Associated Papers
Exploring a novel model for newborn genetic screening in Ningxia, northern China: A retrospective observational study.
Mao X et al.
Medicine, 2024
Application of a next-generation sequencing (NGS) panel in newborn screening efficiently identifies inborn disorders of neonates.
Huang X et al.
Orphanet Journal of Rare Diseases, 2022
Lysine acetylation regulates the interaction between proteins and membranes.
Okada AK et al.
Nature Communications, 2021
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 2019
An enhanced workflow for variant interpretation in UniProtKB/Swiss-Prot improves consistency and reuse in ClinVar.
Famiglietti ML et al.
Database : the Journal of Biological Databases and Curation, 2019
Kinetic mutations in argininosuccinate synthetase deficiency: characterisation and in vitro correction by substrate supplementation.
Diez-Fernandez C et al.
Journal of Medical Genetics, 2016
Improved standards for prenatal diagnosis of citrullinemia.
Miller MJ et al.
Molecular Genetics and Metabolism, 2014
Citrullinemia type I and hypertrophic pyloric stenosis in a 1-month old male infant.
Rhee Y et al.
Clinics and Practice, 2013
Citrullinaemia type I: a common mutation in the Pacific Island population.
Glamuzina E et al.
Journal of Paediatrics and Child Health, 2011
Mutations and polymorphisms in the human argininosuccinate synthetase (ASS1) gene.
Engel K et al.
Human Mutation, 2009
The role of molecular testing and enzyme analysis in the management of hypomorphic citrullinemia.
Dimmock DP et al.
American Journal of Medical Genetics. Part A, 2008
Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients.
Gao HZ et al.
Human Mutation, 2003
Structure of the human argininosuccinate synthetase gene and an improved system for molecular diagnostics in patients with classical and mild citrullinemia.
Häberle J et al.
Human Genetics, 2002
The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis.
Lemke CT et al.
Structure (london, England : 1993), 2001
Additional mutations in argininosuccinate synthetase causing citrullinemia.
Kobayashi K et al.
Molecular Biology & Medicine, 1991
Heterogeneity of mutations in argininosuccinate synthetase causing human citrullinemia.
Kobayashi K et al.
The Journal of Biological Chemistry, 1990