Please wait, while we are loading the content...
Please wait, while we are loading the content...
| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kimani, Joseph Kagunda Wei, Tianying Chol, Kim Li, Ying Yu, Ping Ye, Sheng Huang, Xinwen Qi, Ming |
| Description | Country affiliation: China Author Affiliation: Kimani JK ( Affiliated Children's Hospital, School of Medicine, Zhejiang University, 57 Zhugan Lane, Hangzhou 310003, China); Wei T ( Department of Cell Biology and Medical Genetics, Research Building A 713, School of Medicine, Zhejiang University, Yuhangtang Road 866, Hangzhou, China.); Chol K ( Pyongyang College of Medicine, Pyongyang, DPR Republic of Korea.); Li Y ( Center for Structural Biology, Research Building A 210, Life Sciences Institute, Zhejiang University, Yuhangtang Road 866, Hangzhou, China.); Yu P ( Department of Cell Biology and Medical Genetics, Research Building A 713, School of Medicine, Zhejiang University, Yuhangtang Road 866, Hangzhou, China.); Ye S ( Center for Structural Biology, Research Building A 210, Life Sciences Institute, Zhejiang University, Yuhangtang Road 866, Hangzhou, China.); Huang X ( Affiliated Children's Hospital, School of Medicine, Zhejiang University, 57 Zhugan Lane, Hangzhou 310003, China. Electronic address: xinwenhuang@126.com.); Qi M ( Department of Cell Biology and Medical Genetics, Research Building A 713, School of Medicine, Zhejiang University, Yuhangtang Road 866, Hangzhou, China) |
| Abstract | BACKGROUND: Classical citrullinemia (CTLN1) is an inborn error of the urea cycle caused by reduced/abolished activity of argininosuccinate synthetase due to mutations in the ASS1 gene. To determine the pathogenicity of novel variants detected in patients is often a huge challenge in molecular diagnosis. The purpose of our study was to characterize novel ASS1 gene mutations identified in CTLN1 patients. METHODS: Exon trapping assay with pSPL3 was used to confirm splice aberrations while bioinformatics structural analysis predicted the possible effects of missense mutations. RESULTS: Novel donor site (c.174+1G>A) and missense (p.V141G) mutations were detected in a patient exhibiting a biochemical phenotype only. The splice mutation provoked exon skipping hence the truncated product. The mutation p.V141G, is predicted to disturb a hydrophobic pocket in the ATP binding domain in the ASS. Both mutations are predicted to lower binding of ATP. The second patient presented with early onset neonatal citrullinemia marked by an elevated biochemical profile and a clinical phenotype. Analysis revealed a donor site (c.773+1G>A) mutation leading to both exon skipping and intron retention. Subsequent introduction of premature stop codons would result in severely truncated products likely to be degraded. A previously reported R265C is predicted to distort the citrulline binding site. CONCLUSIONS: Three novel mutations are reported in this study. They expand the spectrum of genetic pathology underlying CTLN1. Overall this study provides new insight of CTLN1 and illustrates a comprehensive protocol investigating inborn errors of metabolism at the molecular level. |
| File Format | HTM / HTML |
| ISSN | 00098981 |
| Volume Number | 438 |
| e-ISSN | 18733492 |
| Journal | Clinica Chimica Acta |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-01-01 |
| Publisher Place | Netherlands |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Discipline Clinical Chemistry Discipline Laboratory Medicine Argininosuccinate Synthase Genetics Citrullinemia Mutation Rna Splicing Adenosine Triphosphate Chemistry Metabolism Amino Acid Sequence Base Sequence Citrulline Diagnosis Enzymology Pathology Exons Female Humans Infant Introns Male Models, Molecular Molecular Sequence Data Pedigree Protein Binding Journal Article Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry (medical) Clinical Biochemistry Biochemistry |
National Digital Library of India (NDLI) is a virtual repository of learning resources which is not just a repository with search/browse facilities but provides a host of services for the learner community. It is sponsored and mentored by Ministry of Education, Government of India, through its National Mission on Education through Information and Communication Technology (NMEICT). Filtered and federated searching is employed to facilitate focused searching so that learners can find the right resource with least effort and in minimum time. NDLI provides user group-specific services such as Examination Preparatory for School and College students and job aspirants. Services for Researchers and general learners are also provided. NDLI is designed to hold content of any language and provides interface support for 10 most widely used Indian languages. It is built to provide support for all academic levels including researchers and life-long learners, all disciplines, all popular forms of access devices and differently-abled learners. It is designed to enable people to learn and prepare from best practices from all over the world and to facilitate researchers to perform inter-linked exploration from multiple sources. It is developed, operated and maintained from Indian Institute of Technology Kharagpur.
Learn more about this project from here.
NDLI is a conglomeration of freely available or institutionally contributed or donated or publisher managed contents. Almost all these contents are hosted and accessed from respective sources. The responsibility for authenticity, relevance, completeness, accuracy, reliability and suitability of these contents rests with the respective organization and NDLI has no responsibility or liability for these. Every effort is made to keep the NDLI portal up and running smoothly unless there are some unavoidable technical issues.
Ministry of Education, through its National Mission on Education through Information and Communication Technology (NMEICT), has sponsored and funded the National Digital Library of India (NDLI) project.
| Sl. | Authority | Responsibilities | Communication Details |
|---|---|---|---|
| 1 | Ministry of Education (GoI), Department of Higher Education |
Sanctioning Authority | https://www.education.gov.in/ict-initiatives |
| 2 | Indian Institute of Technology Kharagpur | Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project | https://www.iitkgp.ac.in |
| 3 | National Digital Library of India Office, Indian Institute of Technology Kharagpur | The administrative and infrastructural headquarters of the project | Dr. B. Sutradhar bsutra@ndl.gov.in |
| 4 | Project PI / Joint PI | Principal Investigator and Joint Principal Investigators of the project |
Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon |
| 5 | Website/Portal (Helpdesk) | Queries regarding NDLI and its services | support@ndl.gov.in |
| 6 | Contents and Copyright Issues | Queries related to content curation and copyright issues | content@ndl.gov.in |
| 7 | National Digital Library of India Club (NDLI Club) | Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach | clubsupport@ndl.gov.in |
| 8 | Digital Preservation Centre (DPC) | Assistance with digitizing and archiving copyright-free printed books | dpc@ndl.gov.in |
| 9 | IDR Setup or Support | Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops | idr@ndl.gov.in |
|
Loading...
|