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Sci. Signal., 13 December 2011
[DOI: 10.1126/scisignal.2002329]

Supplementary Materials for:

H2S-Induced Sulfhydration of the Phosphatase PTP1B and Its Role in the Endoplasmic Reticulum Stress Response

Navasona Krishnan, Cexiong Fu, Darryl J. Pappin, Nicholas K. Tonks*

*To whom correspondence should be addressed. E-mail: tonks{at}cshl.edu

This PDF file includes:

  • Fig. S1. Time-dependent inactivation of PTP1B by H2O2.
  • Fig. S2. Time-dependent inactivation of PTP1B by NO.
  • Fig. S3. Time-dependent reactivation of PTP1B by TR/TRR.
  • Fig. S4. Time-dependent reactivation of PTP1B by GSH.
  • Fig. S5. Mechanism of PTP labeling by the IAP probe.
  • Fig. S6. Induction of ER stress by tunicamycin.
  • Fig. S7. Decrease in CSE by RNAi.
  • Fig. S8. Changes in components of the UPR after exposure to thapsigargin.
  • Fig. S9. Proposed mechanism for persulfide modification of PTP1B.
  • Table S1. Quantitation of the different redox forms of Cys215 in PTP1B observed after induction of ER stress with tunicamycin.

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Citation: N. Krishnan, C. Fu, D. J. Pappin, N. K. Tonks, H2S-Induced Sulfhydration of the Phosphatase PTP1B and Its Role in the Endoplasmic Reticulum Stress Response. Sci. Signal. 4, ra86 (2011).

© 2011 American Association for the Advancement of Science

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