Publications
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“ Prevalence and genotype distribution of human papillomavirus in women in the Henan Province”, vol. 14, pp. 5452-5461, 2015.
, “Bottom-up assembly of RNA nanoparticles containing phi29 motor pRNA to silence the asthma STAT5b gene”, vol. 11, pp. 3236-3245, 2012.
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Castanotto D and Rossi JJ (2009). The promises and pitfalls of RNA-interference-based therapeutics. Nature 457: 426-433.
http://dx.doi.org/10.1038/nature07758
PMid:19158789 PMCid:2702667
Chen C, Sheng S, Shao Z and Guo P (2000). A dimer as a building block in assembling RNA. A hexamer that gears bacterial virus phi29 DNA-translocating machinery. J. Biol. Chem. 275: 17510-17516.
http://dx.doi.org/10.1074/jbc.M909662199
PMid:10748150
Dorsett Y and Tuschl T (2004). siRNAs: applications in functional genomics and potential as therapeutics. Nat. Rev. Drug. Discov. 3: 318-329.
http://dx.doi.org/10.1038/nrd1345
PMid:15060527
Elbashir SM, Lendeckel W and Tuschl T (2001). RNA interference is mediated by 21- and 22-nucleotide RNAs. Genes Dev. 15: 188-200.
http://dx.doi.org/10.1101/gad.862301
PMid:11157775 PMCid:312613
Guo P (2010). The emerging field of RNA nanotechnology. Nat. Nanotechnol. 5: 833-842.
http://dx.doi.org/10.1038/nnano.2010.231
PMid:21102465 PMCid:3149862
Guo S, Tschammer N, Mohammed S and Guo P (2005). Specific delivery of therapeutic RNAs to cancer cells via the dimerization mechanism of phi29 motor pRNA. Hum. Gene Ther. 16: 1097-1109.
http://dx.doi.org/10.1089/hum.2005.16.1097
PMid:16149908 PMCid:2837361
Kraus E, James W and Barclay AN (1998). Cutting edge: novel RNA ligands able to bind CD4 antigen and inhibit CD4+ T lymphocyte function. J. Immunol. 160: 5209-5212.
PMid:9605115
Lee TJ, Schwartz C and Guo P (2009). Construction of bacteriophage phi29 DNA packaging motor and its applications in nanotechnology and therapy. Ann. Biomed. Eng. 37: 2064-2081.
http://dx.doi.org/10.1007/s10439-009-9723-0
PMid:19495981 PMCid:2855900
Maes T, Tournoy KG and Joos GF (2011). Gene therapy for allergic airway diseases. Curr. Allergy Asthma Rep. 11: 163-172.
http://dx.doi.org/10.1007/s11882-011-0177-8
PMid:21243453
North ML, Khanna N, Marsden PA, Grasemann H, et al. (2009). Functionally important role for arginase 1 in the airway hyperresponsiveness of asthma. Am. J. Physiol. Lung Cell Mol. Physiol. 296: L911-L920.
http://dx.doi.org/10.1152/ajplung.00025.2009
PMid:19286931
Shu D, Huang LP, Hoeprich S and Guo P (2003). Construction of phi29 DNA-packaging RNA monomers, dimers, and trimers with variable sizes and shapes as potential parts for nanodevices. J. Nanosci. Nanotechnol. 3: 295-302.
http://dx.doi.org/10.1166/jnn.2003.160
PMid:14598442
Shu D, Moll WD, Deng Z, Mao C, et al. (2004). Bottom-up Assembly of RNA Arrays and Superstructures as Potential Parts in Nanotechnology. Nano Lett. 4: 1717-1723.
http://dx.doi.org/10.1021/nl0494497
PMid:21171616 PMCid:3010238
Shu Y, Shu D, Diao Z, Shen G, et al. (2009). Fabrication of Polyvalent Therapeutic RNA Nanoparticles for Specific Delivery of siRNA, Ribozyme and Drugs to Targeted Cells for Cancer Therapy. IEEE NIH Life Sci. Syst. Appl. Workshop 2009: 9-12.
Tarapore P, Shu Y, Guo P and Ho SM (2011). Application of phi29 motor pRNA for targeted therapeutic delivery of siRNA silencing metallothionein-IIA and survivin in ovarian cancers. Mol. Ther. 19: 386-394.
http://dx.doi.org/10.1038/mt.2010.243
PMid:21063391 PMCid:3034850
Zhang HM, Su Y, Guo S, Yuan J, et al. (2009). Targeted delivery of anti-coxsackievirus siRNAs using ligand-conjugated packaging RNAs. Antiviral Res. 83: 307-316.
http://dx.doi.org/10.1016/j.antiviral.2009.07.005
PMid:19616030
Zhou J, Shu Y, Guo P, Smith DD, et al. (2011). Dual functional RNA nanoparticles containing phi29 motor pRNA and anti-gp120 aptamer for cell-type specific delivery and HIV-1 inhibition. Methods 54: 284-294.
http://dx.doi.org/10.1016/j.ymeth.2010.12.039
PMid:21256218 PMCid:3107903
Zhu J (2010). Transcriptional regulation of Th2 cell differentiation. Immunol. Cell Biol. 88: 244-249.
http://dx.doi.org/10.1038/icb.2009.114
PMid:20065998 PMCid:3477614
Zhu J, Cote-Sierra J, Guo L and Paul WE (2003). Stat5 activation plays a critical role in Th2 differentiation. Immunity 19: 739-748.
http://dx.doi.org/10.1016/S1074-7613(03)00292-9
“Molecular cloning and functional characterization of a mouse ccl6 analog gene in the rat”, vol. 11, pp. 3889-3898, 2012.
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Aarvak T, Chabaud M, Kallberg E, Miossec P, et al. (1999). Change in the Th1/Th2 phenotype of memory T-cell clones from rheumatoid arthritis synovium. Scand. J. Immunol. 50: 1-9.
http://dx.doi.org/10.1046/j.1365-3083.1999.00581.x
PMid:10404044
Belperio JA, Dy M, Burdick MD, Xue YY, et al. (2002). Interaction of IL-13 and C10 in the pathogenesis of bleomycin-induced pulmonary fibrosis. Am. J. Respir. Cell Mol. Biol. 27: 419-427.
PMid:12356575
Berger MS, Kozak CA, Gabriel A and Prystowsky MB (1993). The gene for C10, a member of the beta-chemokine family, is located on mouse chromosome 11 and contains a novel second exon not found in other chemokines. DNA Cell Biol. 12: 839-847.
http://dx.doi.org/10.1089/dna.1993.12.839
PMid:8216854
Gerard C and Rollins BJ (2001). Chemokines and disease. Nat. Immunol. 2: 108-115.
http://dx.doi.org/10.1038/84209
PMid:11175802
Han W, Lou Y, Tang J, Zhang Y, et al. (2001a). Molecular cloning and characterization of chemokine-like factor 1 (CKLF1), a novel human cytokine with unique structure and potential chemotactic activity. Biochem. J. 357: 127-135.
http://dx.doi.org/10.1042/0264-6021:3570127
PMid:11415443 PMCid:1221935
Han WL, Rui M, Zhang YM, Chen YY, et al. (2001b). Stimulatory effect of chemokine-like factor 1 (CKLF1) on the growth of bone marrow cells. Zhongguo Yi Xue Ke Xue Yuan Xue Bao 23: 119-122.
PMid:12905885
Ikadai H, Xuan X, Igarashi I, Tanaka S, et al. (1999). Cloning and expression of a 48-kilodalton Babesia caballi merozoite rhoptry protein and potential use of the recombinant antigen in an enzyme-linked immunosorbent assay. J. Clin. Microbiol. 37: 3475-3480.
PMid:10523537 PMCid:85671
Kaesler S, Regenbogen J, Durka S, Goppelt A, et al. (2002). The healing skin wound: a novel site of action of the chemokine C10. Cytokine 17: 157-163.
http://dx.doi.org/10.1006/cyto.2001.0981
PMid:11895334
Li QJ, Lu S, Ye RD and Martins-Green M (2000). Isolation and characterization of a new chemokine receptor gene, the putative chicken CXCR1. Gene 257: 307-317.
http://dx.doi.org/10.1016/S0378-1119(00)00385-1
Lou Y, Xia D, Han W, Wang Y, et al. (2003). Molecular cloning and characterization of rat chemokine-like factor 1 and 2. Gene 307: 125-132.
http://dx.doi.org/10.1016/S0378-1119(03)00450-5
Nielsen H, Brunak S and von Heijne G (1999). Machine learning approaches for the prediction of signal peptides and other protein sorting signals. Protein Eng. 12: 3-9.
http://dx.doi.org/10.1093/protein/12.1.3
PMid:10065704
Olson TS and Ley K (2002). Chemokines and chemokine receptors in leukocyte trafficking. Am. J. Physiol. Regul. Integr. Comp Physiol. 283: R7-28.
PMid:12069927
Orlofsky A, Berger MS and Prystowsky MB (1991). Novel expression pattern of a new member of the MIP-1 family of cytokine-like genes. Cell Regul. 2: 403-412.
PMid:1832565 PMCid:361810
Orlofsky A, Lin EY and Prystowsky MB (1994). Selective induction of the beta chemokine C10 by IL-4 in mouse macrophages. J. Immunol. 152: 5084-5091.
PMid:8176224
Orlofsky A, Wu Y and Prystowsky MB (2000). Divergent regulation of the murine CC chemokine C10 by Th(1) and Th(2) cytokines. Cytokine 12: 220-228.
http://dx.doi.org/10.1006/cyto.1999.0535
PMid:10704248
Petrenko O, Ischenko I and Enrietto PJ (1995). Isolation of a cDNA encoding a novel chicken chemokine homologous to mammalian macrophage inflammatory protein-1 beta. Gene 160: 305-306.
http://dx.doi.org/10.1016/0378-1119(95)00210-W
Sarafi MN, Garcia-Zepeda EA, MacLean JA, Charo IF, et al. (1997). Murine monocyte chemoattractant protein (MCP)-5: a novel CC chemokine that is a structural and functional homologue of human MCP-1. J. Exp. Med. 185: 99-109.
http://dx.doi.org/10.1084/jem.185.1.99
PMid:8996246 PMCid:2196097
Steinhauser ML, Hogaboam CM, Matsukawa A, Lukacs NW, et al. (2000). Chemokine C10 promotes disease resolution and survival in an experimental model of bacterial sepsis. Infect. Immun. 68: 6108-6114.
http://dx.doi.org/10.1128/IAI.68.11.6108-6114.2000
PMid:11035713 PMCid:97687
Williamson PT, Roth JF, Haddingham T and Watts A (2000). Expression and purification of recombinant neurotensin in Escherichia coli. Protein Expr. Purif. 19: 271-275.
http://dx.doi.org/10.1006/prep.2000.1246
PMid:10873541