Targeting proteins for degradation.

Protacs: Chimeric molecules that target proteins to the Skp1–Cullin–F box complex for ubiquitination and degradation

Sakamoto, K. M., Kim, K. B., Kumagai, A., Mercurio, F., Crews, C. M., & Deshaies, R. J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.141230798 · Cited by 2,609

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

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209

In Vivo Half-Life of a Protein Is a Function of Its Amino-Terminal Residue

Bachmair, A., Finley, D. J., & Varshavsky, A. J. (1986) · Science · doi:10.1126/science.3018930 · Cited by 1,976

Recognition of the polyubiquitin proteolytic signal

Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,769

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome

Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764

A proteomics approach to understanding protein ubiquitination

Peng, J., Schwartz, D., Elias, J. E., Thoreen, C. C., Cheng, D., Marsischky, G., Roelofs, J., Finley, D. J., & Gygi, S. P. (2003) · Nature Biotechnology · doi:10.1038/nbt849 · Cited by 1,601

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

Themes and variations on ubiquitylation

Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,507

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

Jeffrey, P. D., Russo, A. A., Polyák, K., Gibbs, E., Hurwitz, J., Massagué, J., & Pavletich, N. P. (1995) · Nature · doi:10.1038/376313a0 · Cited by 1,455

Quantitative affinity interaction of ubiquitinated and non-ubiquitinated proteins with proteasome subunit Rpn10

Бунеева, О. А., Gnedenko, O. V., Kopylov, A. T., Medvedeva, M. V., Zgoda, V. G., Ivanov, A. S., & Medvedev, A. E. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917090073 · Cited by 7

Comparative proteome analysis reveals VPS28 regulates milk fat synthesis through ubiquitylation in bovine mammary epithelial cells

Liu, L., & Zhang, Q. (2020) · PeerJ · doi:10.7717/peerj.9542 · Cited by 6

Dynamics of Ubiquitination in Differentiation and Dedifferentiation of Pancreatic β-cells: Putative Target for Diabetes

Kumar, A., Francis, M., Bhaskar, S., Vishnuvajhala, S., & Prasanna, J. (2022) · Current Protein and Peptide Science · doi:10.2174/1389203723666220422092023 · Cited by 6

Soluble expression of an amebic cysteine protease in the cytoplasm of Escherichia coli SHuffle Express cells and purification of active enzyme

Jalomo-Khayrova, E., Mares, R. E., Muñoz-Muñoz, P. L. A., Meléndez-López, S. G., Rivero, I. A., & Ramos, M. A. (2018) · BMC Biotechnology · doi:10.1186/s12896-018-0429-y · Cited by 7

Peptides meet ubiquitin: Simple interactions regulating complex cell signaling

Veggiani, G., & Sidhu, S. S. (2018) · Peptide Science · doi:10.1002/pep2.24091 · Cited by 7

In vitro analysis of proteasome-associated USP14 activity for substrate degradation and deubiquitylation

Muniyappan, S., & Lee, B. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.12.028 · Cited by 6

Proteasome Stress Triggers Death of SH-SY5Y and T98G Cells via Different Cellular Mechanisms

Pilchová, I., Klacanova, K., Dibdiaková, K., Saksonova, S., Štefaniková, A., Vidomanová, E., Lichardusová, L., Hatok, J., & Račay, P. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2355-0 · Cited by 6

Chemical inhibition of the integrated stress response impairs the ubiquitin-proteasome system

Xu, S., Gierisch, M. E., Barchi, E., Poser, I., Alberti, S., Salomons, F. A., & Dantuma, N. P. (2024) · Communications Biology · doi:10.1038/s42003-024-06974-0 · Cited by 6

Inhibition of Proteasome, But Not Lysosome, Upregulates Organic Anion Transporter 3 in Vitro and in VivoPreprint

Fan, Y., Wang, H., Yu, Z., Liang, Z., Li, Y., & You, G. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4252414 · Cited by 5

A barley SS2a single base mutation at the splicing site leads to obvious changes in starch

Wang, B., Liu, J., Chen, X., Xu, Q., Zhang, Y., Dong, H., Tang, H., Qi, P., Deng, M., Ma, J., et al. (2023) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2023.10.031 · Cited by 4

Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy

Turner, M., Harkness, R. W., V, Ripstein, Z. A., Huang, R., & Vahidi, S. (2025) · Biochemical Journal · doi:10.1042/bcj20253239 · Cited by 5

Achieving cell-type-specific bioorthogonal chemistry using enzyme-activated caged tetrazines

Knittel, C. H., Chadwick, S. R., Vance, J. A., Kuehling, C., & Devaraj, N. K. (2026) · Nature Chemical Biology · doi:10.1038/s41589-026-02240-y · Cited by 6

Enhanced Waddington landscape model with cell–cell communication can explain molecular mechanisms of self-organization

Fooladi, H., Moradi, P., Sharifi‐Zarchi, A., & Khalaj, B. H. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz201 · Cited by 4

Assessing the Direct Binding of Ark-Like E3 RING Ligases to Ubiquitin and Its Implication on Their Protein Interaction Network

Mintis, D. G., Chasapi, A., Poulas, K. A., Lagoumintzis, G., & Chasapis, C. T. (2020) · Molecules · doi:10.3390/molecules25204787 · Cited by 4

Leveraging efficiency metrics for the optimization of CELMoDs™ as cereblon-based molecular glue degraders

Jia, L., Riggs, J. R., Weiss, D. R., Claus, B. L., Shanmugasundaram, V., Johnson, S. R., & Zapf, C. W. (2025) · RSC Medicinal Chemistry · doi:10.1039/d4md00870g · Cited by 4

Identification of a novel splice variant for mouse and human interleukin-5

Shilovskiy, I. P., Andreev, S. M., Mazurov, D. V., Barvinskaia, E. D., Bolotova, S., Аркадьевич, Н. А., Sergeev, I. V., Владимирович, М. А., Kudlay, D. A., & Khaitov, M. R. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e03586 · Cited by 4

An Investigation into the Performance and Mechanisms of Soymilk-Sized Handmade Xuan Paper at Different Concentrations of Soymilk

Wu, C., Liu, Y., Hu, Y., Ding, M., Cui, X., Liu, Y., Liu, P., Zhang, H., Yang, Y., & Zhang, H. (2023) · Molecules · doi:10.3390/molecules28196791 · Cited by 4

Cold Storage Followed by Transplantation Induces Immunoproteasome in Rat Kidney Allografts: Inhibition of Immunoproteasome Does Not Improve Function

Bhattarai, D., Lee, S.-O., Joshi, N., Jun, S., Lo, S., Jiang, L., Gökden, N., & Parajuli, N. (2024) · Kidney360 · doi:10.34067/kid.0000000000000368 · Cited by 4

A Drosophila genetic screen for suppressors of S6kinase-dependent growth identifies the F-box subunit Archipelago/FBXW7

Zahoor, M. K., Poidevin, M., Lecerf, C., Garrido, D., & Montagne, J. (2019) · Molecular Genetics and Genomics · doi:10.1007/s00438-018-01529-5 · Cited by 4

Characterization of the bipartite degron that regulates ubiquitin-independent degradation of thymidylate synthase

Barbour, K. W., Xing, Y., Peña, E. A., & Berger, F. G. (2012) · Bioscience Reports · doi:10.1042/bsr20120112 · Cited by 4

Scoring Methods in Lead Optimization of Molecular GluesPreprint

Jia, L., Weiss, D. R., Shields, B., Claus, B. L., Shanmugasundaram, V., Johnson, S. R., Riggs, J. R., & Zapf, C. W. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-4hn4s-v2 · Cited by 3

Cobalt chloride affects the death of SH-SY5Y cells induced by inhibition of ubiquitin proteasome system. Role of heat shock protein 70 and caspase 3

Saksonova, S., Brodňanová, M., Dibdiaková, K., Pilchová, I., Klačanová, K., & Hatok, J. (2018) · General Physiology and Biophysics · doi:10.4149/gpb_2018022 · Cited by 3

Identification of a novel compound that simultaneously impairs the ubiquitin-proteasome system and autophagy

Giovannucci, T. A., Salomons, F. A., Stoy, H., Herzog, L. K., Xu, S., Qian, W., Merino, L. G., Gierisch, M. E., Haraldsson, M., Lystad, A. H., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1988359 · Cited by 3

Cell-based screening of extracts of natural sources to search for inhibitors of the ubiquitin–proteasome system and identification of proteasome inhibitors from the fungus Remotididymella sp.

Nishimura, S., Hitora, Y., Kawahara, T., Tanabe, M., Ogata, E., Kato, H., Srikoon, P., Watanabe, T., & Tsukamoto, S. (2022) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2022.128566 · Cited by 3

Pup grows up: in vitro characterization of the degradation of pupylated proteins

Kraut, D. A., & Matouschek, A. T. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.40 · Cited by 3

Bacterial Genome Editing Strategy for Control of Transcription and Protein Stability

Lauritsen, I., Martínez, V., Ronda, C., Nielsen, A. T., & Nørholm, M. H. H. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7295-1_3 · Cited by 3

Erratum: Targeting proteins for degradation

Schrader, E. K., Harstad, K. G., & Matouschek, A. T. (2009) · Nature Chemical Biology · doi:10.1038/nchembio1209-954c · Cited by 3

Light inducible protein degradation in E. coli with the LOVdeg tagPreprint

Tague, N., Coriano-Ortiz, C., Sheets, M. B., & Dunlop, M. J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.25.530042 · Cited by 3

Phosphoglycerate Kinase Can Adopt Topologically Misfolded Forms That Are More Stable Than Its Native State

Xia, Y., Amann, B. T., Gillilan, R. E., Jiang, Y., Sharma, P. A., Sen, S., Fleming, K. G., O’Brien, E. P., & Fried, S. D. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c20740 · Cited by 2

Macrophage Gsα promotes NLRP3 stability and its intervention attenuates abdominal aortic aneurysm in male mice

He, L., Qin, X., Ren, Q., Lu, H., Chen, M., Weinstein, L. S., Zhang, C., Yang, J., Ding, X., Jing, W., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71198-1 · Cited by 2

Quantitative Correlation between the Protein Expression Level inEscherichia Coliand Thermodynamic Stability of Protein In Vitro

Wada, J., Miyazaki, H., Kamada, R., & Sakaguchi, K. (2015) · Chemistry Letters · doi:10.1246/cl.151019 · Cited by 2

Predisposition to atrioventricular septal defects may be caused by SOX7 variants that impair interaction with GATA4

Li, B., Li, Z., Yang, J., Hong, N., Jin, L., Xu, Y., Fu, Q., Sun, K., Yu, Y., Lu, Y., et al. (2022) · Molecular Genetics and Genomics · doi:10.1007/s00438-022-01859-5 · Cited by 2

A new role of low barrier hydrogen bond in mediating protein stability by small moleculesPreprint

Yang, J., Li, Y., Qiu, Q., Wang, R., Wei, Y., Yu, Y., Niu, L., Pei, H., Wei, H., Ouyang, L., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.05.09.443293 · Cited by 2

Biological Activity Characterization of the Diagnostically Relevant Human Papillomavirus 16 E1C RNA

Varghese, C. S., Will, R. D., Tessmer, C., Hofmann, I., Heßling, B., Pawlita, M., & Höfler, D. (2021) · Microbiology Research · doi:10.3390/microbiolres12030038 · Cited by 1

Limiting the Broadcast Range of a Secreting Cell during Intercellular Signaling Using Protease-Mediated Degradation

Cole, J., & Schulman, R. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.4c00042 · Cited by 1

The ubiquitin-proteasome system degrades fatty acid synthase under nitrogen starvation when autophagy is dysfunctional in Saccharomyces cerevisiae

Jang, H.-S., Lee, Y., Kim, Y., & Huh, W. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.150423 · Cited by 1

A thiadiazolylidene-morpholine compound inhibits Pseudomonas aeruginosa by destabilizing the thiamine monophosphate kinase thiL

Li, Y., Lin, J., Chung, Z., Yeo, B. K. Y., Lescar, J., & Pethe, K. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113112 · Cited by 1

Targeting the Proteasome in Melanoma

Sorolla, A., Yeramian, A., Dolcet, X., Abal, L., Ortega, E., Egido, R., Matías‐Guiu, X., & Rosa, M. (2011) · InTech eBooks · doi:10.5772/19099 · Cited by 1

Role of Ubiquilins in Neurodegenerative Diseases

Wang, H. (2018) · Annals of Advanced Biomedical Sciences · doi:10.23880/aabsc-16000101 · Cited by 1

PA28γ, the ring that makes tumors invisible to the immune system?

Cascio, P. (2024) · Biochimie · doi:10.1016/j.biochi.2024.04.003 · Cited by 1

Targeting of PFKFB3

Färnegårdh, K., Shoshan, M. C., & Ährlund‐Richter, L. (2014) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4614-9545-1_8 · Cited by 1

ATP-Dependent Proteases: The Cell's Degradation Machines

Bhattacharyya, S., Wilmington, S. R., & Matouschek, A. T. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9781139003704.014 · Cited by 1

Who Initiates Proteasomal Degradation?

Gsponer, J. A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.08.006 · Cited by 1

Phosphorylation dependent stability control of the deneddylase DenA and its impact on Aspergillus nidulans development

Schinke, J. (2016) · doi:10.53846/goediss-5596 · Cited by 1

The psychiatric referral in primary care practice.

Noori, S. S., Soldatos, C. R., & Kales, J. (1979) · PubMed · Cited by 1

The lysine-rich intracellular loop and cell type-specific co-factors are required for IFITM3 antiviral immunity in hematopoietic stem cellsPreprint

Unali, G., Giordano, A. M. S., Cuccovillo, I., Alezz, M. A., Apolonia, L., Merelli, I., Malim, M. H., Petrillo, C., & Kajaste‐Rudnitski, A. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.04.06.438585 · Cited by 1

Scoring Methods in Lead Optimization of Molecular GluesPreprint

Jia, L., Weiss, D. R., Shields, B., Claus, B. L., Shanmugasundaram, V., Johnson, S. R., Riggs, J. R., & Zapf, C. W. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-4hn4s

Light inducible protein degradation in E. coli with the LOVdeg tagPreprint

Tague, N., Coriano-Ortiz, C., Sheets, M. B., & Dunlop, M. J. (2024) · eLife · doi:10.7554/elife.87303.2 · Cited by 1

Scoring Methods in Lead Optimization of Molecular GluesPreprint

Jia, L., Weiss, D. R., Shields, B., Claus, B. L., Shanmugasundaram, V., Johnson, S. R., Riggs, J. R., & Zapf, C. W. (2024) · ChemRxiv · doi:10.26434/chemrxiv-2023-4hn4s-v3 · Cited by 1

Order from Disorder: Structure, Function, and Dynamics of the HIV‐1 Transactivator of Transcription

Shojania, S., & O’Neil, J. D. (2011) · Wiley eBooks · doi:10.1002/9781118135570.ch9

Papel inmunosupresor y citotóxico de la arginasa I y la disponibilidad de L-arginina en el sistema inmune y cáncer

Navas, R. M. G. (2014) · Gredos (University of Salamanca) · doi:10.14201/gredos.124153

Protein Biosynthesis, Modifications and Degradation

Jahn, M., Jahn, D., Wünschiers, R., Ries, S. J., & Dersch, P. (2012) · Wiley eBooks · doi:10.1002/9781118657072.ch4

Tumorigenesis by Adenovirus Type 12 E1A

Guan, H., & Ricciardi, R. P. (2011) · Springer eBooks · doi:10.1007/978-1-4614-0016-5_20

Decoding the Protein Destruction Code: A Panoramic View

Pilla, E., & Bertolotti, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.028

A yeast selection system for the detection of proteasomal activation

Zhao, W., Bachhav, B., McWhite, C. D., & Segatori, L. (2018) · Protein Engineering Design and Selection · doi:10.1093/protein/gzz006

Inhibition of the ubiquitin-proteasome system by a bioactivatable compoundPreprint

Giovannucci, T. A., Salomons, F. A., Haraldsson, M., Elfman, L. H. M., Wickström, M., Young, P., Lundbäck, T., Eirich, J., Altun, M., Jafari, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.16.435589

Faculty Opinions recommendation of Defining the geometry of the two-component proteasome degron.

Coffino, P. (2011) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.8880963.9430061

Exploring the human Hsp70-Hop-Hsp90 system for Tau recognition

Moll, A. (2022) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-9131

RPT

Maupin-furlow, J. A., & Miranda, H. V. (2012) · Springer eBooks · doi:10.1007/978-1-4419-0461-4_65

Peer Review #2 of "Comparative proteome analysis reveals VPS28 regulates milk fat synthesis through ubiquitylation in bovine mammary epithelial cells (v0.1)"

(2020) · PeerJ · doi:10.7287/peerj.9542v0.1/reviews/2

Faculty Opinions recommendation of Homo-PROTACs: bivalent small-molecule dimerizers of the VHL E3 ubiquitin ligase to induce self-degradation.

Hoppe, T. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.731966527.793570381

RPT

Maupin-furlow, J. A., & Miranda, H. V. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_65

Faculty Opinions recommendation of A reference-based protein degradation assay without global translation inhibitors.

Römisch, K. (2017) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732099717.793539426

The Pup-Proteasome System of Mycobacteria

Bode, N. J., & Darwin, K. H. (2015) · ASM Press eBooks · doi:10.1128/9781555818845.ch32

Three rare variants of SOX7 impairing its interaction with GATA4 may be a predisposing factor to complete AVSDPreprint

Li, B., Li, Z., Yang, J., Hong, N., Jin, L., Xu, Y., Fu, Q., Sun, K., Yu, Y., Lu, Y., et al. (2020) · doi:10.21203/rs.3.rs-30638/v1

Peer Review #1 of "Comparative proteome analysis reveals VPS28 regulates milk fat synthesis through ubiquitylation in bovine mammary epithelial cells (v0.1)"

(2020) · PeerJ · doi:10.7287/peerj.9542v0.1/reviews/1

Light inducible protein degradation in E. coli with LOVtagPreprint

Tague, N., Coriano-Ortiz, C., Sheets, M. B., & Dunlop, M. J. (2023) · eLife · doi:10.7554/elife.87303.1

Reviewer #3 (Public Review): Light inducible protein degradation in E. coli with LOVtag

(2023) · eLife · doi:10.7554/elife.87303.1.sa0

Reviewer #1 (Public Review): Light inducible protein degradation in E. coli with LOVtag

(2023) · eLife · doi:10.7554/elife.87303.1.sa2

Reviewer #2 (Public Review): Light inducible protein degradation in E. coli with LOVtag

(2023) · eLife · doi:10.7554/elife.87303.1.sa1

eLife Assessment: Light inducible protein degradation in E. coli with LOVtag

Landry, C. R. (2023) · eLife · doi:10.7554/elife.87303.1.sa3

Overexpression of deubiquitinase (usp 36) in oral squamous cell carcinoma

Murali, P., Kavitha, B., & Narasimhan, M. (2023) · Journal of Oral and Maxillofacial Pathology · doi:10.4103/jomfp.jomfp_311_23

Global profiling of lysine ubiquitylation in human hypothalamusPreprint

Yang, J., Liu, J., Zhang, Z., Ding, T., Wang, Q., Shi, C., Zhang, X., & Kong, J. (2024) · doi:10.22541/au.171309704.48917699/v1

Revisiting the structure of UBR box from human UBR6

Kim, B., Lee, S., Kim, B. H., Kim, L., & Song, H. K. (2025) · Protein Science · doi:10.1002/pro.70092

Mechanism of Albumin Degradation Under the Action of UV Radiation and Reactive Oxygen Species

Пискарев, И. М. (2025) · IEEE Transactions on Plasma Science · doi:10.1109/tps.2025.3578432

Prefrontal cortex cytosolic and synaptosome proteome reveal molecular signatures of resilience to chronic social isolation stress in rats

Filipović, D., & Turck, C. W. (2025) · Reviews in the Neurosciences · doi:10.1515/revneuro-2025-0081

Global Profiling of Lysine Ubiquitylation in the Human Hypothalamus

Zhang, Z., Ding, T., Kong, J., Wang, Q., Zhang, X., Shi, C., Yang, J., & Liu, J. (2025) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.70029

Etude du rôle de la protéine CDC48 dans l'immunité des plantes

Bègue, H. (2018) · theses.fr (ABES) · doi:10.70675/113dfdaaz2de4z41d6zbf96z59486ceff3c9

Les astrocytes réactifs, des partenaires anti-agrégants dans la maladie de Huntington : identification des mécanismes impliqués dans le dialogue neurone-astrocyte

Abjean, L. (2019) · theses.fr (ABES) · doi:10.70675/f664e003zf93fz467eza6a3z3d953eaffe4e

Towards biocatalyst selection using microfluidically distributed molecular programs

Shenshin, V. (2021) · doi:10.70675/6edd9acbz459az4f96zbd07z0886b7d73a41

Druggability of kinetoplastid-specific mRNA translation-related proteins : Structural investigation by cryo-Electron Microscopy

Cistia, M. L. D. (2022) · theses.fr (ABES) · doi:10.70675/19918f3azade0z4d4fz8194z3eef58ec9e94

A Cell-Permeable β-Hairpin Peptide Biosensor for Real-Time, Single-Cell Quantification of Proteasome Activity

Rahnama, A., Chadwick, A., DeBock, R., Liu, D., Gauthier, T. J., & Melvin, A. T. (2026) · ACS Sensors · doi:10.1021/acssensors.5c04243

Reengineering Protease Inhibitors to Disrupt Hsp70 Chaperone Function

Richards, A., Ariza‐Mateos, A., Ghosh, A., Kim, M., Sandler, S., Yardumian, I., Yawson, G., Baryza, J. L., Serganov, A., & Lupoli, T. J. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.1777033

Reengineering Protease Inhibitors to Disrupt Hsp70 Chaperone Function

Richards, A., Ariza‐Mateos, A., Ghosh, A., Kim, M., Sandler, S., Yardumian, I., Yawson, G., Baryza, J. L., Serganov, A., & Lupoli, T. J. (2026) · Angewandte Chemie · doi:10.1002/ange.1777033

Resolving symmetry-masked allosteric cooperativity in the M. tuberculosis proteasome core particlePreprint

Turner, M., Wittlinger, V., Lento, C., Haris, A., Ujma, J., Bruton, D., Richardson, K., Giles, K., Böttcher, T., Wilson, D., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.02.736129

Cardiovascular Diseases and Cancer: Convergent Proteostasis Networks at the Crossroads of Mechanisms and Therapeutic Opportunities

Torres, J. E. G., Frey, N., & Rangrez, A. Y. (2026) · MedComm · doi:10.1002/mco2.70892

BindingDB Entry 50016672: Cell-based screening of extracts of natural sources to search for inhibitors of the ubiquitin-proteasome system and identification of proteasome inhibitors from the fungus Remotididymella sp.

BindingDB (2023) · UC San Diego · doi:10.7270/q2qc07kf

BindingDB Entry 50045874: A potent and selective inhibitor for the UBLCP1 proteasome phosphatase.

BindingDB (2016) · UC San Diego · doi:10.7270/q2vd7168

Defining the geometry of the two-component proteasome degron

Inobe, T., Fishbain, S., Prakash, S., & Matouschek, A. T. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.521 · Cited by 173

Mechanisms of substrate recognition by the 26S proteasome

Davis, C., Spaller, B. L., & Matouschek, A. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.10.010 · Cited by 66

ATP-Dependent Proteases: The Cell's Degradation Machines

Bhattacharyya, S., Wilmington, S. R., & Matouschek, A. T. (2011) · Cambridge University Press eBooks · doi:10.1017/cbo9781139003704.014 · Cited by 1

Protein targeting to ATP-dependent proteases

Inobe, T., & Matouschek, A. T. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.12.014 · Cited by 46

An unstructured initiation site is required for efficient proteasome-mediated degradation

Prakash, S., Tian, L., Ratliff, K. S., Lehotzky, R. E., & Matouschek, A. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb814 · Cited by 458