Longzuan Tongbi Formula (LZTB) is an effective proved prescription in Zhuang medicine for treating active rheumatoid arthritis (RA). However, its active ingredients, underlying targets, and pharmacological mechanism are still not clear in treating RA. We have applied network pharmacology to study LZTB and found that 8 herbs in LZTB and 67 compounds in the 8 herbs are involved in the regulation of RA-related genes; we have conducted pathway analysis of overlapping genes and found that 7 herbs participate in the regulations of 24 pathways associated with RA and that 5 herbs in the 7 herbs and 25 compounds in the 5 herbs participate in the regulation of hsa05323 (rheumatoid arthritis). The results indicated that all herbs in LZTB and some compounds in those herbs participate in the treatment of RA; 25 compounds are main active ingredients and hsa05323 (rheumatoid arthritis) is the major pathway in the treatment of RA. We have also found that three pathways  might have some effect on the treatment of RA. Toddalia asiatica (TA), Kadsura coccinea (KC), Alangium chinense (AC), Sinomenium acutum (SA), Bauhinia championii (BC), Spatholobus suberectus (SS), Zanthoxylum nitidum (ZN), and Ficus hirta Vahl (FHV). Clinical studies have shown that LZTB can significantly reduce RA patients' erythrocyte sedimentation rate, and that it has a good therapeutic effect on improving RA patients' morning stiffness and joint pain [Rheumatoid arthritis (RA) is a chronic, systemic, and autoimmune disease. It can lead to irreversible joint destruction and deformity, seriously affecting people's quality of life . Diseaseint pain . HoweverCompound preparations in traditional medicine can act on multiple targets through multicomponent reaction, play an indispensable role in core pathways in diseases, and help achieve the purpose of treating diseases . Much athttp://bionet.ncpsb.org/batman-tcm/) was used to predict targets of LZTB for RA. On this platform, drug similarity is used to predict underlying drug targets. Its core idea is to calculate drug similarity and rank potential drug-target interactions by comparing potential and known drug-target interactions [ Ficus hirta Vahl (FHV) as major compound information (PubChem_ID: the details are described in BATMAN-TCM platform (ractions . On BATMDisGeNET (http://www.disgenet.org) database was applied to acquire RA targets .RA targets were acquired through DisGeNET, Gene_IDs of targets were input into String  , speciesTargets of LZTB were acquired through BATMAN-TCM and text retrieval, and herb-compound target network was constructed through Cytoscape3.6.1.Draw Venn Diagram (http://bioinformatics.psb.ugent.be/webtools/Venn/) was applied online to find the intersection of LZTB targets acquired through BATMAN-TCM and RA targets acquired through DisGeNET. Cytoscape3.6.1 was applied to construct LZTB-RA interaction network.In large protein-protein interaction (PPI) networks, topological modules or clusters are defined as the regions where molecular complexes are densely connected , 17, andIn the field of biology, GO analysis is widely used to analyze the functions of genes . It is m p value in enrichment analysis. Target analysis was based on the enrichment analysis of functional items to investigate the potential biological functions and involved biological pathways. The technology roadmap is described in In this study, the ClusterProfiler package of R3.5.0  was adopThere are 1,254 nodes and 11,181 edges in the RA target PPI network. The closer the nodes are to red and the larger the nodes are, the higher the degree of freedom they have. This demonstrates that these genes are closely related to other genes in the network, suggesting that these genes may play an important role in RA. Pathogenic factors may directly influence RA-related genes or indirectly influence RA-related genes by affecting these genes, thereby affecting the development of RA, which suggests that these genes may be the key or central genes. The top 10 proteins with the highest degree of freedom are PIK3CA, APP, MAPK1, TP53, JUN, PTPN11, RAC1, RELA, SRC, and MAPK3. The respective degrees of freedom are 164, 132, 122, 118, 115, 111, 104, 103, 103, and 103. The details are described in Five clusters were found after RA target network was analyzed through MCODE (K-Core=10). This demonstrates that these clusters may be the most relevant to RA in studies at present. The details are described in The biological process (BP) enrichment analysis (p=0.05) of 5 clusters was conducted, and we found the following.Cluster 1 contains 394 biological processes of which those associated with RA mainly include regulation of chemotaxis in immune cells, immune cell migration, angiogenesis, apoptosis, enzyme activity, and immune responses. The details are described in Cluster 2 contains 1,392 biological processes of which those associated with RA mainly include regulation of immune cell migration, chemotaxis in immune cells, cell secretion, biosynthesis of tumor necrosis factor (TNF), enzyme activity, hormone secretion, ossification, apoptosis signaling pathway, immune responses, and phagocytosis. The details are described in Cluster 3 contains 847 biological processes of which those associated with RA mainly include regulation of TNF-mediated signaling pathway, immune cell activation, immune responses, immune cell proliferation, and Wnt signaling pathways. The details are described in Cluster 4 contains 443 biological processes of which those associated with RA mainly include regulation of immune cell activation, inflammatory cell proliferation, and apoptosis signaling pathway. The details are described in p=0.05) was carried out, and 24 pathways associated with RA were found. The details are described in Cluster 5 contains 486 biological processes of which those associated with RA mainly include regulation of immune cell activation, inflammatory cell proliferation, immune responses, and apoptosis. The details are described in In the aforementioned biological processes, regulation of immune responses, immune cell activation, and immune cell proliferation contributes to RA through joint damage caused by boosting immune responses and promoting inflammatory responses; regulation of inflammatory cell proliferation promotes RA through direct joint damage; dysregulation of apoptosis and phagocytosis promotes RA by giving rise to the dysplasia of angiogenesis and provides nutrition pathways for cell hyperplasia, which aggravates the development of RA; abnormal ossification of joints contributes significantly to the joint deformity of RA patients.In the aforementioned pathways, Th17 cell differentiation, IL-17 signaling pathway, and Chemokine signaling pathway participate in the pathological process of RA through inflammatory response; TNF signaling pathway, NF-kappa B signaling pathway, MAPK signaling pathway, PI3K-Akt signaling pathway, apoptosis, apoptosis-multiple species, and phagosome participate in the pathological process of RA by influencing the apoptosis, proliferation, inflammatory response, and autophagy of synovial cells; osteoclast differentiation and AMPK signaling pathway participate in the pathological process of RA by leading to joint deformity through the damage of joint cartilage and bone; Toll-like receptor signaling pathway, Th1 and Th2 cell differentiation, T cell receptor signaling pathway, TGF-beta signaling pathway, and B cell receptor signaling pathway participate in the pathological process of RA by regulating innate and adaptive immunity and influencing the proliferation of synovioblast and pathological angiogenesis; Jak-STAT signaling pathway, FoxO signaling pathway, HIF-1 signaling pathway, and cAMP signaling pathway play an important role in the proliferation and apoptosis of synovial cells, osteocyte differentiation, and immunoregulation as they accept the activation of inflammatory factors and transmit signals to the corresponding targets; rheumatoid arthritis signaling pathway exhibits the pathological process of RA in many aspects, including abnormal activation of immune system, abnormal inflammatory response, abnormal proliferation of synovial cells, pannus formation, and osteoclast differentiation. p value set at 0.05, 74 known compounds in LZTB and 2,987 target genes were retrieved. For Toddalia asiatica (TA), there are 13 compounds and 441 target genes: Chelidimerine (TA-1), Citronellol (TA-2), Isopinocamphone (TA-3), Mexolide (TA-4), Diosphenol (TA-5), Eugenol (TA-6), Alpha-Pinene (TA-7), Oxychelerythrine (TA-8), Tohogenol (TA-9), Robustine (TA-10), Skimmianine (TA-11), Citronellyl Acetate (TA-12), and Eugenol Methyl Ether (TA-13); for Kadsura coccinea (KC), there is 1 compound and 20 target genes: Schisantherin L (KC-1); for Zanthoxylum nitidum (ZN) there is 1 compound and 11 target genes: Oxynitidine (ZN-1); for Bauhinia championii (BC), there are 3 compounds and 24 target genes: Sinensetin (BC-1), 5,7,3′,4′,5′-Pentamethoxyflavone (BC-2), and 5,6,7,3′,4′,5′-Hexamethoxyflavone (BC-3); for Sinomenium acutum (SA), there are 15 compounds and 397 target genes: Stepholidine (SA-1), Magnoflorine (SA-2), Stepharine (SA-3), Dispegatrine (SA-4), Disinomenine (SA-5), Isosinomenine (SA-6), Michelalbine (SA-7), Magnograndiolide (SA-8), Michelenolide (SA-9), Sinactine (SA-10), Tuduranine (SA-11), Stigmasterol (SA-12), Sinomontanine D (SA-13), Gamma-sitosterol (SA-14), and Sinomenine (SA-15); for Spatholobus suberectus (SS), there are 16 compounds and 361 target genes: Licochalcone A (SS-1), Isoliquiritigenin (SS-2), Biochanin A (SS-3), Genistein (SS-4), Vestitol (SS-5), Afrormosin (SS-6), Isosativan (SS-7), Daidzein (SS-7), Formononetin (SS-8), Calycosin (SS-9), Prunetin (SS-10), Campesterol (SS-11), Stigmasterol (SS-12), Odoratin (SS-13), Pendulone (SS-14), and Medicagol (SS-15); for Alangium chinense (AC), there is 1 compound and 71 target genes: (+-)-Anabasine (AC-1); and for Ficus hirta Vahl (FHV), there are 24 compounds and 1,662 target genes: Palmitic acid (FHV-1), Meranzin hydrate (FHV-2), Quercetin (FHV-3), Oleic acid (FHV-4), Luteolin (FHV-5), Bergapten (FHV-6), Umbelliferone (FHV-7), Kaempferol (FHV-8), Sitosterol (FHV-9), Ethyl acetate (FHV-10), Methyleugenol (FHV-11), Narigenin (FHV-12), Hesperidin (FHV-13), p-hydroxybenzoic acid (FHV-14), Tricin (FHV-15), Acacetin (FHV-16), 1,2-benzenedicarboxylic acid, bis(2-methylpropyl) ester (FHV-17), α-amyrin acetate (FHV-18), Physcion (FHV-19), Cyclomorusin (FHV-20), Linoleic acid (FHV-21), β-amyrin acetate (FHV-22), Apigenin (FHV-23), and 4-hydroxy-3-methoxybenzoic acid (FHV-24). The details are described in With cutoff set at 10,The aforementioned results indicate that 8 herbs in LZTB and 67 compounds in the 8 herbs possibly are the material bases that play a key pharmacological role.After the intersection process, we found there is an overlap between 8 herbs in LZTB and RA. Toddalia asiatica (TA) have overlapping genes with RA: Citronellol (TA-2): SHBG, RET, ALDH1A2, ESR1, RHO, GATA3, ALDH1A1, CACNA1S, PGR, VCAM1, ALDH1A3, LRAT, AR; Isopinocamphone (TA-3): AR; Mexolide (TA-4): IL5, TNF, MUC2, RNASE3, NFKB1; Diosphenol (TA-5): ANXA1, ADORA2A, GRIK4, FADS2, NR3C1, CYP19A1, TH, TNF, PTGS2, ESR1, PARK2, TRPV1, TNFSF11, FOS, PGR, CYP17A1, NFKB1, HSD11B1, PTGS1, AR, PDE4A; Eugenol (TA-6): ALOX5, CNR1, CNR2, SEC14L2, NR1I2; Alpha-Pinene (TA-7): EDN1, IGF1, LEP, APOE, FAS, ALDH1A2, ASPA, MIP, ESR1, PPARD, SCGB1A1, FADD, KCNA3, ALDH1A1, PGR, CYP17A1, ALDH1A3, CAT, IL1B, SPARC, LRAT; Oxychelerythrine (TA-8): ADRA1A, PTGS2, ADRA2B, PTGS1; Tohogenol (TA-9): VDR, AR; Robustine (TA-10): ALOX5, FGF1, CHGA, PTPN2, CNR1, ABCB1, SOAT1, ABCG2, CNR2, SOCS1, SEC14L2, SERPINE1, NR1I2, TTPA, CCL3; Skimmianine (TA-11): MTNR1B, MTNR1A; Citronellyl Acetate (TA-12): ESR1, ADRA2B, PGR, AR; Eugenol Methyl Ether (TA-13): CNR1, CNR2.Specifically, 12 compounds in Kadsura coccinea (KC) has 1 overlapping gene with RA: Schisantherin L (KC-1): TOP2B.One compound in Alangium chinense (AC) has overlapping genes with RA: (+)-Anabasine (AC-1): CXCR4, PTK2B, HRH4, ADORA2A, ADRA1A, CYP19A1, TACR2, CHAT, ADRB2, LILRB1, ADRA2B, ADRB3, HTR2A.One compound in Zanthoxylum nitidum (ZN) has overlapping genes with RA: Oxynitidine (ZN-1): ADRA1A, PTGS2, ADRA2B, PTGS1.One compound in Bauhinia championii (BC) have overlapping genes with RA: Sinensetin (BC-1): IL5, TNF, MUC2, RNASE3, NFKB1; 5,7,3′,4′,5′-Pentamethoxyflavone (BC-2): IL5, TNF, MUC2, RNASE3, NFKB; 5,6,7,3′,4′,5′-Hexamethoxyflavone (BC-3): IL5, TNF, MUC2, RNASE3, NFKB1.Three compounds in Spatholobus suberectus (SS) have overlapping genes with RA: Licochalcone A (SS-1): HSD17B1, CNR1, PDE3A, SOAT1, CNR2; Isoliquiritigenin (SS-2): HSD17B1, ALOX5, PPARG, PTGS2, ESR1, CFTR, PTGS1; Biochanin A (CS-3): ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; Genistein (SS-4): HSD17B1, ESR1, CACNA1S, PGR, NR1I2, AR, ESR2; Vestitol (SS-5): ALOX5, FGF1, CHGA, PTPN2, CNR1, ABCB1, SOAT1, ABCG2, CNR2, SOCS1, SEC14L2, SERPINE1, NR1I2, TTPA, CCL3; Afrormosin (SS-6): ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; Isosativan (SS-7): ALOX5, FGF1, CHGA, PTPN2, CNR1, ABCB1, SOAT1, ABCG2, CNR2, SOCS1, SEC14L2, SERPINE1, NR1I2, TTPA, CCL3; Formononetin (SS-9): ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; Calycosin (SS-10): ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; Prunetin (SS-11):ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; Campesterol (SS-12): ANXA1, NR3C1, ESR1, VDR, PGR, AR; Stigmasterol (SS-13): EDN1, IGF1, LEP, APOE, FAS, ALDH1A2, ASPA, MIP, ESR1, PPARD, SCGB1A1, FADD, KCNA3, ALDH1A1, PGR, CYP17A1, ALDH1A3, CAT, IL1B, SPARC, LRAT; Odoratin (SS-14): ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; Pendulone (SS-15): ADRA1A, CNR1, SOAT1, CNR2, ADRA2B.Fourteen compounds in Sinomenium acutum (SA) have overlapping genes with RA: Stepholidine (SA-1): NCF4, RAC1, RAC2, NCF2, NCF1, ESR1, ADRA2B, CYBB, HTR2A, ESR2; Magnoflorine (SA-2): ALOX5, ADRA2B, SEC14L2, HTR2A, NR1I2; Dispegatrine (SA-4): ADRA2B, HTR2A; Disinomenine (SA-5): SHH, ESR1, CREB1, TLR4, HTR2A, ESR2; Isosinomenine (SA-6): SHH, ESR1, CREB1, TLR4, HTR2A, ESR2; Michelalbine (SA-7): NFATC1, NPPB, ADORA2A, ADRA1A, SELE, TNF, ADRB2, VEGFA, ADRA2B, IL2, FOS, ATF2, HIF1A, VCAM1, ADRB3, HTR2A, JUN, HBA1; Magnograndiolide (SA-8): ATP1A1, ITGB2, HMGCR, AR, ITGAL; Michelenolide (SA-9): ADRA1A; Sinactine (SA-10): NCF4, RAC1, ELANE, RAC2, HRH4, NCF2, ADRA1A, SLC22A1, NCF1, ADRA2B, CYBB, TLR4, HTR2A; Tuduranine (SA-11): ADRA2B, HTR2A; Stigmasterol (SA-12): EDN1, IGF1, LEP, APOE, FAS, ALDH1A2, ASPA, MIP, ESR1, PPARD, SCGB1A1, FADD, KCNA3, ALDH1A1, PGR, CYP17A1, ALDH1A3, CAT, IL1B, SPARC, LRAT; Sinomontanine D (SA-13): UGCG, GAA, PADI4; Gamma-Sitosterol (SA-14): CALB1, KL, NR3C1, GC, ESR1, VDR, PML, PGR, CYP17A1, NFKB1, AR, SNAI2, BAX; Sinomenine (SA-15): ESR1, ESR2.Fourteen compounds in Ficus hirta Vahl (FHV) have overlapping genes with RA: palmitic acid (FHV-1): BTG2, EDN1, IGF1, PAK1, SOD2, FGFR1, MTNR1B, NR4A2, F2RL1, EDNRA, GHRL, CNTN2, ADRA1A, LXN, TACR2, F2, PTGS2, BMP2, TAC1, PDE4D, SNCA, NR4A3, PARK2, HYAL2, EPHB1, TRPV1, INS, CRHR1, LPAR3, GDNF, CRH, IL10, CHD7, TYK2, F2R, STRA6, TACR3, ALDH1A3, CAT, ADAM17, ADRB3, ADM, UCN3, CAV2, IL1B, HTR2A, CX3CR1, P2RX7, GNA12, PTEN, PTK2B, RAB3GAP1, CLN8, MECP2, ARHGEF7, NOS1, PTPN11, NPPB, YWHAE, BDKRB2, ADORA2A, CHGA, DLL1, CRHR2, CNR1, FABP3, CDK6, TH, VIM, EDNRB, CDC42, ARRB1, ADRB2, ADA, PARP1, CD34, INHBA, LILRB1, ADRA2B, S1PR1, FOS, MDK, IGF1R, HPRT1, HIF1A, XBP1, GFAP, CREBRF, CDK5, MAP2K1, PTGS1, LPAR1, GHSR; quercetin (FHV-3)ADRA2B, HTR2A; oleic acid (FHV-4): IGF1, ANXA1, NOS1, SHBG, ABCA1, BDKRB2, SCD5, PPARG, ALOX15, RARB, RET, FADS2, ALDH1A2, MAPK9, PTPN2, NR3C1, FABP3, TNF, ABCC2, ITGAV, APOA2, PTGS2, FGF4, GPRC5A, ESR1, SNCA, S100A8, IL13, PTGER4, TRPV1, VDR, PPARD, IHH, FASLG, INS, RARA, SERPINH1, PPARA, GATA3, NAMPT, PTGER2, SP1, JUNB, FGF2, ALDH1A1, SLC3A2, GDF5, PGR, RARG, ALDH1A3, IL1B, PTGS1, PPARGC1B, AR, NOTCH1, CYR61, S100A9, ADIPOQ; bergapten (FHV-6): RARB, TNF, VDR, RARA, RARG; umbelliferone (FHV-7): SOD2, SOD3, SOD1; kaempferol (FHV-8): HSD17B1; sitosterol (FHV-9): COX5A, CALB1, ABCA1, KL, COX8A, ABCB1, NR3C1, GC, ABCC2, COX1, ESR1, SOAT1, VDR, HMGCR, PML, PLA2G1B, ANPEP, PGR, CYP17A1, COX2, AKT1, NFKB1, ABCC8, AR, SNAI2, BAX, ITGAL; ethyl acetate (FHV-10): HSD17B1, PF4, BDKRB2, ARHGEF2, HDAC9, TH, EGLN1, SULT2A1, CDC42, CDH11, WNT10B, GPT, CCL2, SHMT1, CYP1A2, IL10, EDA, SLC16A4, SLC16A3, CCL5, SLC25A12, HDAC1, SIRT1, P4HB, DHODH, SLC52A2; methyleugenol (FHV-11): MTNR1B, DNMT3B, FOLR1, AURKA, DHFR, ABCC2, MPO, CALR, HOXA5, ESR1, TYMS, PDE3A, FOLR2, CALM2, MTNR1A, SHMT1, HYAL2, DNMT1, HIF1A, CALM3, CDKN1A, IL1B, HTR2A, GAS6, ATIC, CALM1, PDE4A; p-hydroxybenzoic acid (FHV-12): ANXA1, ALOX5, AKR1B10, ABCA1, BDKRB2, PPARG, ALOX15, MAPK9, PTPN2, TPMT, FABP3, TNF, MPO, ITGAV, CHUK, APOA2, PTGS2, SNCA, S100A8, IL13, INS, PPARA, NAMPT, PLA2G1B, IKBKB, IFNG, IKBKE, SERPINE1, IL1B, PTGS1, S100A9, ADIPOQ; tricin (FHV-13): ALOX5, CNR1, SOAT1, CNR2, SEC14L2, NR1I2; acacetin (FHV-14): ALOX5, ADORA2A, CNR1, NR3C1, ESR1, SOAT1, CNR2, SEC14L2, NR1I2, HBA1; 1,2-benzenedicarboxylic acid, bis(2-methylpropyl) ester (FHV-15): NFKB2, EDNRA, CRP, PTGS2, CHKA, SLC5A7, ADRA2B, IKBKB, TP53, NFKB1, NFKBIA, PTGS1, RPS6KA3; α-amyrin acetate (FHV-16): NR3C1, CYP19A1, ESR1, ADRA2B, PGR, AR; physcion (FHV-17): CNR1, PTGS2, ESR1, SOAT1, CNR2, PTGS1; cyclomorusin (FHV-18): CNR1, CNR2; linoleic acid (FHV-19): IGF1, ANXA1, NOS1, PCYT1A, SHBG, ABCA1, BDKRB2, SCD5, PPARG, ALOX15, RARB, RET, FADS2, ALDH1A2, MAPK9, PTPN2, NR3C1, FABP3, TNF, ABCC2, ITGAV, APOA2, PTGS2, FGF4, GPRC5A, SNCA, S100A8, IL13, PTGER4, TRPV1, VDR, PPARD, IHH, FASLG, INS, RARA, SERPINH1, PPARA, GATA3, NAMPT, PTGER2, SP1, JUNB, FGF2, ALDH1A1, SLC3A2, GDF5, RARG, ALDH1A3, IL1B, HSD11B1, PTGS1, PPARGC1B, AR, NOTCH1, CYR61, S100A9, ADIPOQ; narigenin (FHV-20): HSD17B1, SUMO1, ALOX5, C3, CNR1, ESR1, SOAT1, CNR2, SEC14L2, AKT1, NR1I2, ESR2; β-amyrin acetate (FHV-21): NR3C1, CYP19A1, ESR1, ADRA2B, PGR, AR; hesperidin (FHV-23): ESR1, ADRB2, SOAT1, VDR, HTR2A, NR1I2, ESR2; 4-hydroxy-3-methoxybenzoic acid (FHV-24): ANXA1, FOXP3, ABCA1, BDKRB2, PPARG, ALOX15, RARB, MAPK9, MAPK14, TNF, ITGAV, PTGS2, FGF4, SNCA, VDR, IHH, INS, RARA, SERPINH1, PPARA, NAMPT, FGF2, GDF5, RARG, TP53, GCG, PTGS1, CDKN2A, ABCC8, NOTCH1, CYR61, ADIPOQ. The details are described in Twenty-one compounds inThe aforementioned results suggest that LZTB has intervention effects on RA as the 8 herbs in LZTB can have effects on RA through multiple compounds and targets.We obtained 3 clusters after conducting clustering analysis for LZTB target-RA target network (K-core=2). The details are described in  Toddalia asiatica (TA), Bauhinia championii (BC), Sinomenium acutum (SA), and Alangium chinense (AC). It indicates that the 8 compounds in the 4 aforementioned Zhuang herbs play an important role in the treatment of RA.Cluster 1 contains 4 compounds: BC-1, BC-2, BC-3, and TA-4; cluster 2 contains 2 compounds: A-10 and AC-1; cluster 3 contains 2 compounds: SA-14 and TA-2. Three clusters contain 8 compounds and 4 Zhuang herbs:Cluster 1 contains 3 genes: MUC2, IL5, and RNASE3; cluster 2 contains 2 genes: HTR2A and ARA2B; and cluster 3 contains 2 genes: AR and PGR. It indicates that the 7 aforementioned genes are key to the treatment of RA with LZTB.p=0.05) showed that cluster 1 contains 20 biological processes of which those associated with RA mainly include regulation of immunoglobulin secretion, immune responses, and B cell proliferation. The details are described in p=0.05), 24 pathways associated with RA were found, and 7 herbs in LZTB participate in the regulations of pathways. The details are described in The GO enrichment analysis of the aforementioned clusters  indicated that it is directly associated with RA. TA-4, TA-5, TA-7, TA-10, BC-1, BC-2, BC-3, SA-5, SA-6, SA-7, SA-8, SA-10, SA-12, SS-5, SS-7, SS-13,FHV-1, FHV-4, FHV-6, FHV-9, FHV-10, FHV-11, FHV-12, FHV-19, and FHV-24 are effective compounds in LZTB that directly intervene with RA pathways, and 13 genes are involved: CCL2, CCL3, CCL5, FOS, IFNG, IL1B, ITGAL, ITGB2, JUN, TLR4, TNF, TNFSF11, and VEGFA. The details are described in TRP channels  are a group of nonselective cation channels throughout the body, and they are Ca 2 + permeable. TRP channels consist of more than 30 members that are divided into 7 subfamilies: TRPC, TRPV, TRPM, TRPA, TRPP, TRPML, and TRPN . Accordiα, PPAR-β, and PPAR-γ. PPAR-γ is more closely related to RA. According to research, the expression of PPAR-γ can be detected in synovial cells involved in rheumatoid arthritis. PPAR-γ agonists can inhibit the hyperplasia of synovial cells and induce their apoptosis [γ agonists can inhibit the generation of key mediators in RA from macrophages, including IL-1β, IL-6, and TNF-α [PPARs (peroxisome proliferation-activated receptors) are ligand-activated transcription factors, comprising of the following three subtypes: PPAR-poptosis , 37. In nd TNF-α . In concα) are released into articular cavity. Then, the activated PI3K in synovioblasts transmits signal to Akt. Regulating multiple transcription factors, the activated Akt helps with cell survival by inhibiting the expression of apoptosis gene  and the activity of proapoptotic protein (Bad) and enhancing the expression of antiapoptotic gene  [Serine/threonine-protein kinase mTOR  belongs to the PIKK (phosphoinostitide-3-kinase-related kinase) family, and it plays a key role in regulating cell growth, proliferation and survival. In RA-related mTOR signaling pathways, PI3K/Akt/mTOR signaling pathway is actively studied . In the , NF—κB) . Akt act, NF—κB) . In summIn conclusion, the three aforementioned signaling pathways of LZTB possibly act on RA.Currently, conventional synthetic disease-modifying antirheumatic drugs remain the first choice for clinical treatment in RA. We found in this study that some compounds in LZTB are directly involved in the regulation of RA pathways and that they possibly are major compounds in LZTB for the treatment of RA, for example, Mexolide, Diosphenol, Alpha-Pinene, Robustine, Sinensetin, 5,7,3′,4′,5′-Pentamethoxyflavone, 5,6,7,3′,4′,5′-Hexamethoxyflavone, Stepholidine, Magnoflorine, Dispegatrine, Disinomenine, Isosinomenine, Michelalbine, Magnograndiolide, Michelenolide, Sinactine, Tuduranine, Stigmasterol, Vestitol, Daidzein, Odoratin, Palmitic acid, Oleic acid, Bergapten, Sitosterol, Ethylacetate, Methyleugenol, Narigenin, Physcion, and 4-hydroxy-3-methoxybenzoicacid. In this study, we applied network-based computational methods to predict and expound the molecular synergy of LZTB for RA. It will provide new ideas for further research on ethnopharmacology, Chinese medicinal herbs and ethnic compounds. The targets, clusters, biological processes, and pathways associated with RA were discovered through this study. LZTB target-RA target network exhibited the effective chemical compounds, potential pharmacology, and molecular mechanism of LZTB for treating RA and also justified the composition of LZTB.


Correction to: Arthritis Res Therhttps://doi.org/10.1186/s13075-017-1399-5Following publication of the original article , the aut1Centre for Prognostic Studies in the Rheumatic Diseases, Toronto Western Hospital, University of Toronto, 1-412, 399 Bathurst Street, Toronto, ON M5T 2S8, Canada.8Department of Rheumatology, Tel Aviv Sourasky Medical Center, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel.


Therefore, the authors’ names and affiliations for this paper should have been presented as follows:1, AYMAN G. MUSTAFA2,4, AMAL ABU OMAR2, AHMED N. AL.DWAIRI1, MOHAMMAD A. ALQUDAH1, MONA S. NAZZAL1, MAHMOUD A. ALFAQIH1, and RAMI A. AL.HADER3OTHMAN A. AL.SHBOUL1Physiology and Biochemistry, and 2Anatomy, Faculty of Medicine, Jordan University of Science and Technology, Irbid 22110; 3Department of Physiology and Biochemistry, Princess Basma Teaching Hospital, Faculty of Medicine, Jordan University of Science and Technology, Irbid 21110, JordanDepartments of Correspondence to: Dr Othman A. Al-Shboul, Department of Physiology and Biochemistry, Faculty of Medicine, Jordan University of Science and Technology, P.O. Box 3030, Irbid 22110, JordanE.mail: oashboul@just.edu.joPresent address: 4Department of Basic Medical Sciences, College of Medicine, Qatar University, Doha, QatarThe authors regret this oversight in terms of their author affiliations, and apologize for any inconvenience caused.


This article has been corrected: During production, the 4th affiliation was mistakenly added to the name of the last author, Dr. Andrew S. Moore. The proper affiliation information is shown below.5755-5767. https://doi.org/10.18632/oncotarget.27206Original article: Oncotarget. 2019; 10:5755–5767. 1,4,*, Christine R.C. Zhang1,4,*, Alexandre S. Cristino1,6, John P. Grady1,5, J. Lynn Fink1 and Andrew S. Moore1,2,3Amanda M. Smith1The University of Queensland Diamantina Institute, The University of Queensland, Woolloongabba, Australia2Oncology Services Group, Queensland Children’s Hospital, South Brisbane, Australia3Child Health Research Centre, The University of Queensland, South Brisbane, Australia4Current address: Washington University in Saint Louis, Saint Louis, Missouri, United States of America5Current address: Garvan Institute of Medical Research, Darlinghurst, Australia6Current address: Griffith Institute for Drug Discovery, Brisbane Innovation Park, Nathan, Australia*These authors contributed equally to this work


O. Box LG 25, Legon, Ghana 2 Department of Biochemistry, Cell and Molecular Biology, University of Ghana, P. O. Box LG 25, Legon, Ghana3 West African Centre for Cell Biology of Infectious Pathogens, University of Ghana, P. O. Box LG 25, Legon, GhanaThe name of country in affiliations provided was: 1 Department of Biomedical Engineering, College of Basic and Applied Sciences, University of Ghana, P. O. Box LG 25, Legon2 Department of Biochemistry, Cell and Molecular Biology, University of Ghana, P. O. Box LG 25, Legon3 West African Centre for Cell Biology of Infectious Pathogens, University of Ghana, P. O. Box LG 25, Legon


Lipoprotein glomerulopathy (LPG) is an uncommon cause of nephrotic syndromeand/or kidney failure. At microscopy, LPG is characterized by the presence oflipoprotein thrombi in dilated glomerular capillaries due to different ApoEmutations. ApoE gene is located on chromosome 19q13.2, and can be identified inalmost all serum lipoproteins. ApoE works as a protective factor inatherosclerosis due its interaction with receptor-mediated lipoprotein clearanceand cholesterol receptor. Most common polymorphisms include ApoE2/2, ApoE3/2,ApoE3/3, ApoE4/2, ApoE4/3, and ApoE4/4. All age-groups can be affected by LPG,with a discrete male predominance. Compromised patients typically revealdyslipidemia, type III hyperlipoproteinemia, and proteinuria. LPG treatmentincludes fenofibrate, antilipidemic drugs, steroids, LDL aphaeresis, plasmaexchange, antiplatelet drugs, anticoagulants, urokinase, and renaltransplantation. Recurrence in kidney graft suggests a pathogenic component(s)of extraglomerular humoral complex resulting from abnormal lipoproteinmetabolism and presumably associated to ApoE. The compromisedglomeruli exhibit ectatic capillary lumina occupied by lipoprotein thrombi.1,4,5,7,12,13,14,15,The first case of LPG described in English literature was by Saito et al, whoreported a patient with resistant nephritic syndrome and accumulation of lipiddroplets in glomeruli loops.1,3,4,7,8,3,4,5,7,12,15,18,1,4,5,9,19,21,22,23,4,7,8,19,25,26,27,13,15,17,19,20,23,29,ApoE is a fundamental component of lipid and lipoprotein metabolism byfunctioning as the ligand for receptor-mediated catabolism of chylomicrons, someHDLs, and VLDLs. ApoE is present in almost all serum lipoproteins and acts as aprotective factor in atherosclerosis due its interaction with receptor-mediatedlipoprotein clearance and cholesterol receptor.1,19,([21]) Matsunaga etal.Arg25Cys is a common mutation of ApoE gene and is known as ApoE Kyoto.12cis or in trans) that can inducedifferent levels of expression of the mutant vs the wild-type allele ; b) an uncommonmutation or a polymorphism in another gene possibly associated to the fullphenotypic expression of LPG; and c) epigenetic processes related to theregulation of a mutant gene.Chen at al.,7,8,19,21,39,19,21,34,41,3,8,13,14,15,17,21,28,19,21,34,41,The most common mutation is the Sendai form, which is characterized by asubstitution of proline for arginine-145. ApoE Sendai can break theα-helical structure of ApoE in the low-density lipoproteinreceptor-binding domain and modify the ApoE protein that are deposited inglomeruli thrombi and mesangium.2,5,6,9,2,7,9,19,22,4,6,15,23,26,30,1,7,10,11,15,16,22,28,4,6,7,9,23,27,1,9,11,15,17,32,The characteristic histologic finding of LPG is the presence of large glomerulidue to ectatic capillary loops, which are occupied with lipoprotein thrombi. The glo1,5,8,15,21,25,5,8,15,21,25,32,45,Associated to histological findings, proteinuria, dyslipidemia, and increasedserum apolipoproteins levels are also hallmarks of LPG. The patients exhibittype III hyperlipoproteinemia and progress to nephritic syndrome in most cases.All age groups can be affected in LPG, with a discrete male predominance.1,8,18,21,32,35,39,41,4,21,32,35,MODENA mutation that wastreated successfully with low-density lipoprotein-apheresis with the Heparininduced extracorporeal lipoprotein precipitation system. Heparin-inducedextracorporeal low-density lipoprotein (LDL) precipitation (HELP) is a selectiveand careful apheresis procedure. Through the application of heparin and loweringthe pH value, lipoproteins and fibrinogen are reduced by 50-60%. In addition,adhesion molecules , which play a key role in thedevelopment and progression of atherosclerosis are also markedly reduced.Many reports describe various therapies such as LDL aphaeresis, plasma exchange,renal transplantation, steroids, antiplatelets, anticoagulants, ACEI, ARB,urokinase, and antilipidemic drugs.4,4,8,12,21,32,1,4,8,12,21,32,35,Although all these treatments determine some benefits to LPG patients, not allpatients respond the same way. A point to be further analyzed is theheterogeneity of the disease and the type of mutation involved. Most mutations,including ApoE Sendai, associated with LPG locate around the receptor-bindingdomain for LDL cholesterol and reduce the receptor-binding activity. Patientsfrequently have accompanying hyperlipidemia. Moreover, several patients withApoE Kyoto or ApoE5 mutations, which locate far from receptor binding sites, arenot complicated with hyperlipidemia. Those mutations indicate that ApoE mutantscausing LPG do not damage glomeruli via hyperlipidemia but might injureglomeruli directly by forming aggregated deposits of lipoproteins that have highaffinity or low clearance in glomeruli.1,21,Since half of the patients with LPG might eventually develop end-stage renaldisease, kidney transplantation should be considered in these patients. However,the long-term outcome of kidney transplantation in patients with LPG remainsuncertain. All of five kidney transplants reported in the literature had LPGrelapse, which were confirmed by renal graft biopsy within 2 years aftertransplantation. It seems that LPG recurrence in a transplanted kidney isinevitable, which is also associated with poor prognosis.12


There are errors in the author affiliations. The correct affiliations are as follows:1,2, Mary Grace Tan2, Woei Bing Poon2Lay Ong Tan1 Department of Paediatrics, KK Women's and Children's Hospital, Singapore, 2 Department of Neonatal & Developmental Medicine, Singapore General Hospital, Singapore.


In the published article, there was an error in affiliations 1 and 2.1, Guohong Wang1,2, Zhengyuan Zhai1, Pengyu Zhou1 and Yanling Hao1,2*Instead of “Xiayin Ma1 Key Laboratory of Functional Dairy, Co-constructed by the Ministry of Education and Beijing Municipality, China Agricultural University, Beijing, China2 The Innovation Centre of Food Nutrition and Human Health (Beijing), College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China,”1,2, Guohong Wang1,2, Zhengyuan Zhai1,2, Pengyu Zhou2 and Yanling Hao1,2*it should be “Xiayin Ma1 Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Food Science and Nutritional Engineering, China Agricultural University, Beijing, China2 Key Laboratory of Functional Dairy, Co-constructed by the Ministry of Education and Beijing Municipality, China Agricultural University, Beijing, China.”The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way. The original article has been updated.


This article has been corrected: The correct author information and affiliations are given below:1, Boris Gole1,2, Laurent Chatre3,4, Paul Walther5, Enrico Calzia6, Anja Palmer7, J. Christof M. Gebhardt7, Miria Ricchetti3,4 and Lisa Wiesmüller1Rahel Stefanie Wiehe1 Department of Obstetrics and Gynecology, Ulm University, Ulm, 89075, Germany2 Present address: Centre for Human Molecular Genetics and Pharmacogenomics, Medical Faculty, University of Maribor, Maribor, SI-2000, Slovenia3 Department of Developmental and Stem Cell Biology, Institute Pasteur, Stem Cells and Development, 75724 Cedex 15, Paris, France4 Team Stability of Nuclear and Mitochondrial DNA, Unit of Stem Cells and Development, CNRS UMR 3738, 75724 Cedex 15, Paris, France5 Central Facility for Electron Microscopy, Ulm University, Ulm, 89081, Germany6 Institute of Anesthesiological Pathophysiology and Process Engineering, Ulm University Hospital, Ulm, 89081, Germany7 Institute of Biophysics, Ulm University, Ulm, 89081, Germanyhttps://doi.org/10.18632/oncotarget.24822Original article: Oncotarget. 2018; 9:18309-18326.


Int J Epidemiol 2013;42:1754-1771, doi:10.1093/ije/dyt198During the preparation of this article, owing to an administrative oversight between the collaborating institutions, we omitted Dr Dermot Maher from the author list. Dr Maher was involved in the early phases of the General Population Cohort (GPC) Study, data from which were used in the individual-level participant data analyses in this manuscript. His role included contributing to the GPC study protocol development, management of initial research ethics application for the GPC, and organisation of initial field programmes at MRC/UVRI Uganda Research Unit on AIDS.As a result, we request that Dr Maher is included in the author list. This results in the following correction:1,2 Deepti Gurdasani,1,2 Johanna Riha,1,2 Kenneth Ekoru,1,2,3 Gershim Asiki,3 Billy N Mayanja,33Dermot Maher, Naomi S Levitt,4 Nigel J Crowther,5 Moffat Nyirenda,6 Marina Njelekela,7 Kaushik Ramaiya,8 Ousman Nyan,9 Olanisun O Adewole,10 Kathryn Anastos,11 Livio Azzoni,12 W Henry Boom,13 Caterina Compostella,14 Joel A Dave,15 Halima Dawood,16 Christian Erikstrup,17 Carla M Fourie,18 Henrik Friis,19 Annamarie Kruger,20 John A Idoko,21 Chris T Longenecker,22 Suzanne Mbondi,23 Japheth E Mukaya,24 Eugene Mutimura,11 Chiratidzo E Ndhlovu,25 George Praygod,26 Eric W Pefura Yone,27 Mar Pujades-Rodriguez,28,29 Nyagosya Range,26 Mahmoud U Sani,30 Aletta E Schutte,18 Karen Sliwa,31 Phyllis C Tien,32 Este H Vorster,33 Corinna Walsh,34 Rutendo Zinyama,35 Fredirick Mashili,7 Eugene Sobngwi,36,37 Clement Adebamowo,38,39 Anatoli Kamali,3 Janet Seeley,3 Elizabeth H Young,1,2 Liam Smeeth,40 Ayesha A Motala,41 Pontiano Kaleebu,3 Manjinder S Sandhu1,2* and on behalf of the African Partnership for Chronic Disease Research (APCDR).David G Dillon,1Department of Public Health and Primary Care, Institute of Public Health, University of Cambridge, Cambridge, UK,2Genetic Epidemiology Group, Wellcome Trust Sanger Institute, Hinxton, Cambridge, UK,3MRC/UVRI Uganda Research Unit on AIDS, Entebbe, Uganda,4Division of Diabetic Medicine and Endocrinology, Department of Medicine, University of Cape Town, Cape Town, South Africa; Chronic Diseases Initiative in Africa,5Department of Chemical Pathology, National Health Laboratory Service, University of the Witwatersrand Medical School, Johannesburg, South Africa,6Malawi-Liverpool-Wellcome Trust Clinical Research Programme, Blantyre, Malawi,7Department of Physiology, Muhimbili University of Health and Allied Sciences, Dar es Salaam, Tanzania,8Department of Medicine, Muhimbili University of Health and Allied Sciences, Dar es Salaam, Tanzania,9Royal Victoria Teaching Hospital, School of Medicine, University of The Gambia, Banjul, The Gambia,10Department of Medicine, Obafemi Awolowo University, Ile Ife, Nigeria,11Women’s Equity in Access to Care &Treatment, Kigali, Rwanda,12HIV-1 Immunopathogenesis Laboratory, Wistar Institute, Philadelphia, PA,13Tuberculosis Research Unit, Department of Medicine, Case Western Reserve University, Cleveland, OH,14Department of Medical and Surgical Sciences, University of Padua, Padua, Italy,15Division of Diabetic Medicine and Endocrinology, Department of Medicine, University of Cape Town, Cape Town, South Africa,16Infectious Diseases Unit, Department of Medicine, Grey’s Hospital, Pietermaritzburg, South Africa,17Department of Clinical Immunology, Aarhus University Hospital, Aarhus, Denmark,18HART (Hypertension in Africa Research Team), North-West University, Potchefstroom, South Africa,19Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark,20Africa Unit for Transdisciplinary Health Research (AUTHeR), North-West University, Potchefstroom, South Africa,21Department of Medicine, Jos University Teaching Hospital, Jos, Nigeria,22University Hospitals Case Medical Center, Cleveland, OH,23German Development Cooperation (GTZ), Yaounde, Cameroon,24Department of Medicine, Makerere University, Kampala, Uganda,25Clinical Epidemiology Resource Training Centre, University of Zimbabwe College of Health Sciences, Harare, Zimbabwe,26National Institute for Medical Research, Dar es Salaam, Tanzania,27Chest Unit of Jamot Hospital, Yaounde, Cameroon,28Epicentre, Médecins Sans Frontie`res, Paris, France,29Clinical Epidemiology Group, Department of Epidemiology and Public Health, University College London, London, UK,30Cardiology Unit, Department of Medicine, Aminu Kano Teaching Hospital, Kano, Nigeria,31Soweto Cardiovascular Research Unit, Chris Hani Baragwanath Hospital, University of the Witwatersrand, Johannesburg, South Africa,32Department of Medicine, University of California, San Francisco, CA, 33Faculty of Health Sciences, North-West University, Potchefstroom, South Africa,34Department of Nutrition and Dietetics, University of the Free State, Bloemfontein, South Africa,35Medical Research Council of Zimbabwe, Department of Medical Laboratory Sciences, University of Zimbabwe, Harare, Zimbabwe,36Faculty of Medicine and Biomedical Sciences, University of Yaounde 1, Yaounde, Cameroon,37Institute of Health and Society, University of Newcastle, Newcastle, UK,38Institute of Human Virology, Abuja, Nigeria,39Department of Epidemiology and Public Health, Institute of Human Virology and Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, MD,40Faculty of Epidemiology and Population Health, London School of Hygiene and Tropical Medicine, London, UK41Department of Diabetes and Endocrinology, Nelson R. Mandela School of Medicine, University of KwaZulu-Natal, Durban, South Africams23@sanger.ac.uk*Corresponding author. International Health Research Group, Department of Public Health and Primary Care, University of Cambridge, Cambridge, UK. E-mail: We apologise for this oversight.


Correction to:Cell Death & Disease10.1038/s41419-018-0970-6, published online 17 September 2018Following publication of this article, the authors realized that there were 1) errors made in the author affiliations and that 2) a typo in a grant number needed to be corrected. The corrected author affiliations and grant numbers are listed below. We apologize for the inconvenience.1,2, Jih-Yang Ko3, Yu-Shan Chen1,2, Huei-Ching Ke1,2, Shin-Long Wu1,2, Chung-Wen Kuo1,2, Feng-Sheng Wang1,2,41) Wei-Shiung Lian1 Core Laboratory for Phenomics and Diagnostic, Kaohsiung Chang Gung Memorial Hospital, Kaohsiung, Taiwan2 Department of Medical Research, Kaohsiung Chang Gung Memorial Hospital, Kaohsiung, Taiwan3 Department of Orthopedic Surgery, Kaohsiung Chang Gung Memorial Hospital, Kaohsiung, Taiwan4 Graduate Institute of Clinical Medical Science, Chang Gung University College of Medicine, Kaohsiung, Taiwan2) In the Acknowledgements section, grant numberCMRPG8H00112 is incorrect. The correct grant number is CMRPG8H0111.This has been corrected in both the PDF and HTML versions of the Article.


Scientific Reports 10.1038/s41598-018-22296-8, published online 07 March 2018Correction to: The original version of this Article contained errors. Affiliations 1 and 3 were incorrectly given as ‘National Oceanography Centre, Southampton, SO14 3ZH, United Kingdom’ and ‘University of Oxford, Department of Zoology, Oxford, OX2 6GG, United Kingdom’ respectively. In addition, an affiliation was omitted, which is now listed as Affiliation 5.Furthermore, the authors of this manuscript were incorrectly affiliated. Lissette Victorero was incorrectly affiliated with ‘National Oceanography Centre, Southampton, SO14 3ZH, United Kingdom’. Katleen Robert was incorrectly affiliated with ‘National Oceanography Centre, Southampton, SO14 3ZH, United Kingdom’. Laura F. Robinson was incorrectly affiliated with ‘University of Oxford, Department of Zoology, Oxford, OX2 6GG, United Kingdom’. Michelle L. Taylor was incorrectly affiliated with ‘University of Bristol, School of Earth Sciences, Bristol, BS8 1RJ, United Kingdom’. Veerle A.I. Huvenne was incorrectly affiliated with ‘University of Southampton, Ocean and Earth Science, Southampton, SO14 3ZH, United Kingdom’.The correct affiliations list and affiliated authors are given below.Affiliation 1:National Oceanography Centre, University of Southampton Waterfront Campus, Southampton, SO14 3ZH, United KingdomLissette VictoreroKatleen RobertVeerle A.I. HuvenneAffiliation 2:University of Southampton, Ocean and Earth Science, Southampton, SO14 3ZH, United KingdomLissette VictoreroAffiliation 3:Fisheries and Marine Institute of Memorial University, St. John’s, NL A1C 5R3, CanadaKatleen RobertAffiliation 4:University of Bristol, School of Earth Sciences, Bristol, BS8 1RJ, United KingdomLaura F. RobinsonAffiliation 5:University of Essex, School of Biological Sciences, Colchester, CO4 3SQ, United KingdomMichelle L. TaylorThese errors have now been corrected in the PDF and HTML versions of the paper, and in the accompanying Supplementary information file.


Brain, awy358, https://doi.org/10.1093/brain/awy358.Peter Rudge, Zane Jaunmuktane, Harpreet Hyare, Matthew Ellis, Martin Koltzenburg, John Collinge, Sebastian Brandner, Simon Mead. Early neurophysiological biomarkers and spinal cord pathology in inherited prion disease. The authors would like to apologise for two of the authors' affiliations being listed incorrectly in the original manuscript, they are listed correctly below:1,2 and Simon Mead1,2John Collinge1 National Prion Clinic, National Hospital for Neurology and Neurosurgery, University College London Hospitals NHS Foundation Trust (UCLH), London, UK 2 MRC Prion Unit at UCL, Institute of Prion Diseases, 33 Cleveland St. London, W1W 7FF, UKThe manuscript has been corrected online.


The affiliations should be as follows:In “Control of the HIV-1 Load Varies by Viral Subtype in a Large Cohort of African Adults With Incident HIV-1 Infection” by Matt A. Price et al [J Infect Dis 2019; 9,15,16,17, Paramesh Chetty,1,14Vinodh A. Edward,1International AIDS Vaccine Initiative, New York, New York;9Department of Environmental Health Sciences, Yale School of Public Health, New Haven, Connecticut;14School of Pathology, Faculty of Health Sciences, University of the Witwatersrand, and15Advancing Care and Treatment for TB/HIV, South African Medical Research Council, Johannesburg, and16Desmond Tutu HIV Foundation, Cape Town, South Africa17Advancing Care and Treatment for TB/HIV, South African Medical Research Council, Johannesburg.