TXNL4A Rabbit Pab

Total Page：16

File Type：pdf, Size：1020Kb

Leader in Biomolecular Solutions for Life Science TXNL4A Rabbit pAb Catalog No.: A10138 Basic Information Background Catalog No. The protein encoded by this gene is a member of the U5 small ribonucleoprotein particle A10138 (snRNP), and is involved in pre-mRNA splicing. This protein contains a thioredoxin-like fold and it is expected to interact with multiple proteins. Protein-protein interactions Observed MW have been observed with the polyglutamine tract-binding protein 1 (PQBP1). Mutations 13kDa in both the coding region and promoter region of this gene have been associated with Burn-McKeown syndrome, which is a rare disorder characterized by craniofacial Calculated MW dysmorphisms, cardiac defects, hearing loss, and bilateral choanal atresia. A 16kDa pseudogene of this gene is found on chromosome 2. Alternative splicing results in multiple transcript variants. Category Primary antibody Applications WB Cross-Reactivity Human, Mouse Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 10907 P83876 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 1-142 of human TXNL4A (NP_006692.1). Synonyms TXNL4A;BMKS;DIB1;DIM1;SNRNP15;TXNL4;U5-15kD Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using TXNL4A antibody (A10138) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 90s. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

Copy Link

Recommended publications

A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
[Show full text]
The Capacity of Long-Term in Vitro Proliferation of Acute Myeloid
The Capacity of Long-Term in Vitro Proliferation of Acute Myeloid Leukemia Cells Supported Only by Exogenous Cytokines Is Associated with a Patient Subset with Adverse Outcome Annette K. Brenner, Elise Aasebø, Maria Hernandez-Valladares, Frode Selheim, Frode Berven, Ida-Sofie Grønningsæter, Sushma Bartaula-Brevik and Øystein Bruserud Supplementary Material S2 of S31 Table S1. Detailed information about the 68 AML patients included in the study. # of blasts Viability Proliferation Cytokine Viable cells Change in ID Gender Age Etiology FAB Cytogenetics Mutations CD34 Colonies (109/L) (%) 48 h (cpm) secretion (106) 5 weeks phenotype 1 M 42 de novo 241 M2 normal Flt3 pos 31.0 3848 low 0.24 7 yes 2 M 82 MF 12.4 M2 t(9;22) wt pos 81.6 74,686 low 1.43 969 yes 3 F 49 CML/relapse 149 M2 complex n.d. pos 26.2 3472 low 0.08 n.d. no 4 M 33 de novo 62.0 M2 normal wt pos 67.5 6206 low 0.08 6.5 no 5 M 71 relapse 91.0 M4 normal NPM1 pos 63.5 21,331 low 0.17 n.d. yes 6 M 83 de novo 109 M1 n.d. wt pos 19.1 8764 low 1.65 693 no 7 F 77 MDS 26.4 M1 normal wt pos 89.4 53,799 high 3.43 2746 no 8 M 46 de novo 26.9 M1 normal NPM1 n.d. n.d. 3472 low 1.56 n.d. no 9 M 68 MF 50.8 M4 normal D835 pos 69.4 1640 low 0.08 n.d.
[Show full text]
PQBP1, a Factor Linked to Intellectual Disability, Affects Alternative Splicing Associated with Neurite Outgrowth
Downloaded from genesdev.cshlp.org on September 26, 2021 - Published by Cold Spring Harbor Laboratory Press PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth Qingqing Wang,1 Michael J. Moore,2 Guillaume Adelmant,3,4,5 Jarrod A. Marto,3,4,5 and Pamela A. Silver1,6,7 1Department of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115, USA; 2Laboratory of Molecular Neuro- Oncology, The Rockefeller University, New York, New York 10065, USA; 3Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA; 4Blais Proteomics Center, 5Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02215, USA; 6Wyss Institute for Biologically Inspired Engineering, Harvard University, Boston, Massachusetts 02115, USA Polyglutamine-binding protein 1 (PQBP1) is a highly conserved protein associated with neurodegenerative disorders. Here, we identify PQBP1 as an alternative messenger RNA (mRNA) splicing (AS) effector capable of influencing splicing of multiple mRNA targets. PQBP1 is associated with many splicing factors, including the key U2 small nuclear ribonucleoprotein (snRNP) component SF3B1 (subunit 1 of the splicing factor 3B [SF3B] protein complex). Loss of functional PQBP1 reduced SF3B1 substrate mRNA association and led to significant changes in AS patterns. Depletion of PQBP1 in primary mouse neurons reduced dendritic outgrowth and altered AS of mRNAs enriched for functions in neuron projection development. Disease-linked PQBP1 mutants were deficient in splicing factor associations and could not complement neurite outgrowth defects. Our results indicate that PQBP1 can affect the AS of multiple mRNAs and indicate specific affected targets whose splice site determination may contribute to the disease phenotype in PQBP1-linked neurological disorders.
[Show full text]
The Intellectual Disability Gene PQBP1 Rescues Alzheimerâ€™S Disease
Molecular Psychiatry (2018) 23:2090–2110 https://doi.org/10.1038/s41380-018-0253-8 ARTICLE The intellectual disability gene PQBP1 rescues Alzheimer’s disease pathology 1 1 1 1 1 2 Hikari Tanaka ● Kanoh Kondo ● Xigui Chen ● Hidenori Homma ● Kazuhiko Tagawa ● Aurelian Kerever ● 2 3 3 4 1 1,5 Shigeki Aoki ● Takashi Saito ● Takaomi Saido ● Shin-ichi Muramatsu ● Kyota Fujita ● Hitoshi Okazawa Received: 9 May 2018 / Revised: 9 August 2018 / Accepted: 6 September 2018 / Published online: 3 October 2018 © The Author(s) 2018. This article is published with open access Abstract Early-phase pathologies of Alzheimer’s disease (AD) are attracting much attention after clinical trials of drugs designed to remove beta-amyloid (Aβ) aggregates failed to recover memory and cognitive function in symptomatic AD patients. Here, we show that phosphorylation of serine/arginine repetitive matrix 2 (SRRM2) at Ser1068, which is observed in the brains of early phase AD mouse models and postmortem end-stage AD patients, prevents its nuclear translocation by inhibiting interaction with T-complex protein subunit α. SRRM2 deﬁciency in neurons destabilized polyglutamine binding protein 1 (PQBP1), a causative gene for intellectual disability (ID), greatly affecting the splicing patterns of synapse-related genes, as 1234567890();,: 1234567890();,: demonstrated in a newly generated PQBP1-conditional knockout model. PQBP1 and SRRM2 were downregulated in cortical neurons of human AD patients and mouse AD models, and the AAV-PQBP1 vector recovered RNA splicing, the synapse phenotype, and the cognitive decline in the two mouse models. Finally, the kinases responsible for the phosphorylation of SRRM2 at Ser1068 were identiﬁed as ERK1/2 (MAPK3/1).
[Show full text]
Analysis of Alternative Splicing Associated with Aging and Neurodegeneration in the Human Brain
Downloaded from genome.cshlp.org on October 2, 2021 - Published by Cold Spring Harbor Laboratory Press Research Analysis of alternative splicing associated with aging and neurodegeneration in the human brain James R. Tollervey,1 Zhen Wang,1 Tibor Hortoba´gyi,2 Joshua T. Witten,1 Kathi Zarnack,3 Melis Kayikci,1 Tyson A. Clark,4 Anthony C. Schweitzer,4 Gregor Rot,5 Tomazˇ Curk,5 Blazˇ Zupan,5 Boris Rogelj,2 Christopher E. Shaw,2 and Jernej Ule1,6 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom; 2MRC Centre for Neurodegeneration Research, King’s College London, Institute of Psychiatry, De Crespigny Park, London SE5 8AF, United Kingdom; 3EMBL–European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, United Kingdom; 4Expression Research, Affymetrix, Inc., Santa Clara, California 95051, USA; 5Faculty of Computer and Information Science, University of Ljubljana, Trzˇasˇka 25, SI-1000 Ljubljana, Slovenia Age is the most important risk factor for neurodegeneration; however, the effects of aging and neurodegeneration on gene expression in the human brain have most often been studied separately. Here, we analyzed changes in transcript levels and alternative splicing in the temporal cortex of individuals of different ages who were cognitively normal, affected by frontotemporal lobar degeneration (FTLD), or affected by Alzheimer’s disease (AD). We identified age-related splicing changes in cognitively normal individuals and found that these were present also in 95% of individuals with FTLD or AD, independent of their age. These changes were consistent with increased polypyrimidine tract binding protein (PTB)– dependent splicing activity. We also identified disease-specific splicing changes that were present in individuals with FTLD or AD, but not in cognitively normal individuals.
[Show full text]
Specificity Profiles of Protein Recognition Domains in the Molecular Medicine
Aus dem Institut für Medizinische Immunologie der Medizinischen Fakultät Charité – Universitätsmedizin Berlin DISSERTATION Specificity Profiles of Protein Recognition Domains in the Molecular Medicine zur Erlangung des akademischen Grades Doctor rerum medicinalium (Dr. rer. medic.) vorgelegt der Medizinischen Fakultät Charité – Universitätsmedizin Berlin von Víctor E. Tapia Mancilla aus Valparaíso, Chile Datum der Promotion: .. 22.06.2014.......................... Inhaltsverzeichnis Zusammenfassung.................................................................................................................................................1 ABSTRAKT......................................................................................................................................................................1 ABSTRACT ....................................................................................................................................................................2 INTRODUCTION ............................................................................................................................................................3 Specificity Profiles......................................................................................................................................................3 BAG-Family Co-Chaperone Commitment in Proteostasis.........................................................................................4 The Intriguing Role of PQBP1 in X-LID.....................................................................................................................5
[Show full text]
Host Cell Factors Necessary for Influenza a Infection: Meta-Analysis of Genome Wide Studies
Host Cell Factors Necessary for Influenza A Infection: Meta-Analysis of Genome Wide Studies Juliana S. Capitanio and Richard W. Wozniak Department of Cell Biology, Faculty of Medicine and Dentistry, University of Alberta Abstract: The Influenza A virus belongs to the Orthomyxoviridae family. Influenza virus infection occurs yearly in all countries of the world. It usually kills between 250,000 and 500,000 people and causes severe illness in millions more. Over the last century alone we have seen 3 global influenza pandemics. The great human and financial cost of this disease has made it the second most studied virus today, behind HIV. Recently, several genome-wide RNA interference studies have focused on identifying host molecules that participate in Influen- za infection. We used nine of these studies for this meta-analysis. Even though the overlap among genes identified in multiple screens was small, network analysis indicates that similar protein complexes and biological functions of the host were present. As a result, several host gene complexes important for the Influenza virus life cycle were identified. The biological function and the relevance of each identified protein complex in the Influenza virus life cycle is further detailed in this paper. Background and PA bound to the viral genome via nucleoprotein (NP). The viral core is enveloped by a lipid membrane derived from Influenza virus the host cell. The viral protein M1 underlies the membrane and anchors NEP/NS2. Hemagglutinin (HA), neuraminidase Viruses are the simplest life form on earth. They parasite host (NA), and M2 proteins are inserted into the envelope, facing organisms and subvert the host cellular machinery for differ- the viral exterior.
[Show full text]
Mutations in the Polyglutamine Binding Protein 1 Gene Cause X
BRIEF COMMUNICATIONS 1. Schrimshaw, N.S. & Murray, E.B. Am. J. Clin. Nutr. 48, 1059–1179 (1988). 9. Dunner, S. et al. Genet. Sel. Evol. 35, 103–118 (2003). 2. Feldman, M.W. & Cavalli-Sforza, L.L. in Mathematical evolutionary theory (ed. 10. Loftus, R.T. et al. Mol. Ecol. 8, 2015–2022 (1999). Feldman, M.W.) 145–173 (Princeton University Press, Princeton, New Jersey, 11. MacHugh, D.E., Loftus, R.T., Cunningham, P. & Bradley, D.G. Anim. Genet. 29, 1989). 333–340 (1998). 3. Midgley, M.S. TRB Culture: The First Farmers of the North European Plain 12. Medjugorac, I., Kustermann, W., Lazar, P., Russ, I. & Pirchner, F. Anim. Genet. 25, (Edinburgh University Press, Edinburgh, 1992). 19–27 (1994). 4. Enattah, N.S. et al. Nat. Genet. 30, 233–237 (2002). 13. Troy, C. et al. Nature 410, 1088–1091 (2001). 5. Ward, R., Honeycutt, L. & Derr, J.N. Genetics 147, 1863–1872 (1997). 14. Hill, A.V., Jepson, A., Plebanski, M. & Gilbert, S.C. Philos. Trans. R. Soc. Lond. B 6. Dudd, S. & Evershed, P. Science 282, 1478–1480 (1998). Biol. Sci. 352, 1317–1325 (1997). 7. Balasse, M. & Tresset, A. J. Archaeol. Sci. 29, 853–859 (2002). 15. Zvelebil, M. in Archaeogenetics: DNA and the Population History of Europe (ed. 8. Tishkoff, S.A. et al. Science 293, 455–462 (2001). Boyle, K.) 57–79 (MacDonald Institute Cambridge, Cambridge, 2000). Mutations in the polyglutamine deleted in affected males of family N40 (ref. 4). In all families, these mutations segregated with the disease and were present in all oblig- binding protein 1 gene cause X- ate heterozygotes that we tested.
[Show full text]
Chromosome 18 Gene Dosage Map 2.0
Human Genetics (2018) 137:961–970 https://doi.org/10.1007/s00439-018-1960-6 ORIGINAL INVESTIGATION Chromosome 18 gene dosage map 2.0 Jannine D. Cody1,2 · Patricia Heard1 · David Rupert1 · Minire Hasi‑Zogaj1 · Annice Hill1 · Courtney Sebold1 · Daniel E. Hale1,3 Received: 9 August 2018 / Accepted: 14 November 2018 / Published online: 17 November 2018 © Springer-Verlag GmbH Germany, part of Springer Nature 2018 Abstract In 2009, we described the first generation of the chromosome 18 gene dosage maps. This tool included the annotation of each gene as well as each phenotype associated region. The goal of these annotated genetic maps is to provide clinicians with a tool to appreciate the potential clinical impact of a chromosome 18 deletion or duplication. These maps are continually updated with the most recent and relevant data regarding chromosome 18. Over the course of the past decade, there have also been advances in our understanding of the molecular mechanisms underpinning genetic disease. Therefore, we have updated the maps to more accurately reflect this knowledge. Our Gene Dosage Map 2.0 has expanded from the gene and phenotype maps to also include a pair of maps specific to hemizygosity and suprazygosity. Moreover, we have revamped our classification from mechanistic definitions (e.g., haplosufficient, haploinsufficient) to clinically oriented classifications (e.g., risk factor, conditional, low penetrance, causal). This creates a map with gradient of classifications that more accurately represents the spectrum between the two poles of pathogenic and benign. While the data included in this manuscript are specific to chro- mosome 18, they may serve as a clinically relevant model that can be applied to the rest of the genome.
[Show full text]
Genome-Wide CRISPR-Cas9 Screens Reveal Loss of Redundancy Between PKMYT1 and WEE1 in Glioblastoma Stem-Like Cells
Article Genome-wide CRISPR-Cas9 Screens Reveal Loss of Redundancy between PKMYT1 and WEE1 in Glioblastoma Stem-like Cells Graphical Abstract Authors Chad M. Toledo, Yu Ding, Pia Hoellerbauer, ..., Bruce E. Clurman, James M. Olson, Patrick J. Paddison Correspondence [email protected] (J.M.O.), [email protected] (P.J.P.) In Brief Patient-derived glioblastoma stem-like cells (GSCs) can be grown in conditions that preserve patient tumor signatures and their tumor initiating capacity. Toledo et al. use these conditions to perform genome-wide CRISPR-Cas9 lethality screens in both GSCs and non- transformed NSCs, revealing PKMYT1 as a candidate GSC-lethal gene. Highlights d CRISPR-Cas9 lethality screens performed in patient brain- tumor stem-like cells d PKMYT1 is identiﬁed in GSCs, but not NSCs, as essential for facilitating mitosis d PKMYT1 and WEE1 act redundantly in NSCs, where their inhibition is synthetic lethal d PKMYT1 and WEE1 redundancy can be broken by over- activation of EGFR and AKT Toledo et al., 2015, Cell Reports 13, 2425–2439 December 22, 2015 ª2015 The Authors http://dx.doi.org/10.1016/j.celrep.2015.11.021 Cell Reports Article Genome-wide CRISPR-Cas9 Screens Reveal Loss of Redundancy between PKMYT1 and WEE1 in Glioblastoma Stem-like Cells Chad M. Toledo,1,2,14 Yu Ding,1,14 Pia Hoellerbauer,1,2 Ryan J. Davis,1,2,3 Ryan Basom,4 Emily J. Girard,3 Eunjee Lee,5 Philip Corrin,1 Traver Hart,6,7 Hamid Bolouri,1 Jerry Davison,4 Qing Zhang,4 Justin Hardcastle,1 Bruce J. Aronow,8 Christopher L.
[Show full text]
Supplementary Table 1: Genes Located on Chromosome 18P11-18Q23, an Area Significantly Linked to TMPRSS2-ERG Fusion
Supplementary Table 1: Genes located on Chromosome 18p11-18q23, an area significantly linked to TMPRSS2-ERG fusion Symbol Cytoband Description LOC260334 18p11 HSA18p11 beta-tubulin 4Q pseudogene IL9RP4 18p11.3 interleukin 9 receptor pseudogene 4 LOC100132166 18p11.32 hypothetical LOC100132166 similar to Rho-associated protein kinase 1 (Rho- associated, coiled-coil-containing protein kinase 1) (p160 LOC727758 18p11.32 ROCK-1) (p160ROCK) (NY-REN-35 antigen) ubiquitin specific peptidase 14 (tRNA-guanine USP14 18p11.32 transglycosylase) THOC1 18p11.32 THO complex 1 COLEC12 18pter-p11.3 collectin sub-family member 12 CETN1 18p11.32 centrin, EF-hand protein, 1 CLUL1 18p11.32 clusterin-like 1 (retinal) C18orf56 18p11.32 chromosome 18 open reading frame 56 TYMS 18p11.32 thymidylate synthetase ENOSF1 18p11.32 enolase superfamily member 1 YES1 18p11.31-p11.21 v-yes-1 Yamaguchi sarcoma viral oncogene homolog 1 LOC645053 18p11.32 similar to BolA-like protein 2 isoform a similar to 26S proteasome non-ATPase regulatory LOC441806 18p11.32 subunit 8 (26S proteasome regulatory subunit S14) (p31) ADCYAP1 18p11 adenylate cyclase activating polypeptide 1 (pituitary) LOC100130247 18p11.32 similar to cytochrome c oxidase subunit VIc LOC100129774 18p11.32 hypothetical LOC100129774 LOC100128360 18p11.32 hypothetical LOC100128360 METTL4 18p11.32 methyltransferase like 4 LOC100128926 18p11.32 hypothetical LOC100128926 NDC80 homolog, kinetochore complex component (S. NDC80 18p11.32 cerevisiae) LOC100130608 18p11.32 hypothetical LOC100130608 structural maintenance
[Show full text]
A New Microdeletion Syndrome Involving TBC1D24, ATP6V0C and PDPK1 Causes Epilepsy, Microcephaly and Developmental Delay. Bettina
Manuscript (All Manuscript Text Pages, including Title Page, References and Figure Legends) A new microdeletion syndrome involving TBC1D24, ATP6V0C and PDPK1 causes epilepsy, microcephaly and developmental delay. Bettina E Mucha1, Siddhart Banka2, Norbert Fonya Ajeawung3, Sirinart Molidperee3, Gary G Chen4, Mary Kay Koenig5, Rhamat B Adejumo5, Marianne Till6, Michael Harbord7, Renee Perrier8, Emmanuelle Lemyre9, Renee-Myriam Boucher10, Brian G Skotko11, Jessica L Waxler11, Mary Ann Thomas8, Jennelle C Hodge12, Jozef Gecz13, Jillian Nicholl14, Lesley McGregor14, Tobias Linden15, Sanjay M Sisodiya16, Damien Sanlaville6, Sau W Cheung17, Carl Ernst4, Philippe M Campeau9 1. Division of Medical Genetics, Department of Specialized Medicine, McGill University Health Centre, Montreal, QC, Canada. 2. Division of Evolution and Genomic Sciences, School of Biological Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, M13 9PL, Manchester, UK. 3. Centre de Recherche du CHU Sainte-Justine, Montreal, QC, Canada 4. Department of Psychiatry, McGill University, Montreal, Canada. 5. Department of Pediatrics, Division of Child & Adolescent Neurology, The University of Texas McGovern Medical School, Houston, Texas, USA. 6. Service de Génétique CHU de Lyon-GH Est, Lyon, France. 7. Department of Pediatrics, Flinders Medical Centre, Bedford Park, South Australia, Australia. ___________________________________________________________________ This is the author's manuscript of the article published in final edited form as: Mucha, B. E., Banka, S., Ajeawung, N. F., Molidperee, S., Chen, G. G., Koenig, M. K., … Campeau, P. M. (2018). A new microdeletion syndrome involving TBC1D24, ATP6V0C , and PDPK1 causes epilepsy, microcephaly, and developmental delay. Genetics in Medicine, 1. https://doi.org/10.1038/s41436-018-0290-3 8. Department of Medical Genetics, University of Calgary, Calgary, AB, Canada.
[Show full text]