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更新于：2025-05-07

RPA1

更新于：2025-05-07

基本信息

别名

HSSB、REPA1、Replication factor A protein 1

+ [10]

简介

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (PubMed:17596542, PubMed:27723717, PubMed:27723720). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (PubMed:9430682). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response (PubMed:24332808). It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage (PubMed:17765923). Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair (PubMed:7697716). Also plays a role in base excision repair (BER) probably through interaction with UNG (PubMed:9765279). Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. Plays a role in telomere maintenance (PubMed:17959650, PubMed:34767620). As part of the alternative replication protein A complex, aRPA, binds single-stranded DNA and probably plays a role in DNA repair. Compared to the RPA2-containing, canonical RPA complex, may not support chromosomal DNA replication and cell cycle progression through S-phase. The aRPA may not promote efficient priming by DNA polymerase alpha but could support DNA synthesis by polymerase delta in presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange (PubMed:19996105). RPA stimulates 5'-3' helicase activity of the BRIP1/FANCJ (PubMed:17596542).

关联

项与 RPA1 相关的药物

JC-229

靶点

RPA1

作用机制

RPA1 inhibitors

在研机构

Rutgers Biomedical & Health Sciences

原研机构

Rutgers Biomedical & Health Sciences

在研适应症

非洲锥虫病

非在研适应症-

最高研发阶段临床前

首次获批国家/地区-

首次获批日期1800-01-20

100 项与 RPA1 相关的临床结果

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100 项与 RPA1 相关的转化医学

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0 项与 RPA1 相关的专利（医药）

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3,394

项与 RPA1 相关的文献（医药）

2025-12-01·Molecular Biology Reports

Rapid detection assays for Bacillus anthracis, Yersinia pestis, and Brucella spp. via triplex-recombinase polymerase amplification

Article

作者: Wang, Yuanzhi ; Feng, Meijie ; Wang, Hengliang ; Wang, Dongshu ; Liu, Xiankai ; Zhang, Yan ; Lyu, Yufei ; Meng, Ying ; Zhu, Li ; Pan, Chao ; Ma, Jinping

BACKGROUNDBacillus anthracis (B. anthracis), Yersinia pestis (Y. pestis), and Brucella spp. are zoonotic bacteria that cause anthrax, plague, and brucellosis, respectively. Outbreaks typically occur in remote regions with poor transportation and limited laboratory testing. Therefore, a simple, sensitive, multiplex nucleic acid detection method is essential for effective disease management and control.METHODSPrimers and probes for the three pathogens were designed to reduce interference from related strains. Three recombinase polymerase amplification (RPA) reactions were conducted at 39 °C for 10 min to produce species-specific fluorescence signals for the three pathogens. These were integrated, and conditions were optimized for rapid, sensitive triplex-RPA assays without cross-reactivity. A triplex-RPA reaction with lateral flow dipsticks (LFDs) was developed and applied to blood samples, newly isolated strains, and simulated samples.RESULTSHighly sensitive and specific primers and probes were developed, achieving a maximum sensitivity of 1 copy/µL in single-reaction RPA. The optimized triplex RPA detection technique, combined with fluorescence, effectively identified B. anthracis, Y. pestis, and Brucella spp. within 20 min, whereas LFDs achieved detection in 10 min. The assay also performed comparably to conventional polymerase chain reaction techniques when tested on blood samples, newly isolated strains, and simulated samples.CONCLUSIONSThis study offers reliable methods for detecting B. anthracis, Y. pestis, and Brucella spp. in rural hospitals and public health initiatives.

2025-09-01·Journal of Pharmaceutical and Biomedical Analysis

Rapid and sensitive Mycoplasma detection in antibody bioprocessing via RPA-CRISPR/Cas12a

Article

作者: Guo, Qingcheng ; Wang, Fugui ; Pan, Zhiyuan ; Xu, Jin ; Guo, Menghui ; Zhang, Dapeng ; Gao, Tianyu ; Guo, Huaizu ; Chen, Yi ; Hou, Sheng ; Wang, Xuekun ; Liu, Tao ; Ren, Yule ; Wang, Chenguang ; Li, Jun ; Sun, Ziqiao ; Zhuang, Huangzhen ; Zhu, Weifan ; Ji, Lusha ; Qian, Weizhu

Mycoplasma species are prevalent microbial contaminants in the production of biological products, such as monoclonal antibodies, posing significant threats to the safety and efficacy of these products. Current regulatory guidelines as well as pharmacopoeias mandate the demonstration of the absence of Mycoplasma in the cell culture and further downstream processing to ensure product safety. Despite recent advancements in sensitive detection techniques for Mycoplasma in eucaryotic expression systems, these methods remain complex and time-consuming. There is a pressing need for a rapid, simple, and sensitive process analytical technology (PAT) for Mycoplasma detection. Here, we report the first development and application of a recombinase polymerase amplification (RPA)-assisted CRISPR-Cas12a (RPA-CRISPR/Cas12a) system spcifically tailored for Mycoplasma detection in biopharmaceutical production. This system combines the high-sensitivity isothermal nucleic acid amplification capabilities of RPA with the trans-cleavage activity of CRISPR-Cas12a reporter probes, enabling the rapid and accurate detection of Mycoplasma, accommodating various experimental requirements and application scenarios. By designing RPA universal primers and crRNA targeting the highly conserved sequences of Mycoplasma 16S rRNA and optimizing reaction conditions, we achieved dual-specific recognition with unprecedented efficiency in bioprocessing samples. All tested Mycoplasma specimens were detectable with limits between 10 and 0.1 copies/μL, with the whole process taking less than 1 hour. We further evaluated the feasibility of this method in detecting Mycoplasma in the cell culture of antibody products and further downstream processing samples. This method reduces the risk of false-positive signals due to non-specific amplification, enhancing detection sensitivity and specificity while significantly reducing analysis, representing the first PAT-compatible method for rapid Mycoplasma monitoring in antibody manufacturing, thereby providing robust assurance for the quality and safety of biological products.

2025-08-01·Cellular Signalling

Decoding the role of nucleic acid binding protein 2 in lipid dysregulation and hepatocellular carcinoma progression through LKB1-mediated mitochondrial dysfunction

Article

作者: Dai, Chengchen ; Zhou, Lihua ; Xu, Nuo ; Liu, Mingyu ; Li, Jinlong ; Chen, Yinqi ; Bian, Saiyan ; Bai, Nan ; Liu, Xiaoquan ; Zheng, Wenjie ; Tong, Yun ; Xu, Banglong ; Zhao, Xuying ; Tang, Zhangzhi ; Lin, Zhaoyi

Nucleic Acid Binding Protein 2 (NABP2), a crucial regulator in the single-stranded DNA-binding protein family, has been linked to the progression of hepatocellular carcinoma (HCC) and poor prognosis. However, the precise mechanisms by which NABP2 regulates HCC development, especially through metabolic pathways, remain unclear. In this study, we evaluated NABP2 expression in clinical HCC samples and analyzed its correlation with patient survival outcomes. Functional assays, including cell proliferation, migration, and lipid metabolism analyses, were performed in vitro and in vivo to investigate the role of NABP2 in tumorigenesis. Additionally, we examined the molecular interactions of NABP2 with the E3 ubiquitin ligase STUB1 and its impact on the LKB1/AMPK signaling pathway. Our results revealed that NABP2 was overexpressed in HCC tissues and associated with worse survival outcomes. NABP2 promoted tumor cell proliferation, migration, and disrupted lipid metabolism. Mechanistically, NABP2 regulated the proteostasis of liver kinase B1 (LKB1) by recruiting STUB1, leading to the inhibition of the LKB1/AMPK signaling axis and mitochondrial dysfunction. In conclusion, our findings suggest that NABP2 may serve as both a biomarker and a potential therapeutic target for HCC, offering novel insights into its role in metabolic reprogramming and tumor progression.

项与 RPA1 相关的新闻（医药）

2024-06-10

·生物探索

NAR | 四川大学韩俊宏团队发现KDM6A-SND1相互作用通过保护新生DNA维持基因组稳定性，并有助于癌症化疗耐药

引言基因组的不稳定性是癌症的标志之一。虽然组蛋白去甲基化酶KDM6A的缺失增加了肿瘤发生的风险，但其在维持基因组稳定性方面的具体作用仍然知之甚少。 2024年6月8日，四川大学韩俊宏团队在Nucleic Acids Research 在线发表题为“KDM6A–SND1 interaction maintains genomic stability by protecting the nascent DNA and contributes to cancer chemoresistance ”的研究论文，该研究提出了KDM6A维持基因组稳定性独立于其去甲基化酶活性的机制。这是通过它与SND1的相互作用发生的，导致建立一个保护性的染色质状态，通过招募RPA和Ku70到新生的DNA链来防止复制叉崩溃。值得注意的是，KDM6A SUMOylation上调了KDM6A-SND1相互作用，而KDM6AK90A突变几乎消除了这种相互作用。 KDM6A或SND1的缺失导致H3K9ac和H4K8ac的富集增加，但减弱了新生DNA链上Ku70和H3K4me3的富集。这随后导致细胞对基因毒素和基因组不稳定性的敏感性增强。与这些发现一致，食管鳞状细胞癌(ESCC)细胞中KDM6A和SND1的敲低会增加基因毒素敏感性。有趣的是，在ESCC患者中发现的KDM6A H101D和P110S、N1156T和D1216N突变通过增加SND1关联促进基因毒素抗性。总之，该研究的发现为KDM6A-SND1在基因组稳定性和化学耐药中的关键作用提供了新的见解，这意味着靶向KDM6A和/或其与SND1的相互作用可能是克服化学耐药的有希望的策略。基因组的稳定性对细胞存活和肿瘤发生的预防至关重要。在整个完整的细胞周期中，诸如DNA复制、染色体分离、常染色质/异染色质转化、转录激活和核小体组装等事件确保了真核染色质的动态性质。真核生物已经进化出复杂而严格的机制来维持基因组的稳定性，确保适当的细胞分裂和精确的DNA复制。基因组稳定性的破坏可触发细胞内DNA损伤反应(DDR)通路，以维持染色质的完整性和功能。该通路受ATM/ATR、BRCA1/2、TP53等多种蛋白和信号调控。新出现的证据表明，多种染色质重塑因子参与基因组稳定性的调节。染色质重塑的失败或抑制会导致DNA损伤。此外，染色质重塑因子也通过组蛋白修饰或蛋白募集直接调节DDR。由于破坏基因组稳定性是肿瘤治疗的重要策略，因此探索其潜在机制至关重要。复制胁迫是引起基因组不稳定的主要内源因素之一。在复制胁迫下，DNA前导链和后导链在Rad51和RPA蛋白的介导下快速翻转，形成末端具有粘性的DNA双链。这种结构可以保护复制分叉的功能，它也被称为Holliday结，并有助于分叉的稳定性。与常规的普通DNA双链类似，核小体组装也可以发生在反向的新生DNA中，有效地防止DNA被核酸酶降解。在这个过程中，组蛋白修饰和染色质重塑因子在保护新生DNA中起着至关重要的作用。例如，组蛋白去甲基化酶KDM5B可以识别双链断裂DNA，并通过招募Ku70和BRCA1蛋白到DNA断裂处启动DNA修复。组蛋白甲基化酶SETD1A可以通过催化新生双链DNA的组蛋白甲基化来保护新合成的DNA不被核酸外切酶降解。然而，其他组蛋白修饰和染色质重塑因子在复制叉重塑中的参与在很大程度上仍然是难以捉摸的。模式图（Credit: Nucleic Acids Research）组蛋白去甲基化酶6A (KDM6A)位于X染色体上，是染色质重塑因子的一员。KDM6A C端Jumonji C (JmjC)结构域特异性催化组蛋白H3第27位赖氨酸的去甲基化。此外，KDM6A N端的四肽重复(TPR)结构域主要介导蛋白-蛋白相互作用(PPI)。此外，其他证据表明KDM6A与胚胎发育和肿瘤发生密切相关。例如，在KDM6A基因敲除小鼠中观察到高肿瘤发生率。然而，KDM6A突变已在多种肿瘤中被发现，促进肿瘤的发生和进展，如膀胱癌、肾细胞癌。有证据表明，KDM6A功能缺失可使多个抑癌基因启动子区域的H3K27me3水平升高，进而促进肿瘤恶性。JmjC或TPR结构域突变诱导的催化失活也可以取消KDM6A的抑瘤功能，这表明KDM6A抑制肿瘤发生不依赖于其组蛋白去甲基化酶的能力。基因组不稳定是癌症的典型特征。基因组稳定性的破坏可能导致染色体断裂、易位和基因突变，这是肿瘤发生的关键。作为一种重要的染色质重塑因子，KDM6A缺乏已被证明会增加肿瘤发生的风险。因此，KDM6A在维持基因组稳定性和防止肿瘤发生和肿瘤进展中发挥关键作用。事实上，有令人信服的证据表明，KDM6A不仅直接通过JmjC结构域催化H3K27去甲基化，而且还分别通过TPR结构域或内在失调区(IDR)介导的PPI和相分离来实现其功能，这表明KDM6A可能以去甲基化酶依赖和/或独立的方式调节基因组稳定性。到目前为止，KDM6A参与复制叉稳定性的调节在很大程度上仍然未知。该研究发现KDM6A与SND1相互作用，SND1是一种染色质结构修饰剂。KDM6A与SND1之间的相互作用通过KDM6A的SUMOylation而增强，而KDM6A的K90A突变几乎消除了这种相互作用。此外，KDM6A敲低通过抑制RAP32磷酸化和降低γH2AX表达而损害基因组稳定性。这种破坏也会影响其与SND1的相互作用，减少新生DNA上Ku70的富集和RPA1的富集，最终导致DNA损伤。此外，在食管鳞状细胞癌(ESCC)患者中发现的KDM6A H101D和P110S、N1156T和D1216N突变与SND1的相互作用增加，对基因毒素的抗性增强。相反，敲低KDM6A和SND1会提高对基因毒素的敏感性。总之，该研究揭示了KDM6A影响ESCC基因组稳定性和耐药性的新机制。原文链接 https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkae487/7689923 责编|探索君排版|探索君文章来源|“iNature” End 往期精选围观一文读透细胞死亡(Cell Death) | 24年Cell重磅综述（长文收藏版）热文 Cell | 是什么决定了细胞的大小？热文 Nature | 2024年值得关注的七项技术热文 Nature | 自身免疫性疾病能被治愈吗？科学家们终于看到了希望热文 CRISPR技术进化史 | 24年Cell综述

基因疗法临床1期

2023-11-14

·SYNAPSE

What are ATR inhibitors and how do you quickly get the latest development progress?

ATR is a key protein in DNA Damage Response (DDR), a member of the Phosphoinositide 3-Kinase-like Kinases (PIKK) family, sharing the same family with ATM, which also participates in DDR. In tumor cells, due to the activation of oncogenes and the loss of G1 checkpoint function, replication stress (RS) significantly increases. When DNA damage occurs, ATR primarily acts as a sensor for RS, participating in the repair of DNA single-strand breaks. When there is RS or DDR production within the cell, Replication Protein A (RPA) wraps single-strand DNA (ssDNA) to form RPA-ssDNA complexes, and recruits regulatory factors needed to activate ATR: ATRIP, 9-1-1 complex (Rad9-Rad1-Hus1), and Topoisomerase II Binding Protein 1 (TopBP1), etc. ATR and its ligand ATRIP bind and are recruited to RPA-ssDNA, forming an ATR-ATRIP complex. At the same time, ATR undergoes autophosphorylation at site T1989. Once ATR is activated, it prevents activation of CDK2 by phosphating CHK1, CHK2, and inactivating CDC25. These alterations also activate WEE1 directly or via CHK1, causing CDK1 and CDK2 to be phosphorylated and inactivated, thereby stalling the G1/S or G2/M cell cycle progression, giving cells more time for DNA damage repair before entering mitosis. If the damage is too extensive, the corresponding senescence or apoptosis pathway is activated. Understanding the role of ATR is essential for developing targeted therapies and interventions in the pharmaceutical industry. How do they work?ATR inhibitors are a type of drug that target and inhibit the activity of the Ataxia Telangiectasia and Rad3-related (ATR) protein. ATR is a key enzyme involved in the DNA damage response pathway, which helps to maintain genomic stability and prevent the replication of damaged DNA. By inhibiting ATR, these inhibitors can disrupt the DNA damage repair process in cancer cells, leading to their death. From a biomedical perspective, ATR inhibitors have gained significant attention in the field of cancer research and therapy. Cancer cells often have high levels of DNA damage due to their rapid and uncontrolled growth. ATR inhibitors can selectively target cancer cells by exploiting their increased reliance on the DNA damage response pathway. By blocking ATR, these inhibitors can enhance the effectiveness of DNA-damaging treatments, such as chemotherapy or radiation therapy, as cancer cells become more vulnerable to DNA damage-induced cell death. ATR inhibitors have shown promise as potential anti-cancer agents and are currently being investigated in preclinical and clinical trials. They hold potential for the treatment of various types of cancer, including those with DNA repair defects or resistance to conventional therapies. However, further research is needed to fully understand their mechanisms of action, optimize their efficacy, and minimize potential side effects. List of ATR InhibitorsThe currently marketed ATR inhibitors include: CeralasertibART-0380BerzosertibGartisertibTuvusertibATRN-119ElimusertibIMP-9064SC-0245TCC1727For more information, please click on the image below. What are ATR inhibitors used for?ATR inhibitors are under investigation for indications that include metastatic non-small cell lung cancer, prostatic cancer, pancreatic cancer, triple negative breast cancer, metastatic renal cell carcinoma, locally advanced pancreatic adenocarcinoma, cholangiocarcinoma, and secondary malignant neoplasm of pancreas For more information, please click on the image below to log in and search. How to obtain the latest development progress of ATR inhibitors?In the Synapse database, you can keep abreast of the latest research and development advances of ATR inhibitors anywhere and anytime, daily or weekly, through the "Set Alert" function. Click on the image below to embark on a brand new journey of drug discovery!

2022-08-28

·佰傲谷BioValley

CAR-Treg工艺优化是商业化的关键

CAR-T在细胞治疗领域备受瞩目，通过将嵌合抗原受体（CAR）导入T细胞，极大地改善了临床对肿瘤的治疗效果。CAR-T的大获成功的同时也加速了CAR-Treg向临床转化的进展。通过CAR技术，CAR-Treg能够绕过MHC限制性和提高治疗靶向性，在自身免疫性疾病及抑制物抗宿主病（GVHD）中表现出很好的治疗潜力，目前已有多家公司参与开发。‍https://www.biopharmadive.com/news/treg-cell-therapy-biotech-startups/629634/然而，尽管CAR-T对肿瘤疗效非常好，但由于生产成本极高，所产生的昂贵治疗费用让普通患者只能望而止步，CAR-Treg自然绕不开这个难题。人们一直在积极寻找CAR-T工艺优化手段，以期改进疗效的同时减少生产成本，进而推动其市场化进程。工艺流程同样，CAR-Treg的生产也大致可以分为以下步骤：获取细胞，分选富集 → 活化 → 基因传递 → 扩增 → 质检、储存、运输、回输Blood Cancer Discov. 2021 Sep;2(5):408-422.工艺优化方向1. 采集，分选富集：CAR-Treg以单采和来自外周血单核细胞（PBMC）为原料，主要也是通过磁珠细胞分选(MACS)，获得维持免疫耐受的主要亚群：CD4+CD25highFoxp3+Treg。目前CAR技术细胞来源均为自体细胞，Treg细胞占外周血CD4+T细胞的5-10%，部分疾病患者Treg含量更低，甚至在之后表现出无法扩增。原材料无法标准化，细胞活力不可控，以及最主要的个性化定制均为造价昂贵的原因，因此细胞健康人的Treg细胞捐献是未来趋势。以及通过CAR-Foxp3共载体转染可以将CD4或CD3T细胞转化为Treg，这也可以解决外周Treg细胞数量少和内源性TregFoxp3表达不足的。推荐阅读：调节Treg的转录因子：FoxP3/RelA/c-Re/...Biomedicines. 2022 Jan 26;10(2):287.2. 基因导入：通过慢病毒转染，将CAR基因传递到Treg细胞中是目前最主要基因导入方式。该方法两个词总结：高效，昂贵。病毒载体生产耗时耗力，并且有引起炎症反应和基因插入的致癌风险。电穿孔技术是应用广泛的非病毒转染策略之一通过短的脉冲使细胞产生短暂通透性，允许目的基因DNA或mRNA进入。但是这种方法容易引起细胞应激。"sleeping beauty"转座子系统（SB）将CAR转基因插入转座子序列中，再将相应质粒和转座子酶（hsSB）一同导入细胞，hsSB会将序列切下来整合到T细胞基因组，该技术整合效率接近病毒。Nat Biotechnol. 2019 Dec;37(12):1502-1512.而且相较于病毒载体，SB系统在转染后质粒水平逐渐降低。而且质粒相对容易设计，在基因破坏方面也有很高的安全性。4. 扩增和产量：扩增在整个制备过程最为耗时、耗材、耗财。原料Treg获取量非常少，所需达到治疗标准的CAR-Treg量非常大，而且考虑储存运输过程的消耗，相较治疗量产品药甚至需要近100倍的数量。扩增所需培养基中必须加入胎牛血清或人血清，使用无血清培养基不但能够节省成本，并能降低外源物的污染。扩增过程包含多种需人工变异操作，需要考虑多种外接因素的影响。(如温度、湿度、气体张力、无菌性等)作为未来各行业的发展趋势，人工智能(半)自动化及封闭性系统在保证操作精细度的同时能确保环境参数稳定，在提高产量的同时大大降低批次间差异。5. 质量检测：用于CAR-Treg的QC检测标准化尚且未制定。常通过流式细胞术对CD4+CD25highFoxp3+Treg进行验证，并辅以Foxp3启动子区域的甲基化分析。常规观察Treg对Tconv的抑制作用非常耗时，而且对体内的预测价值不大。Foxp3对Treg在治疗过程维持表型而不会向Teff转化至关重要，添加雷帕霉素能够通过抑制mTOR通路维持Treg稳定性。或者基于CRISPR/Cas9的表观遗传编辑也可能是维持Treg表型的手段。6. 治疗：Treg细胞能通过分泌TGF-β、IL-10、IL-35能够将T细胞诱导转化成为Treg细胞，但也会在炎症因子IL-6和IL-1的协同刺激下，通过STAT-3依赖途径介导的Foxp3表达下调而转化成为为Teff细胞。以及外周CD25-Treg细胞也容易转化成Th17细胞，并且由于Teff细胞比Treg细胞具有更快的激活速度与增殖能力，从而成为自身免疫性疾病的致病因素或在治疗过程中加重病情。通过细胞工程技术增加“自杀开关”，在Foxp3表达缺失或炎症因子接触时激活Treg细胞“凋亡“以及CAR-T异位表达的Foxp3能够维持抑制功能和阻止细胞转化。在自身免疫性患者中长期使用CAR-Treg进行治疗，将有可能引起潜在的肿瘤免疫抑制和局部机会性感染，为此设计可调平台使CAR-Treg在症状严重时发挥作用，轻微症状时处于休眠状态。每个生产环节的工艺改进都是促进CAR-Treg平民化的关键一步。参考资料‍https://www.biopharmadive.com/news/treg-cell-therapy-biotech-startups/629634/Fritsche E et al. Toward an Optimized Process for Clinical Manufacturing of CAR-Treg Cell Therapy. Trends Biotechnol. 2020 Oct;38(10):1099-1112.Abou-El-Enein M et al. Scalable Manufacturing of CAR T cells for Cancer Immunotherapy. Blood Cancer Discov. 2021 Sep;2(5):408-422.Arjomandnejad M et al. CAR-T Regulatory (CAR-Treg) Cells: Engineering and Applications. Biomedicines. 2022 Jan 26;10(2):287.Querques I et al. A highly soluble Sleeping Beauty transposase improves control of gene insertion. Nat Biotechnol. 2019 Dec;37(12):1502-1512.Diaconu I et al. Inducible Caspase-9 Selectively Modulates the Toxicities of CD19-Specific Chimeric Antigen Receptor-Modified T Cells. Mol Ther. 2017 Mar 1;25(3):580-592.近期热门视频更多精彩视频，尽在佰傲谷视频号，欢迎关注~本周好文推荐如需转载请联系佰傲谷并在醒目位置注明出处﹀点亮在看，传递信息♥

免疫疗法细胞疗法