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

Simplified Synthetic TMC‐95A/B Analogues Retain the Potency of Proteasome Inhibitory Activity

Yang, Z., Kwok, B. H. B., Lin, S., Koldobskiy, M. A., Crews, C. M., & Danishefsky, S. J. (2003) · ChemBioChem · doi:10.1002/cbic.200300560 · Cited by 35

Inhibition of the Ubiquitin-Proteasome System by Natural Products for Cancer Therapy

Tsukamoto, S., & Yokosawa, H. (2010) · Planta Medica · doi:10.1055/s-0029-1240901 · Cited by 31

N-Terminal peptidic boronic acids selectively inhibit human ClpXP

Knott, K. M., Fishovitz, J., Thorpe, S. B., Lee, I., & Santos, W. L. (2010) · Organic & Biomolecular Chemistry · doi:10.1039/c004247a · Cited by 31

Molecular characterization of the boron adducts of the proteasome inhibitor bortezomib with epigallocatechin-3-gallate and related polyphenols

Glynn, S. J., Gaffney, K. J., Sainz, M. A., Louie, S. G., & Petasis, N. A. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob02512a · Cited by 31

Bortezomib In Mantle Cell Lymphoma

Suh, K. S., & Goy, A. H. (2008) · Future Oncology · doi:10.2217/14796694.4.2.149 · Cited by 31

Mixing of peptides and electrophilic traps gives rise to potent, broad-spectrum proteasome inhibitors

Verdoes, M., Florea, B. I., van der Linden, W. A., Renou, D., van den Nieuwendijk, A. M. C. H., van der MAREL, G. A., & Overkleeft, H. S. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b702268a · Cited by 31

Covalent hits and where to find them

Lucas, S. C. C., Blackwell, J. H., Hewitt, S. H., Semple, H., Whitehurst, B. C., & Xu, H. (2024) · SLAS DISCOVERY · doi:10.1016/j.slasd.2024.01.003 · Cited by 30

Interferon-γ Causes Cardiac Myocyte Atrophy via Selective Degradation of Myosin Heavy Chain in a Model of Chronic Myocarditis

Cosper, P. F., Harvey, P. A., & Leinwand, L. A. (2012) · American Journal Of Pathology · doi:10.1016/j.ajpath.2012.08.040 · Cited by 30

A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH]

Islamović, S., Galić, B., & Miloš, M. (2014) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2013.848203 · Cited by 30

The potential of ixazomib, a second-generation proteasome inhibitor, in the treatment of multiple myeloma

Brayer, J. B., & Baz, R. (2017) · Therapeutic Advances in Hematology · doi:10.1177/2040620717710171 · Cited by 30

Bis-benzoxaboroles: Design, Synthesis, and Biological Evaluation as Carbonic Anhydrase Inhibitors

Larcher, A., Nocentini, A., Supuran, C. T., Winum, J., van der Lee, A., Vasseur, J., Laurencin, D., & Smietana, M. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00252 · Cited by 30

Structure and Function of the Ubiquitin–Proteasome System

Chondrogianni, N., & Gonos, E. S. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-397863-9.00002-x · Cited by 31

Development of P22 Viral Capsid Nanocomposites as Anti‐ C ancer Drug, Bortezomib ( BTZ ), Delivery Nanoplatforms

Min, J., Moon, H., Yang, H. J., Shin, H., Hong, S. Y., & Kang, S. (2014) · Macromolecular Bioscience · doi:10.1002/mabi.201300401 · Cited by 29

A new class of α-ketoamide derivatives with potent anticancer and anti-SARS-CoV-2 activities

Wang, J., Liang, B., Chen, Y., Chan, J. F., Yuan, S., Ye, H., Nie, L., Zhou, J., Wu, Y., Wu, M., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113267 · Cited by 29

α‐Hydroxyboronate Esters: Formation and Synthetic Applications

Clark, T. B. (2015) · Asian Journal of Organic Chemistry · doi:10.1002/ajoc.201500284 · Cited by 29

Efficacy of Bortezomib as First-Line Treatment for Patients with Multiple Myeloma

Painuly, U., & Kumar, S. K. (2013) · Clinical Medicine Insights Oncology · doi:10.4137/cmo.s7764 · Cited by 30

Targeting the Ubiquitin Proteasome System: Beyond Proteasome Inhibition

Xolalpa, W., Pérez‐Galán, P., Rodríguez, M. S., & Roué, G. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319220014 · Cited by 30

Identification of a Molecular Target of a Novel Fungal Metabolite, Pyrrolizilactone, by Phenotypic Profiling Systems

Futamura, Y., Kawatani, M., Muroi, M., Aono, H., Nogawa, T., & Osada, H. (2013) · ChemBioChem · doi:10.1002/cbic.201300499 · Cited by 29

Recent Developments in the Chemistry of Boron Heterocycles

Wang, B. J., & Groziak, M. P. (2015) · Advances in heterocyclic chemistry · doi:10.1016/bs.aihch.2015.10.002 · Cited by 29

Bortezomib

Einsele, H. (2009) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-642-01222-8_12 · Cited by 29

Inhibitoren für das konstitutive Proteasom und das Immunoproteasom: aktuelle und zukünftige Tendenzen in der Medikamentenentwicklung

Huber, E. M., & Groll, M. (2012) · Angewandte Chemie · doi:10.1002/ange.201201616 · Cited by 28

Molecular Variations Based on Isosteric Replacements

Ciapetti, P., & Giethlen, B. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374194-3.00015-9 · Cited by 28

High Reactivity of α-Boryl Radical of Potassium Alkyltrifluoroborate in Atom-Transfer Radical Addition

Ueda, M., Kato, Y., Taniguchi, N., & Morisaki, T. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c01807 · Cited by 28

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Hanafi, L., Gauchat, D., Godin-Ethier, J., Possamaï, D., Duvignaud, J., Leclerc, D., Grandvaux, N., & Lapointe, R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0099211 · Cited by 30

Niche-Based Screening in Multiple Myeloma Identifies a Kinesin-5 Inhibitor with Improved Selectivity over Hematopoietic Progenitors

Chattopadhyay, S., Stewart, A. L., Mukherjee, S., Huang, C., Hartwell, K. A., Miller, P. G., Subramanian, R., Carmody, L., Yusuf, R. Z., Sykes, D. B., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.01.017 · Cited by 31

α-Amidoboronate esters by amide-directed alkane C H borylation

Hyland, S. N., Meck, E. A., Tortosa, M., & Clark, T. B. (2019) · Tetrahedron Letters · doi:10.1016/j.tetlet.2019.03.020 · Cited by 27

EGF Receptor Activity Modulates Apoptosis Induced by Inhibition of the Proteasome of Vascular Smooth Muscle Cells

Ying, W., Zhang, H., & Sanders, P. W. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006040333 · Cited by 27

High-Throughput Bioluminescence Screening of Ubiquitin-Proteasome Pathway Inhibitors from Chemical and Natural Sources

Ausseil, F., Samson, A., Aussagues, Y., Vandenberghe, I., Créancier, L., Pouny, I., Kruczynski, A., Massiot, G., & Bailly, C. (2006) · SLAS DISCOVERY · doi:10.1177/1087057106296494 · Cited by 27

Design and synthesis of a novel class of furan-based molecules as potential 20S proteasome inhibitors

Fu, Y., Xu, B., Zou, X., Ma, C., Yang, X., Mou, K., Fu, G., Lü, Y., & Xu, P. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.11.020 · Cited by 26

Recent Developments in the Practical Application of Novel Carboxylic Acid Bioisosteres

Horgan, C. P., & O’Sullivan, T. P. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210820112126 · Cited by 26

Synthesis of boronic acid derivatives of tyropeptin: Proteasome inhibitors

Watanabe, T., Momose, I., Abe, M., Abe, H., Sawa, R., Umezawa, Y., Ikeda, D., Takahashi, Y., & Akamatsu, Y. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.02.117 · Cited by 26

Detrimental effects of proteasome inhibition activity in Drosophila melanogaster: implication of ER stress, autophagy, and apoptosis

Velentzas, P. D., Velentzas, A. D., Mpakou, V., Antonelou, M. H., Margaritis, L. H., Papassideri, I. S., & Stravopodis, D. J. (2012) · Cell Biology and Toxicology · doi:10.1007/s10565-012-9235-9 · Cited by 29

Changes in Cancer Treatment

Tariman, J. D. (2017) · Nursing Clinics of North America · doi:10.1016/j.cnur.2016.10.004 · Cited by 27

Exploring the Proteolysis Mechanism of the Proteasomes

Saha, A., Oanca, G., Mondal, D., & Warshel, A. (2020) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c04435 · Cited by 26

Efficient Solid-Phase Synthesis of Compounds Containing Phenylalanine and Its Derivatives via Side-Chain Attachment to the Polymer Support

Lee, Y., & Silverman, R. B. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991679d · Cited by 26

Development and Characterization of Proteasome Inhibitors

Kim, K. B., Fonseca, F. N., & Crews, C. M. (2005) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(05)99039-3 · Cited by 26

The Development of Photometric Sensors for Boronic Acids

Springsteen, G., Ballard, C. E., Gao, S., Wang, W., & Wang, B. (2001) · Bioorganic Chemistry · doi:10.1006/bioo.2001.1217 · Cited by 26

Safety of Purified Isoflavones in Men With Clinically Localized Prostate Cancer

Kumar, N. B., Krischer, J. P., Allen, K., Riccardi, D., Besterman‐Dahan, K., Salup, R. R., Kang, L., Xu, P., & Pow‐Sang, J. M. (2007) · Nutrition and Cancer · doi:10.1080/01635580701432660 · Cited by 25

Structure-Based Design of Selective LONP1 Inhibitors for Probing In Vitro Biology

Kingsley, L. J., He, X., McNeill, M., Nelson, J. T., Nikulin, V. I., Ma, Z., Lu, W., Zhou, V. W., Manuia, M., Kreusch, A., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02152 · Cited by 25

Facile Analysis and Sequencing of Linear and Branched Peptide Boronic Acids by MALDI Mass Spectrometry

Crumpton, J. B., Zhang, W., & Santos, W. L. (2011) · Analytical Chemistry · doi:10.1021/ac2002565 · Cited by 25

20S proteasome as novel biological target for organochalcogenanes

Piovan, L., Milani, P., Silva, M. S., Moraes, P. G., Demasi, M., & Andrade, L. H. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.12.011 · Cited by 25

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

Xin, B., de Bruin, G., Huber, E. M., Bešše, A., Florea, B. I., Filippov, D. V., van der Marel, G. A., Kisselev, A. F., van der Stelt, M., Driessen, C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00705 · Cited by 25

Bortezomib Is Cytotoxic to the Human Growth Plate and Permanently Impairs Bone Growth in Young Mice

Eriksson, E., Zaman, F., Chrysis, D., Wehtje, H., Heino, T. J., & Savendahl, L. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050523 · Cited by 25

Bortezomib treatment causes long-term testicular dysfunction in young male mice

Hou, M., Eriksson, E., Svechnikov, K., Jahnukainen, K., Söder, O., Meinhardt, A., & Savendahl, L. S. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-155 · Cited by 25

My journey from wool research to insulin

Zahn, H. (2000) · Journal of Peptide Science · doi:10.1002/(sici)1099-1387(200001)6:1 · Cited by 29

Design and synthesis of boronic acid inhibitors of endothelial lipase

O’Connell, D. P., LeBlanc, D. F., Cromley, D. A., Billheimer, J. T., Rader, D. J., & Bachovchin, W. W. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.12.043 · Cited by 24

Proteasome inhibitors mechanism; source for design of newer therapeutic agents

Harer, S. L., Bhatia, M. S., & Bhatia, N. M. (2012) · The Journal of Antibiotics · doi:10.1038/ja.2011.84 · Cited by 24

Sugar-boronate ester scaffold tethered pyridyl-imine palladium( ii ) complexes: synthesis and their in vitro anticancer evaluation

Reddy, E. R., Trivedi, R., Sarma, A. V. S., Sridhar, B., Anantaraju, H. S., Sriram, D., Yogeeswari, P., & Nagesh, N. (2015) · Dalton Transactions · doi:10.1039/c5dt03266k · Cited by 24

Toward Understanding Induction of Oxidative Stress and Apoptosis by Proteasome Inhibitors

Paniagua, G., de Bruin, G., Overkleeft, H. S., & Florea, B. I. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5794 · Cited by 24

The Ubiquitin-Proteasome System (UPS) as a Cancer Drug Target: Emerging Mechanisms and Therapeutics

Mata-Cantero, L., Lobato-Gil, S., Aillet, F., Lang, V., & Rodríguez, M. S. (2014) · Springer eBooks · doi:10.1007/978-94-017-9421-3_11 · Cited by 25

Design, synthesis, and biological evaluation of bone-targeted proteasome inhibitors for multiple myeloma

Agyin, J. K., Santhamma, B., & Roy, S. S. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.09.043 · Cited by 23

Toward the Development of Innovative Bifunctional Agents To Induce Differentiation and To Promote Apoptosis in Leukemia: Clinical Candidates and Perspectives

Vizirianakis, I. S., Chatzopoulou, M., Bonovolias, I. D., Nicolaou, I., Demopoulos, V. J., & Tsiftsoglou, A. S. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100189a · Cited by 24

Proteasome inhibition improves diaphragm function in an animal model for COPD

van Hees, H. W. H., Ottenheijm, C. A. C., Ennen, L., Linkels, M., Dekhuijzen, R. P. N., & Heunks, L. M. A. (2011) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00396.2010 · Cited by 23

P‐Glycoprotein Inhibition Sensitizes Human Breast Cancer Cells to Proteasome Inhibitors

Deshmukh, R. R., Kim, S., Elghoul, Y., & Dou, Q. P. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25783 · Cited by 23

Pharmacological proteasome inhibitors and their therapeutic potential

Dou, Q. P., & Nam, S. (2000) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.10.8.1263 · Cited by 23

Molecular Machines for Protein Degradation

Bochtler, M., Groll, M., Brandstetter, H., Clausen, T., & Huber, R. (2008) · Wiley eBooks · doi:10.1002/9783527610754.dd07 · Cited by 23

Renal cold storage followed by transplantation impairs proteasome function and mitochondrial protein homeostasis

Lo, S., MacMillan-Crow, L. A., & Parajuli, N. (2018) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00316.2018 · Cited by 22

The role of the ubiquitin-proteasome pathway in skin cancer development: 26S proteasome-activated NF-κB signal transduction

Yaagoubi, O. M. E., Oularbi, L., Bouyahya, A., Samaki, H., Antri, S. E., & Aboudkhil, S. (2021) · Cancer Biology & Therapy · doi:10.1080/15384047.2021.1978785 · Cited by 22

In vitroandin vivoantitumor activity of the halogenated boroxine dipotassium-trioxohydroxytetrafluorotriborate (K2[B3O3F4OH])

Ivanković, S., Stojković, R., Galić, Z., Galić, B., Ostojić, J., Marasović, M., & Miloš, M. (2014) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2014.926344 · Cited by 22

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Fuchs, O., Provazníková, D., Marinov, I., Kuželová, K., & Špıčka, I. (2009) · Cardiovascular & Haematological Disorders - Drug Targets · doi:10.2174/187152909787581372 · Cited by 23

Different cytotoxicities and cellular localizations of novel quindoline derivatives with or without boronic acid modifications in cancer cells

Yin, R., Zhang, M., Hao, C., Wang, W., Qiu, P., Wan, S., Zhang, L., & Jiang, T. (2013) · Chemical Communications · doi:10.1039/c3cc45203d · Cited by 22

Palladium salicylaldimine complexes containing boronate esters

Zhang, H., Norman, D. W., Wentzell, T. M., Irving, A. M., Edwards, J. P., Wheaton, S. L., Vogels, C. M., Westcott, S. A., Baerlocher, F. J., & Decken, A. (2005) · Transition Metal Chemistry · doi:10.1007/s11243-004-2851-3 · Cited by 22

Potential peptidic proteasome inhibitors by incorporation of an electrophilic trap based on amino acid derived α-substituted sulfonyl fluorides

Alvarez, N. H., van de Langemheen, H., Brouwer, A. J., & Liskamp, R. M. J. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.07.019 · Cited by 22

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Basler, M., Li, J., & Groettrup, M. (2018) · Immunogenetics · doi:10.1007/s00251-018-1084-0 · Cited by 22

Synthesis and Activity of Tyropeptin A Derivatives as Potent and Selective Inhibitors of Mammalian 20S Proteasome

Momose, I., Umezawa, Y., Hirosawa, S., Iijima, M., IINUMA, H., & Ikeda, D. (2005) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.69.1733 · Cited by 22

3D-QSAR studies on tripeptide aldehyde inhibitors of proteasome using CoMFA and CoMSIA methods

Zhu, Y., Pei, J., Liu, Z., Lai, L., Cui, J., & Li, R. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.10.003 · Cited by 22

Synthesis and reactivity of novel Schiff bases containing boronate esters

Norman, D. W., Edwards, J. P., Vogels, C. M., Decken, A., & Westcott, S. A. (2002) · Canadian Journal of Chemistry · doi:10.1139/v01-188 · Cited by 22

Synthesis and biological evaluation of boron peptide analogues of Belactosin C as proteasome inhibitors

Nakamura, H., Watanabe, M., Ban, H. S., Nabeyama, W., & Asai, A. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.103 · Cited by 24

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Zavrski, I., Jakob, C., Kaiser, M., Fleissner, C., Heider, U., & Sezer, O. (2007) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-540-46091-6_14 · Cited by 22

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Orlowski, R. Z., & Zeger, E. L. (2006) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.15.2.117 · Cited by 22

Drug discovery in the next decade: innovation needed ASAP

Bennani, Y. L. (2011) · Drug Discovery Today · doi:10.1016/j.drudis.2011.12.007 · Cited by 23

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Du, S., Luo, X., An, J., Zhang, Z., Zhang, S., Wang, Y., Ding, Y., Jiang, W., Zhang, B., Ma, Y., et al. (2023) · Pest Management Science · doi:10.1002/ps.7451 · Cited by 21

The covalent modification and regulation of TLR8 in HEK-293 cells stimulated with imidazoquinoline agonists

Rajagopal, R., Waller, A. S., Mendoza, J. D., & Wightman, P. D. (2007) · Biochemical Journal · doi:10.1042/bj20070519 · Cited by 21

Synthesis of a (β-acetamido-α-acetoxyethyl)boronic ester via azido boronic esters

Matteson, D. S., Maliakal, D., & Fabry‐Asztalos, L. (2008) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2008.03.031 · Cited by 21

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Momose, I., Iijima, M., Kawada, M., & Ikeda, D. (2007) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.60697 · Cited by 21

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Koreth, J., Alyea, E. P., Murphy, W. J., & Welniak, L. A. (2009) · Transplantation and Cellular Therapy · doi:10.1016/j.bbmt.2009.07.016 · Cited by 21

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Sooman, L., Gullbo, J., Bergqvist, M., Bergström, S. N., Lennartsson, J., & Ekman, S. (2017) · BMC Research Notes · doi:10.1186/s13104-017-2842-z · Cited by 21

Hydrazino-aza and N -azapeptoids with therapeutic potential as anticancer agents

Bouget, K., Aubin, S., Delcros, J., Arlot‐Bonnemains, Y., & Baudy-Floc’h, M. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2003.09.018 · Cited by 22

Proteasome Inhibitors in Cancer Therapy

Adams, J. (2004) · Humana Press eBooks · doi:10.1007/978-1-59259-767-3_41 · Cited by 21

Use of Proteasome Inhibition in the Treatment of Lung Cancer

Schenkein, D. P. (2004) · Clinical Lung Cancer · doi:10.3816/clc.2004.s.021 · Cited by 21

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Goncalves, M. M., Uday, A. B., Forrester, T. J. B., Currie, S., Kim, A. S., Feng, Y., Jitkova, Y., Vėlyvis, A., Harkness, R. W., V, Kimber, M. S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2419881122 · Cited by 20

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Rentsch, A., Landsberg, D., Brodmann, T., Bülow, L., Girbig, A., & Kalesse, M. (2013) · Angewandte Chemie · doi:10.1002/ange.201207900 · Cited by 20

Efficient synthesis, structural characterization and anti-microbial activity of chiral aryl boronate esters of 1,2-O-isopropylidene-α-d-xylofuranose

Trivedi, R., Reddy, E. R., Kumar, C. K., Sridhar, B., Kumar, K. P., & Rao, M. S. (2011) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2011.05.036 · Cited by 20

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Liu, Y., Meng, H., Messersmith, P. B., Lee, B. P., & Dalsin, J. L. (2016) · Springer eBooks · doi:10.1007/978-3-319-46082-6_15 · Cited by 20

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Hinkes, S. P. A., Kämmerer, S., & Klein, C. D. P. (2020) · Chemical Science · doi:10.1039/d0sc03999c · Cited by 20

Molecular design of a high-performance polymeric carrier for delivery of a variety of boronic acid-containing drugs

Kim, A., Suzuki, Y., & Nagasaki, Y. (2020) · Acta Biomaterialia · doi:10.1016/j.actbio.2020.12.015 · Cited by 20

Bortezomib

Einsele, H. (2014) · Recent results in cancer research/Recent Results in Cancer Research · doi:10.1007/978-3-642-54490-3_20 · Cited by 20

Protein Pool Maintenance During Oxidative Stress

Catalgol, B., & Grune, T. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789058129 · Cited by 20

A Computational Characterization of Boron−Oxygen Multiple Bonding in HN═CH−CH═CH−NH−BO

Larkin, J. D., Bhat, K. L., Markham, G. D., James, T. D., Brooks, B. R., & Bock, C. W. (2008) · The Journal of Physical Chemistry A · doi:10.1021/jp800125p · Cited by 20

Discovery of Carboranes as Inducers of 20S Proteasome Activity

Ban, H. S., Minegishi, H., Shimizu, K., Maruyama, M., Yasui, Y., & Nakamura, H. (2010) · ChemMedChem · doi:10.1002/cmdc.201000112 · Cited by 20

Inhibition of proteasomal degradation of Mcl-1 by cobalt chloride suppresses cobalt chloride-induced apoptosis in HCT116 colorectal cancer cells

Lee, M., Lapham, A. S., Brimmell, M., Wilkinson, H., & Packham, G. (2008) · APOPTOSIS · doi:10.1007/s10495-008-0229-2 · Cited by 20

Probing the proteasome cavity in three steps: bio-orthogonal photo-reactive suicide substrates

Geurink, P. P., Florea, B. I., van der MAREL, G. A., Kessler, B. M., & Overkleeft, H. S. (2010) · Chemical Communications · doi:10.1039/c0cc03322g · Cited by 20

The non-specific resistance of cattle to heartwater.

du Plessis, J. L., & Malan, L. (1987) · PubMed · Cited by 20

Gold-Catalyzed Cyclization/Hydroboration of 1,6-Enynes: Synthesis of Bicyclo[3.1.0]hexane Boranes

Wang, G., Wang, Y., Li, Z., Li, H., Yu, M., Pang, M., & Zhao, X. (2022) · Organic Letters · doi:10.1021/acs.orglett.2c03812 · Cited by 19

Carfilzomib in multiple myeloma

Andreu‐Vieyra, C., & Berenson, J. R. (2014) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2014.953050 · Cited by 19

Design and synthesis of the stabilized analogs of belactosin A with the unnatural cis-cyclopropane structure

Kawamura, S., Unno, Y., Asai, A., Arisawa, M., & Shuto, S. (2013) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob41338a · Cited by 19

Carbohydrate‐Based Ferrocenyl Boronate Esters: Synthesis, Characterization, Crystal Structures, and Antibacterial Activity

Reddy, E. R., Trivedi, R., Giribabu, L., Sridhar, B., Kumar, K. P., Rao, M. S., & Sarma, A. V. S. (2013) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.201300773 · Cited by 19

Isolation of Salsolinol, a Tetrahydroisoquinoline Alkaloid, from the Marine Sponge Xestospongia cf. vansoesti as a Proteasome Inhibitor

Nagasawa, Y., Ueoka, R., Yamanokuchi, R., Horiuchi, N., Ikeda, T., Rotinsulu, H., Mangindaan, R. E. P., Ukai, K., Kobayashi, H., Namikoshi, M., et al. (2011) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.59.287 · Cited by 19

Formulation of benzoxaborole drugs in PLLA: from materials preparation to in vitro release kinetics and cellular assays

Sene, S., McLane, J. S., Schaub, N. J., Bégu, S., Mutin, P. H., Ligon, L. A., Gilbert, R. J., & Laurencin, D. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb02258d · Cited by 19

Flow cytometric chemosensitivity assay using JC-1, a sensor of mitochondrial transmembrane potential, in acute leukemia

Yokosuka, T., Goto, H., Fujii, H., Naruto, T., Takeuchi, M., Tanoshima, R., Kato, H., Yanagimachi, M. D., Kajiwara, R., & Yokota, S. (2013) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-013-2303-x · Cited by 19

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

Adams, J., Behnke, M. L., CHEN, S., Cruickshank, A., Dick, L. R., Grenier, L., Klunder, J. M., MA, Y. ‐., Plamondon, L., & Stein, R. L. (1998) · ChemInform · doi:10.1002/chin.199821191 · Cited by 1

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

Benedik, N. S., Šterman, A., Smrdel, L., Pajk, S., Gobec, S., Časar, Z., Gobec, M., & Sosič, I. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02548 · Cited by 3

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

Zhu, Y., Zhao, X., Zhu, X., Wu, G., Li, Y., Ma, Y., Yuan, Y., Yang, J., Hu, Y., Ai, L., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9005093 · Cited by 75