Jena K.K., Qu P., Baracco L., Saghaei S., Keerti F., Allahyari Z., Boehmer D., Mitchell M., Dillen C.A., Li H.-Y., Liu E., Poli V., Dufies O., van Konijnenburg D.P.H., Spreafico R., Bi C., Hall R., Kruppa M.D., Ma Z., Gravitte A., Lowman D.W., Ensley H.E., Marty P., Boyer L., Collomp R., Williams D.L., Ma V. P.-Y, Lee P.Y., Nigrovic P.A., Karp J.M., Elledge S.J., Wesemann D.R., Wu Y.*, Frieman M., Zanoni I.* (2026) A glycan-based adjuvant expands the breadth and duration of protection of mRNA-based vaccines. Nature Immunology, in press. (IF 27.6)

Fu Y., Hua Y.-X., Zhang Y.-L., Zhang C.-Y., Li H.-Y., Melnikov I, Gabbasov Z. A., Wu Y.*, Liu E.-Q.*, Ji S.-R.* (2026) C-reactive protein exacerbates high-fat diet-induced atherosclerosis via a liver-to-vessel axis that determines therapeutic efficacy of atorvastatin. Atherosclerosis, 412: 120594. (IF 5.7)

Feng J.-R., Li X., Han C., Chang Y., Fu Y., Feng G.-C., Lei Y., Li H.-Y., Tang P.M.K., Ji S.-R.*, Hou Y.*, Wu Y.* (2024) C-Reactive protein induces immunosuppression by activating FcγR2B in pulmonary macrophages to promote lung metastasis. Cancer Research, 84(24): 4184-4198. (IF 16.6) (Featured article; Commentary: https://aacrjournals.org/cancerres/article-abstract/84/24/4121/750405/C-Reactive-Protein-Facilitates-Premetastatic-Niche?redirectedFrom=fulltext)

Ji S.-R.*, Zhang S.-H., Chang Y., Li H.-Y., Wang M.-Y., Lv J.-M., Zhu L., Tang P.M.K., Wu Y.* (2023) C-reactive protein: the most familiar stranger. Journal of Immunology, 210(6): 699-707. (IF 3.4) (Invited review)

Zhou L, Chen S.-J., Chang Y., Liu S.-H., Zhou Y.-F., Huang X.-P., Hua Y.-X., An H., Zhang S.-H., Melnikov I., Gabbasov Z.A., Wu Y.*, Ji S.-R.* (2023) Monomeric C-reactive protein evokes TCR signaling-dependent bystander activation of CD4+ T cells. Molecular Immunology, 157(5): 158-166. (IF 3.0)

Wang M.-Y., Zhang C.-M., Zhou H.-H., Ge Z.-B., Su C.-C., Lou Z.-H., Zhang X.-Y., Xu T.-T., Li S.-Y., Zhu L., Zhou Y.-L., Wu Y.*, Ji S.-R.* (2022) Identification of a distal enhancer that determines the expression pattern of acute phase marker C-reactive protein. Journal of Biological Chemistry, 298(8): 102160. (IF 3.9) (Editor's Pick)

Cheng B., Lv J.-M., Liang Y.-L., Zhu L., Huang X.-P., Li H.-Y., Potempa L.A., Ji S.-R.*, Wu Y.* (2022) Secretory quality control constrains functional selection-associated protein structure innovation. Communications Biology, 5: 268. (IF 5.1)

Li H.-Y., Tang Z.-M., Wang Z., Lv J.-M., Liu X.-L., Liang Y.-L., Cheng B., Gao N., Ji S.-R.*, Wu Y.* (2022) C-reactive protein protects against acetaminophen-induced liver injury by preventing complement overactivation. Cellular and Molecular Gastroenterology and Hepatology, 13(1): 289-307. (IF 7.4) (Featured article;  Commentary: https://www.sciencedirect.com/science/article/pii/S2352345X21002186)

Wang M.-Y., Zhou H.-H., Zhang C.-M., Su H.-X., Li S.-L., Ji S.-R.*, Wu Y.* (2020) A functional genetic variant at C-reactive protein promoter (rs3091244) is not associated with cancer risk in a Chinese population. Frontiers in Immunology, 11: 926. (IF 5.9)

Liu Y., Yuan B., Peng L., Zhao J., Zhou Y., Xiang S., Zhu L.*, Wu Y.* (2020) Single-particle analysis of urea amidolyase reveals its molecular mechanism. Protein Science, 29(5): 1242-1249. (IF 5.2)

Zhang S.-C., Wang M.-Y., Feng J.-R., Chang Y., Ji S.-R.*, Wu Y.* (2020) Reversible promoter methylation determines fluctuating expression of acute phase proteins. eLife, 9: e51317. (IF 7.7)

Li H.-Y., Liu X.-L., Liu Y.-T., Jia Z.-K., Filep J.G., Potempa L.A., Ji S.-R.*, Wu Y.* (2019) Matrix sieving-enforced retrograde transcytosis regulates tissue accumulation of C-reactive protein. Cardiovascular Research, 115(2): 440-452. (IF 13.3)

Zhang L., Li H.-Y., Li W., Shen Z.-Y., Wang Y.-D., Ji S.-R.*, Wu Y.* (2018) An ELISA assay for quantifying monomeric C-reactive protein in plasma. Frontiers in Immunology, 9: 511. (IF 5.9)

Jia Z.-K., Li H.-Y., Liang Y.-L., Potempa L.A., Ji S.-R.*, Wu Y.* (2018) Monomeric C-reactive protein binds and neutralizes receptor activator of NF-κB ligand-induced osteoclast differentiation. Frontiers in Immunology, 9: 234. (IF 5.9)

Lv J.-M., Lv S.-Q., Liu Z.-P., Zhang J., Gao B.-X., Yao Z.-Y., Wu Y.-X., Potempa L.A., Ji S.-R.*, Long M.*, Wu Y.* (2018) Conformational folding and disulfide bonding drive distinct stages of protein structure formation. Scientific Reports, 8: 1494. (IF 3.9)

Li Q.-Y., Li H.-Y., Fu G., Yu F.*, Wu Y.*, Zhao M.-H. (2017) Autoantibodies against C-reactive protein influence complement activation and clinical course in lupus nephritis. Journal of the American Society of Nephrology, 28(10): 3044-3054. (IF 9.4)

Li H.-Y., Wang J., Meng F., Jia Z.-K., Su Y., Bai Q.-F., Lv L.-L., Ma F.-R., Potempa L.A., Ji S.-R.*, Wu Y.* (2016) An intrinsically disordered motif mediates diverse actions of monomeric C-reactive protein. Journal of Biological Chemistry, 291(16): 8795-8804. (IF 3.9)

Zhang L., Liu S.-H., Wright T.T., Shen Z.-Y., Li H.-Y., Zhu W., Potempa L.A., Ji S.-R.*, Szalai A.J.*, Wu Y.* (2015) C-reactive protein directly suppresses T helper 1 cell differentiation and alleviates experimental autoimmune encephalomyelitis. Journal of Immunology, 194(11): 5243-5252. (IF 3.4)

Wang M.-Y., Zhou H.-H., Zhang S.-C., Hui F., Zhu W., Su H.-X., Guo H.-Y., Li X.-W., Ji S.-R.*, Wu Y.* (2014) Recurrent mutations at C-reactive protein gene promoter SNP position -286 in human cancers. Cell Research, 24(4): 505-508. (IF 25.9)

Li H.-Y., Wang J., Wu Y.-X., Zhang L., Liu Z.-P., Filep J.G., Potempa L.A., Wu Y.*, Ji S.-R.* (2014) Topological localization of monomeric C-reactive protein determines pro-inflammatory endothelial cell responses. Journal of Biological Chemistry, 289(20): 14283-14290. (IF 3.9)

Ma X, Ji S.-R., Wu Y.* (2013) Regulated conformation changes in C-reactive protein orchestrate its role in atherogenesis. Science Bulletin, 58(14): 1642-1649. (IF 21.1)

Zhang Y.-J., Shi J.-M., Bai C.-J., Wang H., Li H.-Y., Wu Y.*, Ji S.-R.* (2012) Intra-membrane oligomerization and extra-membrane oligomerization of amyloid-β peptide are competing processes as a result of distinct patterns of motif interplay. Journal of Biological Chemistry, 287(1): 748-756. (IF 3.9)

Wang M.-Y., Ji S.-R., Bai C.-J., El Kebir D., Li H.-Y., Shi J.-M., Zhu W., Costantino S., Zhou H.-H., Potempa L.A., Zhao J., Filep J.G.*, Wu Y.* (2011) A redox switch in C-reactive protein modulates activation of endothelial cells. FASEB Journal, 25(9): 3186-3196. (IF 4.2)

Zhu L., Chen L., Zhou X.-M., Zhang Y.-Y., Zhang Y.-J., Zhao J., Ji S.-R., Wu J.-W.*, Wu Y.* (2011) Structural insights into the architecture and allostery of full-length AMP-activated protein kinase. Structure, 19(4): 515-522. (IF 4.3)

Ji S.-R., Ma L., Bai C.-J., Shi J.-M., Li H.-Y., Filep J.G., Potempa L.A., Zhao J., Wu Y.* (2009) Monomeric C-reactive protein activates endothelial cells via interaction with lipid raft micro-domains. FASEB Journal, 23(6): 1806-1816. (IF 4.2)

Shen Q.T., Bai X.C., Chang L.F., Wu Y., Wang H.W., Sui S.-F.* (2009) Bowl-shaped oligomeric structures on membranes as DegP’s new functional forms in protein quality control. Proceedings of the National Academy of Sciences of the United States of America, 106(12): 4858-4863. (IF 9.1)

Jiang J., Zhang X., Chen Y., Wu Y., Zhou Z.H., Chang Z., Sui S.-F.* (2008) Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proceedings of the National Academy of Sciences of the United States of America, 105(33): 11939-11944. (IF 9.1)

Ji S.-R., Wu Y.*, Zhu L., Potempa L.A., Sheng F.-L., Lu W., Zhao J. (2007) Cell membranes and liposomes dissociate C-reactive protein (CRP) to form a new, biologically active structural intermediate: mCRPm. FASEB Journal, 21(1): 284-294. (IF 4.2)

Ji S.-R., Wu Y.*, Potempa L.A., Liang Y.-H., Zhao J. (2006) Effect of modified C-reactive protein on complement activation: A possible complement regulatory role of mCRP in atherosclerotic lesions. Arteriosclerosis, Thrombosis, and Vascular Biology, 26(4): 935-941. (IF 7.4)

Wu Y., He Y., Bai J., Ji S.-R., Tucker W.C., Chapman E.R.*, Sui S.-F.* (2003) Visualization of synaptotagmin I oligomers assembled on lipid monolayers. Proceedings of the National Academy of Sciences of the United States of America, 100(4): 2082-2087. (IF 9.1)

Ji S.-R., Wu Y., Sui S.-F.* (2002) Cholesterol is an important factor affecting the membrane insertion of beta-amyloid peptide (ABeta 1-40), which may potentially inhibit the fibril formation. Journal of Biological Chemistry, 277(8): 6273-6279. (IF 3.9)