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However, cholesterol metabolism as a key component of this regulation remains largely unexplored. Herein, we found that the low-density lipoprotein receptor (LDLR), which has been previously identified as a transporter for cholesterol, plays a pivotal role in regulating CD8+ T cell antitumor activity. Besides the involvement of cholesterol uptake which is mediated by LDLR in T cell priming and clonal expansion, we also found a non-canonical function of LDLR in CD8+ T cells: LDLR interacts with the T-cell receptor (TCR) complex and regulates TCR recycling and signaling, thus facilitating the effector function of cytotoxic T-lymphocytes (CTLs). Furthermore, we found that the tumor microenvironment (TME) downregulates CD8+ T cell LDLR level and TCR signaling via tumor cell-derived proprotein convertase subtilisin\u002Fkexin type 9 (PCSK9) which binds to LDLR and prevents the recycling of LDLR and TCR to the plasma membrane thus inhibits the effector function of CTLs. Moreover, genetic deletion or pharmacological inhibition of PCSK9 in tumor cells can enhance the antitumor activity of CD8+ T cells by alleviating the suppressive effect on CD8+ T cells and consequently inhibit tumor progression. While previously established as a hypercholesterolemia target, this study highlights PCSK9\u002FLDLR as a potential target for cancer immunotherapy as well.",{"EN":128},"Potentiating CD8+ T cell antitumor activity by inhibiting PCSK9 to promote LDLR-mediated TCR recycling and signaling",{"VOID":130},"[\"1812511259110208036\"]",{"VOID":132},"Abifadel M, Varret M, Rabès JP, Allard D, Ouguerram K, Devillers M, Cruaud C, Benjannet S, Wickham L, Erlich D et al (2003) Mutations in PCSK9 cause autosomal dominant hypercholesterolemia. Nat Genet 34:154–156\nAlcover A, Alarcón B, Di Bartolo V (2018) Cell biology of T cell receptor expression and regulation. 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Stillman; citation_volume=408; citation_publication_date=2000; citation_pages=221-225; citation_id=CR118",{"VOID":628},"10.1007\u002Fs13238-010-0104-0","2024-05-16T14:05:41.769+00:00","https:\u002F\u002Flink.springer.com\u002Farticle\u002F10.1007\u002Fs13238-010-0104-0","https:\u002F\u002Flink.springer.com\u002Fcontent\u002Fpdf\u002F10.1007\u002Fs13238-010-0104-0.pdf",[633,658],{"id":634,"sortIndex":19,"researcher":18,"roles":635,"affiliations":636,"properties":653,"displayName":655,"givenName":18,"familyName":18},"c689b299-b19f-471d-be6a-add9c47ce689",[144],[637,645],{"id":638,"sortIndex":19,"affiliation":639,"properties":18},"a4b1312e-7dd4-4e2b-adcc-e1684c83965e",{"id":638,"createTime":18,"updateTime":18,"relativeEntities":640,"slug":18,"properties":641,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":644,"statistic":18},[],{"title":642},{"VI":643},"Graduate Program, Peking Union Medical 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ubiquitination is an important means of post-translational modification which plays an essential role in the regulation of various aspects of leukocyte development and function. The specificity of ubiquitin tagging to a protein substrate is determined by E3 ubiquitin ligases via defined E3-substrate interactions. In this review, we will focus on two E3 ligases, VHL and Itch, to discuss the latest progress in understanding their roles in the differentiation and function of CD4+ T helper cell subsets, the stability of regulatory T cells, effector function of CD8+ T cells, as well as the development and maturation of innate lymphoid cells. The biological implications of these E3 ubiquitin ligases will be highlighted in the context of normal and dysregulated immune responses including the control of homeostasis, inflammation, auto-immune responses and anti-tumor immunity. Further elucidation of the ubiquitin system in immune cells will help in the design of new therapeutic interventions for human immunological diseases and cancer.",{"EN":753},"Immune regulation by protein ubiquitination: roles of the E3 ligases VHL and Itch",{"VOID":755},"[\"2717386323504193477\"]",{"VOID":757},"Abbott RK, Thayer M, Labuda J, Silva M, Philbrook P, Cain DW, Kojima H, Hatfield S, Sethumadhavan S, Ohta A et al (2016) Germinal center hypoxia potentiates immunoglobulin class switch recombination. J Immunol 197:4014–4020\nAki D, Li H, Zhang W, Zheng M, Elly C, Lee JH, Zou W, Liu YC (2018) The E3 ligases Itch and WWP2 cooperate to limit TH2 differentiation by enhancing signaling through the TCR. Nat Immunol. 19:766–775\nAki D, Zhang W, Liu YC (2015) The E3 ligase itch in immune regulation and beyond. 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EMBO Rep 18:1618–1630",{"VOID":759},"10.1007\u002Fs13238-018-0586-8","2024-09-04T18:43:19.848+00:00","https:\u002F\u002Facademic.oup.com\u002Fproteincell\u002Farticle\u002F10\u002F6\u002F395\u002F6759302",[763,787,800,813,833],{"id":764,"sortIndex":19,"researcher":18,"roles":765,"affiliations":766,"properties":784,"displayName":786,"givenName":18,"familyName":18},"3fb13f2b-adcc-4cb6-ae38-67288b960229",[144],[767,775],{"id":768,"sortIndex":19,"affiliation":769,"properties":18},"dc1f5eae-6fee-4125-ad04-c3720a778c84",{"id":768,"createTime":18,"updateTime":18,"relativeEntities":770,"slug":18,"properties":771,"entityType":18,"verifyStatus":18,"verifyTime":18,"verifyNote":18,"languages":18,"translateLanguages":18,"viewCount":18,"url":18,"parentIds":774,"statistic":18},[],{"title":772},{"VI":773},"Institute for Immunology, Tsinghua-Peking Center for Life Sciences, School of Medicine, Tsinghua University, Beijing, 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particle analysis, which can be regarded as an average of signals from thousands or even millions of particle projections, is an efficient method to study the three-dimensional structures of biological macromolecules. An intrinsic assumption in single particle analysis is that all the analyzed particles must have identical composition and conformation. Thus specimen heterogeneity in either composition or conformation has raised great challenges for high-resolution analysis. For particles with multiple conformations, inaccurate alignments and orientation parameters will yield an averaged map with diminished resolution and smeared density. Besides extensive classification approaches, here based on the assumption that the macromolecular complex is made up of multiple rigid modules whose relative orientations and positions are in slight fluctuation around equilibriums, we propose a new method called as local optimization refinement to address this conformational heterogeneity for an improved resolution. The key idea is to optimize the orientation and shift parameters of each rigid module and then reconstruct their three-dimensional structures individually. Using simulated data of 80S\u002F70S ribosomes with relative fluctuations between the large (60S\u002F50S) and the small (40S\u002F30S) subunits, we tested this algorithm and found that the resolutions of both subunits are significantly improved. Our method provides a proof-of-principle solution for high-resolution single particle analysis of macromolecular complexes with dynamic conformations.",{"EN":927},"A local-optimization refinement algorithm in single particle analysis for macromolecular complex with multiple rigid modules",{"VOID":929},"[\"803682038123847875\"]",{"VOID":931},"Azubel M, Wolf SG, Sperling J, Sperling R (2004) Three-dimensional structure of the native spliceosome by cryo-electron microscopy. Mol Cell 15:833–839\nBai XC, Fernandez IS, McMullan G, Scheres SHW (2013) Ribosome structures to near-atomic resolution from thirty thousand cryo-EM particles. 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Nature 523:47–52\nPenczek PA, Frank J, Spahn CMT (2006a) A method of focused classification, based on the bootstrap 3D variance analysis, and its application to EF-G-dependent translocation. J Struct Biol 154:184–194\nPenczek PA, Yang C, Frank J, Spahn CMT (2006b) Estimation of variance in single-particle reconstruction using the bootstrap technique. J Struct Biol 154:168–183\nPettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (2004) UCSF chimera—a visualization system for exploratory research and analysis. J Comput Chem 25:1605–1612\nScheres SH (2012a) A Bayesian view on cryo-EM structure determination. J Mol Biol 415:406–418\nScheres SHW (2012b) RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519–530\nScheres SHW, Chen SX (2012) Prevention of overfitting in cryo-EM structure determination. Nat Methods 9:853–854\nTaylor DJ, Devkota B, Huang AD, Topf M, Narayanan E, Sali A, Harvey SC, Frank J (2009) Comprehensive molecular structure of the eukaryotic ribosome. Structure 17:1591–1604\nVulovic M, Ravelli RBG, van Vliet LJ, Koster AJ, Lazic I, Lucken U, Rullgard H, Oktem O, Rieger B (2013) Image formation modeling in cryo-electron microscopy. J Struct Biol 183:19–32\nWang Z, Hryc CF, Bammes B, Afonine PV, Jakana J, Chen D-H, Liu X, Baker ML, Kao C, Ludtke SJ (2014) An atomic model of brome mosaic virus using direct electron detection and real-space optimization. Nature communications 5:4808–4819\nZhang L, Ren G (2012) IPET and FETR: experimental approach for studying molecular structure dynamics by cryo-electron tomography of a single-molecule structure. PLos One 7:e30249\nZhang W, Kirnmel M, Spahn CMT, Penczek PA (2008) Heterogeneity of large macromolecular complexes revealed by 3D Cryo-EM variance analysis. 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LD, Chen XZ, Cai Y, Zhuang ZH, Xue YG (1997) Directional screening of nisin-producing Lactococcus lactis and identification of its product. Acta Microbiol Sin 37:292–300. (还连栋, 陈秀珠, 才迎, 庄增辉, 薛禹谷. (1997). 乳链菌肽产生菌的定向筛选及发酵产物的鉴定. 微生物学报, 37, 292–300)",{"id":18,"text":2820,"url":18,"identifiers":18},"Sun Z, Zhong J, Liang XB, Liu JL, Chen XZ, Huan LD (2009) Novel mechanism for nisin resistance via proteolytic degradation of nisin by the nisin resistance protein NSR. Antimicrob Agents Chemother 53:1964–1973",{"id":18,"text":2822,"url":18,"identifiers":18},"Teng KL, Zhang J, Zhang X, Ge XX, Gao Y, Wang J, Lin YH, Zhong J (2014) Identification of ligand specificity determinants in lantibiotic bovicin HJ50 and the receptor BovK, a multitransmembrane histidine kinase. J Biol Chem 289:9823–9832",{"id":18,"text":2824,"url":18,"identifiers":18},"Yuan J, Zhang ZZ, Chen XZ, Yang W, Huan LD (2004) Site-directed mutagenesis of the hinge region of nisin Z and properties of nisin Z mutants. Appl Microbiol Biotechnol 64:806–815",{"id":2826,"createTime":2827,"updateTime":2828,"relativeEntities":2829,"slug":2830,"properties":2831,"entityType":135,"verifyStatus":136,"verifyTime":2842,"verifyNote":138,"languages":18,"translateLanguages":18,"viewCount":19,"primaryUrl":2843,"fullTextUrl":18,"authors":2844,"publicationType":534,"publisherRelationship":2899,"citationCount":18,"citationInfo":18,"publishDate":2962,"publishYear":1117,"citationAnalyzeStatus":2963,"lastCitationAnalyze":2964,"indexDatabases":2965,"openAccess":18,"references":18,"isForceReanalyzing":611},"aa1cf3d8-8038-4f41-80a5-86b37e0ad7a5","2024-02-15T11:56:06.118+00:00","2025-12-21T14:01:25.306+00:00",[],"Intranasal-and-oral-vaccination-with-protein-based-antigens-advantages-challenges-and-formulation-strategies",{"abstract":2832,"title":2834,"gsPaper":2836,"references":2838,"doi":2840},{"EN":2833},"Most pathogens initiate their infections at the human mucosal surface. Therefore, mucosal vaccination, especially through oral or intranasal administration routes, is highly desired for infectious diseases. Meanwhile, protein-based antigens provide a safer alternative to the whole pathogen or DNA based ones in vaccine development. However, the unique biopharmaceutical hurdles that intranasally or orally delivered protein vaccines need to overcome before they reach the sites of targeting, the relatively low immunogenicity, as well as the low stability of the protein antigens, require thoughtful and fine-tuned mucosal vaccine formulations, including the selection of immunostimulants, the identification of the suitable vaccine delivery system, and the determination of the exact composition and manufacturing conditions. This review aims to provide an up-to-date survey of the protein antigen-based vaccine formulation development, including the usage of immunostimulants and the optimization of vaccine delivery systems for intranasal and oral administrations.",{"EN":2835},"Intranasal and oral vaccination with protein-based antigens: advantages, challenges and formulation strategies",{"VOID":2837},"[]",{"VOID":2839},"Abusugra I, Morein B (1999) Iscom is an efficient mucosal delivery system for Mycoplasma mycoides subsp. mycoides (MmmSC) antigens inducing high mucosal and systemic antibody responses. FEMS Immunol Med Microbiol 23:5–12\nAli R, Kumar S, Naqvi RA, Sheikh IA, Rao DN (2013) Multiple antigen peptide consisting of B- and T-cell epitopes of F1 antigen of Y. pestis showed enhanced humoral and mucosal immune response in different strains of mice. Int Immunopharmacol 15:97–105\nAlmeida AJ, Alpar HO (1996) Nasal delivery of vaccines. 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