and Pharmacology.

Phase Ib Study of the Oral Proteasome Inhibitor Ixazomib (MLN9708) and Fulvestrant in Advanced ER+ Breast Cancer Progressing on Fulvestrant.

G. Schwartz, A. Kisselev, K. Shee, 2021, The oncologist.

Proteasome inhibitors: an expanding army attacking a unique target.

H. Overkleeft, A. Kisselev, Wouter A. van der Linden, 2012, Chemistry & biology.

Selective inhibitor of proteasome's caspase-like sites sensitizes cells to specific inhibition of chymotrypsin-like sites.

Matthew Britton, Martijn Verdoes, H. Overkleeft, 2009, Chemistry & biology.

Asymmetric Synthesis of Lysine Analogues with Reduced Basicity, and their Incorporation into Proteasome Inhibitors

H. Overkleeft, B. Florea, A. Kisselev, 2017 .

Proteasome inhibitors: from research tools to drug candidates.

A. Goldberg, A. Kisselev, 2001, Chemistry & biology.

DNA-Histone Cross-Links: Formation and Repair

R. Groisman, A. Kisselev, M. Saparbaev, 2020, Frontiers in Cell and Developmental Biology.

The Ubiquitin Ligase Activity in the DDB2 and CSA Complexes Is Differentially Regulated by the COP9 Signalosome in Response to DNA Damage

Jun-ichi Sawada, Alexei F. Kisselev, R. Drapkin, 2003, Cell.

Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates.

A. Goldberg, A. Kisselev, 2005, Methods in enzymology.

Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown.

A. Goldberg, T. Akopian, A. Kisselev, 1999, Molecular cell.

Range of Sizes of Peptide Products Generated during Degradation of Different Proteins by Archaeal Proteasomes*

Alexei F. Kisselev, A. Goldberg, T. Akopian, 1998, The Journal of Biological Chemistry.

Why Does Threonine, and Not Serine, Function as the Active Site Nucleophile in Proteasomes?*

A. Goldberg, Z. Songyang, A. Kisselev, 2000, The Journal of Biological Chemistry.

Cleavage of the complement system C3 component by HIV-1 proteinase.

A. Kisselev, R. Mentele, K. von der Helm, 1997, Biological chemistry.

Inhibition of the Proteasome β2 Site Sensitizes Triple-Negative Breast Cancer Cells to β5 Inhibitors and Suppresses Nrf1 Activation.

A. Goldberg, H. Overkleeft, M. Cole, 2017, Cell chemical biology.

Mass Polypeptide 2 Rescues Antigen Immunoproteasome Subunit Low Molecular Why the Structure but Not the Activity of the

Reinhold Weber, Michael Basler, Michael Przybylski, 2012 .

Human Immunodeficiency Virus Type 1 Proteinase Is Rapidly and Efficiently Inactivated in Human Plasma by a 2 -Macroglobulin

K. Helm, A. Kisselev, Alexei F. Kisselev, 2009 .

Identification, purification, and cell culture assays of retroviral proteases.

H. Nitschko, A. Kisselev, K. von der Helm, 1994, Methods in enzymology.

A Set of Activity-Based Probes to Visualize Human (Immuno)proteasome Activities.

Mario van der Stelt, H. Overkleeft, G. A. van der Marel, 2016, Angewandte Chemie.

Structure-based design of β1i or β5i specific inhibitors of human immunoproteasomes.

H. Overkleeft, G. A. van der Marel, M. Groll, 2014, Journal of medicinal chemistry.

Processive Degradation of Proteins and Other Catalytic Properties of the Proteasome from Thermoplasma acidophilum*

Alexei F. Kisselev, A. Goldberg, T. Akopian, 1997, The Journal of Biological Chemistry.

Activity-based profiling reveals reactivity of the murine thymoproteasome-specific subunit beta5t.

H. Overkleeft, Keiji Tanaka, S. Murata, 2010, Chemistry & biology.

Azido‐BODIPY Acid Reveals Quantitative Staudinger–Bertozzi Ligation in Two‐Step Activity‐Based Proteasome Profiling

D. Filippov, H. Overkleeft, B. Florea, 2008, Chembiochem : a European journal of chemical biology.

A novel bullet hits the proteasome.

A. Kisselev, 2013, Cancer Cell.

Structure-Based Design of β5c Selective Inhibitors of Human Constitutive Proteasomes.

D. Filippov, H. Overkleeft, G. A. van der Marel, 2016, Journal of medicinal chemistry.

Site-Specific Proteasome Inhibitors

A. Kisselev, 2021, Biomolecules.

Structure‐Based Design of Fluorogenic Substrates Selective for Human Proteasome Subunits

H. Overkleeft, B. Florea, A. Kisselev, 2020, Chembiochem : a European journal of chemical biology.

Structure-based design of beta 1i or beta 5i specific inhibitors of human immunoproteasomes

H. Overkleeft, M. Groll, B. Xin, 2014 .

NEIL3-mediated proteasomal degradation facilitates the repair of cisplatin-induced DNA damage in human cells

F. Renaud, R. Groisman, A. Kisselev, 2023, Scientific Reports.

Structure-Based Design of Inhibitors Selective for Human Proteasome β2c or β2i Subunits

H. Overkleeft, G. A. van der Marel, M. Groll, 2019, Journal of medicinal chemistry.

Use of Proteasome Inhibitors

B. Florea, A. Kisselev, H. Overkleeft, 2015, Current protocols in immunology.

Protein degradation by the proteasome and dissection of its in vivo importance with synthetic inhibitors

A. Goldberg, T. Akopian, A. Kisselev, 1997, Molecular Biology Reports.

Recovery of proteasome activity in cells pulse-treated with proteasome inhibitors is independent of DDI2

A. Kisselev, Ibtisam Ibtisam, 2023, bioRxiv.

An inhibitor of proteasome β2 sites sensitizes myeloma cells to immunoproteasome inhibitors.

P. Richardson, C. Mitsiades, B. Florea, 2018, Blood advances.

An inhibitor of proteasome b 2 sites sensitizes myeloma cells to immunoproteasome inhibitors

C. Mitsiades, B. Florea, A. Kisselev, 2018 .