Asset Details

  • Description:
  • Methylation sites on RSF1 sequence and model of the RRM domain. (A) Peptidic sequence of S. frugiperda RSF1. The folded part corresponding to the RRM domain is shown in blue. Mono‐ (˙) and dimethylated (˙˙) arginines are in bold. Consensus sequence SxGGxRxY is boxed. (B) 3D‐Model of RSF1 RRM domain generated by Swiss‐Model . The side chains of the methylated arginine residues are shown in stick.
  • License:
  • Rights Managed
  • Rights Holder:
  • John Wiley & Sons, Inc.
  • License Rights Holder:
  • Copyright © 2017 Federation of European Biochemical Societies
  • Asset Type:
  • Image
  • Asset Subtype:
  • Figure
  • Image Orientation:
  • Portrait
  • Image Dimensions:
  • 1089 x 1263
  • Image File Size:
  • 532 KB
  • Creator:
  • Vincent Cura, Nils Marechal, Nathalie Troffer‐Charlier, Jean‐Marc Strub, Matthijs J. Haren, Nathaniel I. Martin, Sarah Cianférani, Luc Bonnefond, Jean Cavarelli
  • Credit:
  • Cura, V., Marechal, N., Troffer‐Charlier, N., Strub, J.-M., Haren, M. J., Martin, N. I., Cianférani, S., Bonnefond, L., & Cavarelli, J. (2017). Structural studies of protein arginine methyltransferase 2 reveal its interactions with potential substrates and inhibitors. The FEBS Journal, 284(1), 77-96..
  • Collection:
  • Keywords:
  • Restrictions:
  • Property Release:
  • No
  • Model Release:
  • No
  • Purchasable:
  • Yes
  • Sensitive Materials:
  • No
  • Article Authors:
  • Vincent Cura, Nils Marechal, Nathalie Troffer‐Charlier, Jean‐Marc Strub, Matthijs J. Haren, Nathaniel I. Martin, Sarah Cianférani, Luc Bonnefond, Jean Cavarelli
  • Article Copyright Year:
  • 2017
  • Publication Volume:
  • 284
  • Publication Issue:
  • 1
  • Publication Date:
  • 01/01/2017
  • DOI:

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