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A Method for the Acute and Rapid Degradation of Endogenous Proteins
Open accessAbstract
Methods for the targeted disruption of protein function have revolutionized science and greatly expedited the systematic characterization of genes. Two main approaches are currently used to disrupt protein function: DNA knockout and RNA interference, which act at the genome and mRNA level, respectively. A method that directly alters endogenous protein levels is currently not available. Here, we present Trim-Away, a technique to degrade endogenous proteins acutely in mammalian cells without prior modification of the genome or mRNA. Trim-Away harnesses the cellular protein degradation machinery to remove unmodified native proteins within minutes of application. This rapidity minimizes the risk that phenotypes are compensated and that secondary, non-specific defects accumulate over time. Because Trim-Away utilizes antibodies, it can be applied to a wide range of target proteins using off-the-shelf reagents. Trim-Away allows the study of protein function in diverse cell types, including non-dividing primary cells where genome- and RNA-targeting methods are limited.
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“The Trim-Away mechanism depletes target proteins directly at the protein level, bypassing limitations of transcriptional or RNA-targeting approaches and offering temporally precise control over protein levels.”
From Reverse the progression of Alzheimer’s disease through Nano-ERASER-based adult neuroregeneration (2026) · cites this paper as [21]
In the citing paper
“The longevity of TRIM-away efficacy was assessed to be roughly 3–4 days. However, this was dependent on the levels of target protein within cells, the amount of antibody being applied and the amount of TRIM21 within cells.”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [40]
In the citing paper
“The power of TRIM-away was also shown by its ability to target and degrade Rec8 in mouse oocytes within minutes [40].”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [40]
In the citing paper
“As shown by targeting huntingtin, TRIM-Away was also able to distinguish between wild-type and mutant proteins, depending on the specificity of the delivered antibody [40].”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [40]
In the citing paper
“The system could also be applied to primary cells, in which achieving protein silencing with RNAi or CRISPR/Cas9 is difficult.”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [40]
In the citing paper
“Using a GFP-specific antibody for microinjection into TRIM21 expressing cells, GFP levels were depleted with an apparent half-life of roughly 16 min [40].”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [40]
In the citing paper
“To widen the applicability of the system beyond single cell analysis, the authors developed a bulk cell approach by using electroporation, showing specific effects on signalling pathways like ERK1 or mTOR [40].”
From Advances in targeted degradation of endogenous proteins (2019) · cites this paper as [40]
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Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590
Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., & Tuschl, T. (2001) · Nature · doi:10.1038/35078107 · Cited by 9,456
The new frontier of genome engineering with CRISPR-Cas9
Doudna, J. A., & Charpentier, E. (2014) · Science · doi:10.1126/science.1258096 · Cited by 7,062
Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216
Schroder, K., & Tschopp, J. (2010) · Cell · doi:10.1016/j.cell.2010.01.040 · Cited by 5,475
Introduction to NF-κB: players, pathways, perspectives
Gilmore, T. D. (2006) · Oncogene · doi:10.1038/sj.onc.1209954 · Cited by 2,293
Laplante, M., & Sabatini, D. M. (2009) · Journal of Cell Science · doi:10.1242/jcs.051011 · Cited by 2,284
Altering the Genome by Homologous Recombination
Capecchi, M. R. (1989) · Science · doi:10.1126/science.2660260 · Cited by 2,037
Small Molecule Inhibitor of Mitotic Spindle Bipolarity Identified in a Phenotype-Based Screen
Mayer, T. U., Kapoor, T. M., Haggarty, S. J., King, R. W., Schreiber, S. L., & Mitchison, T. J. (1999) · Science · doi:10.1126/science.286.5441.971 · Cited by 1,752
An auxin-based degron system for the rapid depletion of proteins in nonplant cells
Nishimura, K., Fukagawa, T., Takisawa, H., Kakimoto, T., & Kanemaki, M. (2009) · Nature Methods · doi:10.1038/nmeth.1401 · Cited by 1,663
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Items 201–300 of 533
Coyne, A. N., & Rothstein, J. D. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01228-0 · Cited by 25
Applications of CRISPR-Cas in Bioengineering, Biotechnology, and Translational Research
Lau, C. (2018) · The CRISPR Journal · doi:10.1089/crispr.2018.0026 · Cited by 22
Locus-Specific Knock-In of a Degradable Tag for Target Validation Studies
Brand, M., & Winter, G. E. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9145-7_7 · Cited by 21
Exome sequencing links CEP120 mutation to maternally derived aneuploid conception risk
Tyc, K. M., Yakoubi, W. E., Bag, A., Landis, J. N., Zhan, Y., Treff, N. R., Scott, R. T., Tao, X., Schindler, K., & Xing, J. (2020) · Human Reproduction · doi:10.1093/humrep/deaa148 · Cited by 23
Transcription-Replication Collisions—A Series of Unfortunate Events
Germain, C. S., Zhao, H., & Barlow, J. H. (2021) · Biomolecules · doi:10.3390/biom11081249 · Cited by 21
Targeted protein degradation in mammalian cells: A promising avenue toward future
Zhang, T., Liu, C., Li, W., Kuang, J., Qiu, X., Lu, M., & Zhu, L. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.09.038 · Cited by 23
The translation regulator Zar1l controls timing of meiosis in Xenopus oocytes
Heim, A., Niedermeier, M. L., Stengel, F., & Mayer, T. U. (2022) · Development · doi:10.1242/dev.200900 · Cited by 22
Maternal TDP-43 interacts with RNA Pol II and regulates zygotic genome activation
Nie, X., Xu, Q., Xu, C., Chen, F., Wang, Q., Qin, D., Wang, R., Gao, Z., Lu, X., Yang, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39924-1 · Cited by 25
Takenouchi, O., Sakakibara, Y., & Kitajima, T. S. (2024) · Science · doi:10.1126/science.adn5529 · Cited by 22
Pooled endogenous protein tagging and recruitment for systematic profiling of protein function
Serebrenik, Y. V., Mani, D. R., Maujean, T., Burslem, G. M., & Shalem, O. (2024) · Cell Genomics · doi:10.1016/j.xgen.2024.100651 · Cited by 21
Camlin, N. J., & Evans, J. P. (2019) · Biology of Reproduction · doi:10.1093/biolre/ioz113 · Cited by 21
Recent Progress on Microtubule Degradation Agents
Zhang, C., Zhao, M., Wang, G., & Li, Y. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00517 · Cited by 22
Elaboration of molecular glues that target TRIM21 into TRIMTACs that degrade protein aggregates
de Gialluly, M. A. S., Allen, A. R., Hayes, E. H., Zhuang, P., Goldfarb, R. B., Farrar, A. N., Federov, Y., & Adams, D. (2025) · Nature Communications · doi:10.1038/s41467-025-61818-7 · Cited by 23
CDC25B is required for the metaphase I-metaphase II transition in mouse oocytes
Ferencova, I., Vaškovičová, M., Drutovič, D., Knoblochová, L., Macůrek, L., Schultz, R. M., & Solc, P. (2022) · Journal of Cell Science · doi:10.1242/jcs.252924 · Cited by 21
Dual control of formin-nucleated actin assembly by the chromatin and ER in mouse oocytes
Wang, H., Hu, J., Yi, K., Ma, Z., Song, X., Lee, Y., Kaláb, P., Bershadsky, A. D., Miao, Y., & Li, R. (2022) · Current Biology · doi:10.1016/j.cub.2022.07.058 · Cited by 21
Light-Activating PROTACs in Cancer: Chemical Design, Challenges, and Applications
Negi, A., Kesari, K. K., & Voisin‐Chiret, A. S. (2022) · Applied Sciences · doi:10.3390/app12199674 · Cited by 21
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Cattaneo, A., & Chirichella, M. (2018) · Trends in biotechnology · doi:10.1016/j.tibtech.2018.11.009 · Cited by 20
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Traub, L. M. (2019) · eLife · doi:10.7554/elife.41768 · Cited by 20
Reflections on the use of protein binders to study protein function in developmental biology
Aguilar, G., Viganò, M., Affolter, M., & Matsuda, S. (2019) · Wiley Interdisciplinary Reviews Developmental Biology · doi:10.1002/wdev.356 · Cited by 17
Rothstein, J. D., Keeley, O., Warlick, C., Miller, T. M., Ly, C. V., Glass, J. D., & Coyne, A. N. (2025) · Nature Communications · doi:10.1038/s41467-025-62482-7 · Cited by 28
O’Shea, J. M., Goutou, A., Brydon, J., Sethna, C. R., Wood, C. W., & Greiss, S. (2022) · ChemBioChem · doi:10.1002/cbic.202200321 · Cited by 20
Herpesviruses mimic zygotic genome activation to promote viral replication
Neugebauer, E., Wälter, S., Jiang, T., Drayman, N., Franke, V., van Gent, M., Pennisi, S., Veratti, P., Stein, K. S., Welker, I., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-55928-5 · Cited by 23
Gambini, A., Stein, P., Savy, V., Grow, E. J., Papas, B. N., Zhang, Y., Kenan, A. C., Padilla‐Banks, E., Cairns, B. R., & Williams, C. J. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.04.018 · Cited by 19
A novel cardiomyogenic role for Isl1 + neural crest cells in the inflow tract
Hatzistergos, K. E., Durante, M. A., Valasaki, K., Wanschel, A. C. B. A., Harbour, J. W., & Hare, J. M. (2020) · Science Advances · doi:10.1126/sciadv.aba9950 · Cited by 20
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Self-citationNegi, A., Kieffer, C., & Voisin‐Chiret, A. S. (2022) · ChemistrySelect · doi:10.1002/slct.202200981 · Cited by 19
Liu, Z., Yu, D., Song, H. L., Postings, M. L., Scott, P., Wang, Z., Ren, J., & Qu, X. (2023) · ACS Nano · doi:10.1021/acsnano.2c11476 · Cited by 19
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Boisgerault, N., & Bertrand, P. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115465 · Cited by 22
Synaptonemal Complex in Human Biology and Disease
Llano, E., & Pendás, A. M. (2023) · Cells · doi:10.3390/cells12131718 · Cited by 19
Levitan, D., Liu, C., Yang, T. L., Shima, Y., Lin, J.-Y., Wachutka, J., Marrero-Garcia, Y., Ghoddousi, R. A. M., Beltrame, E. D. V., Richter, T. A., et al. (2020) · eLife · doi:10.7554/elife.61036 · Cited by 18
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Malla, A. B., Yu, H., Farris, D., Kadimi, S., Lam, T. T., Cox, A. L., Smith, Z. D., & Lesch, B. J. (2023) · EMBO Reports · doi:10.15252/embr.202256492 · Cited by 18
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Eisa, A. A., Bang, S., Crawford, K. J., Murphy, E. M., Feng, W. W., Dey, S., Wells, W. A., Kon, N., Gu, W. J., Mehlmann, L. M., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101523 · Cited by 18
Synthetic biology approaches for targeted protein degradation
Chen, R. P., Gaynor, A. S., & Chen, W. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107446 · Cited by 18
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Ahel, J., Balci, A., Faas, V., Grabarczyk, D. B., Harmo, R., Squair, D. R., Zhang, J., Roitinger, E., Lamoliatte, F., Mathur, S., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59444-4 · Cited by 17
New PROTAC Designs for Targeted Protein Degradation in 2021–2025: Novel E3 Ligases and Pre-PROTACs
Peng, W., Pan, X., Wang, S., Huang, G., & Qian, Y. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c03330 · Cited by 19
McPhie, K. A., Esposito, D., Pettinger, J., Norman, D., Werner, T., Mathieson, T., Bush, J. T., & Rittinger, K. (2025) · Chemical Science · doi:10.1039/d5sc01540e · Cited by 18
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Koch, K. C., & Tew, G. N. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114586 · Cited by 16
Deng, C., Li, S., Liu, Y., Bao, W., Xu, C., Zheng, W., Wang, M., & Ma, X. (2023) · Clinical and Translational Medicine · doi:10.1002/ctm2.1382 · Cited by 17
Takada, Y., Fierro, L., Sato, K., Sanada, T., Ishii, A., Yamamoto, T., & Kotani, T. (2023) · Science Advances · doi:10.1126/sciadv.adg6532 · Cited by 15
Utilization of HEPES for Enhancing Protein Transfection into Mammalian Cells
Chen, S., Chao, A., Tsai, C.-L., Sue, S., Lin, C., Lee, Y.-Z., Hung, Y.-L., Chao, A., Cheng, A., Wang, H., et al. (2018) · Molecular Therapy — Methods & Clinical Development · doi:10.1016/j.omtm.2018.12.005 · Cited by 16
Structure‐based design of a photoswitchable affibody scaffold
Woloschuk, R. M., Reed, P. M. M., Jaikaran, A. S. I., Demmans, K. Z., Youn, J., Kanelis, V., Uppalapati, M., & Woolley, G. A. (2021) · Protein Science · doi:10.1002/pro.4196 · Cited by 16
A non-transcriptional function of Yap regulates the DNA replication program in Xenopus laevis
García, R. M., Haccard, O., Chesneau, A., Narassimprakash, H., Roger, J. E., Perron, M., Marheineke, K., & Bronchain, O. J. (2022) · eLife · doi:10.7554/elife.75741 · Cited by 18
Rothstein, J. D., Warlick, C., & Coyne, A. N. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.12.571299 · Cited by 19
Genome Damage Sensing Leads to Tissue Homeostasis in Drosophila
Khan, C., Muliyil, S., & Rao, B. J. (2019) · International review of cytology · doi:10.1016/bs.ircmb.2018.12.001 · Cited by 15
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Miao, H., Liu, C., Ouyang, H., Zhang, P., Liu, Y., Zhang, C., Deng, C., Fu, Y., Niu, J., Zheng, W., et al. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.952237 · Cited by 15
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Yadav, H. K., & Shirumalla, R. K. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08438-w · Cited by 15
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Li, Q., Qiao, G., Wang, X., Wang, M., Cheng, J., Hu, G., Li, X., Wu, J., Liu, J., Gao, C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62050-z · Cited by 17
Takei, N., Sato, K., Takada, Y., Iyyappan, R., Šušor, A., Yamamoto, T., & Kotani, T. (2021) · Current Research in Cell Biology · doi:10.1016/j.crcbio.2021.100009 · Cited by 15
Pan, Y., Wang, Y., & Gou, S. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108491 · Cited by 18
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Degradation of extracellular and membrane proteins in targeted therapy: Status quo and quo vadis
Li, Z., Ma, S., Zhang, S., Ma, Z., Du, L., & Li, M. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103716 · Cited by 14
Joshi, M., Dey, P., & De, A. (2023) · Exploration of Targeted Anti-tumor Therapy · doi:10.37349/etat.2023.00194 · Cited by 15
Shi, C., Su, L., Xu, W., Wang, S., Cao, Y., Yao, M., Wang, X., Liu, F., Nie, G., & Zhou, H. (2025) · Nano Letters · doi:10.1021/acs.nanolett.4c06279 · Cited by 14
Jain, S., & Roy, I. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00226 · Cited by 13
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Sandhof, C. A., Murray, H. F. B., Silva, M. C., & Haggarty, S. J. (2024) · Neurotherapeutics · doi:10.1016/j.neurot.2024.e00499 · Cited by 14
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Huang, J., Ru, G., Sun, J., Sun, L., & Li, Z. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00446-z · Cited by 14
Dey, P., Joshi, M., Mujawar, A., Malhotra, R., & De, A. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00693-6 · Cited by 14
André‐Grégoire, G., Maghe, C., Douanne, T., Rosińska, S., Spinelli, F. M., Thys, A., Trillet, K., Jacobs, K., Ballu, C., Dupont, A., et al. (2022) · iScience · doi:10.1016/j.isci.2022.105118 · Cited by 18
Israel, S., Seyfarth, J., Nolte, T., Drexler, H. C. A., Fuellen, G., & Boiani, M. (2023) · Molecular Human Reproduction · doi:10.1093/molehr/gaad038 · Cited by 14
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Yang, H. M., Zheng, G., Li, G. Y., Alshaye, A., & Orkin, S. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108077 · Cited by 12
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Li, Y., Peng, R., Gao, W., Liu, P., Chen, L.-J., Zhang, X., Zhang, N.-N., Wang, Y., Du, L., Zhu, F., et al. (2019) · Aging · doi:10.18632/aging.101802 · Cited by 12
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Zhao, S., Luo, J., Xu, P., Zeng, J., Yan, G., Yu, F., Qin, L., Zhang, C., Li, P., Cai, M., et al. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142667 · Cited by 11
Israel, S., Drexler, H. C. A., Fuellen, G., & Boiani, M. (2021) · Molecular Human Reproduction · doi:10.1093/molehr/gaab048 · Cited by 11
Graceffa, V. (2023) · Biochimie · doi:10.1016/j.biochi.2023.05.011 · Cited by 12
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Kim, D. S., Park, Y., Tsokos, G. C., Cho, M., & Kwok, S. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01490-5 · Cited by 10
Sun, X., Yu, B., Zhang, R., Wei, J., Pan, G., Li, C., & Zhou, Z. (2022) · Journal of Economic Entomology · doi:10.1093/jee/toac145 · Cited by 10
VanDyke, D., Xu, L., Sargunas, P. R., Gilbreth, R. N., Baca, M., Gao, C., Hunt, J., & Spangler, J. B. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105381 · Cited by 10
Bellou, E., Zielinska, A. P., Mönnich, E. U., Schweizer, N., Politi, A. Z., Wellecke, A., Sibold, C., Tandler-Schneider, A., & Schuh, M. (2024) · Nature Communications · doi:10.1038/s41467-024-54659-3 · Cited by 10
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Metadata
- Authors
- Clift, D., McEwan, W. A., Labzin, L. I., Konieczny, V., Mogessie, B., James, L. C., & Schuh, M.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Max Planck Institute for Biophysical Chemistry (DE)
- Corresponding author
- Clift, Dean
- James, Leo C.
- Schuh, Melina
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-12
- Volume
- 171
- Issue
- 7
- Pages
- 1692-1706.e18
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5733393
- OpenAlex
- W2769995426
- Cited by
- 531
- References
- 65
- Citations by year
- 2026: 65 · 2025: 85 · 2024: 59 · 2023: 72 · 2022: 52 · 2021: 62 · 2020: 58 · 2019: 45 · 2018: 30 · 2017: 2
- FWCI
- 15.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Cell (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Explore Bristol Research (publishedVersion, cc-by)
- GRO (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Bristol Research (University of Bristol) (submittedVersion, cc-by)
- Apollo (University of Cambridge) (submittedVersion, cc-by)
- Apollo (cc-by)
- Funders
- Medical Research Council (MC_U105192711, MC_U105181010)
- European Community’s Seventh Framework Programme (241548)
- European Research Council (ERC (337415)
- Wellcome Trust Investigator Award (200594/Z/16/Z)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › CRISPR and Genetic Engineering
- Keywords
- mammalian cells, gene function analysis
- MeSH terms
- Animals, Antibodies, Biochemistry, Protein Transport, Proteolysis
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