The Rozovsky Lab Primer to Redox Biology

New to redox biology? Here are the Rozovsky group’s members suggestions or the most helpful papers to read.

Those disulfide bonds! 

A helpful review by my colleagues Colin Thorpe and Debbie Fass

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins

DOI: 10.1021/acs.chemrev.7b00123

Thiols and Redox Biology

Jensen, Kristine Steen, Rosa E. Hansen, and Jakob R. Winther. “Kinetic and thermodynamic aspects of cellular thiol–disulfide redox regulation.” Antioxidants & redox signaling 11.5 (2009): 1047-1058.

Selenoproteins, selenium and sulfur chemistry

1. Hatfield D L, Tsuji P A, Carlson B A, et al. Selenium and selenocysteine: roles in cancer, health, and development. Trends in biochemical sciences, 2014, 39(3): 112-120.

This review article describes all 25 human selenoproteins and their possible biological functions.

2. Labunskyy, V. M.; Hatfield, D. L.; Gladyshev, V. N. Selenoproteins: molecular pathways and physiological roles. Physiol. Rev. 2014, 94, 739-777.

A review that goes in depth into selenocysteine (Sec) insertion into proteins and the subsequent physiological roles of these selenoproteins. A general introduction to selenoproteins, which is of course helpful.

3. Arnér, Elias SJ. “Selenoproteins – What unique properties can arise with selenocysteine in place of cysteine?.” Experimental cell research 316.8 (2010): 1296-1303.

This review lists the differences between Sec and Cys and explains why Sec is more reactive.

4.  Liu, Jun, and Sharon Rozovsky. “Membrane-bound selenoproteins.” Antioxidants & redox signaling 23.10 (2015): 795-813.

This review by our group focuses on membrane-bound selenoproteins, including SELENOK and SELENOS, both of which are being studied in our group.

5. Hondal, R. J.; Marino, S. M.; Gladyshev, V. N. Selenocysteine in thiol/disulfide-like exchange reactions. Antioxid. Redox Signal. 2013, 18, 1675-1689. This paper compares cysteine and selenocysteine along with functional roles played by selenocysteine in selected enzymes. It is a good read to help further understand the functional roles of selenocysteine and why it might be chosen over cysteine in a particular enzyme.

6. Reich, H. J.; Hondal, R. J., Why Nature Chose Selenium. ACS Chem Biol 2016,11(4), 821

easy to read and very thorough review of sulfur and selenium properties

 A primer about the ER-associated degradation pathway (ERAD): p97, derlin and SELENOS

1. p97 activity – a review by Bondar and Rapoport 2017

Toward an understanding of the Cdc48/p97 ATPase    2017 Aug 3;6:1318. doi: 10.12688/f1000research.11683.1. eCollection 2017

2. A primer on the ubiquitin-proteasome by Raymond Deshaies. 

3. The structural basis of SELENOS – p97 interactions

Structural basis for nucleotide-modulated p97 association with the ER membrane.

Cell Discovery (2017) 3, 17045


The crystal structure of SELENOS fragment bound to p97