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Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II
A homozygous mutation in the flavoprotein (Fp) gene associated with complex II deficiency was demonstrated in a patient with consanguineous parents. She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharge...
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| Published in: | American journal of medical genetics 2003-07, Vol.120A (1), p.13-18 |
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| cites | cdi_FETCH-LOGICAL-c4322-dcb389075c26ccb10b65bdf9e0fc08d8f9d04a3cbbc8bf5c8af4a5bf5848a3093 |
| container_end_page | 18 |
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| container_title | American journal of medical genetics |
| container_volume | 120A |
| creator | Van Coster, Rudy Seneca, S. Smet, J. Van Hecke, R. Gerlo, E. Devreese, B. Van Beeumen, J. Leroy, J.G. De Meirleir, L. Lissens, W. |
| description | A homozygous mutation in the flavoprotein (Fp) gene associated with complex II deficiency was demonstrated in a patient with consanguineous parents. She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharged glycine at position 555 by glutamic acid. Her clinical course was at variance with the Leigh syndrome in three previously reported patients due to Fp gene mutations. In this proband, CRM for flavoprotein as well as iron‐containing protein (Ip) was decreased, CRM for the entire complex II (130 kDa) being reduced even more. This observation prompts speculation of a labile interaction between Ip and Fp polypeptides and of a key role of the amino acid at position 555 in the interacting domain. © 2003 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/ajmg.a.10202 |
| format | article |
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She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharged glycine at position 555 by glutamic acid. Her clinical course was at variance with the Leigh syndrome in three previously reported patients due to Fp gene mutations. In this proband, CRM for flavoprotein as well as iron‐containing protein (Ip) was decreased, CRM for the entire complex II (130 kDa) being reduced even more. 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J. Med. Genet</addtitle><description>A homozygous mutation in the flavoprotein (Fp) gene associated with complex II deficiency was demonstrated in a patient with consanguineous parents. She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharged glycine at position 555 by glutamic acid. Her clinical course was at variance with the Leigh syndrome in three previously reported patients due to Fp gene mutations. In this proband, CRM for flavoprotein as well as iron‐containing protein (Ip) was decreased, CRM for the entire complex II (130 kDa) being reduced even more. This observation prompts speculation of a labile interaction between Ip and Fp polypeptides and of a key role of the amino acid at position 555 in the interacting domain. © 2003 Wiley‐Liss, Inc.</description><subject>Amino Acids - chemistry</subject><subject>Biological and medical sciences</subject><subject>blue native polyacrylamide gel electrophoresis (Blue Native PAGE)</subject><subject>Cardiomegaly - genetics</subject><subject>Cell Nucleus - metabolism</subject><subject>complex II deficiency</subject><subject>complex instability</subject><subject>Electron Transport - genetics</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>Fibroblasts - metabolism</subject><subject>flavoprotein</subject><subject>Flavoproteins - genetics</subject><subject>Glutamic Acid - genetics</subject><subject>Glutamine - chemistry</subject><subject>Glycine - chemistry</subject><subject>Glycine - genetics</subject><subject>Homozygote</subject><subject>Humans</subject><subject>Infant</subject><subject>Iron - chemistry</subject><subject>iron-containing protein</subject><subject>Medical sciences</subject><subject>Metabolic diseases</subject><subject>Miscellaneous</subject><subject>Models, Molecular</subject><subject>Muscle, Skeletal - metabolism</subject><subject>Mutation</subject><subject>Other metabolic disorders</subject><subject>Oxygen - metabolism</subject><subject>Peptides - chemistry</subject><subject>Phosphorylation</subject><subject>Protein Structure, Tertiary</subject><issn>1552-4825</issn><issn>0148-7299</issn><issn>1552-4833</issn><issn>1096-8628</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqFkU1T1TAYhTuOjiC4c-1koysLadI06ZK5SrkMIs7g4C7zNk0ugbS5JK1S1_xwej-Ena5yFs85J_OeJHmX4YMMY3IIN-3iACZNMHmR7GaMkTQXlL580oTtJG9ivMGYYsaL18lORniZF4LtJg8nvvV_xoUfIqrcyBir3IDaoYfe-g7ZDvXXGnWDchpCqjvlG90gjtHtZ0DGwS-_DL7XE7fQnUYKhqjjZIs91NbZfkTerCOCjksboPdhROoaJoPy7dLpezSf7yevDLio327fveTH8ZfL2Ul69q2az47OUpVTQtJG1VSUmDNFCqXqDNcFqxtTamwUFo0wZYNzoKqulagNUwJMDmxSIhdAcUn3ko-b3OnPd4OOvWxtVNo56PR0AMkpLXJRsP-CBAtBOV-BnzagCj7GoI1cBttCGGWG5WoeuZpHglzPM-Hvt7lD3ermGd7uMQEftgBEBc4E6JSNz1wuRCbWvXTD_bZOj_8slUenX6u_9enGZWOv759cEG5lwSln8uq8kqc_-fHl94uZvKKP8V66SQ</recordid><startdate>20030701</startdate><enddate>20030701</enddate><creator>Van Coster, Rudy</creator><creator>Seneca, S.</creator><creator>Smet, J.</creator><creator>Van Hecke, R.</creator><creator>Gerlo, E.</creator><creator>Devreese, B.</creator><creator>Van Beeumen, J.</creator><creator>Leroy, J.G.</creator><creator>De Meirleir, L.</creator><creator>Lissens, W.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Liss</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20030701</creationdate><title>Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II</title><author>Van Coster, Rudy ; Seneca, S. ; Smet, J. ; Van Hecke, R. ; Gerlo, E. ; Devreese, B. ; Van Beeumen, J. ; Leroy, J.G. ; De Meirleir, L. ; Lissens, W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4322-dcb389075c26ccb10b65bdf9e0fc08d8f9d04a3cbbc8bf5c8af4a5bf5848a3093</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acids - chemistry</topic><topic>Biological and medical sciences</topic><topic>blue native polyacrylamide gel electrophoresis (Blue Native PAGE)</topic><topic>Cardiomegaly - genetics</topic><topic>Cell Nucleus - metabolism</topic><topic>complex II deficiency</topic><topic>complex instability</topic><topic>Electron Transport - genetics</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>Fibroblasts - metabolism</topic><topic>flavoprotein</topic><topic>Flavoproteins - genetics</topic><topic>Glutamic Acid - genetics</topic><topic>Glutamine - chemistry</topic><topic>Glycine - chemistry</topic><topic>Glycine - genetics</topic><topic>Homozygote</topic><topic>Humans</topic><topic>Infant</topic><topic>Iron - chemistry</topic><topic>iron-containing protein</topic><topic>Medical sciences</topic><topic>Metabolic diseases</topic><topic>Miscellaneous</topic><topic>Models, Molecular</topic><topic>Muscle, Skeletal - metabolism</topic><topic>Mutation</topic><topic>Other metabolic disorders</topic><topic>Oxygen - metabolism</topic><topic>Peptides - chemistry</topic><topic>Phosphorylation</topic><topic>Protein Structure, Tertiary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Coster, Rudy</creatorcontrib><creatorcontrib>Seneca, S.</creatorcontrib><creatorcontrib>Smet, J.</creatorcontrib><creatorcontrib>Van Hecke, R.</creatorcontrib><creatorcontrib>Gerlo, E.</creatorcontrib><creatorcontrib>Devreese, B.</creatorcontrib><creatorcontrib>Van Beeumen, J.</creatorcontrib><creatorcontrib>Leroy, J.G.</creatorcontrib><creatorcontrib>De Meirleir, L.</creatorcontrib><creatorcontrib>Lissens, W.</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>American journal of medical genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Coster, Rudy</au><au>Seneca, S.</au><au>Smet, J.</au><au>Van Hecke, R.</au><au>Gerlo, E.</au><au>Devreese, B.</au><au>Van Beeumen, J.</au><au>Leroy, J.G.</au><au>De Meirleir, L.</au><au>Lissens, W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II</atitle><jtitle>American journal of medical genetics</jtitle><addtitle>Am. J. Med. Genet</addtitle><date>2003-07-01</date><risdate>2003</risdate><volume>120A</volume><issue>1</issue><spage>13</spage><epage>18</epage><pages>13-18</pages><issn>1552-4825</issn><issn>0148-7299</issn><eissn>1552-4833</eissn><eissn>1096-8628</eissn><coden>AJMGDA</coden><abstract>A homozygous mutation in the flavoprotein (Fp) gene associated with complex II deficiency was demonstrated in a patient with consanguineous parents. She succumbed at 5½ months of age following a respiratory infection. The c1664G→A transition detected, predicted the substitution of the small uncharged glycine at position 555 by glutamic acid. Her clinical course was at variance with the Leigh syndrome in three previously reported patients due to Fp gene mutations. In this proband, CRM for flavoprotein as well as iron‐containing protein (Ip) was decreased, CRM for the entire complex II (130 kDa) being reduced even more. This observation prompts speculation of a labile interaction between Ip and Fp polypeptides and of a key role of the amino acid at position 555 in the interacting domain. © 2003 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>12794685</pmid><doi>10.1002/ajmg.a.10202</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acids - chemistry Biological and medical sciences blue native polyacrylamide gel electrophoresis (Blue Native PAGE) Cardiomegaly - genetics Cell Nucleus - metabolism complex II deficiency complex instability Electron Transport - genetics Electrophoresis, Polyacrylamide Gel Female Fibroblasts - metabolism flavoprotein Flavoproteins - genetics Glutamic Acid - genetics Glutamine - chemistry Glycine - chemistry Glycine - genetics Homozygote Humans Infant Iron - chemistry iron-containing protein Medical sciences Metabolic diseases Miscellaneous Models, Molecular Muscle, Skeletal - metabolism Mutation Other metabolic disorders Oxygen - metabolism Peptides - chemistry Phosphorylation Protein Structure, Tertiary |
| title | Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II |
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