CKD患者血清FGF-23和血钙、血磷水平与左心功能关系的研究--《北京医学》2015年01期
CKD患者血清FGF-23和血钙、血磷水平与左心功能关系的研究
【摘要】：正慢性肾衰竭(chronic renal failure,CRF)是慢性肾脏病(chronic kidney disease,CKD)终末期并严重威胁人类健康。到目前为止,治疗终末期肾衰竭的有效方法是肾移植术和血液净化治疗,但由于肾源等因素的影响,肾移植治疗的开展受到较大的限制。在血液净化治疗中,维持性血液透析(maintenance hemodialysis,MHD)是常被患者首选的方式。近年
【作者单位】：
【关键词】：
【基金】：
【分类号】：R692.5【正文快照】：
慢性肾衰竭(chronic renal failure,CRF)是慢性肾脏病(chronic kidney disease,CKD)终末期并严重威胁人类健康。到目前为止,治疗终末期肾衰竭的有效方法是肾移植术和血液净化治疗,但由于肾源等因素的影响,肾移植治疗的开展受到较大的限制。在血液净化治疗中,维持性血液透析(ma
欢迎：、、)
支持CAJ、PDF文件格式，仅支持PDF格式
【相似文献】
中国期刊全文数据库
刘卓拉,冀锐锋,王崇刚,赵卉;[J];山西临床医药;1997年03期
吴跃平,黄惠君;[J];广东医学;1999年08期
王小文,陈惠德,万力,顼志敏,赵松,陈宇清,刘昕;[J];中华外科杂志;2000年06期
姚英;刘惠兰;王银娜;刘群;;[J];中国血液净化;2007年08期
崔春黎;陈胜芳;;[J];同济大学学报(医学版);2011年05期
陈勇,农雄伟,陈福明,李京花,王付发,钟丽萍,周少诗,陆振仁;[J];中华劳动卫生职业病杂志;1988年01期
陈少贤;邢玲玲;余孝龙;;[J];浙江医学;1989年05期
李英梅;李彩荣;刘欣艳;余雪君;张莉;刘闻莺;韩敏;车在前;杨根妹;;[J];上海医学;2014年05期
保学明;邓剑波;;[J];岭南急诊医学杂志;2000年03期
任树风,李欣;[J];中国血液净化;2005年08期
中国重要会议论文全文数据库
谢娟;李正胜;黄波;程晓娟;;[A];贵州省中西医结合学会肾病专业委员会成立暨中西医结合诊治肾脏病学习班论文汇编[C];2011年
谢娟;李正胜;黄波;程晓娟;;[A];中西医结合学会肾病专业委员会2013年学术年会暨继续教育学习班资料汇编[C];2013年
周仁;尹潍;;[A];中华医学会第六次全国内分泌学术会议论文汇编[C];2001年
姚英;刘惠兰;王银娜;刘群;;[A];中华医学会肾脏病学分会2006年学术年会论文集[C];2006年
刘耘;朱小华;;[A];中华医学会第九次全国核医学学术会议论文摘要汇编[C];2011年
袁开芬;赵国厚;王瑞丽;张洋;;[A];中华医学会呼吸病学年会——2013第十四次全国呼吸病学学术会议论文汇编[C];2013年
刘丽梅;李蓬秋;张学军;杨艳;吴冀川;;[A];中华医学会第六次全国骨质疏松和骨矿盐疾病学术会议暨中华医学会骨质疏松和骨矿盐疾病分会成立十周年论文汇编[C];2011年
程荣;路凌;黎静;纪莉;朱莉敏;王亚娟;;[A];中国超声医学工程学会第九届全国腹部超声医学学术会议论文汇编[C];2012年
中国硕士学位论文全文数据库
俞啟遥;[D];河北医科大学;2008年
孙志杰;[D];天津医科大学;2011年
曾颖;[D];苏州大学;2011年
唐景华;[D];广西医科大学;2010年
&快捷付款方式
&订购知网充值卡
400-819-9993
《中国学术期刊（光盘版）》电子杂志社有限公司
同方知网数字出版技术股份有限公司
地址：北京清华大学 84-48信箱 知识超市公司
出版物经营许可证 新出发京批字第直0595号
订购热线：400-819-82499
服务热线：010--
在线咨询：
传真：010-
京公网安备75号智能可穿戴设备及其应用--《中国医疗器械信息》2015年03期
智能可穿戴设备及其应用
【摘要】：智能可穿戴设备是可以直接作为配件穿戴在身上的便携式电子设备,在软件支持下感知、记录、分析生命特征,极大的提高了我们的生活质量。随着物联网和移动互联网的发展,智能可穿戴设备与各类应用软件紧密结合,成为其新的发展趋势。本文主要从智能可穿戴设备的种类、技术、市场发展、优势以及存在问题等方面进行综述。
【作者单位】：
【关键词】：
【分类号】：TP368.33【正文快照】：
智能可穿戴设备是一种可以穿在身上或贴近身体并能发送和传递信息的计算设备,它可以利用传感器、射频识别、全球定位系统等信息传感设备,接入移动互联网,实现人与物随时随地的信息交流。智能可穿戴设备分为生活健康、信息咨询和体感控制类设备。其中,生活健康类的设备有运动、
欢迎：、、)
支持CAJ、PDF文件格式，仅支持PDF格式
【参考文献】
中国期刊全文数据库
刘思言;;[J];世界电信;2013年12期
黄蕊;;[J];投资北京;2014年03期
张洋;;[J];新营销;2014年02期
刘思言;;[J];现代电信科技;2014年06期
李靖;张云;;[J];中外管理;2013年11期
【共引文献】
中国期刊全文数据库
李祖平;;[J];科技与出版;2014年11期
赵静;王朝晖;陈平辉;;[J];移动通信;2014年21期
李冶陶;;[J];西部广播电视;2014年20期
李国柱;高凯凯;;[J];电子测试;2014年22期
【相似文献】
中国期刊全文数据库
;[J];电脑爱好者;2000年06期
;[J];现代制造;2007年09期
;[J];电脑爱好者;2013年19期
李春亮;[J];火力与指挥控制;1992年01期
钟捷;[J];农村电气化;1996年03期
庞家林;;[J];少年电世界;1998年02期
范岳;;[J];电子测试;2001年06期
;[J];电脑爱好者;2011年17期
;[J];办公自动化;2012年23期
LaPAr;[J];多媒体世界;2005年06期
中国重要报纸全文数据库
邓健;[N];计算机世界;2008年
马霞;[N];科技日报;2014年
ZHANG LI;[N];电脑报;2003年
小鱼儿;[N];中国电脑教育报;2005年
;[N];中国电脑教育报;2004年
赵冬洋;[N];人民铁道;2008年
马云峰;[N];中国计算机报;2001年
;[N];电脑商报;2004年
;[N];计算机世界;2003年
乐乐2004;[N];中国电脑教育报;2004年
&快捷付款方式
&订购知网充值卡
400-819-9993
《中国学术期刊（光盘版）》电子杂志社有限公司
同方知网数字出版技术股份有限公司
地址：北京清华大学 84-48信箱 知识超市公司
出版物经营许可证 新出发京批字第直0595号
订购热线：400-819-82499
服务热线：010--
在线咨询：
传真：010-
京公网安备75号Human intracellular ISG15 prevents interferon-α/β over-amplification and auto-inflammation.
- PubMed - NCBI
The NCBI web site requires JavaScript to function.
FormatSummarySummary (text)AbstractAbstract (text)MEDLINEXMLPMID ListChoose DestinationFileClipboardCollectionsE-mailOrderMy BibliographyCitation managerFormatSummary (text)Abstract (text)MEDLINEXMLPMID ListCSVCreate File1 selected item: FormatSummarySummary (text)AbstractAbstract (text)MEDLINEXMLPMID ListMeSH and Other DataE-mailSubjectAdditional textE-mailAdd to ClipboardAdd to CollectionsOrder articlesAdd to My BibliographyGenerate a file for use with external citation management software.Create File
2015 Jan 1;517(. doi: 10.1038/nature13801. Epub
2014 Oct 12.Human intracellular ISG15 prevents interferon-α/β over-amplification and auto-inflammation.1, 2, 3, 3, 4, 1, 5, 3, 6, 7, 6, 8, 9, 7, 7, 10, 10, 10, 1, 1, 11, 1, 1, 12, 1, 13, 1, 1, 14, 6, 15, 16, 17, 18, 10, 19, 20, 21, 22, 18, 23, 24, 22, 25, 26.1Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China.21] St. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, New York 10065, USA [2] Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.3Institut Pasteur, Cytokine Signaling Unit, CNRS URA
Paris, France.41] Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA [2] Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA [3] Microbiology Training Area, Graduate School of Biomedical Sciences of Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.51] Division of Immunology, Children's Hospital Boston, Boston, Massachusetts 02115, USA [2] Department of Neuroscience, Rehabilitation, Ophthalmology, Genetics, Maternal and Child Health, University of Genoa, 16132 Genoa, Italy.6Immunology Division and Pediatric Neurology Department, Hacettepe University Children's Hospital, 06100 Ankara, Turkey.7Division of Infectious Diseases and Clinical Immunology, Pediatric Respiratory Diseases Research Center, National Research Institute of Tuberculosis and Lung Diseases, Shahid Beheshti University of Medical Sciences, 4739 Teheran, Iran.8Manchester Academic Health Science Centre, University of Manchester, Genetic Medicine, Manchester, M13 9NT, UK.9Department of Pediatrics, Third Xiangya Hospital, Central South University, Changsha 410013, China.10St. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, New York 10065, USA.11BGI-Shenzhen, Shenzhen 518083, China.12Sangzhi County People's Hospital, Sangzhi 427100, China.13Genetics Laboratory, Hubei Maternal and Child Health Hospital, Wuhan, Hubei 430070, China.141] Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China [2] Center for Cardiovascular Genetics, Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA.15Institut Pasteur, Bacteria-Cell Interactions Unit, 75724 Paris, France.16CNRS UMR5235, Montpellier II University, Place Eugène Bataillon, 34095 Montpellier, France.17Department of Biochemistry, McGill University, Montreal, QC H3A 0G4, Canada.18Paris Descartes University, 75006 Paris, France.191] Laboratory of Human Genetics of Infectious Diseases, Necker Branch, INSERM U1163, Necker Hospital for Sick Children, 75015 Paris, France [2] Paris Descartes University, Imagine Institute, 75015 Paris, France.201] Laboratory of Human Genetics of Infectious Diseases, Necker Branch, INSERM U1163, Necker Hospital for Sick Children, 75015 Paris, France [2] Paris Descartes University, Imagine Institute, 75015 Paris, France [3] Center for the Study of Primary Immunodeficiencies, Necker Hospital for Sick Children, 75015 Paris, France.211] Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA [2] Global Health and Emerging Pathogens Institute, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA [3] Department of Medicine, Division of Infectious Diseases, Icahn School of Medicine at Mount Sinai, New York, New York 10029, USA.221] St. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, New York 10065, USA [2] Laboratory of Human Genetics of Infectious Diseases, Necker Branch, INSERM U1163, Necker Hospital for Sick Children, 75015 Paris, France [3] Paris Descartes University, Imagine Institute, 75015 Paris, France.23Division of Immunology, Children's Hospital Boston, Boston, Massachusetts 02115, USA.241] Manchester Academic Health Science Centre, University of Manchester, Genetic Medicine, Manchester, M13 9NT, UK [2] Paris Descartes University, Imagine Institute, 75015 Paris, France [3] INSERM UMR 1163, Laboratory of Neurogenetics and Neuroinflammation, Imagine Institute, 75006 Paris, France.251] Laboratory of Human Genetics of Infectious Diseases, Necker Branch, INSERM U1163, Necker Hospital for Sick Children, 75015 Paris, France [2] Paris Descartes University, Imagine Institute, 75015 Paris, France [3] Howard Hughes Medical Institute, New York, New York 10065, USA [4] Pediatric Hematology-Immunology Unit, Necker Hospital for Sick Children, 75015 Paris, France [5].261] Institut Pasteur, Cytokine Signaling Unit, CNRS URA
Paris, France [2].AbstractIntracellular ISG15 is an interferon (IFN)-α/β-inducible ubiquitin-like modifier which can covalently bind other proteins in a process called ISG it is an effector of IFN-α/β-dependent antiviral immunity in mice. We previously published a study describing humans with inherited ISG15 deficiency but without unusually severe viral diseases. We showed that these patients were prone to mycobacterial disease and that human ISG15 was non-redundant as an extracellular IFN-γ-inducing molecule. We show here that ISG15-deficient patients also display unanticipated cellular, immunological and clinical signs of enhanced IFN-α/β immunity, reminiscent of the Mendelian autoinflammatory interferonopathies Aicardi-Goutières syndrome and spondyloenchondrodysplasia. We further show that an absence of intracellular ISG15 in the patients' cells prevents the accumulation of USP18, a potent negative regulator of IFN-α/β signalling, resulting in the enhancement and amplification of IFN-α/β responses. Human ISG15, therefore, is not only redundant for antiviral immunity, but is a key negative regulator of IFN-α/β immunity. In humans, intracellular ISG15 is IFN-α/β-inducible not to serve as a substrate for ISGylation-dependent antiviral immunity, but to ensure USP18-dependent regulation of IFN-α/β and prevention of IFN-α/β-dependent autoinflammation. Comment inPMID:
[PubMed - indexed for MEDLINE] PMCID: PMC4303590 a, Sanger sequencing of ISG15 exon 2 from genomic DNA in kindred C, with the variants highlighted. b, The wild type (WT) and three mutant alleles (G55X, L114fs, E127X- ISG15) were inserted into an expression vector and used to transfect HEK293T cells. Other HEK293T cells were mock-transfected (mock) or left untransfected (not transf.). The cell lysates isolated were subjected to western blotting, with recombinant human (Rh)-ISG15 used as a control. c, d, Plasma samples from P1, P2, P3, P5, P6 and the mother and brother of P5/6 were used in cytopathic protection assays, to measure antiviral activity (c) and blocking antibodies against IFN-α were used to assess specificity (d) (experiment was performed one time).Nature. ;517(.a, Lentiviral particles containing luciferase, wild-type (WT) ISG15-RFP or ISG15(ΔGG)-RFP genes were used to transduce hTert-immortalized fibroblasts from C1, a STAT1-/- subject, P1, P2 and P3. RFP-positive cells were obtained by sorting and were cultured for a few weeks. The cells were then treated with 1,000 IU of IFN-α2b for 12 h, washed with PBS and left to rest for 36 h, after which relative mRNA levels for IFIT1 were determined. b, The experimental setting described in a was used in the presence or absence of vehicle control, anti-ISG15 antibodies or control IgG for luciferase and wild-type ISG15–RFP-transduced C1 and P1 hTert-immortalized fibroblasts (showing representative experiments with technical replicates and s.e.m., out of 3 performed).Nature. ;517(.a, Left panels, SV40-immortalized fibroblasts from two controls (C10 and C12) and two ISG15-deficient patients (P1 and P2) were stimulated with IFN-β (500 pM) for 4 to 36 h. Cell lysates (30 ug) were analysed with the indicated antibodies. Right, EBV-transformed B cells from control (C3) and patient P1 were stimulated with IFN-β for 8 to 24 h. Cell lysates (30 ug) were analysed with the indicated antibodies. b, HLLR1-1.4 cells were transfected with control siRNA or ISG15 siRNA. One day post-transfection, IFN-β (500 pM) was added for various amounts of time. Cell lysates (30 ug) were analysed with the indicated antibodies (MxA and MX1 are used synonymously). c, WISH cells were stimulated and lysates analysed as described in b. d, HLLR1-1.4 cells were transfected with control siRNA, USP18 siRNA and UbcH8 (also known as UBE2E2) siRNA (left) or control siRNA, USP18 siRNA and HERC5 siRNA (right). One day post-transfection, cells were left untreated (naive) or were primed for 8 h with IFN-β (500 pM). Cells were washed and left to rest for 16 h before being pulsed for 30 min with 100pM IFN-α2 or IFN-β. Cell lysates (30 ug) were analysed with the indicated antibodies.Nature. ;517(.a, HLLR1-1.4 cells were transfected with either control siRNA or ISG15 siRNA. One day post-transfection, cells were stimulated with IFN-β (500 pM) for 6 h. Cycloheximide (CHX, 20 ugml-1) was then added for various time periods, from 30 min to 5 h. Cell lysates (30 ug) were analysed with the indicated antibodies. b, As in a, with additional controls, cells treated with IFN only. Several interferon-stimulated genes were analysed. c, hTert-immortalized fibroblasts from patient P1 transduced with lentiviral particles expressing RFP and luciferase and wild-type ISG15 (LV ISG15 WT) were stimulated with IFN-β (500 pM) for 6 h. CHX was then added for the indicated times. Cell lysates (15 ug) were analysed by western blotting. d, HEK293T cells were transfected with USP18, HA–ubiquitin and Flag–ISG15 as indicated. Two days later, cells were lysed in modified RIPA buffer, USP18 was immunoprecipitated (IP) and analysed with anti-USP18 antibodies. Left panels, cell lysates (30 ug) were analysed by western blot with the indicated antibodies. Right panels, the immunoprecipitates were gel separated and transferred onto a membrane. The membrane was cut into two parts above the 50 kDa marker, both of which were blotted with anti-USP18 antibodies. The top part was exposed for 2 min, the bottom part for 20 s. Asterisk indicates IgG heavy chain. e, HEK293T cells were transfected with 1 ug of the USP18 construct alone or with 1 ug of HA– ubiquitin, in the presence or absence of Flag-tagged ISG15, either wild type or a mutant form of ISG15 that cannot be conjugated as it lacks the two carboxyterminal glycine residues (Flag–ISG15(ΔGG)). Two days later, cells were lysed in modified RIPA buffer, USP18 was immunoprecipitated and analysed with anti-HA or anti-USP18 antibodies. Asterisk indicates IgG heavy chain. f, hTert-immortalized fibroblasts from patient P3 were transfected with control siRNA or SKP2 siRNA. We added IFN-β (500 pM) 24 h later and the cells were incubated for the indicated times. Cell lysates were analysed with the indicated antibodies and USP18 levels were determined as a function of actin levels.Nature. ;517(.a, b, Serum samples from ISG15-deficient, SLE and AGS patients were evaluated for the presence of IgG and IgA autoantibodies in a blinded experiment. Values for the negative control samples for each antigen were averaged and ratios of each sample to the mean for the negative controls plus 2 standard deviations were calculated, with values greater than 1 considered positive. A heat map of the ratio values was generated with MultiExperiment Viewer software (MeV, DFCI Boston, MA), with values coded as follows: 0, 1, 5, yellow.Nature. ;517(.a, Familial segregation in a family from Turkey (Kindred A), a family from Iran (Kindred B) (previously reported) and a family from China (Kindred C). Asterisk E deno fs, WT, wild type. b, Graphical representation of the proISG15 protein, with the LRLRGG motif required for substrate ISGylation and the eight-amino-acid sequence (black) cleaved to yield ISG15, and the putative proteins synthesized in the patients. c, Axial view cerebral CT scans of P1, P2, P3, P4, P5, P6 and the healthy mother of P4, P5 and P6 (ISG15-/+).Nature. ;517(.a, Relative mRNA levels for IFI27, IFI44L, IFIT1, ISG15, RSAD2 and SIGLEC1 in peripheral blood from patients (n = 3) or controls (C) (n = 24) or in peripheral blood mononuclear cells (PBMCs) from family members (wild type and heterozygous for ISG15 deficiency) (n = 2) and patients (n = 2), as assessed by RT–qPCR, comparison done with unpaired t-tests. ***P & 0.0001; horizontal
RQ defined in reference to C1 unstimulated condition. b, hTert-immortalized fibroblasts from C1, C16, C18, a NEMO-/- subject (as a negative control due to known hyporesponsiveness), P1 and P2 were treated with the indicated doses of IFN-α2b for 12 h, washed with PBS and left to rest for 36 h, after which relative mRNA levels were assessed. b shows a representative experiment of three performed. GUS is used as a housekeeping control gene. NS, not stimulated. c, The same experimental procedure as in b was followed, but the mRNA was used for a microarray experiment, for C1, C6, C16, P1, P2 and P3 cells, with green indicating relative upregulation and red indicating downregulation of the probe concerned. d, In the same experimental setup, we used lentiviral particles containing luciferase–RFP (red fluorescent protein) or wild-type ISG15–RFP genes to transduce hTert-immortalized fibroblasts and then assessed mRNA levels for IFIT1 and MX1 by RT–qPCR. Panel d shows one representative experiment of three performed, where (-) denotes not transduced conditions.Nature. ;517(.a, hTert-immortalized fibroblasts from a control (C18) and patient P3 were treated with 100pM IFN-α2 for 0.5 to 36 h. Cell lysates were analysed by western blot for levels of phosphorylated STAT (pSTAT) proteins and proteins encoded by interferon-stimulated genes. b, hTert-immortalized fibroblasts from controls (C1, C18) and patients P1 and P2 were treated with 100pM IFN-α2 for 12 h, washed and left to rest for 24 or 36 h. Protein levels were assessed by western blot. c, HLLR1-1.4 cells were transfected with control short interfering RNA (siRNA) or with siRNA targeting USP18, ISG15 or both. One day later, cells were left untreated (naive) or were primed for 8 h with 500 pM IFN-β, washed and left to rest for 16 h, and then restimulated for 30 min with 100 pM IFN-α2or IFN-β. Lysates were analysed with the indicated antibodies. d, HLLR1-1.4 cells were transfected with control siRNA, ISG15 siRNA or UBE1L siRNA. One day later, IFN-β (500 pM) was added for various periods of time. Lysates were analysed as indicated. e, hTert-immortalized fibroblasts from P3 transduced with lentiviral particles expressing RFP and luciferase (LV), wild-type ISG15 (LV ISG15 WT) or the IS15(ΔGG) mutant (LV ISG15(ΔGG)) were stimulated with IFN-β (500 pM) for 8 to 36 h and protein levels assessed by western blot.Nature. ;517(.a, hTert-immortalized fibroblasts from control (C18) and patient P3 were left untreated (-) or treated for 6 h with IFN-β (500 pM). Cycloheximide (CHX) was added for an additional 0.5 to 5 h. Lysates were analysed as indicated. b, hTert fibroblasts from P3 transduced with lentiviral particles expressing RFP and luciferase (LV) conjugated to wild-type ISG15 (LV ISG15 WT) or the non-conjugatable ISG15(ΔGG) mutant (LV ISG15(ΔGG)) were processed as in a. c, HEK293T cells were transfected with USP18 expression vector alone or in combination with various amounts of ISG15 (Flag–ISG15), either wild-type or ΔGG. Two days later, lysates were analysed as indicated. Ratios of USP18 or ISG15 to AKT are shown below gels. d, HEK293T cells were cotransfected with USP18 and haemagglutinin (HA)–ubiquitin in the presence of wild-type ISG15 (Flag–ISG15). Two days later, lysates were subjected to immunoprecipitation (IP) with anti-USP18 antibodies. Lysates (left panels) were analysed with antibodies against HA and actin. Immunoprecipitates (right panels) were analysed with antibodies against HA and USP18. Asterisk indicates IgG heavy chain. e, HEK293T cells were transfected with USP18, Flag–SKP2 and Flag–ISG15 expression vectors, as indicated. Two days later, USP18 was immunoprecipitated. Lysates (left panels) and immunoprecipitates (right panels) were analysed with antibodies against SKP2, USP18 and ISG15. Arrowheads indicate two endogenous SKP2 arrow indicates ectopic Flag–SKP2; asterisk, background band (lanes 6, 7 and 9, 10). f, HLLR1-1.4 cells were transfected with control siRNA or SKP2 siRNA and 24 h later IFN-β (500 pM) was added and cells were incubated for various times. Lysates were analysed as indicated. USP18 and ISG15 levels were quantified relative to actin levels.Nature. ;517(.Publication TypesMeSH TermsSubstancesSecondary Source IDGrant SupportFull Text SourcesMiscellaneous
Supplemental Content
External link. Please review our .