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Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites
- Jingjing Huang, P. Willems, J. Messens
- Biology, Environmental ScienceProceedings of the National Academy of Sciences
- 2 October 2019
It is shown that, by replacing Cys181 of recombinant AtMAPK4 by a redox-insensitive serine residue, the kinase activity decreased, indicating the importance of this noncatalytic cysteine for the Kinase mechanism.
Proteome‐Wide Analysis of Cysteine S‐Sulfenylation Using a Benzothiazine‐Based Probe
- L. Fu, Keke Liu, Renan B. Ferreira, K. Carroll, Jing Yang
- Biology, ChemistryCurrent protocols in protein science
- 12 October 2018
This unit describes how a benzothiazine‐based chemoselective probe called BTD and mass spectrometry based chemoproteomics can be used to globally and site‐specifically identify and quantify protein S‐sulfenylation.
A metabolic switch in proteasome inhibitor-resistant multiple myeloma ensures higher mitochondrial metabolism, protein folding and sphingomyelin synthesis
The adaptive changes in MM cell metabolism may provide the basis of resistance to PI, as high glycolytic activity or rewiring glucose metabolism is associated with bortezomib resistance in MM.
Global profiling of distinct cysteine redox forms reveals wide-ranging redox regulation in C. elegans
A comprehensive, quantitative, and site-specific profile of the intrinsic reactivity of the cysteinome in wild-type C. elegans is presented, and redox-sensitive events in translation, growth signaling, and stress response pathways are revealed.
Inhibitors of ERp44, PDIA1, and AGR2 induce disulfide-mediated oligomerization of Death Receptors 4 and 5 and cancer cell death
DDA treatment of breast cancer cells disrupts PDIA1 and ERp44 mixed disulfide bonds with their client proteins, and DDAs are revealed as the first small molecule, active site inhibitors of AGR2 and ER p44, and roles for A GR2 andERp44 in regulating the activity, stability, and localization of DR4 and DR5, and activation of Caspase 8 are demonstrated.
Novel agents that downregulate EGFR, HER2, and HER3 in parallel
The identification of compounds that kill breast cancer cells that overexpress EGFR or HER2 are described and are termed Disulfide Bond Disrupting Agents (DDAs), which may complement existing EGFR-, HER2-, and HER3-targeted agents that function through alternate mechanisms of action and combination regimens with these existing drugs may overcome therapeutic resistance.
Selective and Sequential Aminolysis of Benzotrifuranone: Synergism of Electronic Effects and Ring Strain Gradient.
- M. Baker, Renan B. Ferreira, R. K. Castellano
- ChemistryThe Journal of organic chemistry
- 15 September 2016
The work shows how a combination of electronic effects and ring strain can underpin the design of small molecules capable of stepwise functionalization, of which there are notably few examples.
CUB domain-containing protein 1 and the epidermal growth factor receptor cooperate to induce cell detachment
It is reported that CDCP1 forms ternary protein complexes with Src and EGFR, facilitating Src activation and Src-dependent EGFR transactivation and a class of compounds termed Disulfide bond Disrupting Agents (DDAs) blocksCDCP1/EGFR/Src ternARY complex formation and downstream signaling.
Disulfide bond disrupting agents activate the unfolded protein response in EGFR- and HER2-positive breast tumor cells
It is demonstrated that DDAs activate the Unfolded Protein Response (UPR) and that this plays a role in their ability to kill EGFR+ and HER2+ cancer cells.
Cysteine sulfenylation by CD36 signaling promotes arterial thrombosis in dyslipidemia.
It is found that CD36 signaling generates hydrogen peroxide to oxidize cysteines within platelet proteins, including Src family kinases, and lowers the threshold for platelet activation in dyslipidemia.