Domain Architectures and Characterization of an RNA-binding Protein, TLS

Basic local alignment search tool

Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669 · see citing works

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617 · see citing works

The Protein Data Bank

Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196 · see citing works

NMRPipe: A multidimensional spectral processing system based on UNIX pipes

Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · see citing works

SWISS-MODEL: an automated protein homology-modeling server

Schwede, T. F. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg520 · Cited by 5,592 · see citing works

Estimation of globular protein secondary structure from circular dichroism

Provencher, S. W., & Gloeckner, J. (1981) · Biochemistry · doi:10.1021/bi00504a006 · Cited by 2,167 · see citing works

The 13C Chemical-Shift Index: A simple method for the identification of protein secondary structure using 13C chemical-shift data

Wishart, D. S., & Sykes, B. D. (1994) · Journal of Biomolecular NMR · doi:10.1007/bf00175245 · Cited by 2,144 · see citing works

Gene fusion with an ETS DNA-binding domain caused by chromosome translocation in human tumours

Delattre, O., Zucman, J., Plougastel, B., Desmaze, C., Melot, T., Peter, M., Kovar, H., Joubert, I., de Jong, P., Rouleau, G., et al. (1992) · Nature · doi:10.1038/359162a0 · Cited by 1,907 · see citing works

Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. Thornton

Kelley, L. A., MacCallum, R. M., & Sternberg, M. J. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3741 · Cited by 1,462 · see citing works

[31] PHD: Predicting one-dimensional protein structure by profile-based neural networks

Rost, B. (1996) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(96)66033-9 · Cited by 1,282 · see citing works

Proteomic analysis of NMDA receptor–adhesion protein signaling complexes

Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., & Grant, S. G. N. (2000) · Nature Neuroscience · doi:10.1038/76615 · Cited by 1,194 · see citing works

Sp1- and Krüppel-like transcription factors.

Kaczynski, J., Cook, T. A., & Urrutia, R. A. (2003) · Genome biology · doi:10.1186/gb-2003-4-2-206 · Cited by 976 · see citing works

Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma

Crozat, A., Åman, P., Mandahl, N., & Ron, D. (1993) · Nature · doi:10.1038/363640a0 · Cited by 893 · see citing works

Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm

Piñol-Roma, S., & Dreyfuss, G. (1992) · Nature · doi:10.1038/355730a0 · Cited by 842 · see citing works

A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams

Garrett, D. S., Powers, R., Gronenborn, A. M., & Clore, G. M. (1991) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(91)90341-p · Cited by 682 · see citing works

Recommendations for the presentation of NMR structures of proteins and nucleic acids – IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy

Markley, J. L., Bax, A., Arata, Y., Hilbers, C. W., Kaptein, R., Sykes, B. D., Wright, P. E., & Kurt Wüthrich, A. (1998) · Journal of Biomolecular NMR · doi:10.1023/a:1008290618449 · Cited by 467 · see citing works

Structural basis for recognition of the tra mRNA precursor by the Sex-lethal protein

Handa, N., Nureki, O., Kurimoto, K., Kim, I., Sakamoto, H., Shimura, Y., Muto, Y., & Yokoyama, S. (1999) · Nature · doi:10.1038/19242 · Cited by 372 · see citing works

hTAF(II)68, a novel RNA/ssDNA‐binding protein with homology to the pro‐oncoproteins TLS/FUS and EWS is associated with both TFIID and RNA polymerase II.

Bertolotti, A., Lutz, Y., Heard, D. J., Chambon, P., & Tora, L. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00882.x · Cited by 364 · see citing works

Crystal structure of the spliceosomal U2B″–U2A′ protein complex bound to a fragment of U2 small nuclear RNA

Price, S. R., Evans, P. R., & Nagai, K. (1998) · Nature · doi:10.1038/29234 · Cited by 356 · see citing works

TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling

Zinszner, H., Sok, J., Immanuel, D., Yin, Y., & Ron, D. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.15.1741 · Cited by 350 · see citing works

Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNAPreprint

Ding, J., Hayashi, M. K., Zhang, Y., Manche, L., Krainer, A. R., & Xu, R.-M. (1999) · Genes & Development · doi:10.1101/gad.13.9.1102 · Cited by 322 · see citing works

113Cd NMR spectroscopy of coordination compounds and proteins

Summers, M. F. (1988) · Coordination Chemistry Reviews · doi:10.1016/0010-8545(88)85012-4 · Cited by 295 · see citing works

RNA and RNA Binding Proteins Participate in Early Stages of Cell Spreading through Spreading Initiation Centers

de Hoog, C. L., Foster, L. J., & Mann, M. (2004) · Cell · doi:10.1016/s0092-8674(04)00456-8 · Cited by 262 · see citing works

A novel effector domain from the RNA-binding protein TLS or EWS is required for oncogenic transformation by CHOP.Preprint

Zinszner, H., Albalat, R., & Ron, D. (1994) · Genes & Development · doi:10.1101/gad.8.21.2513 · Cited by 261 · see citing works

EWS, but Not EWS-FLI-1, Is Associated with Both TFIID and RNA Polymerase II: Interactions between Two Members of the TET Family, EWS and hTAF II 68, and Subunits of TFIID and RNA Polymerase II Complexes

Bertolotti, A., Melot, T., Acker, J., Vigneron, M., Delattre, O., & Tora, L. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1489 · Cited by 260 · see citing works

An RNA-binding protein gene, TLS/FUS, is fused to ERG in human myeloid leukemia with t(16;21) chromosomal translocation.

Ichikawa, H., Shimizu, K., Hayashi, Y., & Ohki, M. (1994) · PubMed · Cited by 255 · see citing works

Structural basis for recognition of AU-rich element RNA by the HuD protein.

(2001) · Nature Structural Biology · doi:10.1038/84131 · Cited by 234 · see citing works

Oncoprotein TLS Interacts with Serine-Arginine Proteins Involved in RNA Splicing

Yang, L., Embree, L. J., Tsai, S., & Hickstein, D. D. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27761 · Cited by 224 · see citing works

Epitope Mapping by Label-Free Biomolecular Interaction Analysis

Malmqvist, M. (1996) · Methods · doi:10.1006/meth.1996.0060 · Cited by 223 · see citing works

The structural basis for the interaction between nonsense-mediated mRNA decay factors UPF2 and UPF3

Kadlec, J., Izaurralde, E., & Cusack, S. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb741 · Cited by 205 · see citing works

Identification of an RNA Binding Specificity for the Potential Splicing Factor TLS

Lerga, A., Hallier, M., Delva, L., Orvain, C., Gallais, I., Marie, J., & Moreau-Gachelin, F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008304200 · Cited by 189 · see citing works

A novel mode of RBD-protein recognition in the Y14–Mago complex

Fribourg, S., Gatfield, D., Izaurralde, E., & Conti, E. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb926 · Cited by 170 · see citing works

Recognition of GU‐rich polyadenylation regulatory elements by human CstF‐64 protein

Pérez‐Cañadillas, J. M., & Varani, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg259 · Cited by 163 · see citing works

Structure and Ubiquitin Interactions of the Conserved Zinc Finger Domain of Npl4

Wang, B., Alam, S. L., Meyer, H. H., Payne, M., Stemmler, T. L., Davis, D. R., & Sundquist, W. I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300459200 · Cited by 153 · see citing works

Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein

Alfano, C., Sanfelice, D., Babon, J. J., Kelly, G. P., Jacks, A. J., Curry, S., & Conte, M. R. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb747 · Cited by 141 · see citing works

Structure of the Y14-Magoh Core of the Exon Junction Complex

Lau, C.-K., Diem, M. D., Dreyfuss, G., et al. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00328-2 · Cited by 139 · see citing works

The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS

Hallier, M., Lerga, A., Barnache, S., Tavitian, A., & Moreau-Gachelin, F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.4838 · Cited by 136 · see citing works

The NMR structure of the 38 kDa U1A protein - PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein.

Varani, G., Varani, L., Gunderson, S., Mattaj, I. W., Kay, L. E., & Neuhaus, D. (2000) · Nature Structural Biology · doi:10.1038/74101 · Cited by 135 · see citing works

Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 Å resolution

Shamoo, Y. E., Krueger, U., Rice, L. M., Williams, K. R., & Steitz, T. A. (1997) · Nature Structural Biology · doi:10.1038/nsb0397-215 · Cited by 135 · see citing works

TLS-ERG Leukemia Fusion Protein Inhibits RNA Splicing Mediated by Serine-Arginine Proteins

Yang, L., Embree, L. J., & Hickstein, D. D. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.10.3345-3354.2000 · Cited by 129 · see citing works

Regulation and function of local protein synthesis in neuronal dendrites

Jiang, C., & Schuman, E. M. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02190-4 · Cited by 113 · see citing works

Identification of hnRNP P2 as TLS/FUS using electrospray mass spectrometry.

Calvio, C., Neubauer, G., Mann, M., & Lamond, A. I. (1995) · PubMed Central · Cited by 113 · see citing works

TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors

Powers, C. A., Mathur, M., Raaka, B. M., Ron, D., & Samuels, H. H. (1998) · Molecular Endocrinology · doi:10.1210/mend.12.1.0043 · Cited by 110 · see citing works

Genomic structure of the human RBP56/hTAF68 and FUS/TLS genes

Morohoshi, F., Ootsuka, Y., Arai, K., Ichikawa, H., Mitani, S., Munakata, N., & Ohki, M. (1998) · Gene · doi:10.1016/s0378-1119(98)00463-6 · Cited by 100 · see citing works

Association of SARFH (Sarcoma-Associated RNA-Binding Fly Homolog) with Regions of Chromatin Transcribed by RNA Polymerase II

Immanuel, D., Zinszner, H., & Ron, D. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.8.4562 · Cited by 57 · see citing works

Implications of the zinc‐finger motif found in the DNA‐binding domain of the human XPA protein

Morita, E. H., Ohkubo, T., Kuraoka, I., Shirakawa, M., Tanaka, K., & Morikawa, K. (1996) · Genes to Cells · doi:10.1046/j.1365-2443.1996.d01-252.x · Cited by 42 · see citing works

The Structure of the Zinc Finger Domain from Human Splicing Factor ZNF265 Fold

Plambeck, C. A., Kwan, A. H., Adams, D. J., Westman, B. J., van der Weyden, L., Medcalf, R. L., Morris, B. J., & Mackay, J. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301896200 · Cited by 42 · see citing works

TLS-CHOP and the Role of RNA-Binding Proteins in Oncogenic Transformation

Ron, D. (1997) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-60479-9_8 · Cited by 37 · see citing works

Nuclear Trafficking

Stewart, M. (2003) · Science · doi:10.1126/science.1092863 · Cited by 31 · see citing works

TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration

Lagier-Tourenne, C., Polymenidou, M., & Cleveland, D. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq137 · Cited by 1,021 · see citing works

The neurogenetics of alternative splicing

Vuong, C. K., Black, D. L., & Zheng, S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.27 · Cited by 340 · see citing works

Widespread binding of FUS along nascent RNA regulates alternative splicing in the brain

Rogelj, B., Easton, L. E., Bogu, G. K., Stanton, L. W., Rot, G., Curk, T., Zupan, B., Sugimoto, Y., Modic, M., Haberman, N., et al. (2012) · Scientific Reports · doi:10.1038/srep00603 · Cited by 278 · see citing works

Identification and characterization of FUS/TLS as a new target of ATM

Gardiner, M., Toth, R., Vandermoere, F., Morrice, N. A., & Rouse, J. (2008) · Biochemical Journal · doi:10.1042/bj20081135 · Cited by 111 · see citing works

The LIM/double zinc-finger motif functions as a protein dimerization domain.

Feuerstein, R., Wang, X., Song, D., Cooke, N. E., & Liebhaber, S. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10655 · Cited by 192 · see citing works

Structure and Function of Zinc Finger Proteins in Eucaryon

Li, X. (2009) · Zhongguo shengwu huaxue yu fenzi shengwu xuebao · Cited by 2 · see citing works

Structural view on the role of WT1’s zinc finger 1 in DNA bindingPreprint

Yengo, R. K., Nurmemmedov, E., & Thunnissen, M. M. G. M. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/284489 · Cited by 1 · see citing works

Zinc‐finger Genes

Gell, D. A., Crossley, M., & Mackay, J. P. (2005) · Encyclopedia of Life Sciences · doi:10.1038/npg.els.0005047

The solution structure of the first zinc finger domain of SWI5: a novel structural extension to a common fold

Dutnall, R. N., Neuhaus, D., & Rhodes, D. (1996) · Structure · doi:10.1016/s0969-2126(96)00064-0 · Cited by 38 · see citing works