Active Motif Technical Data Sheet (TDS)

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NCAPH2 antibody (mAb) Catalog Nos: 61681, 61682 Quantities: 100 µg, 10 µg RRID: AB_2793733 Purification: Protein G Chromatography Clone: 5F2G4 Host: Rat Isotype: IgG2a Concentration: 1 µg/µl Application(s): ICC, IF, WB Molecular Weight: 90 kDa Reactivity: Human Background: NCAPH2 (Non-SMC Condensin II Complex, Subunit H2) Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture. May play a role in lineage-specific role in T-cell development. (By similarity) Immunogen: This antibody was raised against a recombinant protein to human NCAPH2. Buffer: Purified IgG in PBS with 30% glycerol and 0.035% sodium azide. Sodium azide is highly toxic. NCAPH2 antibody (mAb) (Clone 5F2G4) Application Notes: tested by immunofluorescence. Formaldehyde fixed HeLa cell stained with the Applications Validated by Active Motif: NCAPH2 antibody. ICC/IF: 1 - 2 µg/ml dilution WB*: 0.5 - 2 µg/ml dilution The addition of 0.1% Tween 20 in the blocking buffer and primary antibody incubation buffer is recommended to aid in detection by Western blot. Individual optimization may be required. *Note: many chromatin-bound proteins are not soluble in a low salt nuclear extract and fractionate to the pellet. Therefore, we recommend a High Salt / Sonication Protocol when preparing nuclear extracts for Western blot. Storage and Guarantee: Some products may be shipped at room temperature. This will not affect their stability or performance. Avoid repeated freeze/thaw cycles by aliquoting items into single-use fractions for storage at -20°C for up to 2 years. Keep all reagents on ice when not in storage. This product is guaranteed for 12 months from date of receipt. This product is for research use only and is not for use in diagnostic procedures. NCAPH2 antibody (mAb) (Clone 5F2G4) tested by Western blot. NCAPH2 antibody detection by Western blot. The analysis was performed using 30 µg of HeLa nuclear extract and NCAPH2 antibody at a 1 µg/ml dilution. Application Key: ChIP = Chromatin Immunoprecipitation; FACS = Flow Cytometry; IF = Immunofluorescence; IHC = Immunohistochemistry; IP = Immunoprecipitation; WB = Western Blot North America 877 222 9543 • Europe +32 (0)2 653 0001 • Japan +81 (0)3 5225 3638 • www.activemotif.com.

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A Commercial Antibody to the Human Condensin II Subunit NCAPH2 Cross-Reacts with a SWI/SNF Complex Component
bioRxiv preprint doi: https://doi.org/10.1101/2020.11.07.372599; this version posted November 9, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-ND 4.0 International license. A commercial antibody to the human condensin II subunit NCAPH2 cross-reacts with a SWI/SNF complex component Erin E. Cutts1*, Gillian C Taylor2*, Mercedes Pardo1, Lu Yu1, Jimi C Wills3, Jyoti S. Choudhary1, Alessandro Vannini1#, Andrew J Wood2# 1 Division of Structural Biology, The Institute of Cancer Research, London SW7 3RP, United Kingdom 2 MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, The University of Edinburgh, Edinburgh, EH4 2XU, UK. 3 Cancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh, EH4 2XU, UK. * Equal contribution # correspondence to: [email protected], [email protected]. Summary Condensin complexes compact and disentangle chromosomes in preparation for cell division. Commercially available antibodies raised against condensin subunits have been widely used to characterise their cellular interactome. Here we have assessed the specificity of a polyclonal antibody (Bethyl A302- 276A) that is commonly used as a probe for NCAPH2, the kleisin subunit of condensin II, in mammalian cells. We find that, in addition to its intended target, this antibody cross-reacts with one or more components of the SWI/SNF family of chromatin remodelling complexes in an NCAPH2- independent manner. This cross-reactivity with an abundant chromatin- associated factor is likely to affect the interpretation of protein and chromatin immunoprecipitation experiments that make use of this antibody probe.
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Supplementary File 2A Revised
Supplementary file 2A. Differentially expressed genes in aldosteronomas compared to all other samples, ranked according to statistical significance. Missing values were not allowed in aldosteronomas, but to a maximum of five in the other samples. Acc UGCluster Name Symbol log Fold Change P - Value Adj. P-Value B R99527 Hs.8162 Hypothetical protein MGC39372 MGC39372 2,17 6,3E-09 5,1E-05 10,2 AA398335 Hs.10414 Kelch domain containing 8A KLHDC8A 2,26 1,2E-08 5,1E-05 9,56 AA441933 Hs.519075 Leiomodin 1 (smooth muscle) LMOD1 2,33 1,3E-08 5,1E-05 9,54 AA630120 Hs.78781 Vascular endothelial growth factor B VEGFB 1,24 1,1E-07 2,9E-04 7,59 R07846 Data not found 3,71 1,2E-07 2,9E-04 7,49 W92795 Hs.434386 Hypothetical protein LOC201229 LOC201229 1,55 2,0E-07 4,0E-04 7,03 AA454564 Hs.323396 Family with sequence similarity 54, member B FAM54B 1,25 3,0E-07 5,2E-04 6,65 AA775249 Hs.513633 G protein-coupled receptor 56 GPR56 -1,63 4,3E-07 6,4E-04 6,33 AA012822 Hs.713814 Oxysterol bining protein OSBP 1,35 5,3E-07 7,1E-04 6,14 R45592 Hs.655271 Regulating synaptic membrane exocytosis 2 RIMS2 2,51 5,9E-07 7,1E-04 6,04 AA282936 Hs.240 M-phase phosphoprotein 1 MPHOSPH -1,40 8,1E-07 8,9E-04 5,74 N34945 Hs.234898 Acetyl-Coenzyme A carboxylase beta ACACB 0,87 9,7E-07 9,8E-04 5,58 R07322 Hs.464137 Acyl-Coenzyme A oxidase 1, palmitoyl ACOX1 0,82 1,3E-06 1,2E-03 5,35 R77144 Hs.488835 Transmembrane protein 120A TMEM120A 1,55 1,7E-06 1,4E-03 5,07 H68542 Hs.420009 Transcribed locus 1,07 1,7E-06 1,4E-03 5,06 AA410184 Hs.696454 PBX/knotted 1 homeobox 2 PKNOX2 1,78 2,0E-06
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Appendix 2. Significantly Differentially Regulated Genes in Term Compared with Second Trimester Amniotic Fluid Supernatant
Appendix 2. Significantly Differentially Regulated Genes in Term Compared With Second Trimester Amniotic Fluid Supernatant Fold Change in term vs second trimester Amniotic Affymetrix Duplicate Fluid Probe ID probes Symbol Entrez Gene Name 1019.9 217059_at D MUC7 mucin 7, secreted 424.5 211735_x_at D SFTPC surfactant protein C 416.2 206835_at STATH statherin 363.4 214387_x_at D SFTPC surfactant protein C 295.5 205982_x_at D SFTPC surfactant protein C 288.7 1553454_at RPTN repetin solute carrier family 34 (sodium 251.3 204124_at SLC34A2 phosphate), member 2 238.9 206786_at HTN3 histatin 3 161.5 220191_at GKN1 gastrokine 1 152.7 223678_s_at D SFTPA2 surfactant protein A2 130.9 207430_s_at D MSMB microseminoprotein, beta- 99.0 214199_at SFTPD surfactant protein D major histocompatibility complex, class II, 96.5 210982_s_at D HLA-DRA DR alpha 96.5 221133_s_at D CLDN18 claudin 18 94.4 238222_at GKN2 gastrokine 2 93.7 1557961_s_at D LOC100127983 uncharacterized LOC100127983 93.1 229584_at LRRK2 leucine-rich repeat kinase 2 HOXD cluster antisense RNA 1 (non- 88.6 242042_s_at D HOXD-AS1 protein coding) 86.0 205569_at LAMP3 lysosomal-associated membrane protein 3 85.4 232698_at BPIFB2 BPI fold containing family B, member 2 84.4 205979_at SCGB2A1 secretoglobin, family 2A, member 1 84.3 230469_at RTKN2 rhotekin 2 82.2 204130_at HSD11B2 hydroxysteroid (11-beta) dehydrogenase 2 81.9 222242_s_at KLK5 kallikrein-related peptidase 5 77.0 237281_at AKAP14 A kinase (PRKA) anchor protein 14 76.7 1553602_at MUCL1 mucin-like 1 76.3 216359_at D MUC7 mucin 7,
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Non-SMC Condensin I Complex Subunit H Mediates Mature
www.nature.com/scientificreports OPEN Non-SMC condensin I complex subunit H mediates mature chromosome condensation and DNA damage in pancreatic cancer cells Jae Hyeong Kim 1*, Yuna Youn1, Kyung-Tae Kim2, Gyubeom Jang2 & Jin-Hyeok Hwang1,3* Non-SMC condensin I complex subunit H (NCAPH) is a vital gene associated with chromosome stability and is required for proper chromosome condensation and segregation. However, the mechanisms through which NCAPH afects pancreatic cancer (PC) and its molecular function remain unclear. In this study, we examined the role of NCAPH in PC cells. Our results showed that NCAPH was overexpressed in clinical PC specimens (GEPIA) and cell lines. In addition, in NCAPH-knockdown cells, colony formation and proliferation were inhibited, and the cell cycle was arrested at the S and G2/M phases owing to failure of mature chromosome condensation (MCC) in poorly condensed chromosomes. Increased cell death in NCAPH-knockdown cells was found to help initiate apoptosis through the activation of caspase-3 and PARP cleavage. Furthermore, NCAPH-knockdown cells showed an increase in chromosomal aberrations and DNA damage via activation of the DNA damage response (Chk1/Chk2) signaling pathways. These data demonstrated that NCAPH played an important role in cell cycle progression and DNA damage by maintaining chromosomal stability through progression of MCC from poorly condensed chromosomes. Ultimately, NCAPH knockdown induced apoptotic cell death, which was partially mediated by caspase-dependent pathways. These fndings highlight the potential role of NCAPH as a therapeutic target for PC. More than 90% of pancreatic cancer (PC) cases are classifed as pancreatic ductal adenocarcinoma (PDA), one of the most lethal human malignant tumors with a poor prognosis1.
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Lecture9'21 Chromatin II
Genetic Organization -Chromosomal Arrangement: From Form to Function. Chapters 9 & 10 in Genes XI The Eukaryotic chromosome – Organized Structures -banding – Centromeres – Telomeres – Nucleosomes – Euchromatin / Heterochromatin – Higher Orders of Chromosomal Structure 2 Heterochromatin differs from euchromatin in that heterochromatin is effectively inert; remains condensed during interphase; is transcriptionally repressed; replicates late in S phase and may be localized to the centromere or nuclear periphery Facultative heterochromatin is not restricted by pre-designated sequence; genes that are moved within or near heterochromatic regions can become inactivated as a result of their new location. Heterochromatin differs from euchromatin in that heterochromatin is effectively inert; remains condensed during interphase; is transcriptionally repressed; replicates late in S phase and may be localized to the centromere or nuclear periphery Facultative heterochromatin is not restricted by pre-designated sequence; genes that are moved within or near heterochromatic regions can become inactivated as a result of their new location. Chromatin inactivation (or heterochromatin formation) occurs by the addition of proteins to the nucleosomal fiber. May be due to: Chromatin condensation -making it inaccessible to transcriptional apparatus Proteins that accumulate and inhibit accessibility to the regulatory sequences Proteins that directly inhibit transcription Chromatin Is Fundamentally Divided into Euchromatin and Heterochromatin • Individual chromosomes can be seen only during mitosis. • During interphase, the general mass of chromatin is in the form of euchromatin, which is slightly less tightly packed than mitotic chromosomes. TF20210119 Regions of compact heterochromatin are clustered near the nucleolus and nuclear membrane Photo courtesy of Edmund Puvion, Centre National de la Recherche Scientifique Chromatin: Basic Structures • nucleosome – The basic structural subunit of chromatin, consisting of ~200 bp of DNA wrapped around an octamer of histone proteins.
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Overlapping and Non-Overlapping Functions of Condensins I and II in Neural Stem Cell Divisions
Overlapping and Non-overlapping Functions of Condensins I and II in Neural Stem Cell Divisions Kenji Nishide, Tatsuya Hirano* Chromosome Dynamics Laboratory, RIKEN, Hirosawa, Wako, Saitama, Japan Abstract During development of the cerebral cortex, neural stem cells (NSCs) divide symmetrically to proliferate and asymmetrically to generate neurons. Although faithful segregation of mitotic chromosomes is critical for NSC divisions, its fundamental mechanism remains unclear. A class of evolutionarily conserved protein complexes, known as condensins, is thought to be central to chromosome assembly and segregation among eukaryotes. Here we report the first comprehensive genetic study of mammalian condensins, demonstrating that two different types of condensin complexes (condensins I and II) are both essential for NSC divisions and survival in mice. Simultaneous depletion of both condensins leads to severe defects in chromosome assembly and segregation, which in turn cause DNA damage and trigger p53-induced apoptosis. Individual depletions of condensins I and II lead to slower loss of NSCs compared to simultaneous depletion, but they display distinct mitotic defects: chromosome missegregation was observed more prominently in NSCs depleted of condensin II, whereas mitotic delays were detectable only in condensin I-depleted NSCs. Remarkably, NSCs depleted of condensin II display hyperclustering of pericentric heterochromatin and nucleoli, indicating that condensin II, but not condensin I, plays a critical role in establishing interphase nuclear architecture. Intriguingly, these defects are taken over to postmitotic neurons. Our results demonstrate that condensins I and II have overlapping and non-overlapping functions in NSCs, and also provide evolutionary insight into intricate balancing acts of the two condensin complexes. Citation: Nishide K, Hirano T (2014) Overlapping and Non-overlapping Functions of Condensins I and II in Neural Stem Cell Divisions.
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Gene Networks Activated by Specific Patterns of Action Potentials in Dorsal Root Ganglia Neurons Received: 10 August 2016 Philip R
www.nature.com/scientificreports OPEN Gene networks activated by specific patterns of action potentials in dorsal root ganglia neurons Received: 10 August 2016 Philip R. Lee1,*, Jonathan E. Cohen1,*, Dumitru A. Iacobas2,3, Sanda Iacobas2 & Accepted: 23 January 2017 R. Douglas Fields1 Published: 03 March 2017 Gene regulatory networks underlie the long-term changes in cell specification, growth of synaptic connections, and adaptation that occur throughout neonatal and postnatal life. Here we show that the transcriptional response in neurons is exquisitely sensitive to the temporal nature of action potential firing patterns. Neurons were electrically stimulated with the same number of action potentials, but with different inter-burst intervals. We found that these subtle alterations in the timing of action potential firing differentially regulates hundreds of genes, across many functional categories, through the activation or repression of distinct transcriptional networks. Our results demonstrate that the transcriptional response in neurons to environmental stimuli, coded in the pattern of action potential firing, can be very sensitive to the temporal nature of action potential delivery rather than the intensity of stimulation or the total number of action potentials delivered. These data identify temporal kinetics of action potential firing as critical components regulating intracellular signalling pathways and gene expression in neurons to extracellular cues during early development and throughout life. Adaptation in the nervous system in response to external stimuli requires synthesis of new gene products in order to elicit long lasting changes in processes such as development, response to injury, learning, and memory1. Information in the environment is coded in the pattern of action-potential firing, therefore gene transcription must be regulated by the pattern of neuronal firing.
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The Genetic Program of Pancreatic Beta-Cell Replication in Vivo
Page 1 of 65 Diabetes The genetic program of pancreatic beta-cell replication in vivo Agnes Klochendler1, Inbal Caspi2, Noa Corem1, Maya Moran3, Oriel Friedlich1, Sharona Elgavish4, Yuval Nevo4, Aharon Helman1, Benjamin Glaser5, Amir Eden3, Shalev Itzkovitz2, Yuval Dor1,* 1Department of Developmental Biology and Cancer Research, The Institute for Medical Research Israel-Canada, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel 2Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot, Israel. 3Department of Cell and Developmental Biology, The Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem 91904, Israel 4Info-CORE, Bioinformatics Unit of the I-CORE Computation Center, The Hebrew University and Hadassah, The Institute for Medical Research Israel- Canada, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel 5Endocrinology and Metabolism Service, Department of Internal Medicine, Hadassah-Hebrew University Medical Center, Jerusalem 91120, Israel *Correspondence: [email protected] Running title: The genetic program of pancreatic β-cell replication 1 Diabetes Publish Ahead of Print, published online March 18, 2016 Diabetes Page 2 of 65 Abstract The molecular program underlying infrequent replication of pancreatic beta- cells remains largely inaccessible. Using transgenic mice expressing GFP in cycling cells we sorted live, replicating beta-cells and determined their transcriptome. Replicating beta-cells upregulate hundreds of proliferation- related genes, along with many novel putative cell cycle components. Strikingly, genes involved in beta-cell functions, namely glucose sensing and insulin secretion were repressed. Further studies using single molecule RNA in situ hybridization revealed that in fact, replicating beta-cells double the amount of RNA for most genes, but this upregulation excludes genes involved in beta-cell function.
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Ki-67 and Condensins Support the Integrity of Mitotic Chromosomes
© 2018. Published by The Company of Biologists Ltd | Journal of Cell Science (2018) 131, jcs212092. doi:10.1242/jcs.212092 RESEARCH ARTICLE Ki-67 and condensins support the integrity of mitotic chromosomes through distinct mechanisms Masatoshi Takagi1,*, Takao Ono2, Toyoaki Natsume3, Chiyomi Sakamoto4, Mitsuyoshi Nakao4, Noriko Saitoh4,5, Masato T. Kanemaki3, Tatsuya Hirano2 and Naoko Imamoto1 ABSTRACT has shown that structures reminiscent of mitotic chromosomes can be in vitro Although condensins play essential roles in mitotic chromosome reconstituted using a limited number of purified factors, α assembly, Ki-67 (also known as MKI67), a protein localizing to the including core histones, three histone chaperones, topoisomerase II α periphery of mitotic chromosomes, had also been shown to make a (topo II ) and condensin I (Shintomi et al., 2015). It is clear, however, contribution to the process. To examine their respective roles, we that this list represents a minimum set of proteins required for building generated a set of HCT116-based cell lines expressing Ki-67 and/or mitotic chromosomes, and that additional proteins must cooperate to condensin subunits that were fused with an auxin-inducible degron for provide them with physical and physicochemical properties that their conditional degradation. Both the localization and the dynamic support and promote their own segregation. Candidates for such behavior of Ki-67 on mitotic chromosomes were not largely affected proteins include linker histones (Maresca et al., 2005), the upon depletion of condensin subunits, and vice versa. When both Ki- chromokinesin KIF4 (Mazumdar et al., 2006; Samejima et al., 67 and SMC2 (a core subunit of condensins) were depleted, ball-like 2012; Takahashi et al., 2016) and Ki-67 (also known as MKI67) chromosome clusters with no sign of discernible thread-like structures (Booth et al., 2016; Takagi et al., 2016).
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1 SUPPLEMENTAL DATA Figure S1. Poly I:C Induces IFN-Β Expression
SUPPLEMENTAL DATA Figure S1. Poly I:C induces IFN-β expression and signaling. Fibroblasts were incubated in media with or without Poly I:C for 24 h. RNA was isolated and processed for microarray analysis. Genes showing >2-fold up- or down-regulation compared to control fibroblasts were analyzed using Ingenuity Pathway Analysis Software (Red color, up-regulation; Green color, down-regulation). The transcripts with known gene identifiers (HUGO gene symbols) were entered into the Ingenuity Pathways Knowledge Base IPA 4.0. Each gene identifier mapped in the Ingenuity Pathways Knowledge Base was termed as a focus gene, which was overlaid into a global molecular network established from the information in the Ingenuity Pathways Knowledge Base. Each network contained a maximum of 35 focus genes. 1 Figure S2. The overlap of genes regulated by Poly I:C and by IFN. Bioinformatics analysis was conducted to generate a list of 2003 genes showing >2 fold up or down- regulation in fibroblasts treated with Poly I:C for 24 h. The overlap of this gene set with the 117 skin gene IFN Core Signature comprised of datasets of skin cells stimulated by IFN (Wong et al, 2012) was generated using Microsoft Excel. 2 Symbol Description polyIC 24h IFN 24h CXCL10 chemokine (C-X-C motif) ligand 10 129 7.14 CCL5 chemokine (C-C motif) ligand 5 118 1.12 CCL5 chemokine (C-C motif) ligand 5 115 1.01 OASL 2'-5'-oligoadenylate synthetase-like 83.3 9.52 CCL8 chemokine (C-C motif) ligand 8 78.5 3.25 IDO1 indoleamine 2,3-dioxygenase 1 76.3 3.5 IFI27 interferon, alpha-inducible
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NCAPG Dynamically Coordinates the Myogenesis of Fetal Bovine Tissue by Adjusting Chromatin Accessibility
International Journal of Molecular Sciences Article NCAPG Dynamically Coordinates the Myogenesis of Fetal Bovine Tissue by Adjusting Chromatin Accessibility 1,2, 1, 3 4 1 1 1 Xin Hu y, Yishen Xing y, Xing Fu , Qiyuan Yang , Ling Ren , Yahui Wang , Qian Li , Junya Li 1,* and Lupei Zhang 1,* 1 Key Laboratory of Animal Genetics Breeding and Reproduction, Ministry of Agriculture and Rural Affairs; Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China; [email protected] (X.H.); [email protected] (Y.X.); [email protected] (L.R.); [email protected] (Y.W.); [email protected] (Q.L.) 2 Molecular and Cellular Biology, Gembloux Agro-Bio Tech, University of Liège, 5030 Gembloux, Belgium 3 School of Animal Sciences, Louisiana State University Agricultural Center, Baton Rouge, LA 70803, USA; [email protected] 4 Department of Molecular, Cell and Cancer Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA; [email protected] * Correspondence: [email protected] (L.Z.); [email protected] (J.L.) These authors contributed equally to this work. y Received: 29 January 2020; Accepted: 11 February 2020; Published: 13 February 2020 Abstract: NCAPG is a subunit of condensin I that plays a crucial role in chromatin condensation during mitosis. NCAPG has been demonstrated to be associated with farm animal growth traits. However, its role in regulating myoblast differentiation is still unclear. We used myoblasts derived from fetal bovine tissue as an in vitro model and found that NCAPG was expressed during myogenic differentiation in the cytoplasm and nucleus. Silencing NCAPG prolonged the mitosis and impaired the differentiation due to increased myoblast apoptosis.
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Mutations in Genes Encoding Condensin Complex Proteins Cause Microcephaly Through Decatenation Failure at Mitosis
Downloaded from genesdev.cshlp.org on September 25, 2021 - Published by Cold Spring Harbor Laboratory Press Mutations in genes encoding condensin complex proteins cause microcephaly through decatenation failure at mitosis Carol-Anne Martin,1,17 Jennie E. Murray,1,17 Paula Carroll,1 Andrea Leitch,1 Karen J. Mackenzie,1 Mihail Halachev,1 Ahmed E. Fetit,1 Charlotte Keith,2 Louise S. Bicknell,1,3 Adeline Fluteau,1 Philippe Gautier,1 Emma A. Hall,1 Shelagh Joss,4 Gabriela Soares,5 João Silva,6,7 Michael B. Bober,8 Angela Duker,8 Carol A. Wise,9,10,11,12 Alan J. Quigley,13 Shubha R. Phadke,14 The Deciphering Developmental Disorders Study,15 Andrew J. Wood,1 Paola Vagnarelli,16 and Andrew P. Jackson1 1MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh EH4 2XU, United Kingdom; 2South East Scotland Cytogenetics Service, Western General Hospital, Edinburgh EH4 2XU, United Kingdom; 3Department of Pathology, Dunedin School of Medicine, University of Otago, Dunedin 9054, New Zealand; 4West of Scotland Genetic Service, Southern General Hospital, Glasgow G51 4TF, United Kingdom; 5Centro de Genética Médica Doutor Jacinto Magalhães, Centro Hospitalar do Porto, 4099-028 Porto, Portugal; 6Instituto de Biologia Molecular e Celular IBMC, 4150 Porto, Portugal; 7Instituto de Investigação e Inovação em Saúde (I3S), Universidade do Porto, 4200-135 Porto, Portugal; 8Division of Genetics, Department of Pediatrics, A.I. duPont Hospital for Children, Wilmington, Delaware 19803, USA; 9Sarah M. and Charles E. Seay
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