1. Chen X, Zhang J, Liu P, Wei Y, Wang XE, Xiao J,Wang CC, Wang L* (2021) Proteolytic regulation of secretory pathway kinase Fam20C by site-1 protease.Proc Natl Acad Sci U S A,118: e2100133118.

2. Wang L*, Yu J,Wang CC(2021) Protein disulfide isomerase is regulated in multiple ways: Consequences for conformation, activities and pathophysiological functions.BioEssays,Nov 6;e2000147. doi: 10.1002/bies.202000147. (invited review)

3. Yu J, Li T, Liu Y, Wang X, Zhang J, Wang Xe, Shi G, Lou J, Wang L,Wang CC, Wang L* (2020) Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress.EMBO J, e103841

(Highlighted byEMBO J'News & Views'; Recommended by F1000Prime)

4. Zhang Y, Li T, Zhang L, Shangguan F, Shi G, Wu X, Cui Y, Wang Xe, Wang X, Liu Y, Lu B, Wei T,Wang CC, Wang L*. (2019) Targeting the functional interplay between endoplasmic reticulum oxidoreductin-1α and protein disulfide isomerase suppresses the progression of cervical cancer.EBioMedicine, 41:408-419.

5. Wu X, Zhang L, Miao Y, Yang J, Wang X,Wang CC, Feng J*, Wang L*. (2019) Homocysteine causes vascular endothelial dysfunction by disrupting endoplasmic reticulum redox homeostasis.Redox Biol., 20:46-59.

6. Zhang J, Zhu Q, Wang X, Yu J, Chen X, Wang J, Wang X, Xiao J,Wang CC, Wang L*. (2018) Secretory kinase Fam20C tunes endoplasmic reticulum redox via phosphorylation of Serine145 of Ero1α.EMBO J., e98699.

7. Fang J, Yang J, Wu X, Zhang G, Li T, Wang X, Zhang H,Wang CC, Liu GH*, Wang L*.(2018) Metformin alleviates human cellular aging by upregulating the endoplasmic reticulum glutathione peroxidase 7.Aging Cell, e12765.

8. Li H, Yang K, Wang W, Niu Y, Li J, Dong Y, Liu Y,Wang CC,Wang L*, Liang H* (2018) Crystal and solution structures of human protein disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity.J. Biol. Chem.,293, 1192-1202.

9. Yang K, Li D, Wang XE, Liang J, Sitia R,Wang CC*, Wang X*. (2016) Crystal structure of the ERp44-peroxiredoxin 4 complex reveals the molecular mechanisms of thiol-mediated protein retention.Structure, 24:1755-1765.

10. Niu Y, Zhang L, Yu J,Wang CC*,Wang L*. (2016) Novel roles of the non-catalytic elements of yeast protein-disulfide isomerase in its interplay with endoplasmic reticulum oxidoreductin 1.J. Biol. Chem.,291(15):8283-94.

11. Wang L, Wang X,Wang CC*.(2015) Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone.Free Radic. Biol. Med.,83:305-13.(invited review)

12. Zhang L, Niu Y, Zhu L, Fang J, Wang XE, Wang L*,Wang CC*.(2014) Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).J. Biol. Chem.,289(45):31188-31199.

13. Wang L*, Zhang L, Niu Y, Sitia R,Wang CC*.(2014) Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding.Antioxid. Redox Signal.,20(4):545-56.　

14. Wang C, Li W, Ren J, Fang J, Ke H, Gong W, Feng W*,Wang CC*.(2013) Structural insights into the redox-regulated dynamic conformations of human protein disulfide isomerase.Antioxid. Redox Signal.,19(1): 36-45.

15. Wang C, Yu J, Huo L, Wang L, Feng W*,Wang CC*.(2012) Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a’.J. Biol. Chem.,287, 1139–1149.

16. Wang X, Wang L, Wang X, Sun F*,Wang CC*.(2012) Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.Biochem. J.,441(1): 113-118.

17. Wang L, Zhu L,Wang CC*.(2011) The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation.Biochem. J.,434, 113–121.

18. Wang C, Chen S, Wang X, Wang L, Wallis AK, Freedman RB*,Wang CC*.(2010) Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance.J. Biol. Chem.,285(35): 26788-26797.

19. Wang L, Li SJ, Sidhu A, Zhu L, Liang Y, Freedman RB,Wang CC*.(2009) Reconstitution of human Ero1-Lα/protein disulfide isomerase oxidative folding pathway in vitro: position-dependent differences in role between the a and a’domains of protein disulfide isomerase.J. Biol. Chem.,284(1): 199–206.

20. Wang L, Wang L, Vavassori S, Li S, Ke H, Anelli T, Degano M, Ronzoni R, Sitia R, Sun F*,Wang CC*.(2008) Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail.EMBO Rep.,9(7): 642–647.

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