FHL1 is a significant host issue of chikungunya virus an infection
Burt, F.J. et al. Chikungunya virus: an replace on the biology and pathogenesis of this rising pathogen. Lancet Infect. Dis. 17, e107 to e117 (2017).
Silva, L.A. & Dermody, T.S. Chikungunya virus: Epidemiology, Replication, Mechanisms of Illness and Methods for Potential Intervention. J. Clin. Make investments. 127, 737-749 (2017).
Greene, W.Ok., Baker, E., Rabbitts, T.H. & Kees, U. Genomic construction, tissue expression and chromosomal localization of the only gene at LIM, SLIM1. Gene 232, 203-207 (1999).
Schessl, J., Feldkirchner, S., Kubny, C. and Schoser, B. Discount of Physique Myopathy and Different Muscle Problems Related to FHL1. Semin. Pediatr. Neurol. 18, 257-263 (2011).
Gueneau, L. et al. Mutations within the FHL1 gene are on the origin of Emery – Dreifuss muscular dystrophy. A m. J. Hum. Broom. 85, 338-353 (2009).
Ooi, Y.S., Stiles, Ok.M., Liu, C.Y., Taylor, G.M. & Kielian, M .. PLoS Pathog. 9, e1003835 (2013).
Karlas, A. et al. A loss-of-function screening on the human genome scale identifies efficient chikungunya antiviral medication. Nat. Widespread. 7, 11320 (2016).
Zhang, R. et al. Mxra8 is a receptor for a number of arthritogenic alphaviruses. Nature 557, 570-574 (2018).
Tanaka, A. et al. Scaling genome screening reveals the significance of N-sulfation of heparan sulfate as a number cell issue for an infection with Chikungunya virus. J. Virol. 91, 1-22 (2017).
Schuffenecker, I. et al. Microevolution of the genome of chikungunya viruses on the origin of the hatching of the Indian Ocean. PLoS Med. three, e263 (2006).
Shathasivam, T., Kislinger, T. and Gramolini, A. O. Genes, proteins and complexes: the multiform nature of proteins of the FHL household in varied tissues. J. Cell. Mol. Med. 14, 2702-2720 (2010).
Brown, S. et al. Characterization of two isoforms of skeletal muscle Protein LIM 1, SLIM1. The localization of SLIM1 at focal adhesions and the thinner isoform within the nucleus of myoblasts and the cytoplasm of myotubes counsel distinct roles within the cytoskeleton and in nuclear-cytoplasmic communication. J. Biol. Chem. 274, 27083-2701 (1999).
Krempler, A., Kollers, S., Fries, R. and Brenig, B. Isolation and characterization of a brand new variant of FHL1 (FHL1C) derived from porcine skeletal muscle. Cytogenet. Cell Genet. 90, 106-114 (2000).
Pen, A.E. et al. A brand new mutation of a single nucleotide splice web site in FHL1 confirms an Emery – Dreifuss plus phenotype with hypoplasia of the pulmonary artery and facial dysmorphology. EUR. J. Med. Broom. 58, 222-222 (2015).
Chan, Ok.Ok. et al. Molecular cloning and characterization of FHL2, a brand new LIM area protein expressed preferentially within the human coronary heart. Gene 210, 345-350 (1998).
Couderc, T. et al. A mouse mannequin for chikungunya: younger age and ineffective signaling of sort I interferon are threat elements for critical sickness. PLoS Pathog. four, e29 (2008).
Roberts, G.C. et al. Analysis of a spread of mammalian cell traces and mosquitoes to be used in Chikungunya virus analysis. Sci. Rep. 7, 14641 (2017).
Kim, D. Y. et al. New and Outdated World Alphaviruses have developed to use totally different elements of stress granules, FXR and G3BP, to assemble viral replication complexes. PLoS Pathog. 12, e1005810 (2016).
Jose, J., Taylor, B. and Kuhn, R. J. Spatial and temporal evaluation of replication and meeting of alphaviruses in mammalian and mosquito cells. mBio eight, e02294-16 (2017).
Götte, B., Liu, L. and McInerney, G. M. The enigmatic alphavirus three non-structural protein (nsP3) lastly reveals its secrets and techniques. Viruses 10, 105 (2018).
Meshram, C.D. et al. A number of host elements work together with the hypervariable area of chikungunya virus nsP3 and decide viral replication in cell – particular mode. J. Virol. 92, e00838-18 (2018).
Mutso, M. et al. The mutation of the CD2AP and SH3KBP1 binding motif within the hypervariable area of alphavirus nsP3 leads to attenuation of the virus. Viruses 10, 226 (2018).
Scholte, F.E.M. et al. The elements of the stress granules G3BP1 and G3BP2 play an early proviral function within the replication of the chikungunya virus. J. Virol. 89, 4457-4469 (2015).
Schessl, J. et al. Proteomic identification of FHL1 as a mutated protein in reductive myopathy in people. J. Clin. Make investments. 118, 904-912 (2008).
Bonne, G., Leturcq, F. and Ben Yaou, R. in GeneReviews (Adam eds, M.P. et al.) (College of Washington, 1993).
Medina, F. et al. Dengue virus: isolation, propagation, quantification and storage. Curr. Protoc. Microbiol. 15, 15D.2.1-15D.2.24 (2012).
Meertens, L. et al. The TIM and TAM households of phosphatidylserine receptors facilitate entry of the dengue virus. Cell Host Microbe 12, 544-557 (2012).
Shalem, O. et al. Screening CRISPR – Cas9 on the genome scale in human cells. Science 343, 84-87 (2014).
Li, W. et al. MAGeCK permits the sturdy identification of important genes from genome-wide CRISPR / Cas9 inactivation screens. Genome Biol. 15, 554 (2014).
Joung, J. et al. Screening for the activation of the CRISPR – Cas9 gene on the genome stage and screening for transcription activation. Nat. Protoc. 12, 828-863 (2017).
Pellet, J. et al. ViralORFeome: an built-in database for producing a flexible assortment of viral ORFs. Nucleic Acids Res. 38, D371 to D378 (2010).
Gläsker, S. et al. Neutralization check of chikungunya virus primarily based on virus replicon particles utilizing Gaussia luciferase as studying. Virol. J. 10, 235 (2013).
Kümmerer, B., Grywna, Ok., Gläsker, S., Wieseler, J. and Drosten, C. Development of an infectious chikungunya virus cDNA clone and secure insertion of mCherry reporter genes on two totally different websites. J. Gen. Virol. 93, 1991-1995 (2012).
Plaskon, N.E., Adelman, Z.N. & Myles, Ok. M. Exact quantization by particular strand of viral RNA. PLoS ONE four, e7468 (2009).
Domenighetti, A.A. et al. Lack of FHL1 induces age-related skeletal muscle myopathy related to myofibrillar and intermyofibrillar disorganization in mice. Hum. Mol. Broom. 23, 209-225 (2014).