Chemically induced proximity in biology and medicine

THE CONSTITUTION AND FUNDAMENTAL PROPERTIES OF SOLIDS AND LIQUIDS. PART I. SOLIDS.

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The new frontier of genome engineering with CRISPR-Cas9

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Reaction-rate theory: fifty years after Kramers

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Selective inhibition of BET bromodomains

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The constitution and fundamental properties of solids and liquids

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Clearance of p16Ink4a-positive senescent cells delays ageing-associated disorders

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Abscisic Acid: Emergence of a Core Signaling Network

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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

Medicinal Chemistry Education: Emphasize Fundamentals and Skillfully Integrate Knowledge

Du, S., Hu, X., Lindsley, C. W., & Zhan, P. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02622 · Cited by 5

Optimizing ABA-based chemically induced proximity for enhanced intracellular transcriptional activation and modification response to ABA

Zhou, Z., Wang, Y., Zheng, X., Zhang, X., Ji, L., Han, J.-Y., Zuo, Z., Mo, W., & Zhang, L. (2024) · Science China Life Sciences · doi:10.1007/s11427-024-2707-9 · Cited by 4

Photoactivatable Plant Hormone-Based Chemical Inducers of Proximity for In Vivo Applications

Pöschko, P., Berrou, C. M., Pakari, K., Ziegler, M. J., Kern, C., Koch, B., Wittbrodt, J., & Wombacher, R. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.4c00592 · Cited by 4

Target agnostic cellular screening in the era of chemically induced proximity

Jin, M. (2025) · RSC Medicinal Chemistry · doi:10.1039/d5md00529a · Cited by 4

A programmable genetic platform for engineering noninvasive biosensors

Chacko, A. N., Dhanabalan, K. M., Wan, J., Chien, R., Anderson, N. T., Xu, B., Pham, K., Tiwari, R., & Mukherjee, A. (2026) · Science Advances · doi:10.1126/sciadv.aec1211 · Cited by 4

Modulating the phosphorylation status of target proteins through bifunctional molecules

He, Q., Wang, Z., Wang, R., Lu, T., Chen, Y., & Lü, S. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104307 · Cited by 4

Split-Small GTPase Reassembly as a Method to Control Cellular Signaling with User-Defined Inputs

He, Y., Faulkner, B. M., Weatherford, R. S., Hyun, E., & Stains, C. I. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00083 · Cited by 4

Fluorescent Investigation of Proteins Using DNA-Synthetic Ligand Conjugates

Winer, L., Motiei, L., & Margulies, D. H. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00203 · Cited by 4

A PASS for protein secretion

Wang, T., & Zhou, Y. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01444-w · Cited by 4

A chemical magnet: Approaches to guide precise protein localization

Kumar, S., & Nabet, B. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117672 · Cited by 3

Enhancing the performance of Magnets photosensors through directed evolutionPreprint

Baumschlager, A., Weber, Y., Cánovas, D., Dionisi, S., & Khammash, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.14.516313 · Cited by 4

Borrowing Transcriptional Kinases to Activate ApoptosisPreprint

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. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.23.563687 · Cited by 4

High-throughput protein binder discovery by rapid in vivo selectionPreprint

Styles, M. J., Pixley, J. A., Wei, T., Basile, C., Lu, S. S., & Dickinson, B. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.06.631531 · Cited by 4

Visible‐Light‐Switchable Molecular Glues for Reversible Control of Protein Function

Zhang, J., Herzog, L. K., Li, S., Chen, X., & Wu, Y. (2025) · Chemistry - A European Journal · doi:10.1002/chem.202403808 · Cited by 3

Nanoparticle‐Mediated Targeted Protein Degradation: An Emerging Therapeutics Technology

Baker, A., Ho, A. P. T., Itzhaki, L. S., & Fruk, L. (2025) · Angewandte Chemie · doi:10.1002/ange.202503958 · Cited by 3

Development and characterization of endolysosomal trafficking targeting chimera degraders of α1A-adrenergic receptor

Chen, J., Wang, S., Li, T., Li, W., Ke, X., Ma, Z., Du, L., & Li, M. (2025) · Journal of Advanced Research · doi:10.1016/j.jare.2025.06.014 · Cited by 3

Spatiotemporal Regulation in Porous Organic Cage Salt–Metal Cluster Hybrids for Efficient Orthogonal Tandem Catalysis

Li, J., Wang, J., Zhou, J., Zhao, K., Liu, S., Zhao, X., Han, S., Yao, L., & Sun, J. (2025) · Angewandte Chemie · doi:10.1002/ange.202509941 · Cited by 3

PANCS-spec-Binders: A system for rapidly discovering isoform- or epitope-specific binders

Pixley, J. A., Styles, M. J., Aphicho, K., Endres, M., Gade, P., Michalska, K., Joachimiak, A., & Dickinson, B. C. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2531008123 · Cited by 3

EGFR activation requires cholesterol interaction at the inner leaflet of the plasma membrane

Kim, D., Triet, H. M., Bocharov, E. V., Park, S., Bershatsky, Y. V., Volynsky, P. E., Kim, E., Efremov, R. G., Cho, W., Park, S., et al. (2025) · Science Advances · doi:10.1126/sciadv.adx2398 · Cited by 3

Targeted stress granule regulation by engineering a non-catalytic O-GlcNAc transferase

Wang, N., Hou, F., Ma, S., 刘思兰, Wei, H., Fang, W., Zhang, K., & Ge, Y. (2026) · Nature Communications · doi:10.1038/s41467-025-66689-6 · Cited by 3

Molecular glue degraders: Rational design, specificity engineering, and advanced delivery

Ma, L., Wang, N., Zhu, J., Wu, L., He, S., & Zhang, B. (2026) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2026.02.020 · Cited by 5

Synthetic Cells on Demand: From Molecular Stimuli to Cellular Functions

Suzuki, M., & KAMIYA, K. (2026) · ChemSystemsChem · doi:10.1002/syst.202500071 · Cited by 3

Engineering of genetically encoded programmable calcium channel inhibitory binders

Liu, X., Ali, S., Lan, T.-H., Wang, D., McKee, B., Nonomura, T., Liu, S., Zhao, F., Zhu, M. X., Huang, Y., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71769-2 · Cited by 3

Epidermal Growth Factor Receptor as a Model Drug Target for Scrutinizing the Status Quo in Drug Discovery and Chemical Biology

Heppner, D. E., MacDonald, M. R., Nasief, N. N., Naik, S. E., & Cunningham, S. (2026) · ACS Bio & Med Chem Au · doi:10.1021/acsbiomedchemau.6c00089 · Cited by 3

De novo design of orthogonal far-red, orange, and green fluorophore-binding proteins for multiplexed imaging

Tran, L., Klein, S., Juergens, D., Sharma, S., Decarreau, J. A., Lee, G. R., Wang, Y., Chen, W., Bera, A. K., Kang, A., et al. (2026) · Science · doi:10.1126/science.aeb0822 · Cited by 14

Crystal packing reveals rapamycin-mediated homodimerization of an FK506-binding domain

Singh, A., Saharan, K., Baral, S., Luan, S., & Vasudevan, D. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.02.107 · Cited by 3

Synthetic Reprogramming of Kinases Expands Cellular Activities of Proteins

Shoba, V. M., Godage, D. N. P. M., Chaudhary, S. K., Deb, A., Siriwardena, S. U., & Choudhary, A. (2022) · Angewandte Chemie · doi:10.1002/ange.202202770 · Cited by 3

Cross‐Linking Profiling of Molecular Glue Degrader‐Induced E3 Ligase Interactome to Expand Target Space

Xu, Y., Zhao, W., Nie, H., Wang, J., Fu, J., Hu, H., Liu, Z., Tao, S., Zhang, M., Zhou, Y., et al. (2025) · Angewandte Chemie · doi:10.1002/ange.202505053 · Cited by 3

Reengineering of a Proteomimetic Pan‐Ras Inhibitor into a Ras Degrader

Ongkingco, J. F., Hong, S. H., Toth, E. D., Nguyễn, T. T., & Arora, P. S. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202507092 · Cited by 4

Protocol for rapid manipulation of mitochondrial morphology in living cells using inducible counter mitochondrial morphology (iCMM)

Miyamoto, T., Han, S., & Shimano, H. (2021) · STAR Protocols · doi:10.1016/j.xpro.2021.100721 · Cited by 3

Amplifying Intermolecular Events by Streptavidin-Induced Proximity

Li, H., Liu, T., & Yang, H. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c03666 · Cited by 3

Synthetic Biology Meets Ca2+ Release-Activated Ca2+ Channel-Dependent Immunomodulation

Bacsa, B., Hopl, V., & Derler, I. (2024) · Cells · doi:10.3390/cells13060468 · Cited by 3

Proximity‐Inducing Bifunctional Molecules Beyond PROTACs

Lai, S., Modell, A. E., & Choudhary, A. (2022) · Wiley eBooks · doi:10.1002/9781119774198.ch12 · Cited by 3

Caffeine-regulated molecular switches for functional control of CAR T cells in vivoPreprint

Sylvander, E., Salzer, B., Emminger, D., Baik, H., D’Accardio, G., Schäfer, M., Mouratidis, K., Buri, M. C., Maresch, D., Urbanetz, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.13.659487 · Cited by 3

Rewiring DNA repair with PARP-based chemical inducers of proximityPreprint

da Camara, B., Bilotta, E. M., Broderick, E., Premashankar, A., Barta, P. A., Carter, T. R., Hargis, L. M., Durocher, D., & Erb, M. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.26.666954 · Cited by 2

Multiplex design and discovery of proximity handles for programmable proteome editingPreprint

Suiter, C. C., Ahn, G., Chiu, M., Fu, Y., Sadre, S., Simon, J. J., Lee, D. S., Fowler, D. M., Maly, D. J., Baker, D. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.13.681693 · Cited by 5

A generalizable approach for programming protease-responsive conformationally inhibited artificial transcriptional factors

Liu, Y., Zhao, L., Long, J., Huang, Z., Long, Y., He, J., & Jiang, J. (2025) · Nature Communications · doi:10.1038/s41467-025-59828-6 · Cited by 2

Nanobody‐Based Light‐Controllable Systems for Investigating Biology

Wu, D., Xia, S., & Chen, X. (2025) · ChemBioChem · doi:10.1002/cbic.202500311 · Cited by 2

Targeting SIX2 as a novel sensitization strategy of sorafenib treatment on advanced hepatocellular carcinoma through modulating METTL9-SLC7A11 axis

Lü, J., Cai, D., Qian, L., Wang, Y., Ai, S., Song, P. K., Sun, F., Sun, Y., Liang, M., Jiang, H., et al. (2025) · npj Precision Oncology · doi:10.1038/s41698-025-01004-6 · Cited by 3

The rise of new targets in melanoma

Bai, X. L., & Flaherty, K. T. (2025) · British Journal of Dermatology · doi:10.1093/bjd/ljaf251 · Cited by 2

How Feasible Is Docking of PROTACs to POI-E3L Complexes? Testing Physics-Based and ML-Based Docking Tools

Jiménez-Boi, R., Miñán, R., Pallara, C., Lozoya, E., Guallar, V., Molina, A., & Soliva, R. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5c01581 · Cited by 2

A Chemically Switchable Synthetic Condensate Platform for Reversible Protein Sequestration and Release

Fukaya, Y., Yoshikawa, M., Aoki, K., Farrants, H., Johnsson, K., & Tsukiji, S. (2025) · ACS Chemical Biology · doi:10.1021/acschembio.5c00719 · Cited by 2

A Reactive Antagonist Strategy: Cysteine‐Directed Covalent Molecular Glue in Plant Hormone Receptor Regulation

Ueda, M., Matsumoto, K., Nomura, T., Takaoka, Y., Okumura, T., Kozaki, W., Hoshikawa, H., Nishizato, Y., Chini, A., Solano, R., et al. (2026) · Advanced Science · doi:10.1002/advs.202517463 · Cited by 3

Diterpene Molecular Glue Stabilizes Protein–Protein Interactions of a Disordered Phosphoprotein that Controls Translational Repression

Ogino, N., Masuda, R., Igaue, S., Arita, M., Matsumura, A., Ieda, Y., Muroi, M., Matsumoto, K., Nakagawa, R., Higuchi, Y., et al. (2026) · JACS Au · doi:10.1021/jacsau.5c01403 · Cited by 2

CF2H: a cell-free two-hybrid platform for rapid protein binder screening

Capin, J., Mayonove, P., DeVisch, A., Becher, A., Ngo, G., Courbet, A., Ragotte, R. J., Cohen‐Gonsaud, M., Espeut, J., & Bonnet, J. P. (2026) · Nature Communications · doi:10.1038/s41467-026-69741-1 · Cited by 2

Small Molecule‐Based Conditional Gene Regulation: Advances and Applications

Ansari, M. A., Sharma, R., Swami, P., & Rode, A. B. (2026) · Chemistry–Methods · doi:10.1002/cmtd.202500137 · Cited by 1

Remodeling synaptic connections via engineered neuron-astrocyte interactions

Kim, S. H., Won, W., Kim, G. H., Kook, Y. H., Son, S., Choi, S., Kang, D. Y., Park, M. G., Choi, Y., Won, S. S., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-71440-w · Cited by 2

Nanotechnology enabled proximity-induced protein degradation from multiscale bottlenecks to precision therapeutics

Pan, X., Jin, H., Song, J., Wang, P., Min, H., Nie, G., & Qi, Y. (2026) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2026.115880 · Cited by 2

Proximity-Induced Phosphatase-Recruiting DNA Feedback Switch for Self-Adaptive Modulation of Receptor Signaling and Cell Behavior

Wu, Y., Yin, G., Zhang, Q., Qi, L., Zhang, B., Chen, M., Liu, L., Zhou, Y., He, L., Wang, H.-H., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c05492 · Cited by 2

Degradation-based protein profiling in target identification and early-stage drug discovery of bioactive natural products

Ni, Z., Shi, Y., & Rao, Y. (2026) · Targetome · doi:10.48130/targetome-0026-0019 · Cited by 2

AI-Guided De Novo Design of a Caffeine-Induced Protein Dissociation System

Nonomura, T., McKee, B., Price, A., Cui, M., Yousuf, Z., Tran, F., He, L., Wang, T., & Zhou, Y. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c02343 · Cited by 2

Molecular glues and PROTACs: unlocking targeted protein degradation in plant biology

Donderis-Fagoaga, C., Orea-Ordóñez, L., & Lozano‐Juste, J. (2026) · Journal of Experimental Botany · doi:10.1093/jxb/erag256 · Cited by 2

The importance of controls in targeted protein degradation: Determining mechanism

Hill-Payne, B., Dilones, S., & Burslem, G. M. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.10.006 · Cited by 3

Discovery of chemical probes that perturb protein complexes using size exclusion chromatography and chemical proteomics

Ng, W., Xu, T., & Guo, Z. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.04.028 · Cited by 2

A genetically encoded actuator selectively boosts L-type calcium channels in diverse physiological settings

Morfin, P. J. D. R., Scala-Chávez, D., Jayaraman, S., Yang, L., Kochiss, A. L., Colecraft, H. M., Liu, X. S., Marx, S. O., Rajadhyaksha, A. M., & Johny, M. B. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2023.11.3224 · Cited by 2

The Emergence of Oligonucleotide Building Blocks in the Multispecific Proximity-Inducing Drug Toolbox of Destruction

Zhou, K. X. T., & Bujold, K. E. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.4c00311 · Cited by 2

Research advancements in molecular glues derived from natural product scaffolds: Chemistry, targets, and molecular mechanisms

Yin, L., Niu, T., Li, L., Yu, W. D., Han, B., Rehman, A., & Zeng, K. (2025) · Chinese Herbal Medicines · doi:10.1016/j.chmed.2025.01.001 · Cited by 2

Ligand-induced assembly of antibody variable fragments for the chemical regulation of biological processes

Rihtar, E., Fink, T., Lebar, T., Lainšček, D., Kolenc, Ž., Kadunc, L., & Jerala, R. (2025) · Cell chemical biology · doi:10.1016/j.chembiol.2025.01.007 · Cited by 3

Emerging pharmacology of targeted protein degraders

Barghout, S. H., & Eldeeb, M. A. (2025) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2025.103694 · Cited by 2

Photoactivatable trimethoprim-based probes for spatiotemporal control of biological processes

Wu, D. Z., Lampson, M. A., & Chenoweth, D. M. (2020) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2020.03.015 · Cited by 2

Immediate and Selective Control of Protein Abundance Using the dTAG System

Nabet, B., & Gray, N. S. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781839160691-00055 · Cited by 2

Combinatorial Approaches for Efficient Design of Photoswitchable Protein-Protein Interactions as In Vivo Actuators

Zhang, X., Pan, Y., Kang, S., & Gu, L. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.844405 · Cited by 4

Reversible optogenetic control of protein function and localization

Wu, D. Z., Lackner, R. M., Aonbangkhen, C., Lampson, M. A., & Chenoweth, D. M. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.05.002 · Cited by 2

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Gomez-Castillo, L., Watanabe, K., Jiang, H., Kang, S., & Gu, L. (2020) · Journal of Visualized Experiments · doi:10.3791/60738 · Cited by 2

Strategies for Tag‐Based Protein Control

Nabet, B., Gray, N. S., & Ferguson, F. M. (2022) · Wiley eBooks · doi:10.1002/9781119774198.ch13 · Cited by 2

Chemically induced proximity reveals mechanotransduction of a meiotic checkpoint at the nuclear envelopePreprint

Liu, C., & Dernburg, A. F. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.28.564506 · Cited by 2

Hijacking the transcriptional activation potential of the BAF complex via Induced ProximityPreprint

Chia, L., Mayhew, D. L., Sherbanee, B., Lahr, D. L., & Taherbhoy, A. M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.18.572217 · Cited by 2

Ion channel inhibition by targeted recruitment of NEDD4-2 with divalent nanobodiesPreprint

Morgenstern, T. J., Darko-Boateng, A., Afriyie, E., Shanmugam, S. K., Zhou, X., Choudhury, P., Desai, M., Kass, R. S., Clarke, O. B., & Colecraft, H. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.28.596281 · Cited by 2

Mapping the diverse topologies of protein-protein interaction fitness landscapesPreprint

Lu, S. S., Styles, M. J., Gao, C. F., Nandy, A., Basile, C., Pixley, J. A., Tao, S., Dinner, A. R., Vaikuntanathan, S., & Dickinson, B. C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.14.682342 · Cited by 2

Design of post-translational, ligand-controlled inverters and switchesPreprint

Swift, S. D., McCarthy, K. S., Baumer, Z. T., Wheeldon, I. R., Cutler, S. R., & Whitehead, T. A. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.05.692672 · Cited by 1

The First‐In‐Class Deubiquitinase‐Targeting Chimera Stabilizes and Activates cGAS

Deng, Z., Chen, L., Qian, C., Liu, J., Wu, Q. D., Song, X., Xiong, Y., Wang, Z., Hu, X., Inuzuka, H., et al. (2024) · Angewandte Chemie · doi:10.1002/ange.202415168 · Cited by 1

Supramolecular Host–Guest Assemblies for Tunable and Modular Lysosome‐Targeting Protein Degradation

Chen, X., Wu, T., Chen, Y., Wu, H., Kang, W., Wang, N., You, Q., Guo, X., & Jiang, Z. (2025) · Angewandte Chemie · doi:10.1002/ange.202506618 · Cited by 1

A SAMBA for chemically induced proximity

Zhou, Y., Ma, X., & Ye, H. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01934-z · Cited by 1

Functional Proximity across an mRNA

Hatfield, B. M., Weidmann, C. A., McCutchin, C. A., Irving, P. S., Nelson, I. M., Felder, S., & Weeks, K. M. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00340 · Cited by 1

A Bird’s-Eye View of the Wings Apart-Like Protein in Cell Biology and Implications for Disease and Therapeutics

Sekhar, P. S., Fahma, A., Subair, S., Gopalakrishnan, A. P., Shivamurthy, P. B., Chakraborty, S., & Raju, R. (2025) · OMICS A Journal of Integrative Biology · doi:10.1177/15578100251374589 · Cited by 1

Readily Adaptable Biosensor-Guided Platform Enables the Selection of Herbicide-Metabolizing CYP2B6 Variants

Zimran, G., & Mosquna, A. (2025) · ACS Synthetic Biology · doi:10.1021/acssynbio.5c00610 · Cited by 2

Repurposing nuclear receptors for ligand-responsive liquid condensate formation and gene regulation

Rihtar, E., Fink, T., Ivanovski, F., Koplan, E., & Jerala, R. (2026) · Nature Communications · doi:10.1038/s41467-026-69099-4 · Cited by 1

Cyclic γ-AApeptide-Based Molecular Glues for RNA m 6 A Editing

Dong, C., Li, S., Xia, X., Tran, T., Kumar, S., Yu, H., Win, Y. Y., Li, S., He, Y. J., Cai, J., et al. (2026) · ACS Chemical Biology · doi:10.1021/acschembio.5c00997 · Cited by 1

From Covalent to Supramolecular: Re‐Thinking Lysosome‐Targeting Chimeras Through Modular and Tunable Proximity Control

Wang, N., Wang, X., Jiang, Z., & Chen, X. (2026) · Chemistry - A European Journal · doi:10.1002/chem.202503647 · Cited by 1

Targeted Protein Degradation: Methods and Prospects

Sklyar, I. V., Рожкова, А. М., Kondratyeva, E. G., & Sinitsyn, A. P. (2026) · Biochemistry (Moscow) · doi:10.1134/s0006297925604034 · Cited by 1

Cooperative Binding Domains Enhance Sensitivity and Overcome the Hook Effect in Two-Component Protein Biosensors

Mutschler, R., Caputo, A. T., Guo, Z., Fiorito, M. M., Hayat, I. F., Newton, S., Zhang, X., Karunathilaka, N., Duval, C. J., Brazel, H., et al. (2026) · ACS Sensors · doi:10.1021/acssensors.6c00488 · Cited by 2

Proteomics‐Driven Strategies for Proximity‐Inducing Drug Discovery

Fan, R., Ni, J., Zhou, T., Jiang, H. Q., Zhao, W., & Tan, M. (2026) · Angewandte Chemie International Edition · doi:10.1002/anie.3307512 · Cited by 1

An Evolutionary Strategy for Identification of Higher Order, Green Fluorescent Host–Guest Pairs Compatible with Living Systems

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