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Genetic Mapping and Exome Sequencing Identify Variants Associated with Five Novel Diseases

Puffenberger, Erik G., Jinks, Robert N., Sougnez, Carrie, Cibulskis, Kristian, Willert, Rebecca A., Achilly, Nathan P., Cassidy, Ryan P., Fiorentini, Christopher J., Heiken, Kory F., Lawrence, Johnny J., Mahoney, Molly H., Miller, Christopher J., Nair, Devika T., Politi, Kristin A., Worcester, Kimberly N., Setton, Roni A., DiPiazza, Rosa, Sherman, Eric A., Eastman, James T., Francklyn, Christopher, Robey-Bond, Susan, Rider, Nicholas L., Gabriel, Stacey, Morton, D. Holmes, Strauss, Kevin A.·2012·PLoS ONE
DOI 10.1371/journal.pone.0028936PMC PMC3260153
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Figures

Figure 1 Corticobasal degeneration in the brain of an infant who died from a homozygous BRAT1 mutation. (A) Throughout frontal, occipital and temporal cortex, there is marked neuronal loss, gliosis with astrocytes (arrowheads) and swollen oligodendroglia. The arrow indicates a perivascular microcalcification (superior frontal gyrus, deep cortex, 10×). (B) The anterior hippocampus is smaller than expected and there is neuronal loss and gliosis in zone CA-1 (Sommer's sector), demarcated from the CA-2 sector by the dotted line (4×). (C) At 60× magnification, the putamen shows a paucity of neurons, abundant Alzheimer Type 2 astrocytes (arrowhead) and scattered microglial nodules (arrow). Heterologous overexpression of N-terminal FLAG-tagged human BRAT1 (D) and hBRAT1 c.638_639insA (E) in mouse IMCD3 cells. Wild-type Brat1 localizes to the nucleus and cytoplasm of mIMCD3 cells. Mutant Brat1 (c.638_639insA) does not localize to the nucleus and instead forms punctate aggregations in the cytoplasm. Similar results were obtained in hARPE-19 cells (data not shown). (F) RT-PCR demonstrating the stability of overexpressed human BRAT1 transcripts (∼2.6 kb) in hARPE-19 cells. A B-actin amplicon (∼450 bp) was used as a loading control on the same gel. (G) Western blot of lysates from human ARPE-19 cells transiently transfected with wt hBRAT1 displaying FLAG-hBRAT1 fusion protein at ∼90 kDa or with hBRAT1 c.638_639insA displaying the truncated FLAG-hBRAT1 mutant fusion protein at ∼44.5 kDa (FLAG-tag and linker = 3.1 kDa). B-actin was labeled as a loading control.
Figure 1 Corticobasal degeneration in the brain of an infant who died from a homozygous BRAT1 mutation. (A) Throughout frontal, occipital and temporal cortex, there is marked neuronal loss, gliosis with astrocytes (arrowheads) and swollen oligodendroglia. The arrow indicates a perivascular microcalcification (superior frontal gyrus, deep cortex, 10×). (B) The anterior hippocampus is smaller than expected and there is neuronal loss and gliosis in zone CA-1 (Sommer's sector), demarcated from the CA-2 sector by the dotted line (4×). (C) At 60× magnification, the putamen shows a paucity of neurons, abundant Alzheimer Type 2 astrocytes (arrowhead) and scattered microglial nodules (arrow). Heterologous overexpression of N-terminal FLAG-tagged human BRAT1 (D) and hBRAT1 c.638_639insA (E) in mouse IMCD3 cells. Wild-type Brat1 localizes to the nucleus and cytoplasm of mIMCD3 cells. Mutant Brat1 (c.638_639insA) does not localize to the nucleus and instead forms punctate aggregations in the cytoplasm. Similar results were obtained in hARPE-19 cells (data not shown). (F) RT-PCR demonstrating the stability of overexpressed human BRAT1 transcripts (∼2.6 kb) in hARPE-19 cells. A B-actin amplicon (∼450 bp) was used as a loading control on the same gel. (G) Western blot of lysates from human ARPE-19 cells transiently transfected with wt hBRAT1 displaying FLAG-hBRAT1 fusion protein at ∼90 kDa or with hBRAT1 c.638_639insA displaying the truncated FLAG-hBRAT1 mutant fusion protein at ∼44.5 kDa (FLAG-tag and linker = 3.1 kDa). B-actin was labeled as a loading control.CC BY · PubMed Central
Figure 2 Microcephaly and chorioretinopathy due to a homozygous TUBGCP6 mutation. (A) An affected infant has marked microcephaly (>4SD below normal), a receding forehead, diminutive anterior fontanelle, and sutural ridging. She has cognitive delay and visual impairment but is socially engaged. (B) Head circumference and length plots for Mennonite microcephaly patients. (C) Brain magnetic resonance imaging (MRI) shows diffuse pachygyria, normal myelination, and (D) a hypoplastic cerebellar vermis.
Figure 2 Microcephaly and chorioretinopathy due to a homozygous TUBGCP6 mutation. (A) An affected infant has marked microcephaly (>4SD below normal), a receding forehead, diminutive anterior fontanelle, and sutural ridging. She has cognitive delay and visual impairment but is socially engaged. (B) Head circumference and length plots for Mennonite microcephaly patients. (C) Brain magnetic resonance imaging (MRI) shows diffuse pachygyria, normal myelination, and (D) a hypoplastic cerebellar vermis.CC BY · PubMed Central
Figure 3 Symptomatic epilepsy and skull dysplasia due to a homozygous SNIP1 mutation. (A) Two affected brothers presented with severe psychomotor delay, intractable seizures, bulbous nose, wide mouth and tongue, broad jaw with protuberant angles, short hands, short tapered fingers, and broad thumbs. (B,C) Brain MRI (B, axial T2; C, coronal T1) MRI showed enlarged ventricles, a thin corpus callosum, hypomyelination, and an irregular, undulating skull surface. (D) Mouse FLAG-SNIP1 (wt) fusion protein, when transiently overexpressed in mIMCD3 cells, localizes to the nucleus in a punctate pattern consistent with transcriptional complexes. (E) Mouse FLAG-SNIP1 (p.Glu353Gly) localizes to the nucleus, but with a more aggregated distribution. (F) Top – Reverse-transcriptase PCR from three wild-type mSNIP1-transfected samples and four c.1058A>G mSNIP1-transfected samples. mSNIP1 amplicon – 400 bp. mGAPDH (loading control) – 1037 bp amplicon. Bottom – Western blot of lysates from mIMCD3 cells transiently transfected with wt (lanes wt1&2) or c.1058A>G (lanes p.Glu353Gly1&2) mSNIP1 displaying the FLAG-mSNIP fusion protein at ∼48 kDa. The 140-kDa non-specific band was used as a loading control. Data shown are two out of four replicate sets of transfections.
Figure 3 Symptomatic epilepsy and skull dysplasia due to a homozygous SNIP1 mutation. (A) Two affected brothers presented with severe psychomotor delay, intractable seizures, bulbous nose, wide mouth and tongue, broad jaw with protuberant angles, short hands, short tapered fingers, and broad thumbs. (B,C) Brain MRI (B, axial T2; C, coronal T1) MRI showed enlarged ventricles, a thin corpus callosum, hypomyelination, and an irregular, undulating skull surface. (D) Mouse FLAG-SNIP1 (wt) fusion protein, when transiently overexpressed in mIMCD3 cells, localizes to the nucleus in a punctate pattern consistent with transcriptional complexes. (E) Mouse FLAG-SNIP1 (p.Glu353Gly) localizes to the nucleus, but with a more aggregated distribution. (F) Top – Reverse-transcriptase PCR from three wild-type mSNIP1-transfected samples and four c.1058A>G mSNIP1-transfected samples. mSNIP1 amplicon – 400 bp. mGAPDH (loading control) – 1037 bp amplicon. Bottom – Western blot of lysates from mIMCD3 cells transiently transfected with wt (lanes wt1&2) or c.1058A>G (lanes p.Glu353Gly1&2) mSNIP1 displaying the FLAG-mSNIP fusion protein at ∼48 kDa. The 140-kDa non-specific band was used as a loading control. Data shown are two out of four replicate sets of transfections.CC BY · PubMed Central
Figure 4 Genetic mapping of seven Plain disorders. The results of autozygosity mapping using Affymetrix GeneChip 10 K or 50 K SNP microarrays are plotted for each disorder. The x-axis depicts chromosomal location on autosomes. Yellow peaks represent the number of contiguous homozygous SNPs shared by affected individuals and the purple peaks depict location scores. (A) Autozygosity mapping of two affected individuals identified a single, large block of homozygosity on chromosome 6 (yellow peak). Genotyping of 6 unaffected siblings excluded this homozygous block, but identified 12 genomic regions greater than 5 Mb in size (red peaks) that were consistent with linkage in the family. (B) List of genomic regions consistent with linkage in the single nuclear family with infantile parkinsonism-dystonia syndrome. Panels C–H provide mapping plots for the other 6 disorders. For two disorders (C,D), 50 K microarrays were used after 10 K microarrays failed to unequivocally localize the disease gene. The other four disorders (E–H) were mapped with 10 K microarrays.
Figure 4 Genetic mapping of seven Plain disorders. The results of autozygosity mapping using Affymetrix GeneChip 10 K or 50 K SNP microarrays are plotted for each disorder. The x-axis depicts chromosomal location on autosomes. Yellow peaks represent the number of contiguous homozygous SNPs shared by affected individuals and the purple peaks depict location scores. (A) Autozygosity mapping of two affected individuals identified a single, large block of homozygosity on chromosome 6 (yellow peak). Genotyping of 6 unaffected siblings excluded this homozygous block, but identified 12 genomic regions greater than 5 Mb in size (red peaks) that were consistent with linkage in the family. (B) List of genomic regions consistent with linkage in the single nuclear family with infantile parkinsonism-dystonia syndrome. Panels C–H provide mapping plots for the other 6 disorders. For two disorders (C,D), 50 K microarrays were used after 10 K microarrays failed to unequivocally localize the disease gene. The other four disorders (E–H) were mapped with 10 K microarrays.CC BY · PubMed Central
Figure 5 Overexpression of mouse Cradd in mIMCD3 cells. (A) Wild-type N-terminal FLAG-Cradd localizes to the cytoplasm and nucleus. (B) Mutant N-terminal FLAG-Cradd (p.Gly128Arg) localizes to the cytoplasm and nucleus in a manner that is indistinguishable from the wild-type localization. (C) Western blot of lysates from mIMCD3 cells transfected with wt FLAG-Cradd and wt V5-mPIDD, wt V5-mPIDD, or FLAG-Cradd (p.Gly128Arg) and wt V5-mPIDD. Blot was labeled with anti-V5 monoclonal antibody. Note that full-length V5-mPIDD (110.5 kDa) was cleaved into a 57.1 kDa N-terminal fragment, suggesting normal autocatalytic activity. (D) Co-transfection of FLAG-Cradd (wt) and wt V5-PIDD death domain (DD) results in uniform colocalization of the fusion proteins throughout the cytoplasm and nucleus (yellow). (E) Overexpressed V5-mPIDD DD (wt) localizes to the cytoplasm and the nucleus. (F) Co-overexpression of FLAG-Cradd (p.Gly128Arg) with V5-mPIDD DD (wt) results in dense aggregations of FLAG-Cradd in the cytoplasm. (G) Co-transfection of FLAG-mCradd (wt) and V5-mPIDD (wt) results in relatively uniform colocalization of the fusion proteins throughout the cytoplasm (yellow); punctate FLAG-mCradd aggregation is also evident (green). FLAG-mCradd (wt) localizes to the nucleus (green), V5-mPIDD does not (red). (H) Overexpressed V5-mPIDD (wt) localizes to the cytoplasm as previously reported (Berube et al., 2005). (I) Co-overexpression of FLAG-mCradd (p. Gly128Arg) with V5-mPIDD (wt) results in dense aggregations of FLAG-mCradd in the cytoplasm, decreased mCradd∶mPIDD colocalization, and a relative loss of localization of mCradd to the nucleus. Green fluorescence – anti-FLAG M2 antibody (1∶1000); Red fluorescence – anti-V5 antibody (1∶200); Blue fluorescence – DAPI-labeled nuclei (1.5 µg/µl); Western blots – anti-FLAG M2 antibody (1∶1000). (J) Co-immunoprecipitation (Co-IP) of V5-tagged mouse Pidd death domain (DD) with FLAG-tagged mouse Cradd DD in mIMCD3 cells. Wild-type FLAG-Cradd DD co-immunoprecipitates wild-type Pidd DD; the FLAG-Cradd DD p.Gly128Arg variant does not. The upper blots were labeled with the anti-FLAG M2 antibody (1∶1000). The lower blots of the same lysates/eluates were labeled with the anti-V5 antibody (1∶5000).
Figure 5 Overexpression of mouse Cradd in mIMCD3 cells. (A) Wild-type N-terminal FLAG-Cradd localizes to the cytoplasm and nucleus. (B) Mutant N-terminal FLAG-Cradd (p.Gly128Arg) localizes to the cytoplasm and nucleus in a manner that is indistinguishable from the wild-type localization. (C) Western blot of lysates from mIMCD3 cells transfected with wt FLAG-Cradd and wt V5-mPIDD, wt V5-mPIDD, or FLAG-Cradd (p.Gly128Arg) and wt V5-mPIDD. Blot was labeled with anti-V5 monoclonal antibody. Note that full-length V5-mPIDD (110.5 kDa) was cleaved into a 57.1 kDa N-terminal fragment, suggesting normal autocatalytic activity. (D) Co-transfection of FLAG-Cradd (wt) and wt V5-PIDD death domain (DD) results in uniform colocalization of the fusion proteins throughout the cytoplasm and nucleus (yellow). (E) Overexpressed V5-mPIDD DD (wt) localizes to the cytoplasm and the nucleus. (F) Co-overexpression of FLAG-Cradd (p.Gly128Arg) with V5-mPIDD DD (wt) results in dense aggregations of FLAG-Cradd in the cytoplasm. (G) Co-transfection of FLAG-mCradd (wt) and V5-mPIDD (wt) results in relatively uniform colocalization of the fusion proteins throughout the cytoplasm (yellow); punctate FLAG-mCradd aggregation is also evident (green). FLAG-mCradd (wt) localizes to the nucleus (green), V5-mPIDD does not (red). (H) Overexpressed V5-mPIDD (wt) localizes to the cytoplasm as previously reported (Berube et al., 2005). (I) Co-overexpression of FLAG-mCradd (p. Gly128Arg) with V5-mPIDD (wt) results in dense aggregations of FLAG-mCradd in the cytoplasm, decreased mCradd∶mPIDD colocalization, and a relative loss of localization of mCradd to the nucleus. Green fluorescence – anti-FLAG M2 antibody (1∶1000); Red fluorescence – anti-V5 antibody (1∶200); Blue fluorescence – DAPI-labeled nuclei (1.5 µg/µl); Western blots – anti-FLAG M2 antibody (1∶1000). (J) Co-immunoprecipitation (Co-IP) of V5-tagged mouse Pidd death domain (DD) with FLAG-tagged mouse Cradd DD in mIMCD3 cells. Wild-type FLAG-Cradd DD co-immunoprecipitates wild-type Pidd DD; the FLAG-Cradd DD p.Gly128Arg variant does not. The upper blots were labeled with the anti-FLAG M2 antibody (1∶1000). The lower blots of the same lysates/eluates were labeled with the anti-V5 antibody (1∶5000).CC BY · PubMed Central
Figure 6 Overexpression of mouse HARS in mIMCD3 cells. (A) Wild-type N-terminal FLAG-HARS localizes to the cytoplasm. (B) Mutant N-terminal FLAG-HARS (p.Tyr454Ser) localizes to the cytoplasm in a manner that is indistinguishable from the wild-type localization shown in A. Transfected and non-transfected cells were labeled with anti-FLAG M2 monoclonal antibody and AlexaFluor 488-conjugated anti-mouse IgG1 (green fluorescence). (C) Reaction velocity vs. human tRNAHis concentration for histidine aminoacylation of tRNAHis by wild-type murine HARS (HARS) and p.Tyr454Ser (Y454S) HARS. Scale bar = 10 µm in A and B.
Figure 6 Overexpression of mouse HARS in mIMCD3 cells. (A) Wild-type N-terminal FLAG-HARS localizes to the cytoplasm. (B) Mutant N-terminal FLAG-HARS (p.Tyr454Ser) localizes to the cytoplasm in a manner that is indistinguishable from the wild-type localization shown in A. Transfected and non-transfected cells were labeled with anti-FLAG M2 monoclonal antibody and AlexaFluor 488-conjugated anti-mouse IgG1 (green fluorescence). (C) Reaction velocity vs. human tRNAHis concentration for histidine aminoacylation of tRNAHis by wild-type murine HARS (HARS) and p.Tyr454Ser (Y454S) HARS. Scale bar = 10 µm in A and B.CC BY · PubMed Central

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Research works printed but not linked: 61

  1. EG Puffenberger, 2003, Genetic heritage of the Old Order Mennonites of Southeastern Pennsylvania., American Journal of Medical Genetics Part C (Semin Med Genet), 121C, 18, 10.1002/ajmg.c.20003 · DOI
  2. KA Strauss, 2009, Genetics, medicine, and the Plain people., Annu Rev Genomics Hum Genet, 10, 513, 10.1146/annurev-genom-082908-150040 · DOI
  3. VA McKusick, 1964, Genetic Studies of the Amish, Background and Potentialities., Bull Johns Hopkins Hosp, 115, 203
  4. VA McKusick, 1964, The Distribution of Certain Genes in the Old Order Amish., Cold Spring Harb Symp Quant Biol, 29, 99, 10.1101/SQB.1964.029.01.015 · DOI
  5. KA Strauss, 2005, Genome-wide SNP arrays as a diagnostic tool: clinical description, genetic mapping, and molecular characterization of Salla disease in an Old Order Mennonite population., Am J Med Genet A, 138, 262, 10.1002/ajmg.a.30961 · DOI
  6. NJ Lohr, 2010, Human ITCH E3 ubiquitin ligase deficiency causes syndromic multisystem autoimmune disease., Am J Hum Genet, 86, 447, 10.1016/j.ajhg.2010.01.028 · DOI
  7. EG Puffenberger, 2004, Mapping of sudden infant death with dysgenesis of the testes syndrome (SIDDT) by a SNP genome scan and identification of TSPYL loss of function., Proc Natl Acad Sci U S A, 101, 11689, 10.1073/pnas.0401194101 · DOI
  8. EG Puffenberger, 2007, Polyhydramnios, megalencephaly and symptomatic epilepsy caused by a homozygous 7-kilobase deletion in LYK5., Brain, 130, 1929, 10.1093/brain/awm100 · DOI
  9. EA Sherman, 2008, Genetic mapping of glutaric aciduria, type 3, to chromosome 7 and identification of mutations in c7orf10., Am J Hum Genet, 83, 604, 10.1016/j.ajhg.2008.09.018 · DOI
  10. KA Strauss, 2008, Clinical application of DNA microarrays: molecular diagnosis and HLA matching of an Amish child with severe combined immune deficiency., Clin Immunol, 128, 31, 10.1016/j.clim.2008.02.016 · DOI
  11. N Anastasio, 2010, Mutations in SCARF2 are responsible for Van Den Ende-Gupta syndrome., Am J Hum Genet, 87, 553, 10.1016/j.ajhg.2010.09.005 · DOI
  12. J Becker, 2011, Exome Sequencing Identifies Truncating Mutations in Human SERPINF1 in Autosomal-Recessive Osteogenesis Imperfecta., Am J Hum Genet
  13. A Bolze, 2010, Whole-exome-sequencing-based discovery of human FADD deficiency., Am J Hum Genet, 87, 873, 10.1016/j.ajhg.2010.10.028 · DOI
  14. M Caliskan, 2011, Exome sequencing reveals a novel mutation for autosomal recessive non-syndromic mental retardation in the TECR gene on chromosome 19p13., Hum Mol Genet
  15. C Gilissen, 2010, Exome sequencing identifies WDR35 variants involved in Sensenbrenner syndrome., Am J Hum Genet, 87, 418, 10.1016/j.ajhg.2010.08.004 · DOI
  16. NL Glazer, 2011, Exome sequencing links gene mutation in angiopoietin-like protein 3 with low-density lipoprotein cholesterol., Circ Cardiovasc Genet, 4, 100, 10.1161/CIRCGENETICS.111.959510 · DOI
  17. TB Haack, 2010, Exome sequencing identifies ACAD9 mutations as a cause of complex I deficiency., Nat Genet, 42, 1131, 10.1038/ng.706 · DOI
  18. JO Johnson, 2010, Exome sequencing reveals VCP mutations as a cause of familial ALS., Neuron, 68, 857, 10.1016/j.neuron.2010.11.036 · DOI · Paper page
  19. PM Krawitz, 2010, Identity-by-descent filtering of exome sequence data identifies PIGV mutations in hyperphosphatasia mental retardation syndrome., Nat Genet, 42, 827, 10.1038/ng.653 · DOI
  20. G Montenegro, 2011, Exome sequencing allows for rapid gene identification in a Charcot-Marie-Tooth family., Ann Neurol
  21. K Musunuru, 2010, Exome sequencing, ANGPTL3 mutations, and familial combined hypolipidemia., N Engl J Med, 363, 2220, 10.1056/NEJMoa1002926 · DOI · Paper page
  22. SB Ng, 2010, Exome sequencing identifies MLL2 mutations as a cause of Kabuki syndrome., Nat Genet, 42, 790, 10.1038/ng.646 · DOI
  23. SB Ng, 2010, Exome sequencing identifies the cause of a mendelian disorder., Nat Genet, 42, 30, 10.1038/ng.499 · DOI · Paper page
  24. P Ostergaard, 2011, Rapid identification of mutations in GJC2 in primary lymphoedema using whole exome sequencing combined with linkage analysis with delineation of the phenotype., J Med Genet
  25. A Sirmaci, 2010, MASP1 mutations in patients with facial, umbilical, coccygeal, and auditory findings of Carnevale, Malpuech, OSA, and Michels syndromes., Am J Hum Genet, 87, 679, 10.1016/j.ajhg.2010.09.018 · DOI
  26. T Walsh, 2010, Whole exome sequencing and homozygosity mapping identify mutation in the cell polarity protein GPSM2 as the cause of nonsyndromic hearing loss DFNB82., Am J Hum Genet, 87, 90, 10.1016/j.ajhg.2010.05.010 · DOI
  27. JL Wang, 2010, TGM6 identified as a novel causative gene of spinocerebellar ataxias using exome sequencing., Brain, 133, 3510, 10.1093/brain/awq323 · DOI
  28. MA Kurian, 2009, Homozygous loss-of-function mutations in the gene encoding the dopamine transporter are associated with infantile parkinsonism-dystonia., J Clin Invest, 119, 1595
  29. VA McKusick, 1966, Chorioretinopathy with hereditary microcephaly., Arch Ophthalmol, 75, 597, 10.1001/archopht.1966.00970050599003 · DOI
  30. JJ Higgins, 1997, An autosomal recessive disorder with posterior column ataxia and retinitis pigmentosa., Neurology, 49, 1717, 10.1212/WNL.49.6.1717 · DOI
  31. AM Rajadhyaksha, 2010, Mutations in FLVCR1 cause posterior column ataxia and retinitis pigmentosa., American journal of human genetics, 87, 643, 10.1016/j.ajhg.2010.10.013 · DOI
  32. JA Aglipay, 2006, ATM activation by ionizing radiation requires BRCA1-associated BAAT1., The Journal of biological chemistry, 281, 9710, 10.1074/jbc.M510332200 · DOI
  33. Z Tan, 2002, Immunohistochemical study of p53-associated proteins in rat brain following lithium-pilocarpine status epilepticus., Brain research, 929, 129, 10.1016/S0006-8993(01)03360-1 · DOI
  34. T Engel, 2010, Reduced hippocampal damage and epileptic seizures after status epilepticus in mice lacking proapoptotic Puma., The FASEB journal: official publication of the Federation of American Societies for Experimental Biology, 24, 853, 10.1096/fj.09-145870 · DOI
  35. LG Morris, 2010, Genetic determinants at the interface of cancer and neurodegenerative disease., Oncogene, 29, 3453, 10.1038/onc.2010.127 · DOI
  36. S Biton, 2008, The neurological phenotype of ataxia-telangiectasia: solving a persistent puzzle., DNA repair, 7, 1028, 10.1016/j.dnarep.2008.03.006 · DOI
  37. A Barzilai, 2010, DNA damage, neuronal and glial cell death and neurodegeneration., Apoptosis: an international journal on programmed cell death, 15, 1371, 10.1007/s10495-010-0501-0 · DOI
  38. H Duan, 1997, RAIDD is a new ‘death’ adaptor molecule., Nature, 385, 86, 10.1038/385086a0 · DOI
  39. M Ahmad, 1997, CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP., Cancer research, 57, 615
  40. Y Lin, 2000, Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis., Nature genetics, 26, 122, 10.1038/79102 · DOI
  41. C Berube, 2005, Apoptosis caused by p53-induced protein with death domain (PIDD) depends on the death adapter protein RAIDD., Proceedings of the National Academy of Sciences of the United States of America, 102, 14314, 10.1073/pnas.0506475102 · DOI
  42. LM Shearwin-Whyatt, 2000, Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD., Cell death and differentiation, 7, 155, 10.1038/sj.cdd.4400632 · DOI
  43. HH Park, 2007, Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex., Cell, 128, 533, 10.1016/j.cell.2007.01.019 · DOI
  44. O Jabado, 2004, RAIDD aggregation facilitates apoptotic death of PC12 cells and sympathetic neurons., Cell death and differentiation, 11, 618, 10.1038/sj.cdd.4401397 · DOI
  45. RH Kim, 2000, A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction., Genes & development, 14, 1605, 10.1101/gad.14.13.1605 · DOI
  46. RH Kim, 2001, SNIP1 inhibits NF-kappa B signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators., The Journal of biological chemistry, 276, 46297, 10.1074/jbc.M103819200 · DOI
  47. M Fujii, 2006, SNIP1 is a candidate modifier of the transcriptional activity of c-Myc on E box-dependent target genes., Molecular cell, 24, 771, 10.1016/j.molcel.2006.11.006 · DOI
  48. U Ueberham, 2009, Smad2 isoforms are differentially expressed during mouse brain development and aging., International journal of developmental neuroscience: the official journal of the International Society for Developmental Neuroscience, 27, 501, 10.1016/j.ijdevneu.2009.04.001 · DOI
  49. K Toyo-oka, 2004, Loss of the Max-interacting protein Mnt in mice results in decreased viability, defective embryonic growth and craniofacial defects: relevance to Miller-Dieker syndrome., Human molecular genetics, 13, 1057, 10.1093/hmg/ddh116 · DOI
  50. K Wei, 2007, Neural crest cell deficiency of c-myc causes skull and hearing defects., Genesis, 45, 382, 10.1002/dvg.20304 · DOI
  51. V Bhattacherjee, 2009, CBP/p300 and associated transcriptional co-activators exhibit distinct expression patterns during murine craniofacial and neural tube development., The International journal of developmental biology, 53, 1097, 10.1387/ijdb.072489vb · DOI
  52. A Wey, 2010, c-myc and N-myc promote active stem cell metabolism and cycling as architects of the developing brain., Oncotarget, 1, 120, 10.18632/oncotarget.116 · DOI
  53. J Viosca, 2010, Syndromic features and mild cognitive impairment in mice with genetic reduction on p300 activity: Differential contribution of p300 and CBP to Rubinstein-Taybi syndrome etiology., Neurobiology of disease, 37, 186, 10.1016/j.nbd.2009.10.001 · DOI
  54. LP Cacheaux, 2009, Transcriptome profiling reveals TGF-beta signaling involvement in epileptogenesis., The Journal of neuroscience: the official journal of the Society for Neuroscience, 29, 8927, 10.1523/JNEUROSCI.0430-09.2009 · DOI
  55. FD Lubin, 2007, Nuclear factor-kappa B regulates seizure threshold and gene transcription following convulsant stimulation., Journal of neurochemistry, 103, 1381, 10.1111/j.1471-4159.2007.04863.x · DOI · Paper page
  56. PD Stenson, 2008, Human Gene Mutation Database: towards a comprehensive central mutation database., J Med Genet, 45, 124, 10.1136/jmg.2007.055210 · DOI
  57. KW Broman, 1999, Long homozygous chromosomal segments in reference families from the centre d'Etude du polymorphisme humain., Am J Hum Genet, 65, 1493, 10.1086/302661 · DOI
  58. MA DePristo, 2011, A framework for variation discovery and genotyping using next-generation DNA sequencing data., Nat Genet, 43, 491, 10.1038/ng.806 · DOI
  59. BA Roe, 1975, Studies on human tRNA. I. The rapid, large scale isolation and partial fractionation of placenta and liver tRNA., Nucleic Acids Res, 2, 21, 10.1093/nar/2.1.21 · DOI
  60. CS Francklyn, 2008, Methods for kinetic and thermodynamic analysis of aminoacyl-tRNA synthetases., Methods, 44, 100, 10.1016/j.ymeth.2007.09.007 · DOI
  61. W Yan, 1996, A tRNA identity switch mediated by the binding interaction between a tRNA anticodon and the accessory domain of a class II aminoacyl-tRNA synthetase., Biochemistry, 35, 6559, 10.1021/bi952889f · DOI

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Authors
Puffenberger, E. G., Jinks, R. N., Sougnez, C., Cibulskis, K., Willert, R. A., Achilly, N. P., Cassidy, R. P., Fiorentini, C. J., Heiken, K. F., Lawrence, J. J., Mahoney, M. H., Miller, C. J., Nair, D. T., Politi, K. A., Worcester, K. N., Setton, R. A., DiPiazza, R., Sherman, E. A., Eastman, J. T., Francklyn, C., Robey-Bond, S., Rider, N. L., Gabriel, S., Morton, D. H., & Strauss, K. A.
Venue
PLoS ONE
Publisher
Public Library of Science (PLoS)
Published
2012-01-17
Volume
7
Issue
1
Pages
e28936
ISSN
1932-6203
DOI
10.1371/journal.pone.0028936
PMC
PMC3260153
Cited by
286
References
3
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (unspecified)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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