ACS Publications. Most Trusted. Most Cited. Most Read
My Activity
CONTENT TYPES

20S Proteasome and Its Inhibitors:  Crystallographic Knowledge for Drug Development

View Author Information
Charité (CCM), Institut für Biochemie, AG Strukturforschung, Monbijoustrasse 2, 10117 Berlin, Germany
Cite this: Chem. Rev. 2007, 107, 3, 687–717
Publication Date (Web):February 23, 2007
https://doi.org/10.1021/cr0502504
Copyright © 2007 American Chemical Society

    Article Views

    4773

    Altmetric

    -

    Citations

    LEARN ABOUT THESE METRICS
    Other access options

    Note: In lieu of an abstract, this is the article's first page.

    Free first page

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. You can change your affiliated institution below.

    *

     To whom correspondence should be addressed. Telephone:  +49-(0)30-450-528304. Fax:  +49-(0)30-450-528903. E-mail:  [email protected].

    Cited By

    This article is cited by 348 publications.

    1. Jie Li, Pei Zhao, Ruoling Li, Wen Yang, Wanxiang Zhao. Rhodium-Catalyzed β-Dehydroborylation of Silyl Enol Ethers: Access to Highly Functionalized Enolates. Organic Letters 2021, 23 (24) , 9580-9585. https://doi.org/10.1021/acs.orglett.1c03796
    2. Rao Song, Wenliang Qiao, Jun He, Jiasheng Huang, Youfu Luo, Tao Yang. Proteases and Their Modulators in Cancer Therapy: Challenges and Opportunities. Journal of Medicinal Chemistry 2021, 64 (6) , 2851-2877. https://doi.org/10.1021/acs.jmedchem.0c01640
    3. Natalia Serrano-Aparicio, Vicent Moliner, Katarzyna Świderek. Nature of Irreversible Inhibition of Human 20S Proteasome by Salinosporamide A. The Critical Role of Lys–Asp Dyad Revealed from Electrostatic Effects Analysis. ACS Catalysis 2021, 11 (6) , 3575-3589. https://doi.org/10.1021/acscatal.0c05313
    4. Wei Su, Rui-Xiao Qiao, Yuan-Ye Jiang, Xiao-Li Zhen, Xia Tian, Jian-Rong Han, Shi-Ming Fan, Qiushi Cheng, Shouxin Liu. Ligand-Free Iron-Catalyzed Regioselectivity-Controlled Hydroboration of Aliphatic Terminal Alkenes. ACS Catalysis 2020, 10 (20) , 11963-11970. https://doi.org/10.1021/acscatal.0c02731
    5. Ying Yu, Meiyu Song, Cailing Chen, Yangyang Du, Chunguang Li, Yu Han, Fei Yan, Zhan Shi, Shouhua Feng. Bortezomib-Encapsulated CuS/Carbon Dot Nanocomposites for Enhanced Photothermal Therapy via Stabilization of Polyubiquitinated Substrates in the Proteasomal Degradation Pathway. ACS Nano 2020, 14 (8) , 10688-10703. https://doi.org/10.1021/acsnano.0c05332
    6. Francisco Martínez-Rojas, Victor C. Diculescu, Francisco Armijo. Electrochemical Immunosensing Platform for the Determination of the 20S Proteasome Using an Aminophenylboronic/Poly-indole-6-carboxylic Acid-Modified Electrode. ACS Applied Bio Materials 2020, 3 (8) , 4941-4948. https://doi.org/10.1021/acsabm.0c00478
    7. Breanna L. Zerfas, Marianne E. Maresh, Darci J. Trader. The Immunoproteasome: An Emerging Target in Cancer and Autoimmune and Neurological Disorders. Journal of Medicinal Chemistry 2020, 63 (5) , 1841-1858. https://doi.org/10.1021/acs.jmedchem.9b01226
    8. Salvatore Pacifico, Valeria Ferretti, Valentina Albanese, Anna Fantinati, Eleonora Gallerani, Francesco Nicoli, Riccardo Gavioli, Francesco Zamberlan, Delia Preti, Mauro Marastoni. Synthesis and Biological Activity of Peptide α-Ketoamide Derivatives as Proteasome Inhibitors. ACS Medicinal Chemistry Letters 2019, 10 (7) , 1086-1092. https://doi.org/10.1021/acsmedchemlett.9b00233
    9. Bo-Tao Xin, Eva M. Huber, Gerjan de Bruin, Wolfgang Heinemeyer, Elmer Maurits, Christofer Espinal, Yimeng Du, Marissa Janssens, Emily S. Weyburne, Alexei F. Kisselev, Bogdan I. Florea, Christoph Driessen, Gijsbert A. van der Marel, Michael Groll, Herman S. Overkleeft. Structure-Based Design of Inhibitors Selective for Human Proteasome β2c or β2i Subunits. Journal of Medicinal Chemistry 2019, 62 (3) , 1626-1642. https://doi.org/10.1021/acs.jmedchem.8b01884
    10. Sanil Bhatia, Viktoria Krieger, Michael Groll, Jeremy D. Osko, Nina Reßing, Heinz Ahlert, Arndt Borkhardt, Thomas Kurz, David W. Christianson, Julia Hauer, Finn K. Hansen. Discovery of the First-in-Class Dual Histone Deacetylase–Proteasome Inhibitor. Journal of Medicinal Chemistry 2018, 61 (22) , 10299-10309. https://doi.org/10.1021/acs.jmedchem.8b01487
    11. Xiaozhou Zhang, Alaknanda Adwal, Andrew G. Turner, David F. Callen, and Andrew D. Abell . New Peptidomimetic Boronates for Selective Inhibition of the Chymotrypsin-like Activity of the 26S Proteasome. ACS Medicinal Chemistry Letters 2016, 7 (12) , 1039-1043. https://doi.org/10.1021/acsmedchemlett.6b00217
    12. Gerjan de Bruin, Bo-Tao Xin, Bogdan I. Florea, and Herman S. Overkleeft . Proteasome Subunit Selective Activity-Based Probes Report on Proteasome Core Particle Composition in a Native Polyacrylamide Gel Electrophoresis Fluorescence-Resonance Energy Transfer Assay. Journal of the American Chemical Society 2016, 138 (31) , 9874-9880. https://doi.org/10.1021/jacs.6b04207
    13. Dennis Bensinger, Theresa Neumann, Christoph Scholz, Constantin Voss, Sabine Knorr, Ulrike Kuckelkorn, Kay Hamacher, Peter-Michael Kloetzel, and Boris Schmidt . Elastase-like Activity Is Dominant to Chymotrypsin-like Activity in 20S Proteasome’s β5 Catalytic Subunit. ACS Chemical Biology 2016, 11 (7) , 1800-1804. https://doi.org/10.1021/acschembio.6b00023
    14. David L. Wilson, Isabel Meininger, Zack Strater, Stephanie Steiner, Frederick Tomlin, Julia Wu, Haya Jamali, Daniel Krappmann, and Marion G. Götz . Synthesis and Evaluation of Macrocyclic Peptide Aldehydes as Potent and Selective Inhibitors of the 20S Proteasome. ACS Medicinal Chemistry Letters 2016, 7 (3) , 250-255. https://doi.org/10.1021/acsmedchemlett.5b00401
    15. Feifei Zhang, Chaoxuan Li, and Wendy L. Kelly . Thiostrepton Variants Containing a Contracted Quinaldic Acid Macrocycle Result from Mutagenesis of the Second Residue. ACS Chemical Biology 2016, 11 (2) , 415-424. https://doi.org/10.1021/acschembio.5b00731
    16. Feifei Zhang and Wendy L. Kelly . Saturation Mutagenesis of TsrA Ala4 Unveils a Highly Mutable Residue of Thiostrepton A. ACS Chemical Biology 2015, 10 (4) , 998-1009. https://doi.org/10.1021/cb5007745
    17. Shun Yoshioka, Masanori Nagatomo, and Masayuki Inoue . Application of Two Direct C(sp3)–H Functionalizations for Total Synthesis of (+)-Lactacystin. Organic Letters 2015, 17 (1) , 90-93. https://doi.org/10.1021/ol503291s
    18. Gerjan de Bruin, Eva M. Huber, Bo-Tao Xin, Eva J. van Rooden, Karol Al-Ayed, Kyung-Bo Kim, Alexei F. Kisselev, Christoph Driessen, Mario van der Stelt, Gijsbert A. van der Marel, Michael Groll, and Herman S. Overkleeft . Structure-Based Design of β1i or β5i Specific Inhibitors of Human Immunoproteasomes. Journal of Medicinal Chemistry 2014, 57 (14) , 6197-6209. https://doi.org/10.1021/jm500716s
    19. Shuhei Kawamura, Yuka Unno, Akira Asai, Mitsuhiro Arisawa, and Satoshi Shuto . Structurally Novel Highly Potent Proteasome Inhibitors Created by the Structure-Based Hybridization of Nonpeptidic Belactosin Derivatives and Peptide Boronates. Journal of Medicinal Chemistry 2014, 57 (6) , 2726-2735. https://doi.org/10.1021/jm500045x
    20. Hui H. Sun, Yoichiro Fukao, Sakiko Ishida, Hiroko Yamamoto, Shugo Maekawa, Masayuki Fujiwara, Takeo Sato, and Junji Yamaguchi . Proteomics Analysis Reveals a Highly Heterogeneous Proteasome Composition and the Post-translational Regulation of Peptidase Activity under Pathogen Signaling in Plants. Journal of Proteome Research 2013, 12 (11) , 5084-5095. https://doi.org/10.1021/pr400630w
    21. Donghui Wei, Lei Fang, Mingsheng Tang, and Chang-Guo Zhan . Fundamental Reaction Pathway for Peptide Metabolism by Proteasome: Insights from First-Principles Quantum Mechanical/Molecular Mechanical Free Energy Calculations. The Journal of Physical Chemistry B 2013, 117 (43) , 13418-13434. https://doi.org/10.1021/jp405337v
    22. Lauren M. Azevedo, Theresa A. Lansdell, Jacob R. Ludwig, Robert A. Mosey, Daljinder K. Woloch, Dillon P. Cogan, Gregory P. Patten, Michael R. Kuszpit, Jason S. Fisk, and Jetze J. Tepe . Inhibition of the Human Proteasome by Imidazoline Scaffolds. Journal of Medicinal Chemistry 2013, 56 (14) , 5974-5978. https://doi.org/10.1021/jm400235r
    23. Sevil Ozcan, Aslamuzzaman Kazi, Frank Marsilio, Bin Fang, Wayne C. Guida, John Koomen, Harshani R. Lawrence, and Saïd M. Sebti . Oxadiazole-isopropylamides as Potent and Noncovalent Proteasome Inhibitors. Journal of Medicinal Chemistry 2013, 56 (10) , 3783-3805. https://doi.org/10.1021/jm400221d
    24. Shuhei Kawamura, Yuka Unno, Anja List, Akirai Mizuno, Motohiro Tanaka, Takuma Sasaki, Mitsuhiro Arisawa, Akira Asai, Michael Groll, and Satoshi Shuto . Potent Proteasome Inhibitors Derived from the Unnatural cis-Cyclopropane Isomer of Belactosin A: Synthesis, Biological Activity, and Mode of Action. Journal of Medicinal Chemistry 2013, 56 (9) , 3689-3700. https://doi.org/10.1021/jm4002296
    25. Audrey Desvergne, Emilie Genin, Xavier Maréchal, Nerea Gallastegui, Laure Dufau, Nicolas Richy, Michael Groll, Joëlle Vidal, and Michèle Reboud-Ravaux . Dimerized Linear Mimics of a Natural Cyclopeptide (TMC-95A) Are Potent Noncovalent Inhibitors of the Eukaryotic 20S Proteasome. Journal of Medicinal Chemistry 2013, 56 (8) , 3367-3378. https://doi.org/10.1021/jm4002007
    26. Theresa A. Lansdell, Michelle A. Hurchla, Jingyu Xiang, Stacy Hovde, Katherine N. Weilbaecher, R. William Henry, and Jetze J. Tepe . Noncompetitive Modulation of the Proteasome by Imidazoline Scaffolds Overcomes Bortezomib Resistance and Delays MM Tumor Growth in Vivo. ACS Chemical Biology 2013, 8 (3) , 578-587. https://doi.org/10.1021/cb300568r
    27. Paul M. Neilsen, Ashok D. Pehere, Kathleen I. Pishas, David F. Callen, and Andrew D. Abell . New 26S Proteasome Inhibitors with High Selectivity for Chymotrypsin-Like Activity and p53-Dependent Cytotoxicity. ACS Chemical Biology 2013, 8 (2) , 353-359. https://doi.org/10.1021/cb300549d
    28. Andrew J. Kale and Bradley S. Moore . Molecular Mechanisms of Acquired Proteasome Inhibitor Resistance. Journal of Medicinal Chemistry 2012, 55 (23) , 10317-10327. https://doi.org/10.1021/jm300434z
    29. Philipp Barbie, Liujie Huo, Rolf Müller, and Uli Kazmaier . Stereoselective Synthesis of Deuterium-Labeled (2S)-Cyclohexenyl Alanines, Biosynthetic Intermediates of Cinnabaramide. Organic Letters 2012, 14 (23) , 6064-6067. https://doi.org/10.1021/ol3029548
    30. Soichiro Kawamorita, Tatsuya Miyazaki, Tomohiro Iwai, Hirohisa Ohmiya, and Masaya Sawamura . Rh-Catalyzed Borylation of N-Adjacent C(sp3)–H Bonds with a Silica-Supported Triarylphosphine Ligand. Journal of the American Chemical Society 2012, 134 (31) , 12924-12927. https://doi.org/10.1021/ja305694r
    31. Donghui Wei, Beilei Lei, Mingsheng Tang, and Chang-Guo Zhan . Fundamental Reaction Pathway and Free Energy Profile for Inhibition of Proteasome by Epoxomicin. Journal of the American Chemical Society 2012, 134 (25) , 10436-10450. https://doi.org/10.1021/ja3006463
    32. Theresa A. Lansdell, Nicole M. Hewlett, Amanda P. Skoumbourdis, Matthew D. Fodor, Ian B. Seiple, Shun Su, Phil. S. Baran, Ken S. Feldman, and Jetze J. Tepe . Palau’amine and Related Oroidin Alkaloids Dibromophakellin and Dibromophakellstatin Inhibit the Human 20S Proteasome. Journal of Natural Products 2012, 75 (5) , 980-985. https://doi.org/10.1021/np300231f
    33. Andrew J. Kale, Ryan P. McGlinchey, Anna Lechner, and Bradley S. Moore . Bacterial Self-Resistance to the Natural Proteasome Inhibitor Salinosporamide A. ACS Chemical Biology 2011, 6 (11) , 1257-1264. https://doi.org/10.1021/cb2002544
    34. Lawrence J. Milo, Jr., Jack H. Lai, Wengen Wu, Yuxin Liu, Hlaing Maw, Youhua Li, Zhiping Jin, Ying Shu, Sarah E. Poplawski, Yong Wu, David G. Sanford, James L. Sudmeier, and William W. Bachovchin . Chemical and Biological Evaluation of Dipeptidyl Boronic Acid Proteasome Inhibitors for Use in Prodrugs and Pro-Soft Drugs Targeting Solid Tumors. Journal of Medicinal Chemistry 2011, 54 (13) , 4365-4377. https://doi.org/10.1021/jm200460q
    35. Jan Deska, Saskia Hähn, and Uli Kazmaier . Stereoselective Synthesis of Deuterated β-Cyclohexenylserine, a Biosynthetic Intermediate of the Salinosporamides. Organic Letters 2011, 13 (12) , 3210-3213. https://doi.org/10.1021/ol201120k
    36. Yongqiang Zhu, Gang Wu, Xinrong Zhu, Yuheng Ma, Xin Zhao, Yuejie Li, Yunxia Yuan, Jie Yang, Sen Yu, Feng Shao, and Meng Lei . 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. Journal of Medicinal Chemistry 2010, 53 (24) , 8619-8626. https://doi.org/10.1021/jm1009742
    37. Beilei Lei, Mohamed Diwan M. Abdul Hameed, Adel Hamza, Marie Wehenkel, Jennifer L. Muzyka, Xiao-Jun Yao, Kyung-Bo Kim, and Chang-Guo Zhan . Molecular Basis of the Selectivity of the Immunoproteasome Catalytic Subunit LMP2-Specific Inhibitor Revealed by Molecular Modeling and Dynamics Simulations. The Journal of Physical Chemistry B 2010, 114 (38) , 12333-12339. https://doi.org/10.1021/jp1058098
    38. Anna Baldisserotto, Valeria Ferretti, Federica Destro, Christian Franceschini, Mauro Marastoni, Riccardo Gavioli and Roberto Tomatis . α,β-Unsaturated N-Acylpyrrole Peptidyl Derivatives: New Proteasome Inhibitors. Journal of Medicinal Chemistry 2010, 53 (17) , 6511-6515. https://doi.org/10.1021/jm100122e
    39. Chunhui Dai and Corey R. J. Stephenson. Total Synthesis of Syringolin A. Organic Letters 2010, 12 (15) , 3453-3455. https://doi.org/10.1021/ol101252y
    40. MaryAnn T. Robak, Melissa A. Herbage and Jonathan A. Ellman. Synthesis and Applications of tert-Butanesulfinamide. Chemical Reviews 2010, 110 (6) , 3600-3740. https://doi.org/10.1021/cr900382t
    41. Paul P. Geurink, Nora Liu, Michiel P. Spaans, Sondra L. Downey, Adrianus M. C. H. van den Nieuwendijk, Gijsbert A. van der Marel, Alexei F. Kisselev, Bogdan I. Florea and Herman S. Overkleeft . Incorporation of Fluorinated Phenylalanine Generates Highly Specific Inhibitor of Proteasome’s Chymotrypsin-like Sites. Journal of Medicinal Chemistry 2010, 53 (5) , 2319-2323. https://doi.org/10.1021/jm9015685
    42. Markus Nett, Tobias A. M. Gulder, Andrew J. Kale, Chambers C. Hughes and Bradley S. Moore. Function-Oriented Biosynthesis of β-Lactone Proteasome Inhibitors in Salinispora tropica. Journal of Medicinal Chemistry 2009, 52 (19) , 6163-6167. https://doi.org/10.1021/jm901098m
    43. Meng Lei, Xin Zhao, Zhanli Wang and Yongqiang Zhu. Pharmacophore Modeling, Docking Studies, and Synthesis of Novel Dipeptide Proteasome Inhibitors Containing Boron Atoms. Journal of Chemical Information and Modeling 2009, 49 (9) , 2092-2100. https://doi.org/10.1021/ci900225s
    44. Michael Groll, Katherine A. McArthur, Venkat R. Macherla, Rama Rao Manam and Barbara C. Potts . Snapshots of the Fluorosalinosporamide/20S Complex Offer Mechanistic Insights for Fine Tuning Proteasome Inhibition. Journal of Medicinal Chemistry 2009, 52 (17) , 5420-5428. https://doi.org/10.1021/jm900559x
    45. Yongqiang Zhu, Xin Zhao, Xinrong Zhu, Gang Wu, Yuejie Li, Yuheng Ma, Yunxia Yuan, Jie Yang, Yang Hu, Li Ai and Qingzhi Gao . 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. Journal of Medicinal Chemistry 2009, 52 (14) , 4192-4199. https://doi.org/10.1021/jm9005093
    46. Leandro H. Andrade and Thiago Barcellos. Lipase-Catalyzed Highly Enantioselective Kinetic Resolution of Boron-Containing Chiral Alcohols. Organic Letters 2009, 11 (14) , 3052-3055. https://doi.org/10.1021/ol901091f
    47. Michael Frezza, Sarmad Sahiel Hindo, Dajena Tomco, Marco M. Allard, Qiuzhi Cindy Cui, Mary Jane Heeg, Di Chen, Q. Ping Dou and Cláudio N. Verani . Comparative Activities of Nickel(II) and Zinc(II) Complexes of Asymmetric [NN′O] Ligands as 26S Proteasome Inhibitors. Inorganic Chemistry 2009, 48 (13) , 5928-5937. https://doi.org/10.1021/ic900276g
    48. Ryan A. Shenvi and E. J. Corey. A Short and Efficient Synthesis of (−)-7-Methylomuralide, a Potent Proteasome Inhibitor. Journal of the American Chemical Society 2009, 131 (16) , 5746-5747. https://doi.org/10.1021/ja901400q
    49. António J. Marques, R. Palanimurugan, Ana C. Matias, Paula C. Ramos and R. Jürgen Dohmen . Catalytic Mechanism and Assembly of the Proteasome. Chemical Reviews 2009, 109 (4) , 1509-1536. https://doi.org/10.1021/cr8004857
    50. Rama Rao Manam, Katherine A. McArthur, Ta-Hsiang Chao, Jeffrey Weiss, Janid A. Ali, Vito J. Palombella, Michael Groll, G. Kenneth Lloyd, Michael A. Palladino, Saskia T. C. Neuteboom, Venkat R. Macherla and Barbara C. M. Potts. Leaving Groups Prolong the Duration of 20S Proteasome Inhibition and Enhance the Potency of Salinosporamides. Journal of Medicinal Chemistry 2008, 51 (21) , 6711-6724. https://doi.org/10.1021/jm800548b
    51. Michael Groll, Emily P. Balskus and Eric N. Jacobsen . Structural Analysis of Spiro β-Lactone Proteasome Inhibitors. Journal of the American Chemical Society 2008, 130 (45) , 14981-14983. https://doi.org/10.1021/ja806059t
    52. Boris Cvek, Vesna Milacic, Jan Taraba and Q. Ping Dou . Ni(II), Cu(II), and Zn(II) Diethyldithiocarbamate Complexes Show Various Activities Against the Proteasome in Breast Cancer Cells. Journal of Medicinal Chemistry 2008, 51 (20) , 6256-6258. https://doi.org/10.1021/jm8007807
    53. Remco Sprangers, Xiaoming Li, Xinliang Mao, John L. Rubinstein, Aaron D. Schimmer and Lewis E. Kay . TROSY-Based NMR Evidence for a Novel Class of 20S Proteasome Inhibitors. Biochemistry 2008, 47 (26) , 6727-6734. https://doi.org/10.1021/bi8005913
    54. Melissa A. Beenen, Chihui An and Jonathan A. Ellman. Asymmetric Copper-Catalyzed Synthesis of α-Amino Boronate Esters from N-tert-Butanesulfinyl Aldimines. Journal of the American Chemical Society 2008, 130 (22) , 6910-6911. https://doi.org/10.1021/ja800829y
    55. Lyndon M. West and D. John Faulkner. Acanthosulfate, a Sulfated Hydroxyhydroquinone Sesterterpenoid from the Sponge Acanthodendrilla sp.. Journal of Natural Products 2008, 71 (2) , 269-271. https://doi.org/10.1021/np070443h
    56. Hao-Chi Hsu, Michelle Wang, Amanda Kovach, Andrew J Darwin, Huilin Li. P. aeruginosa CtpA protease adopts a novel activation mechanism to initiate the proteolytic process. The EMBO Journal 2024, 43 (8) , 1634-1652. https://doi.org/10.1038/s44318-024-00069-6
    57. Miao Yuan, Hanwen Ji, Fengxin Sun, Qiang Chen, Ping Cheng. Rational design of novel phenol ether derivatives as non-covalent proteasome inhibitors through 3D-QSAR, molecular docking and ADMET prediction. Exploration of Drug Science 2023, , 435-453. https://doi.org/10.37349/eds.2023.00029
    58. Giorgia Gazzaroli, Andrea Angeli, Arianna Giacomini, Roberto Ronca. Proteasome inhibitors as anticancer agents. Expert Opinion on Therapeutic Patents 2023, 33 (11) , 775-796. https://doi.org/10.1080/13543776.2023.2272648
    59. Taylor Thomas, David Salcedo-Tacuma, David M. Smith. Structure, Function, and Allosteric Regulation of the 20S Proteasome by the 11S/PA28 Family of Proteasome Activators. Biomolecules 2023, 13 (9) , 1326. https://doi.org/10.3390/biom13091326
    60. Romina A. Guedes, Jorge H. Grilo, Andreia N. Carvalho, Pedro M. P. Fernandes, Ana S. Ressurreição, Vanessa Brito, Adriana O. Santos, Samuel Silvestre, Eleonora Gallerani, Maria João Gama, Riccardo Gavioli, Jorge A. R. Salvador, Rita C. Guedes. New Scaffolds of Proteasome Inhibitors: Boosting Anticancer Potential by Exploiting the Synergy of In Silico and In Vitro Methodologies. Pharmaceuticals 2023, 16 (8) , 1096. https://doi.org/10.3390/ph16081096
    61. Jianhao Liu, Xiaoman Xu, Yanying Li, Jingxia Xu, Ruogang Zhao, Siwei Liu, Jingliang Wu, Li Zhang, Bo Zhang. Bortezomib-loaded mixed micelles realize a “three-in-one” effect for enhanced breast cancer treatment. Biomaterials Science 2023, 11 (14) , 4890-4906. https://doi.org/10.1039/D3BM00254C
    62. Irem Tatar, Sirin Uysal, Sinem Yilmaz, Ayse H. Tarikogullari, Petek Ballar Kirmizibayrak, Zeynep Soyer. Design, synthesis, and biological evaluation of some novel naphthoquinone‐glycine / β‐alanine anilide derivatives as noncovalent proteasome inhibitors. Chemical Biology & Drug Design 2023, 101 (6) , 1283-1298. https://doi.org/10.1111/cbdd.14212
    63. Roberta Panebianco, Maurizio Viale, Fabrizio Loiacono, Valeria Lanza, Danilo Milardi, Graziella Vecchio. Terpyridine Glycoconjugates and Their Metal Complexes: Antiproliferative Activity and Proteasome Inhibition. ChemMedChem 2023, 18 (7) https://doi.org/10.1002/cmdc.202200701
    64. Lucia M. Balsa, Enrique J. Baran, Ignacio E. León. Copper Complexes as Antitumor Agents: In vitro and In vivo Evidence. Current Medicinal Chemistry 2023, 30 (5) , 510-557. https://doi.org/10.2174/0929867328666211117094550
    65. Xiaofeng Zhou. Insights of metal 8-hydroxylquinolinol complexes as the potential anticancer drugs. Journal of Inorganic Biochemistry 2023, 238 , 112051. https://doi.org/10.1016/j.jinorgbio.2022.112051
    66. Grazia R. Tundo, Paolo Cascio, Danilo Milardi, Anna Maria Santoro, Grazia Graziani, Pedro Miguel Lacal, Alessio Bocedi, Francesco Oddone, Mariacristina Parravano, Andrea Coletta, Massimo Coletta, Diego Sbardella. Targeting immunoproteasome in neurodegeneration: A glance to the future. Pharmacology & Therapeutics 2023, 241 , 108329. https://doi.org/10.1016/j.pharmthera.2022.108329
    67. Paul S. Sharp, Maria Stylianou, Luis M. Arellano, Juliana C. Neves, Alfredo M. Gravagnuolo, Abbie Dodd, Katharine Barr, Neus Lozano, Thomas Kisby, Kostas Kostarelos. Graphene Oxide Nanoscale Platform Enhances the Anti‐Cancer Properties of Bortezomib in Glioblastoma Models. Advanced Healthcare Materials 2023, 12 (3) https://doi.org/10.1002/adhm.202201968
    68. Eva M. Huber. Epipolythiodioxopiperazine‐Based Natural Products: Building Blocks, Biosynthesis and Biological Activities. ChemBioChem 2022, 23 (23) https://doi.org/10.1002/cbic.202200341
    69. Xue Xia, Chun-Meng Tang, Gu-Zi Chen, Jia-Jia Han. Proteasome Dysfunction Leads to Suppression of the Hypoxic Response Pathway in Arabidopsis. International Journal of Molecular Sciences 2022, 23 (24) , 16148. https://doi.org/10.3390/ijms232416148
    70. A. Farini, L. Tripodi, C. Villa, F. Napolitano, F. Strati, D. Molinaro, F. Facciotti, B. Cassani, Y. Torrente. Inhibition of the immunoproteasome modulates innate immunity to ameliorate muscle pathology of dysferlin-deficient BlAJ mice. Cell Death & Disease 2022, 13 (11) https://doi.org/10.1038/s41419-022-05416-1
    71. Boya Chen, Haiying Zhu, Bo Yang, Ji Cao. The dichotomous role of immunoproteasome in cancer: Friend or foe?. Acta Pharmaceutica Sinica B 2022, 366 https://doi.org/10.1016/j.apsb.2022.11.005
    72. Fengxiang Zhu, Pengpeng Yin, Xiao-Feng Wu. Regioselective catalytic carbonylation and borylation of alkynes with aryldiazonium salts toward α-unsubstituted β-boryl ketones. Chemical Science 2022, 13 (41) , 12122-12126. https://doi.org/10.1039/D2SC04867A
    73. Laura Ielo, Vincenzo Patamia, Andrea Citarella, Thomas Efferth, Nasim Shahhamzehei, Tanja Schirmeister, Claudio Stagno, Thierry Langer, Antonio Rescifina, Nicola Micale, Vittorio Pace. Novel Class of Proteasome Inhibitors: In Silico and In Vitro Evaluation of Diverse Chloro(trifluoromethyl)aziridines. International Journal of Molecular Sciences 2022, 23 (20) , 12363. https://doi.org/10.3390/ijms232012363
    74. Celso Alves, Joana Silva, Susete Pintéus, Romina A. Guedes, Rita C. Guedes, Rebeca Alvariño, Rafaela Freitas, Márcia I. Goettert, Helena Gaspar, Amparo Alfonso, Maria C. Alpoím, Luis M. Botana, Rui Pedrosa. Bromoditerpenes from the Red Seaweed Sphaerococcus coronopifolius as Potential Cytotoxic Agents and Proteasome Inhibitors and Related Mechanisms of Action. Marine Drugs 2022, 20 (10) , 652. https://doi.org/10.3390/md20100652
    75. D. Couchie, T. Medali, V. Diderot, M. Raymondjean, B. Friguet, M. Rouis. Circadian rhythmicity of the thioredoxin system in cultured murine peritoneal macrophages. Biochimie 2022, 198 , 76-85. https://doi.org/10.1016/j.biochi.2022.03.006
    76. Carlota Leonardo-Sousa, Andreia Neves Carvalho, Romina A. Guedes, Pedro M. P. Fernandes, Natália Aniceto, Jorge A. R. Salvador, Maria João Gama, Rita C. Guedes. Revisiting Proteasome Inhibitors: Molecular Underpinnings of Their Development, Mechanisms of Resistance and Strategies to Overcome Anti-Cancer Drug Resistance. Molecules 2022, 27 (7) , 2201. https://doi.org/10.3390/molecules27072201
    77. Jonathan E. Dannatt, Anshu Yadav, Milton R. Smith, Robert E. Maleczka. Amide directed iridium C(sp3)–H borylation catalysis with high N-methyl selectivity. Tetrahedron 2022, 109 , 132578. https://doi.org/10.1016/j.tet.2021.132578
    78. Mingyu Chen, Sarun Juengpanich, Shijie Li, Win Topatana, Ziyi Lu, Qiang Zheng, Jiasheng Cao, Jiahao Hu, Esther Chan, Lidan Hou, Jiang Chen, Fang Chen, Yu Liu, Sukanda Jiansirisomboon, Zhen Gu, Suparat Tongpeng, Xiujun Cai. Bortezomib‐Encapsulated Dual Responsive Copolymeric Nanoparticles for Gallbladder Cancer Targeted Therapy. Advanced Science 2022, 9 (7) https://doi.org/10.1002/advs.202103895
    79. Zhenzhen Zhang, Xin Liu, Liyun Zhao, Yaru Zhou, Jianyou Shi, Weini Chen, Jinqi Li. A review on the treatment of multiple myeloma with small molecular agents in the past five years. European Journal of Medicinal Chemistry 2022, 229 , 114053. https://doi.org/10.1016/j.ejmech.2021.114053
    80. Alexei F. Kisselev. Site-Specific Proteasome Inhibitors. Biomolecules 2022, 12 (1) , 54. https://doi.org/10.3390/biom12010054
    81. Puneet Labana, Mark H. Dornan, Matthew Lafrenière, Tomasz L. Czarny, Eric D. Brown, John P. Pezacki, Christopher N. Boddy. Armeniaspirols inhibit the AAA+ proteases ClpXP and ClpYQ leading to cell division arrest in Gram-positive bacteria. Cell Chemical Biology 2021, 28 (12) , 1703-1715.e11. https://doi.org/10.1016/j.chembiol.2021.07.001
    82. Patrick D. Fischer, Evangelos Papadopoulos, Jon M. Dempersmier, Zi-Fu Wang, Radosław P. Nowak, Katherine A. Donovan, Joann Kalabathula, Christoph Gorgulla, Pierre P.M. Junghanns, Eihab Kabha, Nikolaos Dimitrakakis, Ognyan I. Petrov, Constantine Mitsiades, Christian Ducho, Vladimir Gelev, Eric S. Fischer, Gerhard Wagner, Haribabu Arthanari. A biphenyl inhibitor of eIF4E targeting an internal binding site enables the design of cell-permeable PROTAC-degraders. European Journal of Medicinal Chemistry 2021, 219 , 113435. https://doi.org/10.1016/j.ejmech.2021.113435
    83. Terri J. Harford, Fariba Rezaee, Manveen K. Gupta, Vladimir Bokun, Sathyamangla V. Naga Prasad, Giovanni Piedimonte. Respiratory syncytial virus induces β 2 -adrenergic receptor dysfunction in human airway smooth muscle cells. Science Signaling 2021, 14 (685) https://doi.org/10.1126/scisignal.abc1983
    84. Luciana C. Furtado, Anelize Bauermeister, Rafael de Felicio, Raquel Ortega, Francisco das Chagas L. Pinto, João Agostinho Machado-Neto, Daniela B. B. Trivella, Otilia D. L. Pessoa, Diego V. Wilke, Norberto P. Lopes, Paula C. Jimenez, Leticia V. Costa-Lotufo. Marine Streptomyces sp. Isolated From the Brazilian Endemic Tunicate Euherdmania sp. Produces Dihydroeponemycin and Analogs With Potent Antiglioma Activity. Frontiers in Marine Science 2021, 8 https://doi.org/10.3389/fmars.2021.644730
    85. Mahadev L. Shegavi, Suresh Saini, Ramesh Bhawar, Meghana Desai Vishwantha, Shubhankar Kumar Bose. Recyclable Copper Nanoparticles‐Catalyzed Hydroboration of Alkenes and β‐Borylation of α,β‐Unsaturated Carbonyl Compounds with Bis(Pinacolato)Diboron. Advanced Synthesis & Catalysis 2021, 363 (9) , 2408-2416. https://doi.org/10.1002/adsc.202001616
    86. Sheng-hong Du, Yu-jiao Xiang, Lu Liu, Mu Nie, Yu Hou, Ling Wang, Ban-ban Li, Miao Xu, Qing-liang Teng, Jun Peng, Ming Hou, Yan Shi. Co-Inhibition of the Immunoproteasome Subunits LMP2 and LMP7 Ameliorates Immune Thrombocytopenia. Frontiers in Immunology 2021, 11 https://doi.org/10.3389/fimmu.2020.603278
    87. Michèle Reboud-Ravaux. Le protéasome, la seconde vie d’une cible thérapeutique validée : aspects structuraux et nouveaux inhibiteurs. Biologie Aujourd’hui 2021, 215 (1-2) , 1-23. https://doi.org/10.1051/jbio/2021005
    88. Zhang-Xu He, Yun-Peng Gong, Xin Zhang, Li-Ying Ma, Wen Zhao. Pyridazine as a privileged structure: An updated review on anticancer activity of pyridazine containing bioactive molecules. European Journal of Medicinal Chemistry 2021, 209 , 112946. https://doi.org/10.1016/j.ejmech.2020.112946
    89. Sirin Uysal, Zeynep Soyer, Merve Saylam, Ayse H. Tarikogullari, Sinem Yilmaz, Petek Ballar Kirmizibayrak. Design, synthesis and biological evaluation of novel naphthoquinone-4-aminobenzensulfonamide/carboxamide derivatives as proteasome inhibitors. European Journal of Medicinal Chemistry 2021, 209 , 112890. https://doi.org/10.1016/j.ejmech.2020.112890
    90. Youdong Mao. Structure, Dynamics and Function of the 26S Proteasome. 2021, 1-151. https://doi.org/10.1007/978-3-030-58971-4_1
    91. Levente M. Mihalovits, György G. Ferenczy, György M. Keserű. Mechanistic and thermodynamic characterization of oxathiazolones as potent and selective covalent immunoproteasome inhibitors. Computational and Structural Biotechnology Journal 2021, 19 , 4486-4496. https://doi.org/10.1016/j.csbj.2021.08.008
    92. Jyoti Singh, Amruta Suryan, Sandeep Kumar, Shweta Sharma. Phthalazinone Scaffold: Emerging Tool in the Development of Target Based Novel Anticancer Agents. Anti-Cancer Agents in Medicinal Chemistry 2020, 20 (18) , 2228-2245. https://doi.org/10.2174/1871520620666200807220146
    93. Yajun Yang, Ke Wang, Bo Wu, Ying Yang, Fangfang Lai, Xiaoguang Chen, Zhiyan Xiao. Design, synthesis and biological evaluation of triaryl compounds as novel 20S proteasome inhibitors. Bioorganic & Medicinal Chemistry Letters 2020, 30 (21) , 127508. https://doi.org/10.1016/j.bmcl.2020.127508
    94. Anna Maria Santoro, Alessandro D’Urso, Alessandra Cunsolo, Danilo Milardi, Roberto Purrello, Diego Sbardella, Grazia R. Tundo, Donatella Diana, Roberto Fattorusso, Antonio Di Dato, Antonella Paladino, Marco Persico, Massimo Coletta, Caterina Fattorusso. Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States. International Journal of Molecular Sciences 2020, 21 (19) , 7190. https://doi.org/10.3390/ijms21197190
    95. G.R. Tundo, D. Sbardella, A.M. Santoro, A. Coletta, F. Oddone, G. Grasso, D. Milardi, P.M. Lacal, S. Marini, R. Purrello, G. Graziani, M. Coletta. The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges. Pharmacology & Therapeutics 2020, 213 , 107579. https://doi.org/10.1016/j.pharmthera.2020.107579
    96. Paula Guzmán-Téllez, Diana Martínez-Valencia, Angélica Silva-Olivares, Rosa M. del Ángel, Jesús Serrano-Luna, Mineko Shibayama. Naegleria fowleri and Naegleria gruberi 20S proteasome: identification and characterization. European Journal of Cell Biology 2020, 99 (5) , 151085. https://doi.org/10.1016/j.ejcb.2020.151085
    97. Imen Boualia, Abdelmadjid Debache, Raouf Boulcina, Thierry Roisnel, Fabienne Berrée, Joëlle Vidal, Bertrand Carboni. Synthesis of novel 3-(quinazol-2-yl)-quinolines via SNAr and aluminum chloride-induced (hetero) arylation reactions and biological evaluation as proteasome inhibitors. Tetrahedron Letters 2020, 61 (17) , 151805. https://doi.org/10.1016/j.tetlet.2020.151805
    98. Anna Maria Santoro, Valeria Lanza, Francesco Bellia, Diego Sbardella, Grazia R. Tundo, Alessandra Cannizzo, Giuseppe Grasso, Mariaconcetta Arizzi, Vincenzo G. Nicoletti, Stefano Alcaro, Giosuè Costa, Adriana Pietropaolo, Gaetano Malgieri, Gianluca D'Abrosca, Roberto Fattorusso, Sara García‐Viñuales, Ikhlas M. M. Ahmed, Massimiliano Coletta, Danilo Milardi. Pyrazolones Activate the Proteasome by Gating Mechanisms and Protect Neuronal Cells from β‐Amyloid Toxicity. ChemMedChem 2020, 15 (3) , 302-316. https://doi.org/10.1002/cmdc.201900612
    99. Stanley C. Xie, Lawrence R. Dick, Alexandra Gould, Stephen Brand, Leann Tilley. The proteasome as a target for protozoan parasites. Expert Opinion on Therapeutic Targets 2019, 23 (11) , 903-914. https://doi.org/10.1080/14728222.2019.1685981
    100. Guedes, Aniceto, Andrade, Salvador, Guedes. Chemical Patterns of Proteasome Inhibitors: Lessons Learned from Two Decades of Drug Design. International Journal of Molecular Sciences 2019, 20 (21) , 5326. https://doi.org/10.3390/ijms20215326
    Load more citations

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    Pair your accounts.

    Export articles to Mendeley

    Get article recommendations from ACS based on references in your Mendeley library.

    You’ve supercharged your research process with ACS and Mendeley!

    STEP 1:
    Click to create an ACS ID

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    MENDELEY PAIRING EXPIRED
    Your Mendeley pairing has expired. Please reconnect