Cited by 480Gene Regulatory Network AnalysisProtein Degradation and InhibitorsChemical Synthesis and Analysis

The DOI matches its Crossref record; 103 of the 104 references it cites were found in a registry or an index.

Chemically induced proximity in biology and medicine

Open access

Stanton, Benjamin Z., Chory, Emma J., Crabtree, Gerald R.·2018·Science

DOI 10.1126/science.aao5902PMC PMC6417506

Open this paper in CoChat — free account

Abstract

Regulating molecule proximity: The physical distance, or proximity, between molecules often directs biological events. The development of membrane-permeable small molecules that reversibly regulate proximity has enabled advances in fields such as synthetic biology, signal transduction, transcription, protein degradation, epigenetic memory, and chromatin dynamics. This “induced proximity” can also be applied to the development of new therapeutics. Stanton et al. review the wide range of advances and speculate on future applications of this fundamental approach. Science , this issue p. eaao5902

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1126/science.aao5902

Cites

103 of 103 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

THE CONSTITUTION AND FUNDAMENTAL PROPERTIES OF SOLIDS AND LIQUIDS. PART I. SOLIDS.
Langmuir, I. (1916) · Journal of the American Chemical Society · doi:10.1021/ja02268a002 · Cited by 10,017
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
Reaction-rate theory: fifty years after Kramers
Hänggi, P., Talkner, P., & Borkovec, M. (1990) · Reviews of Modern Physics · doi:10.1103/revmodphys.62.251 · Cited by 6,154
Selective inhibition of BET bromodomains
Filippakopoulos, P., Qi, J., Picaud, S., Shen, Y., Smith, W. B., Fedorov, O., Morse, E. M., Keates, T., Hickman, T. T., Felletar, I., et al. (2010) · Nature · doi:10.1038/nature09504 · Cited by 4,262
The constitution and fundamental properties of solids and liquids
Langmuir, I. (1917) · Journal of the Franklin Institute · doi:10.1016/s0016-0032(17)90938-x · Cited by 3,787
Clearance of p16Ink4a-positive senescent cells delays ageing-associated disorders
Baker, D. J., Wijshake, T., Tchkonia, T., LeBrasseur, N. K., Childs, B. G., van de Sluis, B., Kirkland, J. L., & van Deursen, J. M. (2011) · Nature · doi:10.1038/nature10600 · Cited by 3,670 · cited 2×
“This CIP “suicideswitch” strategy was extended to a senescent cell–clearing mouse to study age-related pathologies (94).”
Background
Abscisic Acid: Emergence of a Core Signaling Network
Cutler, S. R., Rodrı́guez, P. L., Finkelstein, R. R., & Abrams, S. R. (2010) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042809-112122 · Cited by 3,227
BET Bromodomain Inhibition as a Therapeutic Strategy to Target c-Myc
Delmore, J. E., Issa, G. C., Lemieux, M. E., Rahl, P. B., Shi, J., Jacobs, H. M., Kastritis, E., Gilpatrick, T., Paranal, R. M., Qi, J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.017 · Cited by 2,888
Naturally occurring p16Ink4a-positive cells shorten healthy lifespan
Baker, D. J., Childs, B. G., Durik, M., Wijers, M. E., Sieben, C. J., Zhong, J., A. Saltness, R., Jeganathan, K. B., Verzosa, G. C., Pezeshki, A., et al. (2016) · Nature · doi:10.1038/nature16932 · Cited by 2,876
SH2 domains recognize specific phosphopeptide sequences
Songyang, Z. (1993) · Cell · doi:10.1016/0092-8674(93)90404-e · Cited by 2,620

Flagged first, then by citations

Show all 104 references

1 of the 104 references couldn’t be matched to a known paper.

Sorted by citations

Targeted protein degradation: mechanisms, strategies and application
Zhao, L., Zhao, J., Zhong, K., Tong, A., & Jia, D. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00966-4 · Cited by 1,035
The Rise of Molecular Glues
Schreiber, S. L. (2021) · Cell · doi:10.1016/j.cell.2020.12.020 · Cited by 598
Differential PROTAC substrate specificity dictated by orientation of recruited E3 ligase
Smith, B. E., Wang, S. L., Jaime-Figueroa, S., Harbin, A., Wang, J., Hamman, B. D., & Crews, C. M. (2019) · Nature Communications · doi:10.1038/s41467-018-08027-7 · Cited by 517
Microenvironment mapping via Dexter energy transfer on immune cells
Geri, J. B., Oakley, J. V., Reyes-Robles, T., Wang, T., McCarver, S. J., White, C. H., Rodriguez-Rivera, F. P., Parker, D. L., Hett, E. C., Fadeyi, O. O., et al. (2020) · Science · doi:10.1126/science.aay4106 · Cited by 481
The CDK inhibitor CR8 acts as a molecular glue degrader that depletes cyclin K
Słabicki, M., Kozicka, Z., Petzold, G., Li, Y.-D., Manojkumar, M., Bunker, R. D., Donovan, K. A., Sievers, Q. L., Koeppel, J., Suchyta, D., et al. (2020) · Nature · doi:10.1038/s41586-020-2374-x · Cited by 433
Molecular Glues for Targeted Protein Degradation: From Serendipity to Rational Discovery
Dong, G., Ding, Y., He, S., & Sheng, C. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00895 · Cited by 369
Late-Stage Diversification of Natural Products
Hong, B., Luo, T., & Lei, X. (2020) · ACS Central Science · doi:10.1021/acscentsci.9b00916 · Cited by 346
Multispecific drugs herald a new era of biopharmaceutical innovation
Deshaies, R. J. (2020) · Nature · doi:10.1038/s41586-020-2168-1 · Cited by 270
Payload diversification: a key step in the development of antibody–drug conjugates
Conilh, L., Sadilkova, L., Viricel, W., & Dumontet, C. (2023) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01397-y · Cited by 257
Proximity-Based Modalities for Biology and Medicine
Liu, X., & Ciulli, A. (2023) · ACS Central Science · doi:10.1021/acscentsci.3c00395 · Cited by 206
Unifying principles of bifunctional, proximity-inducing small molecules
Gerry, C. J., & Schreiber, S. L. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0469-1 · Cited by 199
In Silico Modeling of PROTAC-Mediated Ternary Complexes: Validation and Application
Drummond, M. L., & Williams, C. I. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00872 · Cited by 199
Phosphorylation-Inducing Chimeric Small Molecules
Siriwardena, S. U., Godage, D. N. P. M., Shoba, V. M., Lai, S., Shi, M., Wu, P., Chaudhary, S. K., Schreiber, S. L., & Choudhary, A. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.0c05537 · Cited by 195
Chasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200
DNA-based memory devices for recording cellular events
Sheth, R. U., & Wang, H. H. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0052-8 · Cited by 179
FKBP Ligands—Where We Are and Where to Go?
Kolos, J. M., Voll, A. M., Bauder, M., & Hausch, F. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01425 · Cited by 158
Rewiring cancer drivers to activate apoptosis
Gourisankar, S. P., Krokhotin, A., Ji, W., Liu, X., Chang, C.-Y., Kim, S. H., Li, Z., Wenderski, W., Simanauskaite, J., Yang, H., et al. (2023) · Nature · doi:10.1038/s41586-023-06348-2 · Cited by 174
Self-citation
Histone hyperacetylation disrupts core gene regulatory architecture in rhabdomyosarcoma
Gryder, B. E., Pomella, S., Sayers, C. M., Wu, X., Song, Y., Chiarella, A. M., Bagchi, S., Chou, H.-C., Sinniah, R., Walton, A., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0534-4 · Cited by 164
Self-citation
Targeted protein degradation: current and future challenges
Hanzl, A., & Winter, G. E. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.11.012 · Cited by 157
Visible-Light Photocatalysis as an Enabling Technology for Drug Discovery: A Paradigm Shift for Chemical Reactivity
Li, P., Terrett, J. A., & Zbieg, J. R. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00436 · Cited by 145
Cancer therapies based on targeted protein degradation — lessons learned with lenalidomide
Jan, M., Sperling, A. S., & Ebert, B. L. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-021-00479-z · Cited by 137
Defining molecular glues with a dual-nanobody cannabidiol sensor
Cao, S., Kang, S., Mao, H., Yao, J., Gu, L., & Zheng, N. (2022) · Nature Communications · doi:10.1038/s41467-022-28507-1 · Cited by 125
Fragment-based covalent ligand discovery
Lu, W., Kostic, M., Zhang, T., Che, J., Patricelli, M. P., Jones, L. H., Chouchani, E. T., & Gray, N. S. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00222d · Cited by 136
Facts, Patterns, and Principles in Drug Discovery: Appraising the Rule of 5 with Measured Physicochemical Data
Tinworth, C. P., & Young, R. J. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01596 · Cited by 132
Synthetic biology in the clinic: engineering vaccines, diagnostics, and therapeutics
Tan, X., Letendre, J. H., Collins, J. J., & Wong, W. W. (2021) · Cell · doi:10.1016/j.cell.2021.01.017 · Cited by 134
A DNA‐Mediated Chemically Induced Dimerization (D‐CID) Nanodevice for Nongenetic Receptor Engineering To Control Cell Behavior
Li, H., Wang, M., Shi, T., Yang, S. Z., Zhang, J., Wang, H., & Nie, Z. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201806155 · Cited by 130
Engineering a Proximity-Directed O-GlcNAc Transferase for Selective Protein O-GlcNAcylation in Cells
Ramirez, D. H., Aonbangkhen, C., Wu, H., Naftaly, J. A., Tang, S., O’Meara, T. R., & Woo, C. M. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00074 · Cited by 128
DNA Barcoding a Complete Matrix of Stereoisomeric Small Molecules
Gerry, C. J., Wawer, M. J., Clemons, P. A., & Schreiber, S. L. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b01203 · Cited by 117
Targeted protein acetylation in cells using heterobifunctional molecules
Wang, W. W., Chen, L.-Y., Wozniak, J. M., Jadhav, A. M., Anderson, H., Malone, T. E., & Parker, C. G. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.1c07850 · Cited by 114
Molecular glues and bifunctional compounds: Therapeutic modalities based on induced proximity
Schreiber, S. L. (2024) · Cell Chemical Biology · doi:10.1016/j.chembiol.2024.05.004 · Cited by 112
Selective degradation of multimeric proteins by TRIM21-based molecular glue and PROTAC degraders
Lu, P., Cheng, Y., Xue, L., Ren, X., Xu, X., Chen, C., Cao, L., Li, J., Wu, Q., Sun, S., et al. (2024) · Cell · doi:10.1016/j.cell.2024.10.015 · Cited by 119
Recent achievements and current trajectories of diversity-oriented synthesis
Gerry, C. J., & Schreiber, S. L. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.08.008 · Cited by 107
Prodrugs as empowering tools in drug discovery and development: recent strategic applications of drug delivery solutions to mitigate challenges associated with lead compounds and drug candidates
Subbaiah, M. A. M., Rautio, J., & Meanwell, N. A. (2024) · Chemical Society Reviews · doi:10.1039/d2cs00957a · Cited by 109
Bifunctional chemical probes inducing protein–protein interactions
Maniaci, C., & Ciulli, A. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.07.003 · Cited by 100
Binding and sensing diverse small molecules using shape-complementary pseudocycles
An, L., Said, M. Y., Tran, L., Majumder, S., Goreshnik, I., Lee, G. R., Juergens, D., Dauparas, J., Anishchenko, I. V., Coventry, B., et al. (2024) · Science · doi:10.1126/science.adn3780 · Cited by 113
Protein degradation technology: a strategic paradigm shift in drug discovery
Li, H., Dong, J., Cai, M., Xu, Z., Cheng, X., & Qin, J. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01146-7 · Cited by 96
Post-translational modifications and their implications in cancer
Dutta, H., & Jain, N. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1240115 · Cited by 96
Nucleosome Turnover Regulates Histone Methylation Patterns over the Genome
Chory, E. J., Calarco, J. P., Hathaway, N. A., Bell, O., Neel, D. S., & Crabtree, G. R. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.028 · Cited by 83
Self-citation
Rapid biosensor development using plant hormone receptors as reprogrammable scaffolds
Beltrán, J., Steiner, P. J., Bedewitz, M. A., Wei, S., Peterson, F. C., Li, Z., Hughes, B. E., Hartley, Z., Robertson, N. R., Medina‐Cucurella, A. V., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01364-5 · Cited by 88
Targeted Biomolecule Regulation Platform: A Split-and-Mix PROTAC Approach
Yang, F., Luo, Q., Wang, Y., Liang, H., Wang, Y., Hou, Z., Wan, C., Wang, Y., Liu, Z., Ye, Y., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12824 · Cited by 88
Development of a Brigatinib degrader (SIAIS117) as a potential treatment for ALK positive cancer resistance
Sun, N., Ren, C., Kong, Y., Zhong, H., Chen, J., Li, Y., Zhang, J., Zhou, Y., Qiu, X., Lin, H., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112190 · Cited by 85
DNA-encoded library-enabled discovery of proximity-inducing small molecules
Mason, J. W., Chow, Y. T., Hudson, L., Tutter, A., Michaud, G., Westphal, M. V., Shu, W., Ma, X., Tan, Z. Y., Coley, C. W., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-023-01458-4 · Cited by 83
Synthetic Biological Approaches for Optogenetics and Tools for Transcriptional Light‐Control in Bacteria
Baumschlager, A., & Khammash, M. (2021) · Advanced Biology · doi:10.1002/adbi.202000256 · Cited by 80
Synthetic Protein Condensates That Inducibly Recruit and Release Protein Activity in Living Cells
Yoshikawa, M., Yoshii, T., Ikuta, M., & Tsukiji, S. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c12375 · Cited by 81
Context-specific functions of chromatin remodellers in development and disease
Gourisankar, S. P., Krokhotin, A., Wenderski, W., & Crabtree, G. R. (2023) · Nature Reviews Genetics · doi:10.1038/s41576-023-00666-x · Cited by 88
Self-citation
Multi-input chemical control of protein dimerization for programming graded cellular responses
Wink, G., Wang, Z., Wei, C. T., Greisen, P. J., Warner, K., Cunningham‐Bryant, D., Park, K., Brunette, T., Sheffler, W., Baker, D. A., et al. (2019) · Nature Biotechnology · doi:10.1038/s41587-019-0242-8 · Cited by 79
A Chemical Biology View of Bioactive Small Molecules and a Binder‐Based Approach to Connect Biology to Precision Medicines
Schreiber, S. L. (2018) · Israel Journal of Chemistry · doi:10.1002/ijch.201800113 · Cited by 78
Light‐Induced Dimerization Approaches to Control Cellular Processes
Klewer, L., & Wu, Y. (2019) · Chemistry - A European Journal · doi:10.1002/chem.201900562 · Cited by 77
Nongenetic engineering strategies for regulating receptor oligomerization in living cells
Li, J., Wang, L., Tian, J., Zhou, Z.-L., Li, J., & Yang, H. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00473d · Cited by 75
Inducible and reversible RNA N6-methyladenosine editing
Shi, H., Xu, Y., Tian, N., Yang, M., & Liang, F. (2022) · Nature Communications · doi:10.1038/s41467-022-29665-y · Cited by 79
Advancing targeted protein degradation for metabolic diseases therapy
Zhou, Q., Xiao, H., Yang, F., Wang, Y., Li, P., & Zheng, Z. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106627 · Cited by 77
Relocalizing transcriptional kinases to activate apoptosis
Sarott, R. C., Gourisankar, S. P., Karim, B. A., Nettles, S. A., Yang, H., Dwyer, B. G., Simanauskaite, J., Tse, J., Abuzaid, H. Z., Krokhotin, A., et al. (2024) · Science · doi:10.1126/science.adl5361 · Cited by 80
Self-citation
Inducing protein-protein interactions with molecular glues
Che, Y., Gilbert, A. M., Shanmugasundaram, V., & Noe, M. C. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.04.046 · Cited by 72
Molecular glue-mediated targeted protein degradation: A novel strategy in small-molecule drug development
Tan, X., Huang, Z., Pei, H., Jia, Z., & Zheng, J. (2024) · iScience · doi:10.1016/j.isci.2024.110712 · Cited by 66
Learning of Signaling Networks: Molecular Mechanisms
Csermely, P., Kunšič, N., Mendik, P., Kerestély, M., Faragó, T., Veres, D. V., & Tompa, P. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2019.12.005 · Cited by 73
Amino acid homorepeats in proteins
Chavali, S., Singh, A. K., Santhanam, B., & Babu, M. M. (2020) · Nature Reviews Chemistry · doi:10.1038/s41570-020-0204-1 · Cited by 70
Drug Inducible CRISPR/Cas Systems
Zhang, J., Chen, L., Zhang, J., & Wang, Y. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.07.015 · Cited by 77
The rise of degrader drugs
Teng, M., & Gray, N. S. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.020 · Cited by 63
Targeted protein posttranslational modifications by chemically induced proximity for cancer therapy
Peng, Y., Liu, J., Inuzuka, H., & Wei, W. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104572 · Cited by 68
Strategies to Target ISG15 and USP18 Toward Therapeutic Applications
Fernandez, D. J., Hess, S., & Knobeloch, K. (2020) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00923 · Cited by 65
Beyond Proteolysis-Targeting Chimeric Molecules: Designing Heterobifunctional Molecules Based on Functional Effectors
Hua, L., Zhang, Q., Zhu, X., Wang, R., You, Q., & Wang, L. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00316 · Cited by 69
Unraveling the mechanisms that specify molecules for secretion in extracellular vesicles
Leidal, A. M., & Debnath, J. (2020) · Methods · doi:10.1016/j.ymeth.2020.01.008 · Cited by 67
Patterns of substrate affinity, competition, and degradation kinetics underlie biological activity of thalidomide analogs
Sperling, A. S., Burgess, M. W., Keshishian, H., Gasser, J. A., Bhatt, S., Jan, M., Slabicki, M. M., Sellar, R. S., Fink, E. C., Miller, P. G., et al. (2019) · Blood · doi:10.1182/blood.2019000789 · Cited by 65
LSH mediates gene repression through macroH2A deposition
Ni, K., Ren, J., Xu, X., He, Y., Finney, R., Braun, S. M. G., Hathaway, N. A., Crabtree, G. R., & Muegge, K. (2020) · Nature Communications · doi:10.1038/s41467-020-19159-0 · Cited by 52
Self-citation
COMBINES-CID: An Efficient Method for De Novo Engineering of Highly Specific Chemically Induced Protein Dimerization Systems
Kang, S., Davidsen, K., Gomez-Castillo, L., Jiang, H., Fu, X., Li, Z., Liang, Y. T., Jahn, M., Moussa, M., DiMaio, F., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b03522 · Cited by 64
Fast-acting chemical tools to delineate causality in transcriptional control
Jaeger, M. G., & Winter, G. E. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.02.015 · Cited by 62
Screening for molecular glues – Challenges and opportunities
Holdgate, G. A., Bardelle, C., Berry, S. K., Lanne, A., & Cuomo, M. E. (2023) · SLAS DISCOVERY · doi:10.1016/j.slasd.2023.12.008 · Cited by 60
Opportunities for Therapeutic Modulation of O-GlcNAc
Cheng, S. S., Mody, A. C., & Woo, C. M. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00417 · Cited by 64
Rational design and implementation of a chemically inducible heterotrimerization system
Wu, H. D., Kikuchi, M., Dağliyan, O., Aragaki, A. K., Nakamura, H., Dokholyan, N. V., Umehara, T., & Inoue, T. (2020) · Nature Methods · doi:10.1038/s41592-020-0913-x · Cited by 58
Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules
Ma, B., Khan, K. S., Xu, T., Amada, J. X., Guo, Z., Huang, Y., Yan, Y., Lam, H., Cheng, A. S. L., & Ng, W. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c14380 · Cited by 55
Spatiotemporal control of phosphatidic acid signaling with optogenetic, engineered phospholipase Ds
Tei, R., & Baskin, J. M. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201907013 · Cited by 52
Bifunctional modalities for repurposing protein function
Modell, A. E., Lai, S., Nguyen, T. M., & Choudhary, A. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.06.005 · Cited by 52
Molecular glues and induced proximity: An evolution of tools and discovery
Robinson, S. A., Co, J., & Banik, S. M. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.04.001 · Cited by 58
BAF complexes drive proliferation and block myogenic differentiation in fusion-positive rhabdomyosarcoma
Laubscher, D., Gryder, B. E., Sunkel, B. D., Andrésson, Þ., Wachtel, M., Das, S., Roschitzki, B., Wolski, W., Wu, X., Chou, H.-C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-27176-w · Cited by 58
Self-citation
Chemical Knockdown of Phosphorylated p38 Mitogen-Activated Protein Kinase (MAPK) as a Novel Approach for the Treatment of Alzheimer′s Disease
Son, S. H., Lee, N., Gee, M. S., Song, C. W., Lee, S., Lee, S., Lee, Y., Kim, H. J., Lee, J. K., Inn, K., et al. (2023) · ACS Central Science · doi:10.1021/acscentsci.2c01369 · Cited by 55
Reversible Control of Protein Localization in Living Cells Using a Photocaged-Photocleavable Chemical Dimerizer
Aonbangkhen, C., Zhang, H., Wu, D. Z., Lampson, M. A., & Chenoweth, D. M. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b07753 · Cited by 52
A fluorogenic chemically induced dimerization technology for controlling, imaging and sensing protein proximity
Bottone, S., Joliot, O., Cakil, Z. V., El Hajji, L., Rakotoarison, L.-M., Boncompain, G., Perez, F., & Gautier, A. (2023) · Nature Methods · doi:10.1038/s41592-023-01988-8 · Cited by 48
Modeling the Effect of Cooperativity in Ternary Complex Formation and Targeted Protein Degradation Mediated by Heterobifunctional Degraders
Park, D. J., Izaguirre, J. A., Coffey, R., & Xu, H. (2022) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.2c00037 · Cited by 54
A Binding Site Hotspot Map of the FKBP12–Rapamycin–FRB Ternary Complex by Photoaffinity Labeling and Mass Spectrometry-Based Proteomics
Flaxman, H. A., Chang, C., Wu, H., Nakamoto, C. H., & Woo, C. M. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b03764 · Cited by 51
Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence
Duran-Frigola, M., Cigler, M., & Winter, G. E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c11098 · Cited by 50
Next-Generation Drugs and Probes for Chromatin Biology: From Targeted Protein Degradation to Phase Separation
Čermáková, K., & Hodges, H. C. (2018) · Molecules · doi:10.3390/molecules23081958 · Cited by 51
Engineered platelets as targeted protein degraders and application to breast cancer models
Chen, Y., Pal, S., Li, W., Liu, F., Yuan, S., & Hu, Q. (2024) · Nature Biotechnology · doi:10.1038/s41587-024-02494-8 · Cited by 49
Proximity-inducing modalities: the past, present, and future
Singh, S., Tian, W., Severance, Z. C., Chaudhary, S. K., Anokhina, V. S., Mondal, B., Pergu, R., Singh, P. R., Dhawa, U., Singha, S., et al. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00943a · Cited by 47
An orthogonalized PYR1-based CID module with reprogrammable ligand-binding specificity
Park, S., Qiu, J., Wei, S., Peterson, F. C., Beltrán, J., Medina‐Cucurella, A. V., Vaidya, A. S., Xing, Z., Volkman, B. F., Nusinow, D. A., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01447-7 · Cited by 45
Nanoparticle‐Mediated Targeted Protein Degradation: An Emerging Therapeutics Technology
Baker, A., Ho, A. P. T., Itzhaki, L. S., & Fruk, L. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202503958 · Cited by 44
Mandipropamid as a chemical inducer of proximity for in vivo applications
Ziegler, M. J., Yserentant, K., Dunsing, V., Middel, V., Gralak, A. J., Pakari, K., Bargstedt, J., Kern, C., Petrich, A., Chiantia, S., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00922-3 · Cited by 44
Enhancing Prime Editing Efficiency and Flexibility with Tethered and Split pegRNAs
Feng, Y., Liu, S., Mo, Q., Xiao, X., Liu, P., & Ma, H. (2022) · Protein & Cell · doi:10.1093/procel/pwac014 · Cited by 42
E3-Specific Degrader Discovery by Dynamic Tracing of Substrate Receptor Abundance
Hanzl, A., Barone, E., Bauer, S., Yue, H., Nowak, R. P., Hahn, E., Pankevich, E. V., Koren, A., Kubicek, S., Fischer, E. S., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c10784 · Cited by 40
Reversible Dual-Covalent Molecular Locking of the 14-3-3/ERRγ Protein–Protein Interaction as a Molecular Glue Drug Discovery Approach
Somsen, B. A., Schellekens, R. J. C., Verhoef, C. J. A., Arkin, M. R., Ottmann, C., Cossar, P. J., & Brunsveld, L. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.2c12781 · Cited by 42
From bench to bedside: current development and emerging trend of KRAS-targeted therapy
Chen, Y., Liu, Q.-P., Xie, H., & Ding, J. (2023) · Acta Pharmacologica Sinica · doi:10.1038/s41401-023-01194-4 · Cited by 45
Small-molecule binding and sensing with a designed protein family
(2026) · doi:10.1038/s41467-026-70953-8 · Cited by 41
Engineering synthetic phosphorylation signaling networks in human cells
Yang, X., Rocks, J. W., Jiang, K., Walters, A. J., Rai, K., Liu, J., Nguyen, J., Olson, S. D., Mehta, P., Collins, J. J., et al. (2025) · Science · doi:10.1126/science.adm8485 · Cited by 41
Harnessing Effective Molarity to Design an Electrochemical DNA‐based Platform for Clinically Relevant Antibody Detection
Rossetti, M., Brannetti, S., Mocenigo, M., Marini, B., Ippodrino, R., & Porchetta, A. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202005124 · Cited by 39
PROTACs, molecular glues and bifunctionals from bench to bedside: Unlocking the clinical potential of catalytic drugs
Maneiro, M., Vita, E. D., Conole, D., Kounde, C. S., Zhang, Q., & Tate, E. W. (2021) · Progress in medicinal chemistry · doi:10.1016/bs.pmch.2021.01.002 · Cited by 38
Emerging Trends in Cancer Drug Discovery—From Drugging the “Undruggable” to Overcoming Resistance
Rudolph, J., Settleman, J., & Malek, S. (2021) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-0260 · Cited by 42
A DNA‐Mediated Chemically Induced Dimerization (D‐CID) Nanodevice for Nongenetic Receptor Engineering To Control Cell Behavior
Li, H., Wang, M., Shi, T., Yang, S. Z., Zhang, J., Wang, H., & Nie, Z. (2018) · Angewandte Chemie · doi:10.1002/ange.201806155 · Cited by 38
Applications of protein ubiquitylation and deubiquitylation in drug discovery
Chen, Y., Xue, H., & Jin, J. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107264 · Cited by 41
Creating Red Light-Switchable Protein Dimerization Systems as Genetically Encoded Actuators with High Specificity
Huang, Z., Li, Z., Zhang, X., Kang, S., Dong, R., Sun, L., Fu, X., Vaisar, D., Watanabe, K., & Gu, L. (2020) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00397 · Cited by 39
A rational blueprint for the design of chemically-controlled protein switches
Shui, S., Gaínza, P., Scheller, L., Yang, C., Kurumida, Y., Rosset, S., Georgeon, S., Roberto, R. B. D., Castellanos-Rueda, R., Reddy, S. T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25735-9 · Cited by 36
Chemically inducible split protein regulators for mammalian cells
Rihtar, E., Lebar, T., Lainšček, D., Kores, K., Lešnik, S., Bren, U., & Jerala, R. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01136-x · Cited by 37

Authors: Stanton, B. Z., Chory, E. J., & Crabtree, G. R.
Affiliations: Stanford Medicine (US)
Howard Hughes Medical Institute (US)
Corresponding author: Stanton, Benjamin Z.
Chory, Emma J.
Crabtree, Gerald R.
ORCID: Stanton, Benjamin Z.
Chory, Emma J.
Crabtree, Gerald R.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2018-03-09
Volume: 359
Issue: 6380
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.aao5902
PMC: PMC6417506
OpenAlex: W2789732912
Cited by: 475
References: 104
Citations by year: 2026: 75 · 2025: 92 · 2024: 59 · 2023: 64 · 2022: 55 · 2021: 39 · 2020: 45 · 2019: 30 · 2018: 15
FWCI: 3.21
Type: journal article
Language: en
Open access: green
europepmc.org
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
Funders: National Institutes of Health (NIH Javits Neuroscience Investigator Award R37 NS046789-12, F31 CA203228-02)
Howard Hughes Medical Institute
U.S. Department of Energy (CDMRP Breast Cancer Research Breakthrough Award)
National Cancer Institute (NIH 5R01CA163915-04)
Simons Foundation Autism Research Initiative
Simons Foundation
NSF Office of the Director
Ruth L. Kirschstein National Research Service Award (F31 CA203228-02)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gene Regulatory Network Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: protein-protein interaction, post-translational modification, transcriptional regulation, signaling pathways, chromatin regulation, protein folding, protein degradation, CRISPR, synthetic biology, gene therapy, cancer therapy
MeSH terms: Biological Mimicry, Animals, Chromatin, Humans, Ligands, Protein Processing, Post-Translational, Proteins, Transcription, Genetic, Genetic Therapy, Signal Transduction, Tacrolimus, Protein Folding, Proteolysis, CRISPR-Cas Systems, Cell- and Tissue-Based Therapy

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Chemically induced proximity in biology and medicine

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks