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

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Chemically induced proximity in biology and medicine

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

DOI 10.1126/science.aao5902PMC PMC6417506

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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

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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

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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

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