Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids

Lange's handbook of chemistry

Lange, N. A., & Speight, J. G. (1992) · Choice Reviews Online · doi:10.5860/choice.30-1849 · Cited by 7,163

STRUCTURE AND FUNCTIONS OF THE 20S AND 26S PROTEASOMES

Coux, O., Tanaka, K., & Goldberg, A. L. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.004101 · Cited by 2,438

Structure of 20S proteasome from yeast at 2.4Å resolution

Groll, M., Ditzel, L., Löwe, J., Stock, D., Bochtler, M., Bartunik, H. D., & Huber, R. (1997) · Nature · doi:10.1038/386463a0 · Cited by 2,265

Crystal Structure of the 20 S Proteasome from the Archaeon T. acidophilum at 3.4 Å Resolution

Löwe, J., Stock, D., Jap, B. K., Zwickl, P., Baumeister, W. P., & Huber, R. (1995) · Science · doi:10.1126/science.7725097 · Cited by 1,540

Inhibition of the serine proteases leukocyte elastase, pancreatic elastase, cathepsin G, and chymotrypsin by peptide boronic acids.

Kettner, C. A., & Shenvi, A. B. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42521-x · Cited by 294

The selective inhibition of thrombin by peptides of boroarginine.

Kettner, C. A., Mersinger, L. J., & Knabb, R. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44751-x · Cited by 254

Inhibition of serine proteases by peptidyl fluoromethyl ketones

Imperiali, B., & Abeles, R. H. (1986) · Biochemistry · doi:10.1021/bi00361a005 · Cited by 248

R-1-Acetamido-2-phenylethaneboronic acid. A specific transition-state analog for chymotrypsin

Matteson, D. S., Sadhu, K. M., & Lienhard, G. E. (1981) · Journal of the American Chemical Society · doi:10.1021/ja00407a051 · Cited by 153

Design, synthesis, and kinetic evaluation of a unique class of elastase inhibitors, the peptidyl .alpha.-ketobenzoxazoles, and the x-ray crystal structure of the covalent complex between porcine pancreatic elastase and Ac-Ala-Pro-Val-2-benzoxazole

Edwards, P. D., Meyer, E. F., Vijayalakshmi, J., Tuthill, P. A., Andisik, D., Gomes, B. C., & Strimpler, A. M. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00031a046 · Cited by 145

Kinetic Characterization of the Chymotryptic Activity of the 20S Proteasome

Stein, R. L., Melandri, F. D., & Dick, L. R. (1996) · Biochemistry · doi:10.1021/bi952262x · Cited by 138

Fulvestrant (ICI 182,780) down-regulates androgen receptor expression and diminishes androgenic responses in LNCaP human prostate cancer cells

Bhattacharyya, R. S., Krishnan, A. V., Swami, S., & Feldman, D. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-06-0065 · Cited by 56

Organoboron Compounds: Effective Antibacterial and Antiparasitic Agents

Coghi, P. S., Zhu, Y., Xie, H., Hosmane, N. S., & Zhang, Y. (2021) · Molecules · doi:10.3390/molecules26113309 · Cited by 55

Progress on the Application of Bortezomib and Bortezomib-Based Nanoformulations

Liu, J., Zhao, R., Jiang, X., Li, Z., & Zhang, B. (2021) · Biomolecules · doi:10.3390/biom12010051 · Cited by 59

Development of Peptide-Based Reversing Agents for P-Glycoprotein-Mediated Resistance to Carfilzomib

Ao, L., Wu, Y., Kim, D., Jang, E. R., Kim, K., Lee, D.-M., Kim, K. B., & Lee, W. (2012) · Molecular Pharmaceutics · doi:10.1021/mp300044b · Cited by 55

Towards the control of intracellular protein turnover: Mitochondrial Lon protease inhibitors versus proteasome inhibitors

Bayot, A., Basse, N., Lee, I., Gareil, M., Pirotte, B., Bulteau, A., Friguet, B., & Reboud‐Ravaux, M. (2007) · Biochimie · doi:10.1016/j.biochi.2007.10.010 · Cited by 54

Proteasome inhibition by new dual warhead containing peptido vinyl sulfonyl fluorides

Brouwer, A. J., Álvarez, N. H., Ciaffoni, A., van de Langemheen, H., & Liskamp, R. M. J. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.05.042 · Cited by 54

Proteasome inhibition attenuates coxsackievirus-induced myocardial damage in mice

Gao, G., Zhang, J., Si, X., Wong, J. T., Cheung, C., McManus, B. M., & Luo, H. (2008) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00292.2008 · Cited by 54

The ubiquitin proteasome system and efficacy of proteasome inhibitors in diseases

Selvarajan, C., Ganesan, N., & Gopalakrishnan, R. (2012) · International Journal of Rheumatic Diseases · doi:10.1111/j.1756-185x.2012.01737.x · Cited by 54

Substituent Effects on Oxidation‐Induced Formation of Quinone Methides from Arylboronic Ester Precursors

Cao, S., Christiansen, R., & Peng, X. (2013) · Chemistry - A European Journal · doi:10.1002/chem.201300539 · Cited by 53

The Matteson Reaction

Matteson, D. S., Collins, B. S. L., Aggarwal, V. K., & Ciganek, E. (2021) · Organic reactions · doi:10.1002/0471264180.or105.03 · Cited by 53

A panel of subunit-selective activity-based proteasome probes

Verdoes, M., Willems, L. I., van der Linden, W. A., Duivenvoorden, B. A., van der Marel, G. A., Florea, B. I., Kisselev, A. F., & Overkleeft, H. S. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/c001036g · Cited by 52

Flotillin-1 stabilizes caveolin-1 in intestinal epithelial cells

Vassilieva, E. V., Ivanov, A. I., & Nusrat, A. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.12.118 · Cited by 52

Structure-based design of derivatives of tyropeptin A as the potent and selective inhibitors of mammalian 20S proteasome

Momose, I., Umezawa, Y., Hirosawa, S., IINUMA, H., & Ikeda, D. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.02.013 · Cited by 52

Proteasome inhibition with bortezomib: A new therapeutic strategy for non‐Hodgkin's lymphoma

Leonard, J. P., Furman, R. R., & Coleman, M. (2006) · International Journal of Cancer · doi:10.1002/ijc.21805 · Cited by 52

Inhibition of Proteasome Activity Impairs Centrosome-dependent Microtubule Nucleation and Organization

Didier, C., Merdes, A., Gairin, J.-E., & Jabrane‐Ferrat, N. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-12-1140 · Cited by 52

Peptide‐Based Proteasome Inhibitors in Anticancer Drug Design

Micale, N., Scarbaci, K., Troiano, V., Ettari, R., Grasso, S., & Zappalà, M. (2014) · Medicinal Research Reviews · doi:10.1002/med.21312 · Cited by 53

The role of interleukin-2 receptor alpha in cancer

Deborah, J. K. (2005) · Frontiers in bioscience · doi:10.2741/1631 · Cited by 51

A convergent approach to synthesis of bortezomib: the use of TBTU suppresses racemization in the fragment condensation

Ivanov, A. S., Zhalnina, A. A., & Shishkov, S. V. (2009) · Tetrahedron · doi:10.1016/j.tet.2009.06.042 · Cited by 50

Small-Molecule Inhibitors of Proteasome Activity

Gaczynska, M. E., & Osmulski, P. A. (2005) · Humana Press eBooks · doi:10.1385/1-59259-895-1:003 · Cited by 49

Diagnostic and therapeutic potential of protease inhibition

Ćwilichowska, N., Świderska, K. W., Dobrzyń, A., Drąg, M., & Poręba, M. (2022) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2022.101144 · Cited by 53

Potent Proteasome Inhibitors Derived from the Unnatural cis-Cyclopropane Isomer of Belactosin A: Synthesis, Biological Activity, and Mode of Action

Kawamura, S., Unno, Y., List, A., Mizuno, A., Tanaka, M., Sasaki, T., Arisawa, M., Asai, A., Groll, M., & Shuto, S. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4002296 · Cited by 48

TMC‐95A Analogues with Endocyclic Biphenyl Ether Group as Proteasome Inhibitors

Kaiser, M., Milbradt, A. G., Siciliano, C., Assfalg‐Machleidt, I., Machleidt, W., Groll, M., Renner, C., & Moroder, L. (2004) · Chemistry & Biodiversity · doi:10.1002/cbdv.200490008 · Cited by 50

CuII and Cu0 Catalyzed Mono Borylation of Unsaturated Hydrocarbons with B2pin2: Entering into the Water

Stavber, G., & Časar, Z. (2014) · ChemCatChem · doi:10.1002/cctc.201402176 · Cited by 48

The Clinically Approved Proteasome Inhibitor PS-341 Efficiently Blocks Influenza A Virus and Vesicular Stomatitis Virus Propagation by Establishing an Antiviral State

Dudek, S. E., Luig, C., Pauli, E.-K., Schubert, U., & Ludwig, S. (2010) · Journal of Virology · doi:10.1128/jvi.00533-10 · Cited by 49

Proteasome inhibitors induce growth inhibition and apoptosis in myeloma cell lines and in human bone marrow myeloma cells irrespective of chromosome 13 deletion

Fleissner, C., Eucker, J., Possinger, K., Zavrski, I., Naujokat, C., Niem�ller, K., Jakob, C., Heider, U., Langelotz, C., & Sezer, O. (2003) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-003-0454-6 · Cited by 48

Emerging role of carfilzomib in treatment of relapsed and refractory lymphoid neoplasms and multiple myeloma

Jain, S. S., Diefenbach, C., Zain, J. M., & O’Connor (2011) · Core evidence · doi:10.2147/ce.s13838 · Cited by 47

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

Basler, M., Lauer, C., Moebius, J., Weber, R., Przybylski, M., Kisselev, A. F., Tsu, C. A., & Groettrup, M. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103592 · Cited by 47

The proteasome as a target for protozoan parasites

Xie, S. C., Dick, L. R., Gould, A. E., Brand, S. L., & Tilley, L. M. (2019) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1685981 · Cited by 47

Studies of the Synthesis of All Stereoisomers of MG-132 Proteasome Inhibitors in the Tumor Targeting Approach

Mroczkiewicz, M., Winkler, K., Nowis, D., Placha, G., Gołąb, J., & Ostaszewski, R. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901619n · Cited by 47

Ubiquitin proteasome pathway: implications and advances in cancer therapy

Shah, S. A., Potter, M. W., & Callery, M. P. (2001) · Surgical Oncology · doi:10.1016/s0960-7404(01)00018-4 · Cited by 48

Review. Clinical pharmacokinetics of bortezomib.

Levêque, D., Carvalho, M. C. M., & Maloisel, F. (2007) · PubMed · Cited by 47

Cancerous Inhibitor of Protein Phosphatase 2A Mediates Bortezomib-Induced Autophagy in Hepatocellular Carcinoma Independent of Proteasome

Yu, H.-C., Hou, D., Liu, C., Lin, C., Shiau, C., Cheng, A., & Chen, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055705 · Cited by 46

Synthetic peptide conjugates—tailor-made probes for the biology of protein modification and protein processing

Seitz, O., Heinemann, I., Mattes, A., & Waldmann, H. (2001) · Tetrahedron · doi:10.1016/s0040-4020(00)01115-7 · Cited by 46

Novel antitrypanosomal agents

Steverding, D., & Tyler, K. M. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.8.939 · Cited by 45

Clinical and Marketed Proteasome Inhibitors for Cancer Treatment

Zhang, J., Wu, P., & Hu, Y. (2013) · Current Medicinal Chemistry · doi:10.2174/09298673113209990122 · Cited by 46

A Genetically Encoded Boronate‐Containing Amino Acid

Brustad, E. M., Bushey, M. L., Lee, J. W., Groff, D., Liu, W. R., & Schultz, P. G. (2008) · Angewandte Chemie · doi:10.1002/ange.200803240 · Cited by 45

Adaptive modification and flexibility of the proteasome system in response to proteasome inhibition

Naujokat, C., Fuchs, D., & Berges, C. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.05.007 · Cited by 45

Targeting the Ubiquitin—Proteasome Pathway in Breast Cancer

Cardoso, F., Ross, J. S., Piccart, M. J., Sotiriou, C. P., & Durbecq, V. (2004) · Clinical Breast Cancer · doi:10.3816/cbc.2004.n.020 · Cited by 45

A review of the proteasome inhibitor bortezomib in multiple myeloma

Richardson, P. G. G. (2004) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.5.6.1321 · Cited by 46

Three-dimensional structure-activity relationship study of belactosin A and its stereo- and regioisomers: development of potent proteasome inhibitors by a stereochemical diversity-oriented strategy

Yoshida, K., Yamaguchi, K., Mizuno, A., Unno, Y., Asai, A., Sone, T., Yokosawa, H., Matsuda, A., Arisawa, M., & Shuto, S. (2009) · Organic & Biomolecular Chemistry · doi:10.1039/b900384c · Cited by 44

Large library docking for novel SARS‐CoV ‐2 main protease non‐covalent and covalent inhibitors

Fink, E. A., Bardine, C., Gahbauer, S., Singh, I., Detomasi, T. C., White, K. M., Gu, S., Wan, X., Chen, J. S., Ary, B. E., et al. (2023) · Protein Science · doi:10.1002/pro.4712 · Cited by 45

Synergy between Proteasome Inhibitors and Imatinib Mesylate in Chronic Myeloid Leukemia

Hu, Z., Pan, X., Wu, F., Ma, L., Liu, D., Liu, Y., Feng, T., Meng, F., Liu, X., Jiang, Q., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006257 · Cited by 43

Design of proteasome inhibitors with oral efficacy in vivo against Plasmodium falciparum and selectivity over the human proteasome

Xie, S. C., Metcalfe, R. D., Mizutani, H., Puhalovich, T., Hanssen, E. G., Morton, C. J., Du, Y., Dogovski, C., Huang, S., Ciavarri, J. P., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2107213118 · Cited by 43

Opportunities for structure-based design of protease-directed drugs

Mittl, P. R. E., & Grütter, M. G. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.014 · Cited by 43

Contribution of the autophagy-lysosomal and ubiquitin-proteasomal proteolytic systems to total proteolysis in rainbow trout (Oncorhynchus mykiss) myotubes

Seiliez, I., Dias, K., & Cleveland, B. M. (2014) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00370.2014 · Cited by 42

Identification of the Proteasome Inhibitor MG262 as a Potent ATP-Dependent Inhibitor of the Salmonella enterica serovar Typhimurium Lon Protease

Frase, H., Hudak, J. E., & Lee, I. (2006) · Biochemistry · doi:10.1021/bi060542e · Cited by 43

Fluorescent behaviors and reaction mechanism of 10-hydroxybenzo[h]quinolone on the detection of phenylboronic acid

Yang, Y., Liu, Y., Zhai, H., Jia, X., He, Y., Ma, Q., Zhang, R., Liu, Y., & Jiang, K. (2020) · Journal of Luminescence · doi:10.1016/j.jlumin.2020.117224 · Cited by 42

Prostratin and Bortezomib are Novel Inducers of Latent Kaposi'S Sarcoma-Associated Herpesvirus

Brown, H. J., McBride, W. H., Zack, J. A., & Sun, R. (2005) · Antiviral Therapy · doi:10.1177/135965350501000609 · Cited by 42

Selective proteasome inhibitors: modulators of antigen presentation?

Groettrup, M., & Schmidtke, G. (1999) · Drug Discovery Today · doi:10.1016/s1359-6446(98)01292-6 · Cited by 42

Targeting the Ubiquitin-Proteasome System in Atherosclerosis: Status Quo, Challenges, and Perspectives

Wilck, N., & Ludwig, A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5805 · Cited by 43

Bortezomib: A valuable new antineoplastic strategy in multiple myeloma

Bladé, J., Cibeira, M. T., & Rosiñol, L. (2005) · Acta Oncologica · doi:10.1080/02841860510030002 · Cited by 41

Proteasome inhibitors: fromin vitro uses to clinical trials

Rivett, A. J., & Gardner, R. C. (2000) · Journal of Peptide Science · doi:10.1002/1099-1387(200009)6:9 · Cited by 43

Optimization of a series of dipeptides with a P3 threonine residue as non-covalent inhibitors of the chymotrypsin-like activity of the human 20S proteasome

Blackburn, C., Barrett, C., Blank, J. L., Bruzzese, F. J., Bump, N. J., Dick, L. R., Fleming, P. E., Garcia, K., Hales, P., Hu, Z., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.09.032 · Cited by 41

Discovery of boron-containing compounds as Aβ aggregation inhibitors and antioxidants for the treatment of Alzheimer's disease

Lu, C., Hu, J., Wang, Z., Xie, S., Pan, T., Huang, L., & Li, X. (2018) · MedChemComm · doi:10.1039/c8md00315g · Cited by 40

A nano-catalytic approach for C–B bond formation reactions

Verma, P. K., Shegavi, M. L., Bose, S. K., & Geetharani, K. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob02958f · Cited by 40

Proteasome inhibitors as therapeutics

Mitsiades, C. S., Mitsiades, N., Hideshima, T., Richardson, P. G. G., & Anderson, K. C. (2005) · Essays in Biochemistry · doi:10.1042/eb0410205 · Cited by 40

Facile Formation of β-Hydroxyboronate Esters by a Cu-Catalyzed Diboration/Matteson Homologation Sequence

Moore, C. M., Medina, C. R., Cannamela, P. C., McIntosh, M. L., Ferber, C. J., Roering, A. J., & Clark, T. (2014) · Organic Letters · doi:10.1021/ol502767m · Cited by 39

Water‐Dispersible Polydopamine‐Coated Nanofibers for Stimulation of Neuronal Growth and Adhesion

Sieste, S., Mack, T., Synatschke, C. V., Schilling, C., zu Reckendorf, C. M., Pendi, L., Harvey, S., Ruggeri, F. S., Knowles, T. P. J., Meier, C. A., et al. (2018) · Advanced Healthcare Materials · doi:10.1002/adhm.201701485 · Cited by 40

Viral entry and the ubiquitin‐proteasome system

Schneider, S. M., Lee, B. H., & Nicola, A. V. (2020) · Cellular Microbiology · doi:10.1111/cmi.13276 · Cited by 39

Efficient Calculation of QM/MM Frequencies with the Mobile Block Hessian

Ghysels, A., Woodcock, H. L., Larkin, J. D., Miller, B. T., Shao, Y., Kong, J., Neck, D. V., Speybroeck, V. V., Waroquier, M., & Brooks, B. R. (2011) · Journal of Chemical Theory and Computation · doi:10.1021/ct100473f · Cited by 39

Secomycalolide A: A New Proteasome Inhibitor Isolated from a Marine Sponge of the Genus Mycale

Tsukamoto, S., Koimaru, K., & Ohta, T. (2005) · Marine Drugs · doi:10.3390/md302029 · Cited by 39

Influence of irofulven, a transcription-coupled repair-specific antitumor agent, on RNA polymerase activity, stability and dynamics in living mammalian cells

Escargueil, A. E., Poindessous, V., Soares, D. G., Sarasin, A. R., Cook, P. R., & Larsen, A. K. (2008) · Journal of Cell Science · doi:10.1242/jcs.023259 · Cited by 39

Targeting the proteasome pathway

Tsukamoto, S., & Yokosawa, H. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220902866851 · Cited by 38

Activity‐based probes for the multicatalytic proteasome

Hewings, D. S., Flygare, J. A., Wertz, I. E., & Bogyo, M. S. (2017) · FEBS Journal · doi:10.1111/febs.14016 · Cited by 42

Proteasome inhibition as novel treatment strategy in leukaemia

Vink, J., Cloos, J. J., & Kaspers, G. J. L. (2006) · British Journal of Haematology · doi:10.1111/j.1365-2141.2006.06170.x · Cited by 38

Retro Hydrazino-azapeptoids as Peptidomimetics of Proteasome Inhibitors

Aubin, S., Martin, B., Delcros, J., Arlot‐Bonnemains, Y., & Baudy-Floc’h, M. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm049455f · Cited by 38

The Proteasome Inhibitor Carfilzomib Functions Independently of p53 to Induce Cytotoxicity and an Atypical NF-κB Response in Chronic Lymphocytic Leukemia Cells

Gupta, S. V., Hertlein, E. K., Lu, Y., Sass, E. J., Lapalombella, R., Chen, T. L., Davis, M. E., Woyach, J. A., Lehman, A., Jarjoura, D. G., et al. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2754 · Cited by 40

Molecular Variations Based on Isosteric Replacements

Ciapetti, P., & Giethlen, B. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-417205-0.00008-0 · Cited by 38

The ubiquitin–proteasome system in HIV replication: potential targets for antiretroviral therapy

Klinger, P., & Schubert, U. (2005) · Expert Review of Anti-infective Therapy · doi:10.1586/14787210.3.1.61 · Cited by 38

Plasma cell depletion with bortezomib in the treatment of refractory N‐methyl‐ d ‐aspartate (NMDA) receptor antibody encephalitis. Rational developments in neuroimmunological treatment

Keddie, S., Crisp, S. J., Blackaby, J., Cox, A., Coles, A. J., Hart, M., Church, A. J., Vincent, A. C., Zandi, M. S., & Lunn, M. P. (2018) · European Journal of Neurology · doi:10.1111/ene.13759 · Cited by 37

The Proteasome as a Drug Target in the Metazoan Pathogen, Schistosoma mansoni

Bibo‐Verdugo, B., Wang, S. C., Almaliti, J., Ta, A. P., Jiang, Z., Wong, D. A., Lietz, C. B., Suzuki, B. M., El‐Sakkary, N., HOOK, V. Y. H., et al. (2019) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.9b00237 · Cited by 38

Hydroboration of Enynes and Mechanistic Insights

Mao, L., & Bose, S. K. (2020) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.202000603 · Cited by 37

The boron-oxygen core of borinate esters is responsible for the store-operated calcium entry potentiation ability

Dellis, O., Mercier, P., & Chomienne, C. (2011) · BMC Pharmacology · doi:10.1186/1471-2210-11-1 · Cited by 36

Bortezomib for the treatment of non-Hodgkin’s lymphoma

Bose, P., Batalo, M., Holkova, B., & Grant, S. (2014) · Expert Opinion on Pharmacotherapy · doi:10.1517/14656566.2014.965142 · Cited by 38

Built to bind: biosynthetic strategies for the formation of small-molecule protease inhibitors

Kaysser, L. (2019) · Natural Product Reports · doi:10.1039/c8np00095f · Cited by 36

trans-Hydroboration of Propiolamides: Access to Primary and Secondary (E)-β-Borylacrylamides

Grams, R. J., Fritzemeier, R. G., Slebodnick, C., & Santos, W. L. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b02408 · Cited by 36

Tyropeptins A and B, New Proteasome Inhibitors Produced by Kitasatospora sp. MK993-dF2. II. Structure Determination and Synthesis.

Momose, I., Sekizawa, R., Hirosawa, S., Ikeda, D., NAGANAWA, H., IINUMA, H., & TAKEUCHI, T. (2001) · The Journal of Antibiotics · doi:10.7164/antibiotics.54.1004 · Cited by 36

Proteasome Inhibition Up-regulates p53 and Apoptosis-Inducing Factor in Chondrocytes Causing Severe Growth Retardation in Mice

Zaman, F., Menéndez-Benito, V., Eriksson, E., Chagin, A. S., Takigawa, M., Fadeel, B., Dantuma, N. P., Chrysis, D., & Savendahl, L. S. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-3982 · Cited by 36

Control of Chronic Pain by the Ubiquitin–Proteasome System in the Spinal Cord

Ossipov, M. H., Bazov, I., Gardell, L. R., Kowal, J., Yakovleva, T., Усынин, И. Ф., Ekström, T. J., Porreca, F., & Bakalkin, G. Y. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.5126-06.2007 · Cited by 35

Bortezomib and its role in the management of patients with multiple myeloma

Orlowski, R. Z. (2004) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.4.2.171 · Cited by 35

Bortezomib Warhead-Switch Confers Dual Activity against Mycobacterial Caseinolytic Protease and Proteasome and Selectivity against Human Proteasome

Moreira, W., Santhanakrishnan, S., Dymock, B. W., & Dick, T. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00746 · Cited by 34

Synthesis and Applications of β‐Aminoalkylboronic Acid Derivatives

Li, X., & Hall, D. G. (2020) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.202000690 · Cited by 34

Use of pH-Active Catechol-Bearing Polymeric Nanogels with Glutathione-Responsive Dissociation to Codeliver Bortezomib and Doxorubicin for the Synergistic Therapy of Cancer

Qiu, Y., Bai, J., Feng, Y., Shi, X., & Zhao, X. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c10328 · Cited by 34

A unique quinolineboronic acid-based supramolecular structure that relies on double intermolecular B–N bonds for self-assembly in solid state and in solution

Zhang, Y., Li, M., Chandrasekaran, S., Gao, X., Fang, X., Lee, H., Hardcastle, K. I., Yang, J. J., & Wang, B. (2007) · Tetrahedron · doi:10.1016/j.tet.2007.02.042 · Cited by 34

Covalent complexes of proteasome model with peptide aldehyde inhibitors MG132 and MG101: docking and molecular dynamics study

Zhang, S., Shi, Y., Jin, H., Liu, Z., Zhang, L., & Zhang, L. (2009) · Journal of Molecular Modeling · doi:10.1007/s00894-009-0515-0 · Cited by 34

Ethanol withdrawal induced CYP2E1 degradation in vivo, blocked by proteasomal inhibitor PS-341 1 1This article is part of a series of reviews on “Alcohol, Oxidative Stress and Cell Injury”. The full list of papers may be found on the homepage of the journal.

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Plk4 Regulates Centriole Asymmetry and Spindle Orientation in Neural Stem Cells

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Polymerization of dopamine accompanying its coupling to induce self-assembly of block copolymer and application in drug delivery

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Incorporation of Fluorinated Phenylalanine Generates Highly Specific Inhibitor of Proteasome’s Chymotrypsin-like Sites

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Chemical Tools To Study the Proteasome

Verdoes, M., Florea, B. I., van der Marel, G. A., & Overkleeft, H. S. (2009) · European Journal of Organic Chemistry · doi:10.1002/ejoc.200900075 · Cited by 36

Developing structure–activity relationships from an HTS hit for inhibition of the Cks1–Skp2 protein–protein interaction

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Target identification of covalently binding drugs by activity-based protein profiling (ABPP)

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(Immuno)proteasomes as therapeutic target in acute leukemia

Cloos, J. J., Roeten, M. S. F., Franke, N. E., van Meerloo, J., Zweegman, S., Kaspers, G. J. L., & Jansen, G. (2017) · Cancer and Metastasis Reviews · doi:10.1007/s10555-017-9699-4 · Cited by 33

Elucidation of the α‐Keto‐Aldehyde Binding Mechanism: A Lead Structure Motif for Proteasome Inhibition

Graewert, M. A., Gallastegui, N., Stein, M., Schmidt, B., Kloetzel, P., Huber, R., & Groll, M. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201005488 · Cited by 35

Elucidation of the Structure and Intermolecular Interactions of a Reversible Cyclic‐Peptide Inhibitor of the Proteasome by NMR Spectroscopy and Molecular Modeling

Stauch, B., Simon, B., Basile, T., Schneider, G., Malek, N. P., Kalesse, M., & Carlomagno, T. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201000140 · Cited by 32

Access to Cyclic Amino Boronates via Rhodium-Catalyzed Functionalization of Alkyl MIDA Boronates

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Proteasome Inhibitors

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Solid phase synthesis of peptide vinyl sulfone and peptide epoxyketone proteasome inhibitors

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NF-κB Signaling in Targeting Tumor Cells by Oncolytic Viruses—Therapeutic Perspectives

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P′-extended α-ketoamide inhibitors of proteasome

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ChemInform Abstract: Potent and Selective Inhibitors of the Proteasome: Dipeptidyl Boronic Acids.

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α-Aminoboronic Acid Moieties in Boro Dipeptides Modulate Proteasome Subunit Selectivity and Provide Access to Compounds with Potent Anticancer and Anti-Inflammatory Activity

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Synthesis, in Vitro and in Vivo Biological Evaluation, and Comprehensive Understanding of Structure−Activity Relationships of Dipeptidyl Boronic Acid Proteasome Inhibitors Constructed from β-Amino Acids

Zhu, Y., Wu, G., Zhu, X., Ma, Y., Zhao, X., Li, Y., Yuan, Y., Yang, J., Yu, S., Shao, F., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm1009742 · Cited by 38

Synthesis, in Vitro and in Vivo Biological Evaluation, Docking Studies, and Structure−Activity Relationship (SAR) Discussion of Dipeptidyl Boronic Acid Proteasome Inhibitors Composed of β-Amino Acids

Zhu, Y., Zhu, X., Wu, G., Ma, Y., Li, Y., Zhao, X., Yuan, Y., Yang, J., Yu, S., Shao, F., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901407s · Cited by 39

Design, Synthesis, Biological Evaluation, and Structure−Activity Relationship (SAR) Discussion of Dipeptidyl Boronate Proteasome Inhibitors, Part I: Comprehensive Understanding of the SAR of α-Amino Acid Boronates

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