The DOI matches its Crossref record; 74 of the 76 references it cites were found in a registry or an index.
Molecular glues and bifunctional compounds: Therapeutic modalities based on induced proximity
Open accessPublished version of a preprint
Abstract
This Perspective explores molecular glues and bifunctional compounds-proximity-inducing compounds-and offers a framework to understand and exploit their similarity to hotspots, missense mutations, and posttranslational modifications (PTMs). This view is also shown to be relevant to intramolecular glues, where compounds induce contacts between distinct domains of the same protein. A historical perspective of these compounds is presented that shows the field has come full circle from molecular glues targeting native proteins, to bifunctionals targeting fusion proteins, and back to molecular glues and bifunctionals targeting native proteins. Modern screening methods and data analyses with pre-selected target proteins are shown to yield either cooperative molecular glues or bifunctional compounds that induce proximity, thereby enabling novel functional outcomes.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Taken together, our findings provide another example that the underlying principles of molecular glue mechanisms might be rooted in the partial mimicry of naturally occurring PPIs at preexisting sites of high PPI propensity, interactions that are further enhanced by a matching molecular glue1,10,11,50–54.”
From Cereblon induces G3BP2 neosubstrate degradation using molecular surface mimicry (2026) · cites this paper as [1]
Citations
Cites
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Self-citationPROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395
The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416
Identification of a Primary Target of Thalidomide Teratogenicity
Ito, T., Ando, H., Suzuki, T., Ogura, T., Hotta, K., Imamura, Y., Yamaguchi, Y., & Handa, H. (2010) · Science · doi:10.1126/science.1177319 · Cited by 2,136
A mammalian protein targeted by G1-arresting rapamycin–receptor complex
Brown, E. J., Albers, M. W., Bum Shin, T., ichikawa, K., Keith, C. T., Lane, W. S., & Schreiber, S. L. (1994) · Nature · doi:10.1038/369756a0 · Cited by 2,053
Self-citationA Hot Spot of Binding Energy in a Hormone-Receptor Interface
Clackson, T., & Wells, J. A. (1995) · Science · doi:10.1126/science.7529940 · Cited by 1,987
Lenalidomide Causes Selective Degradation of IKZF1 and IKZF3 in Multiple Myeloma Cells
Krönke, J., Udeshi, N. D., Narla, A., Grauman, P., Hurst, S. N., McConkey, M., Svinkina, T., Heckl, D., Comer, E., Li, X., et al. (2014) · Science · doi:10.1126/science.1244851 · Cited by 1,879
Self-citationThe Myeloma Drug Lenalidomide Promotes the Cereblon-Dependent Destruction of Ikaros Proteins
Lu, G., Middleton, R. E., Sun, H., Naniong, M., Ott, C. J., Mitsiades, C. S., Wong, K.-K., Bradner, J. E., & Kaelin, W. G. (2014) · Science · doi:10.1126/science.1244917 · Cited by 1,583
Inducible Apoptosis as a Safety Switch for Adoptive Cell Therapy
Di Stasi, A., Tey, S.-K., Dotti, G., Fujita, Y., Kennedy-Nasser, A., Martinez, C., Straathof, K., Liu, E., Durett, A. G., Grilley, B., et al. (2011) · New England Journal of Medicine · doi:10.1056/nejmoa1106152 · Cited by 1,512
Sabatini, D. M., Erdjument-Bromage, H., Lui, M., Tempst, P., & Snyder, S. H. (1994) · Cell · doi:10.1016/0092-8674(94)90570-3 · Cited by 1,509
The dTAG system for immediate and target-specific protein degradation
Nabet, B., Roberts, J. M., Buckley, D. L., Paulk, J., Dastjerdi, S., Yang, A., Leggett, A. L., Erb, M. A., Lawlor, M. A., Souza, A., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0021-8 · Cited by 1,118
mTOR kinase structure, mechanism and regulation
Yang, H., Rudge, D. G., Koos, J. D., Vaidialingam, B., Yang, H. J., & Pavletich, N. P. (2013) · Nature · doi:10.1038/nature12122 · Cited by 1,075
Encoded combinatorial chemistry.
Brenner, S., & Lerner, R. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5381 · Cited by 1,014
Structure of the FKBP12-Rapamycin Complex Interacting with Binding Domain of Human FRAP
Choi, J., Chen, J., Schreiber, S. L., & Clardy, J. (1996) · Science · doi:10.1126/science.273.5272.239 · Cited by 933
Self-citationAllosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases
Chen, Y.-N. P., LaMarche, M. J., Chan, H. M., Fekkes, P., Garcia-Fortanet, J., Acker, M. G., Antonakos, B., Chen, C. H.-T., Chen, Z., Cooke, V. G., et al. (2016) · Nature · doi:10.1038/nature18621 · Cited by 925
Controlling Signal Transduction with Synthetic Ligands
Spencer, D. M., Wandless, T. J., Schreiber, S. L., & Crabtree, G. R. (1993) · Science · doi:10.1126/science.7694365 · Cited by 845
Self-citationSchreiber, S. L. (2021) · Cell · doi:10.1016/j.cell.2020.12.020 · Cited by 598
Self-citationStructure of the E6/E6AP/p53 complex required for HPV-mediated degradation of p53
Martinez-Zapien, D., Ruiz, F. X., Poirson, J., Mitschler, A., Ramirez, J., Forster, A., Cousido-Siah, A., Masson, M., Pol, S. V., PODJARNY, A. D., et al. (2016) · Nature · doi:10.1038/nature16481 · Cited by 518
Chemically induced proximity in biology and medicine
Stanton, B. Z., Chory, E. J., & Crabtree, G. R. (2018) · Science · doi:10.1126/science.aao5902 · Cited by 475
Signaling Network Model of Chromatin
Schreiber, S. L., & Bernstein, B. (2002) · Cell · doi:10.1016/s0092-8674(02)01196-0 · Cited by 399
Self-citationBurgin, A. B., Magnússon, Ó. Þ., Singh, J., Witte, P., Staker, B. L., Björnsson, J. M., Þorsteinsdóttir, M., Hrafnsdóttir, S., Hagen, T. J., Kiselyov, A. S., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1598 · Cited by 396
Rheb Activates mTOR by Antagonizing Its Endogenous Inhibitor, FKBP38
Bai, X., Ma, D., Liu, A., Shen, X., Wang, Q. J., Liu, Y., & Jiang, Y. (2007) · Science · doi:10.1126/science.1147379 · Cited by 382
Probing Immunosuppressant Action with a Nonnatural Immunophilin Ligand
Bierer, B. E., Somers, P. K., Wandless, T. J., Burakoff, S. J., & Schreiber, S. L. (1990) · Science · doi:10.1126/science.1700475 · Cited by 351
Self-citationPeterson, R. T., Beal, P. A., Comb, M. J., & Schreiber, S. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.7416 · Cited by 340
Self-citationGarcia Fortanet, J., Chen, C. H.-T., Chen, Y.-N. P., Chen, Z., Deng, Z., Firestone, B., Fekkes, P., Fodor, M., Fortin, P. D., Fridrich, C., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00680 · Cited by 298
Udaka, K., Tsomides, T. J., & Eisen, H. N. (1992) · Cell · doi:10.1016/0092-8674(92)90617-l · Cited by 272
Phase Separation of Disease-Associated SHP2 Mutants Underlies MAPK Hyperactivation
Zhu, G., Xie, J., Kong, W., Xie, J., Li, Y., Du, L., Zheng, Q., Sun, L., Guan, M., Li, H., et al. (2020) · Cell · doi:10.1016/j.cell.2020.09.002 · Cited by 267
Chemical remodeling of a cellular chaperone to target the active state of mutant KRAS
Schulze, C. J., Seamon, K. J., Zhao, Y., Yang, Y. C., Cregg, J., Kim, D., Tomlinson, A., Choy, T. J., Wang, Z., Sang, B., et al. (2023) · Science · doi:10.1126/science.adg9652 · Cited by 264
Haggarty, S. J., Mayer, T. U., Miyamoto, D. T., Fathi, R., King, R. W., Mitchison, T. J., & Schreiber, S. L. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00101-0 · Cited by 251
Self-citationChemical probes and drug leads from advances in synthetic planning and methodology
Gerry, C. J., & Schreiber, S. L. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.53 · Cited by 232
Self-citationTomasello, G., Armenia, I., & Molla, G. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa009 · Cited by 232
Targeted protein degradation via intramolecular bivalent glues
Hsia, O., Hinterndorfer, M., Cowan, A. D., Iso, K., Ishida, T., Sundaramoorthy, R., Nakasone, M. A., Imrichova, H., Schätz, C., Rukavina, A., et al. (2024) · Nature · doi:10.1038/s41586-024-07089-6 · Cited by 222
Molecular glue CELMoD compounds are regulators of cereblon conformation
Watson, E. R., Novick, S., Matyskiela, M. E., Chamberlain, P. P., H. de la Peña, A., Zhu, J., Tran, E., Griffin, P. R., Wertz, I. E., & Lander, G. C. (2022) · Science · doi:10.1126/science.add7574 · Cited by 208
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
Self-citationLiberles, S. D., Diver, S. T., Austin, D. J., & Schreiber, S. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.7825 · Cited by 199
Self-citationPhosphorylation-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
Self-citationThe E3 ligase adapter cereblon targets the C-terminal cyclic imide degron
Ichikawa, S., Flaxman, H. A., Xu, W., Vallavoju, N., Lloyd, H. C., Wang, B., Shen, D., Pratt, M. R., & Woo, C. M. (2022) · Nature · doi:10.1038/s41586-022-05333-5 · Cited by 195
A Small Molecule Targeting Mutagenic Translesion Synthesis Improves Chemotherapy
Wojtaszek, J. L., Chatterjee, N., Najeeb, J., Ramos, A., Lee, M., Bian, K., Xue, J. Y., Fenton, B. A., Park, H., Li, D., et al. (2019) · Cell · doi:10.1016/j.cell.2019.05.028 · Cited by 194
Kelly, J. D., Haldeman, B. A., Grant, F. J., et al. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31541-2 · Cited by 193
Dekker, C., Mattes, H., Wright, M., Boettcher, A., Hinniger, A., Hughes, N., Kapps-Fouthier, S., Eder, J., Erbel, P. J. A., Stiefl, N., et al. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167309 · Cited by 183
Molecular structures reveal synergistic rescue of Δ508 CFTR by Trikafta modulators
Fiedorczuk, K., & Chen, J. (2022) · Science · doi:10.1126/science.ade2216 · Cited by 176
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
Functional analysis of Fas signaling in vivo using synthetic inducers of dimerization
Spencer, D. M., Belshaw, P. J., Chen, L., Ho, S. N., Randazzo, F. M., Crabtree, G. R., & Schreiber, S. L. (1996) · Current Biology · doi:10.1016/s0960-9822(02)00607-3 · Cited by 144
Self-citationMechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2
Pádua, R. A. P., Sun, Y., Marko, I., Pitsawong, W., Stiller, J. B., Otten, R., & Kern, D. (2018) · Nature Communications · doi:10.1038/s41467-018-06814-w · Cited by 133
Stabilization of the Max Homodimer with a Small Molecule Attenuates Myc-Driven Transcription
Struntz, N. B., Chen, A., Deutzmann, A., Wilson, R. M., Stefan, E., Evans, H. L., Ramirez, M. A., Liang, T., Caballero, F., Wildschut, M. H. E., et al. (2019) · Cell Chemical Biology · doi:10.1016/j.chembiol.2019.02.009 · Cited by 130
Rapamycin-inspired macrocycles with new target specificity
Guo, Z., Hong, S. Y., Wang, J., Rehan, S., Liu, W., Peng, H., Das, M., Li, W., Bhat, S., Peiffer, B., et al. (2019) · Nature Chemistry · doi:10.1038/s41557-018-0187-4 · Cited by 120
A novel pathway regulating the mammalian target of rapamycin (mTOR) signaling
Chen, J., & Fang, Y. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01263-7 · Cited by 119
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
Self-citationThe expanding reaction toolkit for DNA-encoded libraries
Fair, R. J., Walsh, R. T., & Hupp, C. D. (2021) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2021.128339 · Cited by 110
SnapShot: Ca2+-Calcineurin-NFATSignaling
Crabtree, G. R., & Schreiber, S. L. (2009) · Cell · doi:10.1016/j.cell.2009.06.026 · Cited by 105
Self-citationAhn, G., Banik, S. M., & Bertozzi, C. R. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.02.024 · Cited by 98
Rational Design of Orthogonal Receptor–Ligand Combinations
Belshaw, P. J., Schoepfer, J. G., Liu, K., Morrison, K. L., & Schreiber, S. L. (1995) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199521291 · Cited by 93
Self-citationWestphal, M. V., Hudson, L., Mason, J. W., Pradeilles, J. A., Zécri, F. J., Briner, K., & Schreiber, S. L. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b13186 · Cited by 89
Self-citationStructure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase
Garvie, C. W., Wu, X., Papanastasiou, M., Lee, S., Fuller, J., Schnitzler, G. R., Horner, S. W., Baker, A., Zhang, T., Mullahoo, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24495-w · Cited by 85
Proximity versus allostery: the role of regulated protein dimerization in biology
Austin, D. J., Schreiber, S. L., & Crabtree, G. R. (1994) · Chemistry & Biology · doi:10.1016/1074-5521(94)90002-7 · Cited by 84
Self-citationDNA-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
Self-citationShigdel, U. K., Lee, S.-J., Sowa, M. E., Bowman, B. R., Robison, K., Zhou, M., Pua, K. H., Stiles, D. T., Blodgett, J. A. V., Udwary, D. W., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006560117 · Cited by 80
Schreiber, S. L. (2018) · Israel Journal of Chemistry · doi:10.1002/ijch.201800113 · Cited by 78
Self-citationThe protein organization of a red blood cell
Sae-Lee, W., McCafferty, C. L., Verbeke, E. J., Havugimana, P. C., Papoulas, O., McWhite, C. D., Houser, J. R., Vanuytsel, K., Murphy, G. J., Drew, K., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111103 · 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
Systematic discovery of mutation-directed neo-protein-protein interactions in cancer
Mo, X., Niu, Q., Ivanov, A. A., Tsang, Y. H., Tang, C., Shu, C., Li, Q., Qian, K., Wahafu, A., Doyle, S. P., et al. (2022) · Cell · doi:10.1016/j.cell.2022.04.014 · Cited by 73
Quancard, J., Klein, T., Fung, S.-Y., Renatus, M., Hughes, N., Israël, L., Priatel, J. J., Kang, S., Blank, M. A., Viner, R. I., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-018-0222-1 · Cited by 72
Induced protein degradation for therapeutics: past, present, and future
Yoon, H., Rutter, J. C., Li, Y.-D., & Ebert, B. L. (2024) · Journal of Clinical Investigation · doi:10.1172/jci175265 · Cited by 72
Small-Molecule Kinase Downregulators
Jones, L. H. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.10.011 · Cited by 69
Rational Screening for Cooperativity in Small-Molecule Inducers of Protein–Protein Associations
Liu, S., Tong, B., Mason, J. W., Ostrem, J. M. L., Tutter, A. V., Hua, B. K., Tang, S. A., Bonazzi, S., Briner, K., Berst, F., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c08307 · Cited by 69
Self-citationCytokines and cell growth control.
Goldring, M. B., & Goldring, S. R. (1991) · PubMed · Cited by 65
Optimization of PROTAC Ternary Complex Using DNA Encoded Library Approach
Chen, Q., Liu, C., Wang, W., Meng, X., Cheng, X., Li, X.-Y., Cai, L., Luo, L., He, X., Qu, H., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00797 · Cited by 55
Gibson, W. J., Sadagopan, A., Shoba, V. M., Choudhary, A., Meyerson, M. M., & Schreiber, S. L. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c06179 · Cited by 51
Self-citationConverging mechanism of UM171 and KBTBD4 neomorphic cancer mutations
Xie, X., Zhang, O., Yeo, M. J. R., Lee, C., Tao, R., Harry, S. A., Payne, N. C., Nam, E., Paul, L., Li, Y., et al. (2025) · Nature · doi:10.1038/s41586-024-08533-3 · Cited by 50
Solid-phase synthesis of DNA-encoded libraries via an “aldehyde explosion” strategy
Paciaroni, N. G., Ndungu, J. M., & Kodadek, T. J. (2020) · Chemical Communications · doi:10.1039/d0cc01474e · Cited by 45
Heitel, P. (2023) · Molecules · doi:10.3390/molecules28020690 · Cited by 27
Chemical inducers of dimerization: The atomic structure of FKBP12-FK1012A-FKBP12
Schultz, L. W., & Clardy, J. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(97)10195-0 · Cited by 21
Diversity-oriented synthesis encoded by deoxyoligonucleotides
Hudson, L., Mason, J. W., Westphal, M. V., Richter, M. J. R., Thielman, J. R., Hua, B. K., Gerry, C. J., Xia, G., Osswald, H. L., Knapp, J. M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40575-5 · Cited by 15
Self-citationBinge, D. (1992) · Current Biology · doi:10.1016/0960-9822(92)90028-9 · Cited by 5
Research works printed but not linked: 2
- First International Congress on FK 506. August 21-24, 1991, Pittsburgh, PA (1991). Transplant. Proc. 23, 2709–3380.
- Xie, 2024, KBTBD4 Cancer Hotspot Mutations Drive Neomorphic Degradation of HDAC1/2 Corepressor Complexes, bioRxiv
Cited by
Sorted by citations
Targeted protein degradation for cancer therapy
Hinterndorfer, M., Spiteri, V. A., Ciulli, A., & Winter, G. E. (2025) · Nature reviews. Cancer · doi:10.1038/s41568-025-00817-8 · Cited by 263
“By binding the first protein, they modify its surface or conformation to enhance its binding affinity to the other protein 45,59 .”
Mining the CRBN target space redefines rules for molecular glue-induced neosubstrate recognition
Petzold, G., Gainza, P., Annunziato, S., Lamberto, I., Trenh, P., McAllister, L. A., DeMarco, B., Schwander, L., Bunker, R. D., Zlotosch, M., et al. (2025) · Science · doi:10.1126/science.adt6736 · Cited by 117
Cracking the EGFR code: Cancer biology, resistance mechanisms, and future therapeutic frontiers
Du, Y.-F., Karatekin, F., Wang, W. K., Hong, W., & Gandhi, T. K. B. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100076 · Cited by 88
Routes to molecular glue degrader discovery
Liu, Y., Bai, J., Li, D., & Cang, Y. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.12.006 · Cited by 51
Lessons learned in linking PROTACs from discovery to the clinic
Pike, A., Lee, E. C. Y., Michaelides, I. N., Schade, M., Sharma, A., Scott, J. S., & Srivastava, A. (2025) · Nature Reviews Chemistry · doi:10.1038/s41570-025-00784-6 · Cited by 54
“CRBN was found to be the molecular target of thalidomide, and subsequently, the molecular glue degrader mechanism-of-action 113,114 of thalidomide and other immunomodulatory imide drugs (IMiDs) (such as thalidomide, lenalidomide and pomalidomide) was elucidated 115,116 .”
Metadata
- Authors
- Schreiber, S. L.
- Affiliations
- Broad Institute (US)
- Corresponding author
- Schreiber, Stuart L.
- ORCID
- Schreiber, Stuart L.
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2024-06
- Volume
- 31
- Issue
- 6
- Pages
- 1050-1063
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- OpenAlex
- W4399491693
- Semantic Scholar
- bdf154bc8ee372bd5acec4d6a1562bb429223611
- Cited by
- 112
- References
- 76
- Citations by year
- 2026: 41 · 2025: 62 · 2024: 9
- FWCI
- 4.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell chemical biology (publishedVersion, cc-by-nc-nd)
- ChemRxiv (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences
- National Cancer Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Keywords
- molecular glues, bifunctional molecules, induced proximity, protein-protein interaction, fusion protein, missense mutations, post-translational modification, drug screening
- MeSH terms
- Humans, Protein Processing, Post-Translational, Proteins, Mutation, Missense
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