The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Controlling Signal Transduction with Synthetic Ligands
Abstract
Dimerization and oligomerization are general biological control mechanisms contributing to the activation of cell membrane receptors, transcription factors, vesicle fusion proteins, and other classes of intra- and extracellular proteins. Cell permeable, synthetic ligands were devised that can be used to control the intracellular oligomerization of specific proteins. To demonstrate their utility, these ligands were used to induce intracellular oligomerization of cell surface receptors that lacked their transmembrane and extracellular regions but contained intracellular signaling domains. Addition of these ligands to cells in culture resulted in signal transmission and specific target gene activation. Monomeric forms of the ligands blocked the pathway. This method of ligand-regulated activation and termination of signaling pathways has the potential to be applied wherever precise control of a signal transduction pathway is desired.
Overview
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
Cites
Statistics
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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-citationThe mechanism of action of cyclosporin A and FK506
Schreiber, S. L., & Crabtree, G. R. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90111-j · Cited by 2,127
Self-citationChemistry and Biology of the Immunophilins and Their Immunosuppressive Ligands
Schreiber, S. L. (1991) · Science · doi:10.1126/science.1702904 · Cited by 1,494
Self-citation
Cited by
Hunter, T. (2000) · Cell · doi:10.1016/s0092-8674(00)81688-8 · Cited by 2,586
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
Self-citationA mechanistic role for cardiac myocyte apoptosis in heart failure
Wencker, D., Chandra, M., Nguyen, K., Miao, W., Garantziotis, S., Factor, S. M., Shirani, J., Armstrong, R. C., & Kitsis, R. N. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17664 · Cited by 765
Redesigning an FKBP–ligand interface to generate chemical dimerizers with novel specificity
Clackson, T., Yang, W., Rozamus, L. W., Hatada, M., Amara, J. F., Rollins, C. T., Stevenson, L. F., Magari, S. R., Wood, S. A., Courage, N. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10437 · Cited by 558
Gene therapy: trials and tribulations
Somia, N., & Verma, I. M. (2000) · Nature Reviews Genetics · doi:10.1038/35038533 · Cited by 554
Rapid Chemically Induced Changes of PtdIns(4,5)P 2 Gate KCNQ Ion Channels
Suh, B.-C., Inoue, T., Meyer, T., & Hille, B. (2006) · Science · doi:10.1126/science.1131163 · Cited by 505
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
Self-citationDynamics and Memory of Heterochromatin in Living Cells
Hathaway, N. A., Bell, O., Hodges, C., Miller, E. L., Neel, D. S., & Crabtree, G. R. (2012) · Cell · doi:10.1016/j.cell.2012.03.052 · Cited by 446
Self-citationTargeting proteins for degradation.
Schrader, E. K., Harstad, K. G., & Matouschek, A. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.250 · Cited by 287
Sinars, C. R., Cheung-Flynn, J., Rimerman, R. A., Scammell, J. G., Smith, D. F., & Clardy, J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0231020100 · Cited by 254
Maniaci, C., Hughes, S. J., Testa, A., Chen, W., Lamont, D. J., Rocha, S., Alessi, D. R., Romeo, R., & Ciulli, A. (2017) · Nature Communications · doi:10.1038/s41467-017-00954-1 · Cited by 245
FKBP51, a novel T-cell-specific immunophilin capable of calcineurin inhibition
Baughman, G., Wiederrecht, G. J., Campbell, N. F., Martin, M. M., & Bourgeois, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4395 · Cited by 173
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
Targeted protein degradation and the enzymology of degraders
Fisher, S. L., & Phillips, A. J. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.05.004 · Cited by 126
Optogenetic Control of Synaptic Composition and Function
Sinnen, B. L., Bowen, A. B., Forte, J. S., Hiester, B. G., Crosby, K. C., Gibson, E. S., Dell’Acqua, M. L., & Kennedy, M. J. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.037 · Cited by 124
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
Self-citationBifunctional 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
Chemical reprogramming for cell fate manipulation: Methods, applications, and perspectives
Wang, J., Sun, S., & Deng, H. (2023) · Cell Stem Cell · doi:10.1016/j.stem.2023.08.001 · Cited by 91
Shipman, S. L., & Nicoll, R. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217633109 · Cited by 75
Endomembrane PtdIns(3,4,5)P3 activates the PI3K-Akt pathway
Jethwa, N., Chung, G. H. C., Lete, M. G., Alonso, A., Byrne, R. D., Calleja, V., & Larijani, B. (2015) · Journal of Cell Science · doi:10.1242/jcs.172775 · Cited by 68
Proximity and orientation underlie signaling by the non‐receptor tyrosine kinase ZAP70
Graef, I. A., Holsinger, L. J., Diver, S., Schreiber, S. L., & Crabtree, G. R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5618 · Cited by 67
Self-citationBottone, 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
IFITM proteins assist cellular uptake of diverse linked chemotypes
Lou, K., Wassarman, D. R., Yang, T., Paung, Y., Zhang, Z., O’Loughlin, T. A., Moore, M. K., Egan, R. K., Greninger, P., Benes, C. H., et al. (2022) · Science · doi:10.1126/science.abl5829 · Cited by 42
Xia, Y., DiPrimio, N., Keppel, T. R., Vo, B., Fraser, K., Battaile, K. P., Egan, C., Bystroff, C., Lovell, S., Weis, D. D., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja407644b · Cited by 33
Targeted protein modification as a paradigm shift in drug discovery
Amirian, R., Azadi Badrbani, M., Izadi, Z., Samadian, H., Bahrami, G., Sarvari, S., Abdolmaleki, S., Nabavi, S. M., Derakhshankhah, H., & Jaymand, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115765 · Cited by 18
Modulation of Shank3 PDZ Domain Ligand‐Binding Affinity by Dimerization
Iskenderian‐Epps, W. S., & Imperiali, B. (2010) · ChemBioChem · doi:10.1002/cbic.201000246 · Cited by 8
Metadata
- Authors
- Spencer, D. M., Wandless, T. J., Schreiber, S. L., & Crabtree, G. R.
- Venue
- Science
- Published
- 1993-11-12
- Volume
- 262
- Issue
- 5136
- Pages
- 1019-1024
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2029852810
- Cited by
- 843
- References
- 3
- FWCI
- 7.37
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
