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Johnson CN, Xu X, Holloway SP, et al. The . Biomol NMR Assign. 2022;doi: 10.1007/s12104-021-10061-4.
Johnson, C. N., Xu, X., Holloway, S. P., & Libich, D. S. (2022). The . Biomolecular NMR assignments, . https://doi.org/10.1007/s12104-021-10061-4
Johnson, Courtney N, et al. "The ." Biomolecular NMR assignments vol. (2022). doi: https://doi.org/10.1007/s12104-021-10061-4
Johnson CN, Xu X, Holloway SP, Libich DS. The . Biomol NMR Assign. 2022 Jan 07; doi: 10.1007/s12104-021-10061-4. Epub 2022 Jan 07. PMID: 34994941.
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Biomol NMR Assign. 2022 Jan 07; doi: 10.1007/s12104-021-10061-4. Epub 2022 Jan 07.

The .

Biomolecular NMR assignments

Courtney N Johnson, Xiaoping Xu, Stephen P Holloway, David S Libich

Affiliations

  1. Department of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, 8403 Floyd Curl Dr., San Antonio, TX, 78229, USA.
  2. Greehey Children's Cancer Research Institute, The University of Texas Health Science Center at San Antonio, 8403 Floyd Curl Dr., San Antonio, TX, 78229, USA.
  3. Department of Biochemistry and Structural Biology, The University of Texas Health Science Center at San Antonio, 8403 Floyd Curl Dr., San Antonio, TX, 78229, USA. [email protected].
  4. Greehey Children's Cancer Research Institute, The University of Texas Health Science Center at San Antonio, 8403 Floyd Curl Dr., San Antonio, TX, 78229, USA. [email protected].

PMID: 34994941 DOI: 10.1007/s12104-021-10061-4

Abstract

The RNA-binding protein EWS is a multifunctional protein with roles in the regulation of transcription and RNA splicing. It is one of the FET (FUS, EWS and TAF15) family of RNA binding proteins that contain an intrinsically disordered, low-complexity N-terminal domain. The FET family proteins are prone to chromosomal translocations, often fusing their low-complexity domain with a transcription factor derived DNA-binding domain, that are oncogenic drivers in several leukemias and sarcomas. The fusion protein disrupts the normal function of cells through non-canonical DNA binding and alteration of normal transcriptional programs. However, the exact mechanism for how the intrinsically disordered domain contributes to aberrant DNA binding and abnormal transcription is unknown. The purification and

© 2022. The Author(s), under exclusive licence to Springer Nature B.V.

Keywords: EWS-FLI1; Ewing sarcoma; Intrinsically disordered protein; NMR; Oncogenic fusion

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