Form 4 4 Minus 4 The Reasons Why We Love Form 4 4 Minus 4
Kennedy, L. et al. Dramatic tissue-specific alteration breadth increases are an aboriginal atomic accident in Huntington ache pathogenesis. Hum. Mol. Genet. 12, 3359–3367 (2003).
Lopez Castel, A., Cleary, J. D. & Pearson, C. E. Echo alternation as the abject for animal diseases and as a abeyant ambition for therapy. Nat. Rev. Mol. Corpuscle Biol. 11, 165–170 (2010).
Mirkin, S. M. Expandable DNA repeats and animal disease. Nature 447, 932–940 (2007).
Pearson, C. E., Nichol Edamura, K. & Cleary, J. D. Echo instability: mechanisms of activating mutations. Nat. Rev. Genet. 6, 729–742 (2005).
Sathasivam, K., Amaechi, I., Mangiarini, L. & Bates, G. Identification of an HD accommodating with a (CAG)180 echo amplification and the advancement of awful broadcast CAG repeats in lambda phage. Hum. Genet. 99, 692–695 (1997).
Morales, F. et al. Actual alternation of the broadcast CTG leash echo in myotonic dystrophy blazon 1 is a ancestral quantitative affection and modifier of ache severity. Hum. Mol. Genet. 21, 3558–3567 (2012).
Swami, M. et al. Actual amplification of the Huntington’s ache CAG echo in the academician is associated with an beforehand age of ache onset. Hum. Mol. Genet. 18, 3039–3047 (2009).
Bettencourt, C. et al. DNA adjustment pathways underlie a accepted abiogenetic apparatus modulating access in polyglutamine diseases. Ann. Neurol. 79, 983–990 (2016).
Genetic Modifiers of Huntington’s Ache Consortium Identification of abiogenetic factors that adapt analytic access of Huntington’s disease. Corpuscle 162, 516–526 (2015).
Genetic Modifiers of Huntington’s Ache (GeM-HD) Consortium. CAG echo not polyglutamine breadth determines timing of Huntington’s ache onset. Corpuscle 178, 887–900.e14 (2019).
Hensman Moss, D. J. et al. Identification of abiogenetic variants associated with Huntington’s ache progression: a genome-wide affiliation study. Lancet Neurol. 16, 701–711 (2017).
Gusella, J. F. & MacDonald, M. E. Atomic genetics: apprehension polyglutamine triggers in neurodegenerative disease. Nat. Rev. Neurosci. 1, 109–115 (2000).
Rosenblatt, A. et al. Age, CAG echo length, and analytic progression in Huntington’s disease. Mov. Disord. 27, 272–276 (2012).
Axford, M. M. et al. Apprehension of slipped-DNAs at the trinucleotide repeats of the myotonic dystrophy blazon I ache locus in accommodating tissues. PLoS Genet. 9, e1003866 (2013).
Goula, A. V. et al. Stoichiometry of abject abatement adjustment proteins correlates with added actual CAG alternation in striatum over cerebellum in Huntington’s ache transgenic mice. PLoS Genet. 5, e1000749 (2009).
Lin, Y., Dent, S. Y., Wilson, J. H., Wells, R. D. & Napierala, M. R loops activate abiogenetic alternation of CTG·CAG repeats. Proc. Natl Acad. Sci. USA 107, 692–697 (2010).
Pearson, C. E. et al. Slipped-strand DNAs formed by continued (CAG)·(CTG) repeats: slipped-out repeats and slip-out junctions. Nucleic Acids Res. 30, 4534–4547 (2002).
Reddy, K. et al. Processing of double-R-loops in (CAG)·(CTG) and C9orf72 (GGGGCC)·(GGCCCC) repeats causes instability. Nucleic Acids Res. 42, 10473–10487 (2014).
Schmidt, M. H. & Pearson, C. E. Disease-associated echo alternation and conflict repair. DNA Adjustment 38, 117–126 (2016).
Tome, S. et al. Msh3 polymorphisms and protein levels affect CAG echo alternation in Huntington’s ache mice. PLoS Genet. 9, e1003280 (2013).
Nakamori, M., Pearson, C. E. & Thornton, C. A. Bidirectional archetype stimulates amplification and abbreviating of broadcast (CTG)·(CAG) repeats. Hum. Mol. Genet. 20, 580–588 (2011).
Lin, Y. & Wilson, J. H. Nucleotide abatement repair, conflict repair, and R-loops attune allied transcription-induced corpuscle afterlife and echo instability. PLoS ONE 7, e46807 (2012).
Panigrahi, G. B., Slean, M. M., Simard, J. P., Gileadi, O. & Pearson, C. E. Abandoned abbreviate CTG/CAG DNA slip-outs are repaired calmly by hMutSβ, but amassed slip-outs are ailing repaired. Proc. Natl Acad. Sci. USA 107, 12593–12598 (2010).
Hagihara, M. & Nakatani, K. Inhibition of DNA archetype by a d(CAG) echo bounden ligand. Nucleic Acids Symp. Ser. 50, 147–148 (2006).
Hagihara, M., He, H. & Nakatani, K. Baby atom modulates ambit structures in CAG trinucleotide repeats. ChemBioChem 12, 1686–1689 (2011).
Nakatani, K. et al. Small-molecule ligand induces nucleotide flipping in (CAG)n trinucleotide repeats. Nat. Chem. Biol. 1, 39–43 (2005).
Nielsen, P. E., Zhen, W. P., Henriksen, U. & Buchardt, O. Sequence-influenced interactions of oligoacridines with DNA detected by backward gel electrophoretic migrations. Biochemistry 27, 67–73 (1988).
Pluciennik, A. et al. Extrahelical (CAG)/(CTG) leash echo elements abutment proliferating corpuscle nuclear antigen loading and MutLα endonuclease activation. Proc. Natl Acad. Sci. USA 110, 12277–12282 (2013).
Shelbourne, P. F. et al. Leash echo alteration breadth assets associate with cell-type specific vulnerability in Huntington ache brain. Hum. Mol. Genet. 16, 1133–1142 (2007).
Silveira, I. et al. Trinucleotide repeats in 202 families with ataxia: a baby broadcast (CAG)n allele at the SCA17 locus. Arch. Neurol. 59, 623–629 (2002).
Sanchez-Contreras, M. & Cardozo-Pelaez, F. Age-related breadth airheadedness of polymorphic CAG repeats. DNA Adjustment 49, 26–32 (2017).
Gao, R. et al. Alternation of broadcast CAG/CAA repeats in spinocerebellar anarchy blazon 17. Eur. J. Hum. Genet. 16, 215–222 (2008).
Gallon, R. et al. A acute and scalable microsatellite alternation appraisal to analyze built-in conflict adjustment absence by sequencing of borderline claret leukocytes. Hum. Mutat. 40, 649–655 (2019).
Keohavong, P., Xi, L. & Grant, S. G. Atomic assay of mutations in the animal HPRT gene. Methods Mol. Biol. 291, 161–170 (2005).
Keohavong, P., Xi, L. & Grant, S. G. Atomic assay of mutations in the animal HPRT gene. Methods Mol. Biol. 1105, 291–301 (2014).
Albertini, R. J. et al. Mutagenicity ecology afterward battlefield exposures: longitudinal abstraction of HPRT mutations in Gulf War I veterans apparent to depleted uranium. Environ. Mol. Mutagen. 56, 581–593 (2015).
Nicklas, J. A. et al. Mutagenicity ecology afterward battlefield exposures: atomic assay of HPRT mutations in Gulf War I veterans apparent to depleted uranium. Environ. Mol. Mutagen. 56, 594–608 (2015).
Poon, S. L., McPherson, J. R., Tan, P., Teh, B. T. & Rozen, S. G. Alteration signatures of carcinogen exposure: genome-wide apprehension and new opportunities for blight prevention. Genome Med. 6, 24 (2014).
Behjati, S. et al. Mutational signatures of ionizing radiation in additional malignancies. Nat. Commun. 7, 12605 (2016).
Phillips, D. H. Mutational spectra and mutational signatures: insights into blight aetiology and mechanisms of DNA accident and repair. DNA Adjustment 71, 6–11 (2018).
Alexandrov, L. B. et al. The repertoire of mutational signatures in animal cancer. Preprint at bioRxiv https://doi.org/10.1101/322859 (2019).
Kucab, J. E. et al. A abstract of mutational signatures of ecology agents. Corpuscle 177, 821–836.e16 (2019).
Behjati, S. et al. Genome sequencing of accustomed beef reveals adorning lineages and mutational processes. Nature 513, 422–425 (2014).
Rouhani, F. J. et al. Mutational history of a animal corpuscle birth from actual to induced pluripotent axis cells. PLoS Genet. 12, e1005932 (2016).
Shlien, A. et al. Combined ancestral and actual mutations of archetype absurdity adjustment genes aftereffect in accelerated access of ultra-hypermutated cancers. Nat. Genet. 47, 257–262 (2015).
Chalmers, Z. R. et al. Assay of 100,000 animal blight genomes reveals the mural of bump mutational burden. Genome Med. 9, 34 (2017).
Campbell, B. B. et al. Comprehensive assay of hypermutation in animal cancer. Corpuscle 171, 1042–1056.e10 (2017).
Hodel, K. P. et al. Explosive alteration accession triggered by heterozygous animal Pol epsilon proofreading-deficiency is apprenticed by abolishment of conflict repair. eLife 7, e32692 (2018).
Rayner, E. et al. A accoutrements of errors: polymerase proofreading area mutations in cancer. Nat. Rev. Blight 16, 71–81 (2016).
Nakamori, M., Gourdon, G. & Thornton, C. A. Stabilization of broadcast (CTG)·(CAG) repeats by antisense oligonucleotides. Mol. Ther. 19, 2222–2227 (2011).
Su, X. A. & Freudenreich, C. H. Cytosine deamination and abject abatement adjustment account R-loop-induced CAG echo airiness and alternation in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 114, E8392–E8401 (2017).
Lin, Y., Hubert, L. Jr. & Wilson, J. H. Archetype destabilizes leash repeats. Mol. Carcinog. 48, 350–361 (2009).
Tomé, S. et al. MSH2 ATPase area alteration affects CTG·CAG echo alternation in transgenic mice. PLoS Genet. 5, e1000482 (2009).
McMurray, C. T. Hijacking of the conflict adjustment arrangement to account CAG amplification and corpuscle afterlife in neurodegenerative disease. DNA Adjustment 7, 1121–1134 (2008).
Morales, F. et al. A polymorphism in the MSH3 conflict adjustment gene is associated with the levels of actual alternation of the broadcast CTG echo in the claret DNA of myotonic dystrophy blazon 1 patients. DNA Adjustment 40, 57–66 (2016).
Flower, M. et al. MSH3 modifies actual alternation and ache severity in Huntington’s and myotonic dystrophy blazon 1. Academician 142, 1876–1886 (2019).
Panigrahi, G. B., Lau, R., Montgomery, S. E., Leonard, M. R. & Pearson, C. E. Slipped (CTG)*(CAG) repeats can be accurately repaired, escape adjustment or abide error-prone repair. Nat. Struct. Mol. Biol. 12, 654–662 (2005).
Zhang, T., Huang, J., Gu, L. & Li, G. M. In vitro adjustment of DNA hairpins absolute assorted numbers of CAG/CTG trinucleotide repeats. DNA Adjustment 11, 201–209 (2012).
Lai, Y. et al. Crosstalk amid MSH2–MSH3 and polβ promotes trinucleotide echo amplification during abject abatement repair. Nat. Commun. 7, 12465 (2016).
Tian, L. et al. Conflict acceptance protein MutSβ does not annex (CAG)n ambit adjustment in vitro. J. Biol. Chem. 284, 20452–20456 (2009).
Nakatani, R., Nakamori, M., Fujimura, H., Mochizuki, H. & Takahashi, M. P. Ample amplification of CTG·CAG repeats is affronted by MutSβ in animal cells. Sci. Rep. 5, 11020 (2015).
Chen, H., Lisby, M. & Symington, L. S. RPA coordinates DNA end resection and prevents accession of DNA hairpins. Mol. Corpuscle 50, 589–600 (2013).
Nguyen, B. et al. Diffusion of animal archetype protein A forth single-stranded DNA. J. Mol. Biol. 426, 3246–3261 (2014).
Tsurimoto, T. & Stillman, B. Assorted archetype factors augment DNA amalgam by the two eukaryotic DNA polymerases, alpha and delta. EMBO J. 8, 3883–3889 (1989).
Tsurimoto, T. & Stillman, B. Archetype factors appropriate for SV40 DNA archetype in vitro. I. DNA structure-specific acceptance of a primer–template alliance by eukaryotic DNA polymerases and their accent proteins. J. Biol. Chem. 266, 1950–1960 (1991).
Chan, N. L. et al. The Werner affection protein promotes CAG/CTG echo adherence by absolute ample (CAG)n/(CTG)n hairpins. J. Biol. Chem. 287, 30151–30156 (2012).
Callahan, J. L., Andrews, K. J., Zakian, V. A. & Freudenreich, C. H. Mutations in aggrandize archetype proteins that access CAG/CTG expansions additionally access echo fragility. Mol. Cell. Biol. 23, 7849–7860 (2003).
Raji, N. S., Krishna, T. H. & Rao, K. S. DNA-polymerase α, β, Δ and ε activities in abandoned neuronal and astroglial corpuscle fractions from developing and crumbling rat bookish cortex. Int. J. Dev. Neurosci. 20, 491–496 (2002).
Kovalenko, M. et al. Msh2 acts in medium-spiny striatal neurons as an enhancer of CAG alternation and aberrant huntingtin phenotypes in Huntington’s ache knock-in mice. PLoS ONE 7, e44273 (2012).
Mangiarini, L. et al. Alternation of awful broadcast CAG repeats in mice transgenic for the Huntington’s ache mutation. Nat. Genet. 15, 197–200 (1997).
Chiang, C. et al. Complex about-face and absolute non-homologous adjustment afterward chromosomal accident in karyotypically counterbalanced germline rearrangements and transgenic integration. Nat. Genet. 44, 390–397 (2012).
Larson, E., Fyfe, I., Morton, A. J. & Monckton, D. G. Age-, tissue- and length-dependent bidirectional actual CAG·CTG echo alternation in an allelic alternation of R6/2 Huntington ache mice. Neurobiol. Dis. 76, 98–111 (2015).
Kennedy, L. & Shelbourne, P. F. Dramatic alteration alternation in HD abrasion striatum: does polyglutamine amount accord to cell-specific vulnerability in Huntington’s disease? Hum. Mol. Genet. 9, 2539–2544 (2000).
Ishiguro, H. et al. Age-dependent and tissue-specific CAG echo alternation occurs in abrasion knock-in for a aberrant Huntington’s ache gene. J. Neurosci. Res. 65, 289–297 (2001).
Gonitel, R. et al. DNA alternation in postmitotic neurons. Proc. Natl Acad. Sci. USA 105, 3467–3472 (2008).
De Rooij, K. E., De Koning Gans, P. A., Roos, R. A., Van Ommen, G. J. & Den Dunnen, J. T. Actual amplification of the (CAG)n echo in Huntington ache brains. Hum. Genet. 95, 270–274 (1995).
Lee, J. M., Pinto, R. M., Gillis, T., St Claire, J. C. & Wheeler, V. C. Quantification of age-dependent actual CAG echo alternation in Hdh CAG knock-in mice reveals altered amplification dynamics in striatum and liver. PLoS ONE 6, e23647 (2011).
Lee, J. M. et al. A atypical access to investigate tissue-specific trinucleotide echo instability. BMC Syst. Biol. 4, 29 (2010).
Wheeler, V. C. et al. Factors associated with HD CAG echo alternation in Huntington disease. J. Med. Genet. 44, 695–701 (2007).
Higham, C. F., Morales, F., Cobbold, C. A., Haydon, D. T. & Monckton, D. G. High levels of actual DNA assortment at the myotonic dystrophy blazon 1 locus are apprenticed by ultra-frequent amplification and abbreviating mutations. Hum. Mol. Genet. 21, 2450–2463 (2012).
Veitch, N. J. et al. Inherited CAG.CTG allele breadth is a above modifier of actual alteration breadth airheadedness in Huntington disease. DNA Adjustment 6, 789–796 (2007).
Hornsby, P. J. & Didenko, V. V. In situ ligation: a decade and a bisected of experience. Methods Mol. Biol. 682, 49–63 (2011).
Majtnerova, P. & Rousar, T. An overview of apoptosis assays audition DNA fragmentation. Mol. Biol. Rep. 45, 1469–1478 (2018).
Iannicola, C. et al. Aboriginal alterations in gene announcement and corpuscle assay in a abrasion archetypal of Huntington’s disease. J. Neurochem. 75, 830–839 (2000).
Turmaine, M. et al. Nonapoptotic neurodegeneration in a transgenic abrasion archetypal of Huntington’s disease. Proc. Natl Acad. Sci. USA 97, 8093–8097 (2000).
Yu, Z. X. et al. Aberrant huntingtin causes context-dependent neurodegeneration in mice with Huntington’s disease. J. Neurosci. 23, 2193–2202 (2003).
DiFiglia, M. et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277, 1990–1993 (1997).
Li, S. H. & Li, X. J. Aggregation of N-terminal huntingtin is abased on the breadth of its glutamine repeats. Hum. Mol. Genet. 7, 777–782 (1998).
Becher, M. W. et al. Intranuclear neuronal inclusions in Huntington’s ache and dentatorubral and pallidoluysian atrophy: alternation amid the body of inclusions and IT15 CAG leash echo length. Neurobiol. Dis. 4, 387–397 (1998).
Li, H. et al. Ultrastructural localization and accelerating accession of neuropil aggregates in Huntington’s ache transgenic mice. Hum. Mol. Genet. 8, 1227–1236 (1999).
Li, H., Li, S. H., Johnston, H., Shelbourne, P. F. & Li, X. J. Amino-terminal bits of aberrant huntingtin appearance careful accession in striatal neurons and synaptic toxicity. Nat. Genet. 25, 385–389 (2000).
Carty, N. et al. Characterization of HTT admittance size, location, and timing in the zQ175 abrasion archetypal of Huntington’s disease: an in vivo high-content imaging study. PLoS ONE 10, e0123527 (2015).
Kaytor, M. D., Wilkinson, K. D. & Warren, S. T. Modulating huntingtin half-life alters polyglutamine-dependent accumulated accession and corpuscle toxicity. J. Neurochem. 89, 962–973 (2004).
Coufal, M. et al. Discovery of a atypical small-molecule targeting careful approval of aberrant huntingtin fragments. J. Biomol. Screen. 12, 351–360 (2007).
Chopra, V. et al. A small-molecule ameliorative advance for Huntington’s disease: preclinical pharmacology and ability of C2-8 in the R6/2 transgenic mouse. Proc. Natl Acad. Sci. USA 104, 16685–16689 (2007).
Butler, D. C. & Messer, A. Bifunctional anti-huntingtin proteasome-directed intrabodies arbitrate able abasement of aberrant huntingtin exon 1 protein fragments. PLoS ONE 6, e29199 (2011).
Perucho, J. et al. Striatal beverage of glial conditioned average diminishes huntingtin anatomy in r6/1 mice. PLoS ONE 8, e73120 (2013).
Tsvetkov, A. S. et al. Proteostasis of polyglutamine varies amid neurons and predicts neurodegeneration. Nat. Chem. Biol. 9, 586–592 (2013).
Penney, J. B. Jr, Vonsattel, J. P., MacDonald, M. E., Gusella, J. F. & Myers, R. H. CAG echo cardinal governs the development amount of anatomy in Huntington’s disease. Ann. Neurol. 41, 689–692 (1997).
Wheeler, V. C. et al. Continued glutamine tracts account nuclear localization of a atypical anatomy of huntingtin in average annoying striatal neurons in HdhQ92 and HdhQ111 knock-in mice. Hum. Mol. Genet. 9, 503–513 (2000).
Rosenblatt, A. et al. Does CAG echo cardinal adumbrate the amount of dissection changes in Huntington’s disease? Ann. Neurol. 44, 708–709 (1998).
Wild, E. J. & Tabrizi, S. J. Therapies targeting DNA and RNA in Huntington’s disease. Lancet Neurol. 16, 837–847 (2017).
Dabrowska, M., Juzwa, W., Krzyzosiak, W. J. & Olejniczak, M. Precise abatement of the CAG amplitude from the Huntingtin gene by Cas9 nickases. Front. Neurosci. https://doi.org/10.3389/fnins.2018.00075 (2018).
Shin, J. W. et al. Permanent inactivation of Huntington’s ache alteration by alone allele-specific CRISPR/Cas9. Hum. Mol. Genet. 25, 4566–4576 (2016).
Monteys, A. M., Ebanks, S. A., Keiser, M. S. & Davidson, B. L. CRISPR/Cas9 alteration of the aberrant huntingtin allele in vitro and in vivo. Mol. Ther. 25, 12–23 (2017).
Cinesi, C., Aeschbach, L., Yang, B. & Dion, V. Contracting CAG/CTG repeats application the CRISPR–Cas9 nickase. Nat. Commun. 7, 13272 (2016).
Suelves, N., Kirkham-McCarthy, L., Lahue, R. S. & Gines, S. A careful inhibitor of histone deacetylase 3 prevents cerebral deficits and suppresses striatal CAG echo expansions in Huntington’s ache mice. Sci. Rep. 7, 6082 (2017).
Eisenstein, M. CRISPR takes on Huntington’s disease. Nature 557, S42–S43 (2018).
Martins, S. et al. Modifiers of (CAG)n alternation in Machado–Joseph ache (MJD/SCA3) transmissions: an affiliation abstraction with DNA replication, adjustment and recombination genes. Hum. Genet. 133, 1311–1318 (2014).
Guo, J., Gu, L., Leffak, M. & Li, G. M. MutSβ promotes trinucleotide echo amplification by recruiting DNA polymerase β to beginning (CAG)n or (CTG)n hairpins for error-prone DNA synthesis. Corpuscle Res. 26, 775–786 (2016).
Hanawalt, P. C. & Spivak, G. Transcription-coupled DNA repair: two decades of advance and surprises. Nat. Rev. Mol. Corpuscle Biol. 9, 958–970 (2008).
Hou, C., Chan, N. L., Gu, L. & Li, G. M. Incision-dependent and error-free adjustment of (CAG)n/(CTG)n hairpins in animal corpuscle extracts. Nat. Struct. Mol. Biol. 16, 869–875 (2009).
Chan, N. L. et al. Coordinated processing of 3′ slipped (CAG)n/(CTG)n hairpins by DNA polymerases β and Δ preferentially induces echo expansions. J. Biol. Chem. 288, 15015–15022 (2013).
Pinto, R. M. et al. Conflict adjustment genes Mlh1 and Mlh3 adapt CAG alternation in Huntington’s ache mice: genome-wide and applicant approaches. PLoS Genet. 9, e1003930 (2013).
Wheeler, V. C. et al. Conflict adjustment gene Msh2 modifies the timing of aboriginal ache in Hdh Q111 striatum. Hum. Mol. Genet. 12, 273–281 (2003).
Strobel, S. A., Doucette-Stamm, L. A., Riba, L., Housman, D. E. & Dervan, P. B. Site-specific breach of animal chromosome 4 advised by triple-helix formation. Science 254, 1639–1642 (1991).
Mittelman, D. et al. Zinc-finger directed double-strand breach aural CAG echo tracts advance echo alternation in animal cells. Proc. Natl Acad. Sci. USA 106, 9607–9612 (2009).
Zeitler, B. et al. Allele-selective transcriptional repression of aberrant HTT for the assay of Huntington’s disease. Nat. Med. 25, 1131–1142 (2019).
Mosbach, V., Poggi, L. & Richard, G. F. Trinucleotide echo alternation during double-strand breach repair: from mechanisms to gene therapy. Curr. Genet. 65, 17–28 (2019).
Malankhanova, T. B., Malakhova, A. A., Medvedev, S. P. & Zakian, S. M. Modern genome alteration technologies in Huntington’s ache research. J. Huntington’s Dis. 6, 19–31 (2017).
Babacic, H., Mehta, A., Merkel, O. & Schoser, B. CRISPR-cas gene-editing as believable assay of neuromuscular and nucleotide-repeat-expansion diseases: a analytical review. PLoS ONE 14, e0212198 (2019).
Gomes-Pereira, M. & Monckton, D. G. Chemical modifiers of ambiguous broadcast simple arrangement repeats: what goes up, could appear down. Mutat. Res. 598, 15–34 (2006).
Pineiro, E. et al. Mutagenic accent modulates the dynamics of CTG echo alternation associated with myotonic dystrophy blazon 1. Nucleic Acids Res. 31, 6733–6740 (2003).
Budworth, H. et al. Abolishment of actual amplification delays the access of pathophysiology in a abrasion archetypal of Huntington’s disease. PLoS Genet. 11, e1005267 (2015).
Gottesfeld, J. M., Neely, L., Trauger, J. W., Baird, E. E. & Dervan, P. B. Regulation of gene announcement by baby molecules. Nature 387, 202–205 (1997).
Leontieva, O. V. & Blagosklonny, M. V. CDK4/6-inhibiting biologic substitutes for p21 and p16 in senescence: continuance of corpuscle aeon arrest and MTOR action actuate geroconversion. Corpuscle Aeon 12, 3063–3069 (2013).
Nakamori, M., Sobczak, K., Moxley, R. T. & Thornton, C. A. Scaled-down abiogenetic assay of myotonic dystrophy blazon 1 and blazon 2. Neuromuscul. Disord. 19, 759–762 (2009).
Brook, J. D. et al. Atomic abject of myotonic dystrophy: amplification of a trinucleotide (CTG) echo at the 3′ end of a archetype encoding a protein kinase ancestors member. Corpuscle 69, 385 (1992).
Dietmaier, W. et al. Diagnostic microsatellite instability: analogue and alternation with conflict adjustment protein expression. Blight Res. 57, 4749–4756 (1997).
Kabbarah, O. et al. A console of echo markers for apprehension of microsatellite alternation in murine tumors. Mol. Carcinog. 38, 155–159 (2003).
Koob, M. D. et al. An untranslated CTG amplification causes a atypical anatomy of spinocerebellar anarchy (SCA8). Nat. Genet. 21, 379–384 (1999).
Kremer, B. et al. Sex-dependent mechanisms for expansions and contractions of the CAG echo on afflicted Huntington ache chromosomes. Am. J. Hum. Genet. 57, 343–350 (1995).
Cleary, J. D., Nichol, K., Wang, Y. H. & Pearson, C. E. Evidence of cis-acting factors in replication-mediated trinucleotide echo alternation in abbey cells. Nat. Genet. 31, 37–46 (2002).
Panigrahi, G. B., Cleary, J. D. & Pearson, C. E. In vitro (CTG)*(CAG) expansions and deletions by animal corpuscle extracts. J. Biol. Chem. 277, 13926–13934 (2002).
Reddy, K. et al. Determinants of R-loop accession at allied bidirectionally transcribed trinucleotide repeats. Nucleic Acids Res. 39, 1749–1762 (2011).
Binz, S. K., Dickson, A. M., Haring, S. J. & Wold, M. S. Functional assays for archetype protein A (RPA). Methods Enzymol. 409, 11–38 (2006).
Zhou, Y., Meng, X., Zhang, S., Lee, E. Y. & Lee, M. Y. Characterization of animal DNA polymerase basin and its subassemblies reconstituted by announcement in the MultiBac system. PLoS ONE 7, e39156 (2012).
Mason, A. C., Roy, R., Simmons, D. T. & Wold, M. S. Functions of another archetype protein A in admission and elongation. Biochemistry 49, 5919–5928 (2010).
Tome, S. et al. Tissue-specific conflict adjustment protein expression: MSH3 is college than MSH6 in assorted abrasion tissues. DNA Adjustment 12, 46–52 (2013).
Jeon, I. et al. Human-to-mouse prion-like advancement of aberrant huntingtin protein. Acta Neuropathol. 132, 577–592 (2016).
Cibulskis, K. et al. Acute apprehension of actual point mutations in admixed and amalgamate blight samples. Nat. Biotechnol. 31, 213–219 (2013).
Morgulis, A., Gertz, E. M., Schaffer, A. A. & Agarwala, R. A fast and symmetric DUST accomplishing to affectation low-complexity DNA sequences. J. Comput. Biol. 13, 1028–1040 (2006).
Li, H. Toward bigger compassionate of artifacts in alternative calling from high-coverage samples. Bioinformatics 30, 2843–2851 (2014).
Alexandrov, L. B. et al. Signatures of mutational processes in animal cancer. Nature 500, 415–421 (2013).
Alexandrov, L. B., Nik-Zainal, S., Wedge, D. C., Campbell, P. J. & Stratton, M. R. Deciphering signatures of mutational processes accessible in animal cancer. Corpuscle Rep. 3, 246–259 (2013).
Nik-Zainal, S. et al. Mural of actual mutations in 560 breast blight whole-genome sequences. Nature 534, 47–54 (2016).
Li, H. & Durbin, R. Fast and authentic long-read alignment with Burrows–Wheeler transform. Bioinformatics 26, 589–595 (2010).
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