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Author Correction: Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation

Author

Listed:
  • Benjamin A. Nacev

    (University of Pittsburgh School of Medicine
    University of Pittsburgh School of Medicine
    UPMC Hillman Cancer Center)

  • Yakshi Dabas

    (The Rockefeller University)

  • Matthew R. Paul

    (The Rockefeller University)

  • Christian Pacheco

    (The Rockefeller University)

  • Michelle Mitchener

    (Princeton University)

  • Yekaterina Perez

    (University of Pennsylvania)

  • Yan Fang

    (The Rockefeller University
    Memorial Sloan Kettering Cancer Center)

  • Alexey A. Soshnev

    (The Rockefeller University
    The University of Texas at San Antonio)

  • Douglas Barrows

    (The Rockefeller University)

  • Thomas Carroll

    (The Rockefeller University)

  • Nicholas D. Socci

    (Memorial Sloan Kettering Cancer Center)

  • Samantha C. Jean

    (Memorial Sloan Kettering Cancer Center)

  • Sagarika Tiwari

    (University of Pittsburgh School of Medicine
    UPMC Hillman Cancer Center)

  • Michael J. Gruss

    (University of Pittsburgh School of Medicine
    UPMC Hillman Cancer Center)

  • Sebastien Monette

    (Memorial Sloan Kettering Cancer Center)

  • William D. Tap

    (Memorial Sloan Kettering Cancer Center)

  • Benjamin A. Garcia

    (Washington University School of Medicine)

  • Tom Muir

    (Princeton University)

  • C. David Allis

    (The Rockefeller University)

Abstract

No abstract is available for this item.

Suggested Citation

  • Benjamin A. Nacev & Yakshi Dabas & Matthew R. Paul & Christian Pacheco & Michelle Mitchener & Yekaterina Perez & Yan Fang & Alexey A. Soshnev & Douglas Barrows & Thomas Carroll & Nicholas D. Socci & S, 2024. "Author Correction: Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation," Nature Communications, Nature, vol. 15(1), pages 1-1, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53502-z
    DOI: 10.1038/s41467-024-53502-z
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