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3. ALG1‐CDG: Clinical and Molecular Characterization of 39 Unreported Patients

Author

Ng, Bobby G, Shiryaev, Sergey A, Rymen, Daisy, Eklund, Erik A, Raymond, Kimiyo, Kircher, Martin, Abdenur, Jose E, Alehan, Fusun, Midro, Alina T, Bamshad, Michael J, Barone, Rita, Berry, Gerard T, Brumbaugh, Jane E, Buckingham, Kati J, Clarkson, Katie, Cole, F Sessions, O'Connor, Shawn, Cooper, Gregory M, Coster, Rudy, Demmer, Laurie A, Diogo, Luisa, Fay, Alexander J, Ficicioglu, Can, Fiumara, Agata, Gahl, William A, Ganetzky, Rebecca, Goel, Himanshu, Harshman, Lyndsay A, He, Miao, Jaeken, Jaak, James, Philip M, Katz, Daniel, Keldermans, Liesbeth, Kibaek, Maria, Kornberg, Andrew J, Lachlan, Katherine, Lam, Christina, Yaplito‐Lee, Joy, Nickerson, Deborah A, Peters, Heidi L, Race, Valerie, Régal, Luc, Rush, Jeffrey S, Rutledge, S Lane, Shendure, Jay, Souche, Erika, Sparks, Susan E, Trapane, Pamela, Sanchez‐Valle, Amarilis, Vilain, Eric, Vøllo, Arve, Waechter, Charles J, Wang, Raymond Y, Wolfe, Lynne A, Wong, Derek A, Wood, Tim, Yang, Amy C, Genomics, University of Washington Center for Mendelian, Matthijs, Gert, and Freeze, Hudson H

Subjects
Biochemistry and Cell Biology, Biomedical and Clinical Sciences, Biological Sciences, Pediatric, Clinical Research, Rare Diseases, Genetics, 2.1 Biological and endogenous factors, Aetiology, Biomarkers, Congenital Disorders of Glycosylation, Female, Genes, Lethal, Glycosylation, Humans, Male, Mannosyltransferases, Mutation, Polysaccharides, Sequence Analysis, DNA, Survival Analysis, CDG, asparagine-linked glycosylation protein 1, carbohydrate-deficient transferrin, xeno-tetrasaccharide, University of Washington Center for Mendelian Genomics, Clinical Sciences, Genetics & Heredity, Clinical sciences
Abstract

Congenital disorders of glycosylation (CDG) arise from pathogenic mutations in over 100 genes leading to impaired protein or lipid glycosylation. ALG1 encodes a β1,4 mannosyltransferase that catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation. ALG1 mutations cause a rare autosomal recessive disorder termed ALG1-CDG. To date 13 mutations in 18 patients from 14 families have been described with varying degrees of clinical severity. We identified and characterized 39 previously unreported cases of ALG1-CDG from 32 families and add 26 new mutations. Pathogenicity of each mutation was confirmed based on its inability to rescue impaired growth or hypoglycosylation of a standard biomarker in an alg1-deficient yeast strain. Using this approach we could not establish a rank order comparison of biomarker glycosylation and patient phenotype, but we identified mutations with a lethal outcome in the first two years of life. The recently identified protein-linked xeno-tetrasaccharide biomarker, NeuAc-Gal-GlcNAc2 , was seen in all 27 patients tested. Our study triples the number of known patients and expands the molecular and clinical correlates of this disorder.

Published
2016

5. The relationship between beta-ureidopropionase deficiency due to UPB1 variants and human phenotypes is uncertain

Author

Righetti, Sarah, Allcock, Richard J. N., Yaplito-Lee, Joy, Adams, Louisa, Ellaway, Carolyn, Jones, Kristi J., Selvanathan, Arthavan, Fletcher, Janice, Pitt, James, van Kuilenburg, André B. P., Delatycki, Martin B., Laing, Nigel G., Kirk, Edwin P., Laboratory Genetic Metabolic Diseases, and Amsterdam Gastroenterology Endocrinology Metabolism

Subjects
Literature review, Purine-Pyrimidine Metabolism, Inborn Errors, Brain Diseases, Movement Disorders, Carrier frequency, Endocrinology, Diabetes and Metabolism, UPB1, Beta-ureidopropionase deficiency, Biochemistry, Phenotype, Endocrinology, β-ureidopropionase, Genetics, Humans, Variant, Molecular Biology
Abstract

Background: Beta-ureidopropionase deficiency, caused by variants in UPB1, has been reported in association with various neurodevelopmental phenotypes including intellectual disability, seizures and autism. Aim: We aimed to reassess the relationship between variants in UPB1 and a clinical phenotype. Methods: Literature review, calculation of carrier frequencies from population databases, long-term follow-up of a previously published case and reporting of additional cases. Results: Fifty-three published cases were identified, and two additional cases are reported here. Of these, 14 were asymptomatic and four had transient neurological features; clinical features in the remainder were variable and included non-neurological presentations. Several of the variants previously reported as pathogenic are present in population databases at frequencies higher than expected for a rare condition. In particular, the variant most frequently reported as pathogenic, p.Arg326Gln, is very common among East Asians, with a carrier frequency of 1 in 19 and 1 in 907 being homozygous for the variant in gnomAD v2.1.1. Conclusion: Pending the availability of further evidence, UPB1 should be considered a ‘gene of uncertain clinical significance’. Caution should be used in ascribing clinical significance to biochemical features of beta-ureidopropionase deficiency and/or UPB1 variants in patients with neurodevelopmental phenotypes. UPB1 is not currently suitable for inclusion in gene panels for reproductive genetic carrier screening. Synopsis: The relationship between beta-ureidopropionase deficiency due to UPB1 variants and clinical phenotypes is uncertain.

Published
2022

7. A cryptic pathogenicNDUFV1variant identified by RNA ‐seq in a patient with normal complex I activity in muscle and transient magnetic resonance imaging changes

Author

Kiss, Sharmila, primary, Christodoulou, John, additional, Thorburn, David R., additional, Freeman, Jeremy L., additional, Kornberg, Andrew J., additional, Mandelstam, Simone, additional, Compton, Alison G., additional, Cummings, Beryl, additional, Pais, Lynn, additional, Yaplito‐Lee, Joy, additional, and White, Susan M., additional

Published
2023
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8. MOGS‐ CDG: Quantitative analysis of the diagnosticGlc 3 Mantetrasaccharide and clinical spectrum of six new cases

Author

Post, Merel A., primary, de Wit, Isis, additional, Zijlstra, Fokje S. M., additional, Engelke, Udo F. H., additional, van Rooij, Arno, additional, Christodoulou, John, additional, Tan, Tiong Yang, additional, Le Fevre, Anna, additional, Jin, Danqun, additional, Yaplito‐Lee, Joy, additional, Lee, Beom Hee, additional, Low, Karen J., additional, Mallick, Andrew A., additional, Õunap, Katrin, additional, Pitt, James, additional, Reardon, William, additional, Vals, Mari‐Anne, additional, Wortmann, Saskia B., additional, Wessels, Hans J. C. T., additional, Bärenfänger, Melissa, additional, van Karnebeek, Clara D. M., additional, and Lefeber, Dirk J., additional

Published
2023
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10. A scoring system predicting the clinical course of CLPB defect based on the foetal and neonatal presentation of 31 patients

Author

Pronicka, Ewa, Ropacka-Lesiak, Mariola, Trubicka, Joanna, Pajdowska, Magdalena, Linke, Markus, Ostergaard, Elsebet, Saunders, Carol, Horsch, Sandra, van Karnebeek, Clara, Yaplito-Lee, Joy, Distelmaier, Felix, Õunap, Katrin, Rahman, Shamima, Castelle, Martin, Kelleher, John, Baris, Safa, Iwanicka-Pronicka, Katarzyna, Steward, Colin G., Ciara, Elżbieta, Wortmann, Saskia B., Piekutowska-Abramczuk, Dorota, Rokicki, Dariusz, Fałek, Olga, Nowak, Anna, Brązert, Krystyna, Green, Andrew, Mayr, Johannes A., and Additional individual contributors

Published
2017
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11. A cryptic pathogenic NDUFV1 variant identified by RNA‐seq in a patient with normal complex I activity in muscle and transient magnetic resonance imaging changes.

Author

Kiss, Sharmila, Christodoulou, John, Thorburn, David R., Freeman, Jeremy L., Kornberg, Andrew J., Mandelstam, Simone, Compton, Alison G., Cummings, Beryl, Pais, Lynn, Yaplito‐Lee, Joy, and White, Susan M.

Abstract

Mitochondrial respiratory chain disorders (MRC) are amongst the most common group of inborn errors of metabolism. MRC, of which complex I deficiency accounts for approximately a quarter, are very diverse, causing a wide range of clinical problems and can be difficult to diagnose. We report an illustrative MRC case whose diagnosis was elusive. Clinical signs included failure to thrive caused by recurrent vomiting, hypotonia and progressive loss of motor milestones. Initial brain imaging suggested Leigh syndrome but without expected diffusion restriction. Muscle respiratory chain enzymology was unremarkable. Whole‐genome sequencing identified a maternally inherited NDUFV1 missense variant [NM_007103.4 (NDUFV1):c.1157G > A; p.(Arg386His)] and a paternally inherited synonymous variant [NM_007103.4 (NDUFV1):c.1080G > A; (p.Ser360=)]. RNA sequencing demonstrated aberrant splicing. This case emphasizes the diagnostic odyssey of a patient in whom a confirmed diagnosis was elusive because of atypical features and normal muscle respiratory chain enzyme (RCE) activities, along with a synonymous variant, which are often filtered out from genomic analyses. It also illustrates the following points: (1) complete resolution of magnetic resonance imaging changes may be part of the picture in mitochondrial disease; (2) analysis for synonymous variants is important for undiagnosed patients; and (3) RNA‐seq is a powerful tool to demonstrate pathogenicity of putative splicing variants. [ABSTRACT FROM AUTHOR]

Published
2023
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12. MOGS‐CDG: Quantitative analysis of the diagnostic Glc3Man tetrasaccharide and clinical spectrum of six new cases.

Author

Post, Merel A., de Wit, Isis, Zijlstra, Fokje S. M., Engelke, Udo F. H., van Rooij, Arno, Christodoulou, John, Tan, Tiong Yang, Le Fevre, Anna, Jin, Danqun, Yaplito‐Lee, Joy, Lee, Beom Hee, Low, Karen J., Mallick, Andrew A., Õunap, Katrin, Pitt, James, Reardon, William, Vals, Mari‐Anne, Wortmann, Saskia B., Wessels, Hans J. C. T., and Bärenfänger, Melissa

Abstract

Congenital disorders of glycosylation (CDG) are a clinically and biochemically heterogeneous subgroup of inherited metabolic disorders. Most CDG with abnormal N‐glycosylation can be detected by transferrin screening, however, MOGS‐CDG escapes this routine screening. Combined with the clinical heterogeneity of reported cases, diagnosing MOGS‐CDG can be challenging. Here, we clinically characterize ten MOGS‐CDG cases including six previously unreported individuals, showing a phenotype characterized by dysmorphic features, global developmental delay, muscular hypotonia, and seizures in all patients and in a minority vision problems and hypogammaglobulinemia. Glycomics confirmed accumulation of a Glc3Man7GlcNAc2 glycan in plasma. For quantification of the diagnostic Glcα1‐3Glcα1‐3Glcα1‐2Man tetrasaccharide in urine, we developed and validated a liquid chromatography‐mass spectrometry method of 2‐aminobenzoic acid (2AA) labeled urinary glycans. As an internal standard, isotopically labeled 13C6‐2AA Glc3Man was used, while labeling efficiency was controlled by use of 12C6‐2AA and 13C6‐2AA labeled laminaritetraose. Recovery, linearity, intra‐ and interassay coefficients of variability of these labeled compounds were determined. Furthermore, Glc3Man was specifically identified by retention time matching against authentic MOGS‐CDG urine and compared with Pompe urine. Glc3Man was increased in all six analyzed cases, ranging from 34.1 to 618.0 μmol/mmol creatinine (reference <5 μmol). In short, MOGS‐CDG has a broad manifestation of symptoms but can be diagnosed with the use of a quantitative method for analysis of urinary Glc3Man excretion. [ABSTRACT FROM AUTHOR]

Published
2023
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14. FGF21 outperforms GDF15 as a diagnostic biomarker of mitochondrial disease in children

Author

Riley, Lisa G., primary, Nafisinia, Michael, additional, Menezes, Minal J., additional, Nambiar, Reta, additional, Williams, Andrew, additional, Barnes, Elizabeth H., additional, Selvanathan, Arthavan, additional, Lichkus, Kate, additional, Bratkovic, Drago, additional, Yaplito-Lee, Joy, additional, Bhattacharya, Kaustuv, additional, Ellaway, Carolyn, additional, Kava, Maina, additional, Balasubramaniam, Shanti, additional, and Christodoulou, John, additional

Published
2022
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17. Mitochondrial oxidative phosphorylation disorders presenting in neonates: clinical manifestations and enzymatic and molecular diagnoses

Author

Gibson, Kate, Halliday, Jane L., Kirby, Denise M., Yaplito-Lee, Joy, Thorburn, David R., and Boneh, Avihu

Subjects
Mitochondrial diseases -- Diagnosis, Mitochondrial diseases -- Care and treatment, Mitochondrial diseases -- Research, Oxidative phosphorylation -- Research, Infants (Newborn) -- Diseases, Infants (Newborn) -- Care and treatment, Infants (Newborn) -- Research
Published
2008

22. Neuronal ceroid lipofuscinosis type 2: an Australian case series

Author

Johnson, Alexandra M, primary, Mandelstam, Simone, additional, Andrews, Ian, additional, Boysen, Katja, additional, Yaplito‐Lee, Joy, additional, Fietz, Michael, additional, Nagarajan, Lakshmi, additional, Rodriguez‐Casero, Victoria, additional, Ryan, Monique M, additional, Smith, Nicholas, additional, Scheffer, Ingrid E, additional, and Ellaway, Carolyn, additional

Published
2020
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28. Genetic, Radiologic, and Clinical Variability in Brown-Vialetto-van Laere Syndrome

Author

Woodcock, Ian R., primary, Menezes, Manoj P., additional, Coleman, Lee, additional, Yaplito-Lee, Joy, additional, Peters, Heidi, additional, White, Susan M., additional, Stapleton, Rachel, additional, Phelan, Dean G., additional, Chong, Belinda, additional, Lunke, Sebastian, additional, Stark, Zornitza, additional, Pitt, James, additional, Ryan, Monique M., additional, Robertson, Colin, additional, and Yiu, Eppie M., additional

Published
2018
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29. ALG1-CDG:Clinical and Molecular Characterization of 39 Unreported Patients

Author

Ng, Bobby G, Shiryaev, Sergey A, Rymen, Daisy, Eklund, Erik A, Raymond, Kimiyo, Kircher, Martin, Abdenur, Jose E, Alehan, Fusun, Midro, Alina T, Bamshad, Michael J, Barone, Rita, Berry, Gerard T, Brumbaugh, Jane E, Buckingham, Kati J, Clarkson, Katie, Cole, F Sessions, O'Connor, Shawn, Cooper, Gregory M, Van Coster, Rudy, Demmer, Laurie A, Diogo, Luisa, Fay, Alexander J, Ficicioglu, Can, Fiumara, Agata, Gahl, William A, Ganetzky, Rebecca, Goel, Himanshu, Harshman, Lyndsay A, He, Miao, Jaeken, Jaak, James, Philip M, Katz, Daniel, Keldermans, Liesbeth, Kibæk, Maria, Kornberg, Andrew J, Lachlan, Katherine, Lam, Christina, Yaplito-Lee, Joy, Nickerson, Deborah A, Peters, Heidi L, Race, Valerie, Régal, Luc, Rush, Jeffrey S, Rutledge, S Lane, Shendure, Jay, Souche, Erika, Sparks, Susan E, Trapane, Pamela, Sanchez-Valle, Amarilis, and Vilain, Eric

Subjects
xeno-tetrasaccharide, asparagine-linked glycosylation protein 1, CDG, carbohydrate-deficient transferrin
Abstract

Congenital disorders of glycosylation (CDG) arise from pathogenic mutations in over 100 genes leading to impaired protein or lipid glycosylation. ALG1 encodes a β1,4 mannosyltransferase that catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation. ALG1 mutations cause a rare autosomal recessive disorder termed ALG1-CDG. To date 13 mutations in 18 patients from 14 families have been described with varying degrees of clinical severity. We identified and characterized 39 previously unreported cases of ALG1-CDG from 32 families and add 26 new mutations. Pathogenicity of each mutation was confirmed based on its inability to rescue impaired growth or hypoglycosylation of a standard biomarker in an alg1-deficient yeast strain. Using this approach we could not establish a rank order comparison of biomarker glycosylation and patient phenotype, but we identified mutations with a lethal outcome in the first two years of life. The recently identified protein-linked xeno-tetrasaccharide biomarker, NeuAc-Gal-GlcNAc2 , was seen in all 27 patients tested. Our study triples the number of known patients and expands the molecular and clinical correlates of this disorder.

Published
2016

30. ALG1-CDG: Clinical and Molecular Characterization of 39 Unreported Patients

Author

Ng, Bobby G., Shiryaev, Sergey A., Rymen, Daisy, Eklund, Erik A., Raymond, Kimiyo, Kircher, Martin, Abdenur, Jose E., Alehan, Fusun, Midro, Alina T., Bamshad, Michael J., Barone, Rita, Berry, Gerard T., Brumbaugh, Jane E., Buckingham, Kati J., Clarkson, Katie, Cole, F. Sessions, O'Connor, Shawn, Cooper, Gregory M., Van Coster, Rudy, Demmer, Laurie A., Diogo, Luisa, Fay, Alexander J., Ficicioglu, Can, Fiumara, Agata, Gahl, William A., Ganetzky, Rebecca, Goel, Himanshu, Harshman, Lyndsay A., He, Miao, Jaeken, Jaak, James, Philip M., Katz, Daniel, Keldermans, Liesbeth, Kibaek, Maria, Kornberg, Andrew J., Lachlan, Katherine, Lam, Christina, Yaplito-Lee, Joy, Nickerson, Deborah A., Peters, Heidi L., Race, Valerie, Régal, Luc, Rush, Jeffrey S., Rutledge, S. Lane, Shendure, Jay, Souche, Erika, Sparks, Susan E., Trapane, Pamela, Sanchez-Valle, Amarilis, Vilain, Eric, Vollo, Arve, Waechter, Charles J., Wang, Raymond Y., Wolfe, Lynne A., Wong, Derek A., Wood, Tim, Yang, Amy C., Washington, Univ, Matthijs, Gert, Freeze, Hudson H., and Pediatrics

Subjects
Male, Glycosylation, Clinical Sciences, Lethal, Mannosyltransferases, Congenital Disorders of Glycosylation, Rare Diseases, xeno-tetrasaccharide, Polysaccharides, Clinical Research, Genetics, Humans, 2.1 Biological and endogenous factors, Aetiology, University of Washington Center for Mendelian Genomics, carbohydrate-deficient transferrin, Pediatric, Genetics & Heredity, asparagine-linked glycosylation protein 1, DNA, Survival Analysis, Genes, Mutation, Female, CDG, Sequence Analysis, Biomarkers
Abstract

Congenital disorders of glycosylation (CDG) arise from pathogenic mutations in over 100 genes leading to impaired protein or lipid glycosylation. ALG1 encodes a β1,4 mannosyltransferase that catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate required for proper N-linked glycosylation. ALG1 mutations cause a rare autosomal recessive disorder termed ALG1-CDG. To date 13 mutations in 18 patients from 14 families have been described with varying degrees of clinical severity. We identified and characterized 39 previously unreported cases of ALG1-CDG from 32 families and add 26 new mutations. Pathogenicity of each mutation was confirmed based on its inability to rescue impaired growth or hypoglycosylation of a standard biomarker in an alg1-deficient yeast strain. Using this approach we could not establish a rank order comparison of biomarker glycosylation and patient phenotype, but we identified mutations with a lethal outcome in the first two years of life. The recently identified protein-linked xeno-tetrasaccharide biomarker, NeuAc-Gal-GlcNAc2 , was seen in all 27 patients tested. Our study triples the number of known patients and expands the molecular and clinical correlates of this disorder.

Published
2016

31. ALG1-CDG: Clinical and Molecular Characterization of 39 Unreported Patients

Author

Ng, Bobby G., Shiryaev, Sergey A., Rymen, Daisy, Eklund, Erik A., Raymond, Kimiyo, Kircher, Martin, Abdenur, Jose E., Alehan, Fusun, Midro, Alina T., Bamshad, Michael J., Barone, Rita, Berry, Gerard T., Brumbaugh, Jane E., Buckingham, Kati J., Clarkson, Katie, Cole, F. Sessions, O'Connor, Shawn, Cooper, Gregory M., Van Coster, Rudy, Demmer, Laurie A., Diogo, Luisa, Fay, Alexander J., Ficicioglu, Can, Fiumara, Agata, Gahl, William A., Ganetzky, Rebecca, Goel, Himanshu, Harshman, Lyndsay A., He, Miao, Jaeken, Jaak, James, Philip M., Katz, Daniel, Keldermans, Liesbeth, Kibaek, Maria, Kornberg, Andrew J., Lachlan, Katherine, Lam, Christina, Yaplito-Lee, Joy, Nickerson, Deborah A., Peters, Heidi L., Race, Valerie, Régal, Luc, Rush, Jeffrey S., Rutledge, S. Lane, Shendure, Jay, Souche, Erika, Sparks, Susan E., Trapane, Pamela, Sanchez-Valle, Amarilis, Vilain, Eric, Vøllo, Arve, Waechter, Charles J., Wang, Raymond Y., Wolfe, Lynne A., Wong, Derek A., Wood, Tim, Yang, Amy C., Matthijs, Gert, and Freeze, Hudson H.

Subjects
Male, Glycosylation, Xenotetrasacharide, Sequence Analysis, DNA, Mannosyltransferases, Survival Analysis, CDG, Asparagine-linked glycosylation protein 1, Carbohydrate-deficient transferrin, Article, Congenital Disorders of Glycosylation, Polysaccharides, Mutation, Humans, CDG, Female, Genes, Lethal, Asparagine-linked glycosylation protein 1, Biomarkers
Abstract

Congenital disorders of glycosylation (CDG) arise from pathogenic mutations in over one hundred genes leading to impaired protein or lipid glycosylation. ALG1 encodes a β1,4 mannosyltransferase that catalyzes the addition of the first of nine mannose moieties to form a dolichol-lipid linked oligosaccharide intermediate (DLO) required for proper N-linked glycosylation. ALG1 mutations cause a rare autosomal recessive disorder termed ALG1-CDG. To date thirteen mutations in eighteen patients from fourteen families have been described with varying degrees of clinical severity. We identified and characterized thirty-nine previously unreported cases of ALG1-CDG from thirty-two families and add twenty-six new mutations. Pathogenicity of each mutation was confirmed based on its inability to rescue impaired growth or hypoglycosylation of a standard biomarker in an alg1-deficient yeast strain. Using this approach we could not establish a rank order comparison of biomarker glycosylation and patient phenotype, but we identified mutations with a lethal outcome in the first two years of life. The recently identified protein-linked xeno-tetrasaccharide biomarker, NeuAc-Gal-GlcNAc2, was seen in all twenty-seven patients tested. Our study triples the number of known patients and expands the molecular and clinical correlates of this disorder.

Published
2015

33. A prospective evaluation of whole-exome sequencing as a first-tier molecular test in infants with suspected monogenic disorders

Author

Stark, Zornitza, primary, Tan, Tiong Y., additional, Chong, Belinda, additional, Brett, Gemma R., additional, Yap, Patrick, additional, Walsh, Maie, additional, Yeung, Alison, additional, Peters, Heidi, additional, Mordaunt, Dylan, additional, Cowie, Shannon, additional, Amor, David J., additional, Savarirayan, Ravi, additional, McGillivray, George, additional, Downie, Lilian, additional, Ekert, Paul G., additional, Theda, Christiane, additional, James, Paul A., additional, Yaplito-Lee, Joy, additional, Ryan, Monique M., additional, Leventer, Richard J., additional, Creed, Emma, additional, Macciocca, Ivan, additional, Bell, Katrina M., additional, Oshlack, Alicia, additional, Sadedin, Simon, additional, Georgeson, Peter, additional, Anderson, Charlotte, additional, Thorne, Natalie, additional, Gaff, Clara, additional, and White, Susan M., additional

Published
2016
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34. CLPB Mutations Cause 3-Methylglutaconic Aciduria, Progressive Brain Atrophy, Intellectual Disability, Congenital Neutropenia, Cataracts, Movement Disorder

Author

Wortmann, Saskia B., primary, Ziętkiewicz, Szymon, additional, Kousi, Maria, additional, Szklarczyk, Radek, additional, Haack, Tobias B., additional, Gersting, Søren W., additional, Muntau, Ania C., additional, Rakovic, Aleksandar, additional, Renkema, G. Herma, additional, Rodenburg, Richard J., additional, Strom, Tim M., additional, Meitinger, Thomas, additional, Rubio-Gozalbo, M. Estela, additional, Chrusciel, Elzbieta, additional, Distelmaier, Felix, additional, Golzio, Christelle, additional, Jansen, Joop H., additional, van Karnebeek, Clara, additional, Lillquist, Yolanda, additional, Lücke, Thomas, additional, Õunap, Katrin, additional, Zordania, Riina, additional, Yaplito-Lee, Joy, additional, van Bokhoven, Hans, additional, Spelbrink, Johannes N., additional, Vaz, Frédéric M., additional, Pras-Raves, Mia, additional, Ploski, Rafal, additional, Pronicka, Ewa, additional, Klein, Christine, additional, Willemsen, Michel A.A.P., additional, de Brouwer, Arjan P.M., additional, Prokisch, Holger, additional, Katsanis, Nicholas, additional, and Wevers, Ron A., additional

Published
2015
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36. De Novo Truncating Mutations in AHDC1 in Individuals with Syndromic Expressive Language Delay, Hypotonia, and Sleep Apnea

Author

Xia, Fan, primary, Bainbridge, Matthew N., additional, Tan, Tiong Yang, additional, Wangler, Michael F., additional, Scheuerle, Angela E., additional, Zackai, Elaine H., additional, Harr, Margaret H., additional, Sutton, V. Reid, additional, Nalam, Roopa L., additional, Zhu, Wenmiao, additional, Nash, Margot, additional, Ryan, Monique M., additional, Yaplito-Lee, Joy, additional, Hunter, Jill V., additional, Deardorff, Matthew A., additional, Penney, Samantha J., additional, Beaudet, Arthur L., additional, Plon, Sharon E., additional, Boerwinkle, Eric A., additional, Lupski, James R., additional, Eng, Christine M., additional, Muzny, Donna M., additional, Yang, Yaping, additional, and Gibbs, Richard A., additional

Published
2014
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37. Mitochondrial Carbonic Anhydrase VA Deficiency Resulting from CA5A Alterations Presents with Hyperammonemia in Early Childhood

Author

van Karnebeek, Clara D., primary, Sly, William S., additional, Ross, Colin J., additional, Salvarinova, Ramona, additional, Yaplito-Lee, Joy, additional, Santra, Saikat, additional, Shyr, Casper, additional, Horvath, Gabriella A., additional, Eydoux, Patrice, additional, Lehman, Anna M., additional, Bernard, Virginie, additional, Newlove, Theresa, additional, Ukpeh, Henry, additional, Chakrapani, Anupam, additional, Preece, Mary Anne, additional, Ball, Sarah, additional, Pitt, James, additional, Vallance, Hilary D., additional, Coulter-Mackie, Marion, additional, Nguyen, Hien, additional, Zhang, Lin-Hua, additional, Bhavsar, Amit P., additional, Sinclair, Graham, additional, Waheed, Abdul, additional, Wasserman, Wyeth W., additional, and Stockler-Ipsiroglu, Sylvia, additional

Published
2014
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39. SURF1 deficiency: a multi-centre natural history study

Author

Wedatilake, Yehani, primary, Brown, Ruth M, additional, McFarland, Robert, additional, Yaplito-Lee, Joy, additional, Morris, Andrew A M, additional, Champion, Mike, additional, Jardine, Phillip E, additional, Clarke, Antonia, additional, Thorburn, David R, additional, Taylor, Robert W, additional, Land, John M, additional, Forrest, Katharine, additional, Dobbie, Angus, additional, Simmons, Louise, additional, Aasheim, Erlend T, additional, Ketteridge, David, additional, Hanrahan, Donncha, additional, Chakrapani, Anupam, additional, Brown, Garry K, additional, and Rahman, Shamima, additional

Published
2013
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41. Successful Treatment of Molybdenum Cofactor Deficiency Type A With cPMP

Author

Veldman, Alex, primary, Santamaria-Araujo, José Angel, additional, Sollazzo, Silvio, additional, Pitt, James, additional, Gianello, Robert, additional, Yaplito-Lee, Joy, additional, Wong, Flora, additional, Ramsden, Clive Andrew, additional, Reiss, Jochen, additional, Cook, Iain, additional, Fairweather, Jon, additional, and Schwarz, Guenter, additional

Published
2010
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42. Three Mendelian disorders (chronic granulomatous disease, retinitis pigmentosa, ornithine transcarbamylase deficiency) in a young woman with an X chromosome deletion, del(X)(p11.4p21.1)

Author

Coman, David, primary, Yaplito-Lee, Joy, additional, La, Phung, additional, Nasioulas, Steven, additional, Bruno, Damien, additional, Slater, Howard R., additional, Stock-Myer, Sharyn E., additional, Lynch, Elly L., additional, and Gardner, R.J. McKinlay, additional

Published
2010
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43. Expanded Newborn Screening: Outcome in Screened and Unscreened Patients at Age 6 Years

Author

Wilcken, Bridget, primary, Haas, Marion, additional, Joy, Pamela, additional, Wiley, Veronica, additional, Bowling, Francis, additional, Carpenter, Kevin, additional, Christodoulou, John, additional, Cowley, David, additional, Ellaway, Carolyn, additional, Fletcher, Janice, additional, Kirk, Edwin P., additional, Lewis, Barry, additional, McGill, Jim, additional, Peters, Heidi, additional, Pitt, James, additional, Ranieri, Enzo, additional, Yaplito-Lee, Joy, additional, and Boneh, Avihu, additional

Published
2009
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45. Diagnosis and stabilisation of familial chylomicronemia syndrome in two infants presenting with hypertriglyceridemia-induced acute pancreatitis.

Author

Heath O, Allender B, Smith J, Savva E, Spencer L, Bannister EG, Brown NJ, Evans MS, Kiss S, Rozen TH, and Yaplito-Lee J

Abstract

Familial chylomicronemia syndrome (FCS) is a rare disorder of triglyceride (TG) metabolism caused by loss of function variants in one of five known canonical genes involved in chylomicron lipolysis and clearance- LPL , APOC2 , APOA5 , LMF1 , and GPIHBP1 . Pathogenic variants in LPL , which encodes the hydrolytic enzyme lipoprotein lipase, account for over 80%-90% of cases. FCS may present in infancy with hypertriglyceridemia-induced acute pancreatitis and is challenging to manage both acutely and in the long-term. Here, we report our experience managing two unrelated infants consecutively diagnosed with hypertriglyceridemia-induced acute pancreatitis caused by LPL deficiency. Both had elevated TGs at presentation (205 and 30 mmol/L, respectively) and molecular genetic testing confirmed each infant carried a different homozygous pathogenic variant in the LPL gene, specifically, c.987C>A (p.Tyr329Ter) and c.632C>A (p.Thr211Lys). The more severely affected infant had cutaneous xanthomata, lipemia retinalis and lipemic plasma at presentation, and required management in an intensive care setting. Acute stabilisation was achieved using insulin and heparin infusions together with the iterative implementation of a fat-restricted diet, low in long chain triglycerides (LCT) and supplemented with medium chain triglycerides (MCT). In both cases, provision of adequate caloric intake (~110-120 kcal/kg/day) was also found to be important for a sustained TG reduction during the acute phase of management. In summary, a high index of suspicion is required to diagnose FCS in infants with hypertriglyceridemia-induced acute pancreatitis, management of which can be challenging, highlighting the need for more evidence-based recommendations., Competing Interests: Oliver Heath, Brooke Allender, Joel Smith, Lucy Spencer, Elena Savva, Thomas H. Rozen, Natasha J. Brown, Elizabeth G. Bannister, Maureen S. Evans, Sharmila Kiss, and Joy Yaplito‐Lee have approved the manuscript and declare that they have no conflict of interest. They did not receive reimbursements/fees/funds/salaries from an organisation that may in any way gain or lose financially from the results reported in the reviewed manuscript in the last 5 years and have no other competing financial or non‐financial interests, as outlined in the JIMD Conflict of Interest form., (© 2024 The Authors. JIMD Reports published by John Wiley & Sons Ltd on behalf of SSIEM.)

Published
2024
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46. MOGS-CDG: Quantitative analysis of the diagnostic Glc 3 Man tetrasaccharide and clinical spectrum of six new cases.

Author

Post MA, de Wit I, Zijlstra FSM, Engelke UFH, van Rooij A, Christodoulou J, Tan TY, Le Fevre A, Jin D, Yaplito-Lee J, Lee BH, Low KJ, Mallick AA, Õunap K, Pitt J, Reardon W, Vals MA, Wortmann SB, Wessels HJCT, Bärenfänger M, van Karnebeek CDM, and Lefeber DJ

Subjects
Humans, Mass Spectrometry methods, Oligosaccharides metabolism, Polysaccharides, Seizures, Congenital Disorders of Glycosylation genetics
Abstract

Congenital disorders of glycosylation (CDG) are a clinically and biochemically heterogeneous subgroup of inherited metabolic disorders. Most CDG with abnormal N-glycosylation can be detected by transferrin screening, however, MOGS-CDG escapes this routine screening. Combined with the clinical heterogeneity of reported cases, diagnosing MOGS-CDG can be challenging. Here, we clinically characterize ten MOGS-CDG cases including six previously unreported individuals, showing a phenotype characterized by dysmorphic features, global developmental delay, muscular hypotonia, and seizures in all patients and in a minority vision problems and hypogammaglobulinemia. Glycomics confirmed accumulation of a Glc 3 Man 7 GlcNAc 2 glycan in plasma. For quantification of the diagnostic Glcα1-3Glcα1-3Glcα1-2Man tetrasaccharide in urine, we developed and validated a liquid chromatography-mass spectrometry method of 2-aminobenzoic acid (2AA) labeled urinary glycans. As an internal standard, isotopically labeled 13 C 6 -2AA Glc 3 Man was used, while labeling efficiency was controlled by use of 12 C 6 -2AA and 13 C 6 -2AA labeled laminaritetraose. Recovery, linearity, intra- and interassay coefficients of variability of these labeled compounds were determined. Furthermore, Glc 3 Man was specifically identified by retention time matching against authentic MOGS-CDG urine and compared with Pompe urine. Glc 3 Man was increased in all six analyzed cases, ranging from 34.1 to 618.0 μmol/mmol creatinine (reference <5 μmol). In short, MOGS-CDG has a broad manifestation of symptoms but can be diagnosed with the use of a quantitative method for analysis of urinary Glc 3 Man excretion., (© 2023 The Authors. Journal of Inherited Metabolic Disease published by John Wiley & Sons Ltd on behalf of SSIEM.)

Published
2023
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