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

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

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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×

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

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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

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 signature motif in transcriptional co-activators mediates binding to nuclear receptors

Heery, D. M., Kalkhoven, E., Hoare, S., & Parker, M. G. (1997) · Nature · doi:10.1038/42750 · Cited by 2,128

A transcriptional co-repressor that interacts with nuclear hormone receptors

Chen, J. D., & Evans, R. M. (1995) · Nature · doi:10.1038/377454a0 · Cited by 1,794

Phthalimide conjugation as a strategy for in vivo target protein degradation

Winter, G. E., Buckley, D. L., Paulk, J., Roberts, J. M., Souza, A., Dhe-Paganon, S., & Bradner, J. E. (2015) · Science · doi:10.1126/science.aab1433 · Cited by 1,760

Targeted Degradation of CTCF Decouples Local Insulation of Chromosome Domains from Genomic Compartmentalization

Nora, E. P., Goloborodko, A., Valton, A.-L., Gibcus, J. H., Uebersohn, A., Abdennur, N., Dekker, J., Mirny, L. A., & Bruneau, B. G. (2017) · Cell · doi:10.1016/j.cell.2017.05.004 · Cited by 1,709 · cited 2×

Mechanism of auxin perception by the TIR1 ubiquitin ligase

Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688

An auxin-based degron system for the rapid depletion of proteins in nonplant cells

Nishimura, K., Fukagawa, T., Takisawa, H., Kakimoto, T., & Kanemaki, M. (2009) · Nature Methods · doi:10.1038/nmeth.1401 · Cited by 1,663

Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation

Clipstone, N. A., & Crabtree, G. R. (1992) · Nature · doi:10.1038/357695a0 · Cited by 1,635

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

Catalytic in vivo protein knockdown by small-molecule PROTACs

Bondeson, D. P., Mares, A., Smith, I. E. D., Ko, E., Campos, S., Miah, A. H., Mulholland, K. E., Routly, N., Buckley, D. L., Gustafson, J. L., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1858 · Cited by 1,356

Structure of the DDB1–CRBN E3 ubiquitin ligase in complex with thalidomide

Fischer, E. S., Böhm, K., Lydeard, J. R., Yang, H., Stadler, M. B., Cavadini, S., Nagel, J., Serluca, F., Acker, V., Lingaraju, G. M., et al. (2014) · Nature · doi:10.1038/nature13527 · Cited by 1,141

Hijacking the E3 Ubiquitin Ligase Cereblon to Efficiently Target BRD4

Lu, J., Qian, Y., Altieri, M., Dong, H., Wang, J., Raina, K., Hines, J., Winkler, J. D., Crew, A. P., Coleman, K., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.009 · Cited by 1,140

A Rapid, Reversible, and Tunable Method to Regulate Protein Function in Living Cells Using Synthetic Small Molecules

Banaszynski, L. A., Chen, L.-C., Maynard-Smith, L. A., Ooi, A. G. L., & Wandless, T. J. (2006) · Cell · doi:10.1016/j.cell.2006.07.025 · Cited by 902

ChromEMT: Visualizing 3D chromatin structure and compaction in interphase and mitotic cells

Ou, H. D., Phan, S., Deerinck, T. J., Thor, A., Ellisman, M. H., & O’Shea, C. C. (2017) · Science · doi:10.1126/science.aag0025 · Cited by 887

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

A split-Cas9 architecture for inducible genome editing and transcription modulation

Zetsche, B., Volz, S. E., & Zhang, F. (2015) · Nature Biotechnology · doi:10.1038/nbt.3149 · Cited by 722

Rapid protein depletion in human cells by auxin-inducible degron tagging with short homology donors

Natsume, T., Kiyomitsu, T., Saga, Y., & Kanemaki, M. T. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.001 · Cited by 673

Modular PROTAC design for the degradation of oncogenic BCR-ABL

Lai, A. C., Toure, M., Hellerschmied, D., Salami, J., Jaime‐Figueroa, S., Ko, E., Hines, J., & Crews, C. M. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201507634 · Cited by 618

Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation

Luik, R. M., Wang, B., Prakriya, M., Wu, M. M., & Lewis, R. S. (2008) · Nature · doi:10.1038/nature07065 · Cited by 588

The auxin-inducible degradation (AID) system enables versatile conditional protein depletion in C. elegans

Zhang, L., Ward, J. D., Cheng, Z., & Dernburg, A. F. (2015) · Development · doi:10.1242/dev.129635 · Cited by 586

Reversible compartmentalization of de novo purine biosynthetic complexes in living cells

An, S., Kumar, R., Sheets, E. D., & Benkovic, S. J. (2008) · Science · doi:10.1126/science.1152241 · Cited by 585 · cited 1×

Targeting the von Hippel-Lindau E3 ubiquitin ligase using small molecules to disrupt the VHL/HIF-1α interaction

Buckley, D. L., Van Molle, I., Gareiss, P. C., Tae, H. S., Michel, J., Noblin, D. J., Jorgensen, W. L., Ciulli, A., & Crews, C. M. (2012) · Journal of the American Chemical Society · doi:10.1021/ja209924v · Cited by 569

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

The Anchor-Away Technique: Rapid, Conditional Establishment of Yeast Mutant Phenotypes

Haruki, H., Nishikawa, J., & Laemmli, U. K. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.020 · Cited by 547

A humanized system for pharmacologic control of gene expression

Rivera, V. M., Clackson, T., Natesan, S., Pollock, R. M., Amara, J. F., Keenan, T. P., Magari, S. R., Phillips, T., Courage, N. L., Cerasoli, F., et al. (1996) · Nature Medicine · doi:10.1038/nm0996-1028 · Cited by 528

Infusion of donor-derived CD19-redirected virus-specific T cells for B-cell malignancies relapsed after allogeneic stem cell transplant: a phase 1 study

Cruz, C. C., Micklethwaite, K. P., Savoldo, B., Ramos, C. A., Lam, S., Ku, S., Diouf, O., Liu, E., Barrett, A. J., Ito, S., et al. (2013) · Blood · doi:10.1182/blood-2013-06-506741 · Cited by 515

HaloPROTACS: Use of Small Molecule PROTACs to Induce Degradation of HaloTag Fusion Proteins

Buckley, D. L., Raina, K., Darricarrere, N., Hines, J., Gustafson, J. L., Smith, I. E., Miah, A. H., Harling, J. D., & Crews, C. M. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00442 · Cited by 488

A Comprehensive Mathematical Model for Three-Body Binding Equilibria

Douglass, E. F., Miller, C. J., Sparer, G., Shapiro, H., & Spiegel, D. A. (2013) · Journal of the American Chemical Society · doi:10.1021/ja311795d · Cited by 472

Dosage-dependent modifiers of polycomb and antennapedia mutations in Drosophila.

Kennison, J. A., & Tamkun, J. W. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.21.8136 · Cited by 469

Treating B-cell cancer with T cells expressing anti-CD19 chimeric antigen receptors

Kochenderfer, J. N., & Rosenberg, S. A. (2013) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2013.46 · Cited by 460

Dynamics 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

Chronic myeloid leukemia stem cells are not dependent on Bcr-Abl kinase activity for their survival

Hamilton, A., Helgason, G. V., Schemionek, M., Zhang, B., Myssina, S., Allan, E. K., Nicolini, F. E., Müller‐Tidow, C., Bhatia, R., Brunton, V. G., et al. (2011) · Blood · doi:10.1182/blood-2010-12-326843 · Cited by 440

An expanded tool kit for the auxin‐inducible degron system in budding yeast

Morawska, M., & Ulrich, H. D. (2013) · Yeast · doi:10.1002/yea.2967 · Cited by 414

BET bromodomain inhibition targets both c-Myc and IL7R in high-risk acute lymphoblastic leukemia

Ott, C. J., Kopp, N., Bird, L., Paranal, R. M., Qi, J., Bowman, T. V., Rodig, S. J., Kung, A. L., Bradner, J. E., & Weinstock, D. M. (2012) · Blood · doi:10.1182/blood-2012-02-413021 · Cited by 385

Regulation of Protein Secretion Through Controlled Aggregation in the Endoplasmic Reticulum

Rivera, V. M., Wang, X., Wardwell, S., Courage, N. L., Volchuk, A., Keenan, T. P., Holt, D. A., Gilman, M. Z., Orci, L., Cerasoli, F., et al. (2000) · Science · doi:10.1126/science.287.5454.826 · Cited by 338

Complex transcriptional modulation with orthogonal and inducible dCas9 regulators

Gao, Y., Xiong, X., Wong, S. S., Charles, E. J., Lim, W. A., & Qi, L. S. (2016) · Nature Methods · doi:10.1038/nmeth.4042 · Cited by 335

Fat apoptosis through targeted activation of caspase 8: a new mouse model of inducible and reversible lipoatrophy

Pajvani, U. B., Trujillo, M. E., Combs, T. P., Iyengar, P., Jelicks, L., Roth, K. A., Kitsis, R. N., & Scherer, P. E. (2005) · Nature Medicine · doi:10.1038/nm1262 · Cited by 322

Engineering the ABA Plant Stress Pathway for Regulation of Induced Proximity

Liang, F., Ho, W. Q., & Crabtree, G. R. (2011) · Science Signaling · doi:10.1126/scisignal.2001449 · Cited by 314

Transcription control by the ENL YEATS domain in acute leukaemia

Erb, M. A., Scott, T. G., Li, B. E., Xie, H., Paulk, J., Seo, H., Souza, A., Roberts, J. M., Dastjerdi, S., Buckley, D. L., et al. (2017) · Nature · doi:10.1038/nature21688 · Cited by 313

Inducible, reversible system for the rapid and complete degradation of proteins in mammalian cells

Holland, A. J., Fachinetti, D., Han, J. S., & Cleveland, D. W. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216880109 · Cited by 309

Regulated Delivery of Therapeutic Proteins After in Vivo Somatic Cell Gene Transfer

Ye, X., Rivera, V. M., Zoltick, P. W., Cerasoli, F., Schnell, M. A., Gao, G., Hughes, J. V., Gilman, M. Z., & Wilson, J. M. (1999) · Science · doi:10.1126/science.283.5398.88 · Cited by 308

Solution Structure of FKBP, a Rotamase Enzyme and Receptor for FK506 and Rapamycin

Michnick, S. W., Rosen, M. K., Wandless, T. J., Karplus, M., & Schreiber, S. L. (1991) · Science · doi:10.1126/science.1709301 · Cited by 305

Dynamics of BAF–Polycomb complex opposition on heterochromatin in normal and oncogenic states

Kadoch, C., Williams, R. T., Calarco, J. P., Miller, E. L., Weber, C. M., Braun, S. M. G., Pulice, J. L., Chory, E. J., & Crabtree, G. R. (2016) · Nature Genetics · doi:10.1038/ng.3734 · Cited by 305

TOR kinase domains are required for two distinct functions, only one of which is inhibited by rapamycin

Zheng, X.-F., Fiorentino, D. F., Chen, J., Crabtree, G. R., & Schreiber, S. L. (1995) · Cell · doi:10.1016/0092-8674(95)90058-6 · Cited by 300

Evidence that Loading of Cohesin Onto Chromosomes Involves Opening of Its SMC Hinge

Gruber, S., Arumugam, P., Katou, Y., Kuglitsch, D., Helmhart, W., Shirahige, K., & Nasmyth, K. (2006) · Cell · doi:10.1016/j.cell.2006.08.048 · Cited by 286

Manipulation of nuclear architecture through CRISPR-mediated chromosomal looping

Morgan, S. L., Mariano, N. C., Bermudez, A., Arruda, N. L., Wu, F., Luo, Y., Shankar, G., Jia, L., Chen, H., Hu, J.-F., et al. (2017) · Nature Communications · doi:10.1038/ncomms15993 · Cited by 279

Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins.

Belshaw, P. J., Ho, S. N., Crabtree, G. R., & Schreiber, S. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4604 · Cited by 278

Long-term pharmacologically regulated expression of erythropoietin in primates following AAV-mediated gene transfer

Rivera, V. M., Gao, G., Grant, R. L., Schnell, M. A., Zoltick, P. W., Rozamus, L. W., Clackson, T., & Wilson, J. M. (2004) · Blood · doi:10.1182/blood-2004-06-2501 · Cited by 272

Structure of human cyclophilin and its binding site for cyclosporin A determined by X-ray crystallography and NMR spectroscopy

Kallen, J., Spitzfaden, C. E., Zurini, M. G. M., Wider, G., Widmer, H., Kurt Wüthrich, A., & Walkinshaw, M. D. (1991) · Nature · doi:10.1038/353276a0 · Cited by 271

BAF complexes facilitate decatenation of DNA by topoisomerase IIα

Dykhuizen, E. C., Hargreaves, D. C., Miller, E. L., Cui, K., Korshunov, A., Kool, M., Pfister, S. M., Cho, Y., Zhao, K., & Crabtree, G. R. (2013) · Nature · doi:10.1038/nature12146 · Cited by 270

Dimeric ligands define a role for transcriptional activation domains in reinitiation

Ho, S. N., Biggar, S. R., Spencer, D. M., Schreiber, S. L., & Crabtree, G. R. (1996) · Nature · doi:10.1038/382822a0 · Cited by 261

Inducible Caspase-9 Selectively Modulates the Toxicities of CD19-Specific Chimeric Antigen Receptor-Modified T Cells

Diaconu, I., Ballard, B. C., Zhang, M., Chen, Y., West, J., Dotti, G., & Savoldo, B. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.01.011 · Cited by 257

Oligomerization activates c-Raf-1 through a Ras-dependent mechanism

Luo, Z., Tzivion, G., Belshaw, P. J., Vavvas, D. G., Marshall, M. S., & Avruch, J. (1996) · Nature · doi:10.1038/383181a0 · Cited by 238

Rapid and orthogonal logic gating with a gibberellin-induced dimerization system

Miyamoto, T., DeRose, R., Suarez, A., Ueno, T., Chen, M., Sun, T.-P., Wolfgang, M. J., Mukherjee, C., Meyers, D. J., & Inoue, T. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.922 · Cited by 230

Inducible caspase-9 suicide gene controls adverse effects from alloreplete T cells after haploidentical stem cell transplantation

Zhou, X., Dotti, G., Krance, R. A., Martinez, C. A., Naik, S., Kamble, R. T., Durett, A. G., Dakhova, O., Savoldo, B., Stasi, A. D., et al. (2015) · Blood · doi:10.1182/blood-2015-02-628354 · Cited by 216

Smarca4 ATPase mutations disrupt direct eviction of PRC1 from chromatin

Stanton, B. Z., Hodges, H. C., Calarco, J. P., Braun, S. M. G., Ku, W. L., Kadoch, C., Zhao, K., & Crabtree, G. R. (2016) · Nature Genetics · doi:10.1038/ng.3735 · Cited by 215

Rapamycin Analogs with Differential Binding Specificity Permit Orthogonal Control of Protein Activity

Bayle, J. H., Grimley, J. S., Stankunas, K., Gestwicki, J. E., Wandless, T. J., & Crabtree, G. R. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.10.017 · Cited by 211

Localized light-induced protein dimerization in living cells using a photocaged dimerizer

Ballister, E. R., Aonbangkhen, C., Mayo, A. M., Lampson, M. A., & Chenoweth, D. M. (2014) · Nature Communications · doi:10.1038/ncomms6475 · Cited by 209

Plk4 haploinsufficiency causes mitotic infidelity and carcinogenesis

Ko, M. A., Rosario, C. O., Hudson, J. W., Kulkarni, S., Pollett, A. F., Dennis, J. W., & Swallow, C. J. (2005) · Nature Genetics · doi:10.1038/ng1605 · Cited by 206

AG10 inhibits amyloidogenesis and cellular toxicity of the familial amyloid cardiomyopathy-associated V122I transthyretin

Penchala, S., Connelly, S., Wang, Y., Park, M. S., Zhao, L., Baranczak, A., Rappley, I., Vogel, H. S., Liedtke, M., Witteles, R. M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300761110 · Cited by 203

Cell signaling can direct either binary or graded transcriptional responses

Biggar, S. R., & Crabtree, G. R. (2001) · The EMBO Journal · doi:10.1093/emboj/20.12.3167 · Cited by 201

Harnessing Chaperones to Generate Small-Molecule Inhibitors of Amyloid ß Aggregation

Gestwicki, J. E., Crabtree, G. R., & Graef, I. A. (2004) · Science · doi:10.1126/science.1101262 · Cited by 200

Synthetic activation of caspases: Artificial death switches

MacCorkle, R. A., Freeman, K. W., & Spencer, D. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3655 · Cited by 187

Long-term outcome after haploidentical stem cell transplant and infusion of T cells expressing the inducible caspase 9 safety transgene

Zhou, X., Stasi, A. D., Tey, S., Krance, R. A., Martinez, C. A., Leung, K. S., Durett, A. G., Wu, M.-F., Liu, H., Leen, A. M., et al. (2014) · Blood · doi:10.1182/blood-2014-01-551671 · Cited by 180

Conditional Protein Splicing: A New Tool to Control Protein Structure and Function in Vitro and in Vivo

Mootz, H. D., Blum, E. S., Tyszkiewicz, A. B., & Muir, T. W. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0362813 · Cited by 170

Rapid and reversible epigenome editing by endogenous chromatin regulators

Braun, S. M. G., Kirkland, J. G., Chory, E. J., Husmann, D., Calarco, J. P., & Crabtree, G. R. (2017) · Nature Communications · doi:10.1038/s41467-017-00644-y · Cited by 166

p53 protects against genome instability following centriole duplication failure

Lambrus, B. G., Uetake, Y., Clutario, K. M., Daggubati, V., Snyder, M., Sluder, G., & Holland, A. J. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502089 · Cited by 147

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

Signal transduction in T lymphocytes using a conditional allele of Sos.

Holsinger, L. J., Spencer, D. M., Austin, D. J., Schreiber, S. L., & Crabtree, G. R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9810 · Cited by 135

Selective Protein−Protein Interactions Direct Channeling of Intermediates between Polyketide Synthase Modules

Tsuji, S. Y., Cane, D. E., & Khosla, C. (2001) · Biochemistry · doi:10.1021/bi002463n · Cited by 129

Conditional Protein Alleles Using Knockin Mice and a Chemical Inducer of Dimerization

Stankunas, K., Bayle, J. H., Gestwicki, J. E., Lin, Y., Wandless, T. J., & Crabtree, G. R. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00491-x · Cited by 129

The Cyc8–Tup1 complex inhibits transcription primarily by masking the activation domain of the recruiting proteinPreprint

Wong, K. H., & Struhl, K. (2011) · Genes & Development · doi:10.1101/gad.179275.111 · Cited by 129

Chemical rescue of cleft palate and midline defects in conditional GSK-3β mice

Liu, K. J., Arron, J. R., Stankunas, K., Crabtree, G. R., & Longaker, M. T. (2007) · Nature · doi:10.1038/nature05557 · Cited by 127

Improved Artificial Death Switches Based on Caspases and FADD

Fan, L.-W., Freeman, K. W., Khan, T. M., Pham, E., & Spencer, D. M. (1999) · Human Gene Therapy · doi:10.1089/10430349950016924 · Cited by 108

Rapid targeting of nuclear proteins to the cytoplasm

Klemm, J. D., Beals, C. R., & Crabtree, G. R. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00290-9 · Cited by 107

Rapid and Reversible Chemical Inactivation of Synaptic Transmission in Genetically Targeted Neurons

Karpova, A. Y., Tervo, D. G. R., Gray, N. W., & Svoboda, K. (2005) · Neuron · doi:10.1016/j.neuron.2005.11.015 · Cited by 100

Condensin aids sister chromatid decatenation by topoisomerase II

Charbin, A., Bouchoux, C., & Uhlmann, F. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt882 · Cited by 93

Golgi Membranes Remain Segregated from the Endoplasmic Reticulum during Mitosis in Mammalian Cells

Pecot, M., & Malhotra, V. (2004) · Cell · doi:10.1016/s0092-8674(03)01068-7 · Cited by 92

Controlling programmed cell death with a cyclophilincyclosporin-based chemical inducer of dimerization

Belshawl, P. J., Spencer, D. M., Crabtree, G. R., & Schreiber, S. L. (1996) · Chemistry & Biology · doi:10.1016/s1074-5521(96)90249-5 · Cited by 89

TOP2 synergizes with BAF chromatin remodeling for both resolution and formation of facultative heterochromatin

Miller, E. L., Hargreaves, D. C., Kadoch, C., Chang, C.-Y., Calarco, J. P., Hodges, H. C., Buenrostro, J. D., Cui, K., Greenleaf, W. J., Zhao, K., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3384 · Cited by 89

Auxin-inducible protein depletion system in fission yeast

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Nucleosome depletion at yeast terminators is not intrinsic and can occur by a transcriptional mechanism linked to 3’-end formation

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