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Mutations in FLNB cause boomerang dysplasia
Boomerang dysplasia (BD) is a perinatal lethal osteochondrodysplasia, characterised by absence or underossification of the limb bones and vertebrae. The BD phenotype is similar to a group of disorders including atelosteogenesis I, atelosteogenesis III, and dominantly inherited Larsen syndrome that w...
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| Published in: | Journal of medical genetics 2005-07, Vol.42 (7), p.e43-e43 |
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| container_end_page | e43 |
| container_issue | 7 |
| container_start_page | e43 |
| container_title | Journal of medical genetics |
| container_volume | 42 |
| creator | Bicknell, L S Morgan, T Bonafé, L Wessels, M W Bialer, M G Willems, P J Cohn, D H Krakow, D Robertson, S P |
| description | Boomerang dysplasia (BD) is a perinatal lethal osteochondrodysplasia, characterised by absence or underossification of the limb bones and vertebrae. The BD phenotype is similar to a group of disorders including atelosteogenesis I, atelosteogenesis III, and dominantly inherited Larsen syndrome that we have recently shown to be associated with mutations in FLNB, the gene encoding the actin binding cytoskeletal protein, filamin B. We report the identification of mutations in FLNB in two unrelated individuals with boomerang dysplasia. The resultant substitutions, L171R and S235P, lie within the calponin homology 2 region of the actin binding domain of filamin B and occur at sites that are evolutionarily well conserved. These findings expand the phenotypic spectrum resulting from mutations in FLNB and underline the central role this protein plays during skeletogenesis in humans. |
| doi_str_mv | 10.1136/jmg.2004.029967 |
| format | article |
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The BD phenotype is similar to a group of disorders including atelosteogenesis I, atelosteogenesis III, and dominantly inherited Larsen syndrome that we have recently shown to be associated with mutations in FLNB, the gene encoding the actin binding cytoskeletal protein, filamin B. We report the identification of mutations in FLNB in two unrelated individuals with boomerang dysplasia. The resultant substitutions, L171R and S235P, lie within the calponin homology 2 region of the actin binding domain of filamin B and occur at sites that are evolutionarily well conserved. These findings expand the phenotypic spectrum resulting from mutations in FLNB and underline the central role this protein plays during skeletogenesis in humans.</description><identifier>ISSN: 0022-2593</identifier><identifier>ISSN: 1468-6244</identifier><identifier>EISSN: 1468-6244</identifier><identifier>DOI: 10.1136/jmg.2004.029967</identifier><identifier>PMID: 15994868</identifier><identifier>CODEN: JMDGAE</identifier><language>eng</language><publisher>England: BMJ Publishing Group Ltd</publisher><subject>Abnormalities, Multiple - genetics ; Aborted Fetus - diagnostic imaging ; actin binding ; Amino Acid Substitution ; Animals ; Binding Sites - genetics ; boomerang dysplasia ; Conserved Sequence - genetics ; Contractile Proteins - genetics ; Deoxyribonucleic acid ; DNA ; DNA Mutational Analysis ; Electronic Letter ; Enzymes ; Female ; Fetuses ; filamin ; Filamins ; Heterozygote ; Humans ; Microfilament Proteins - genetics ; Mutation ; Osteochondrodysplasias - genetics ; Phenotype ; Pregnancy ; Pregnancy Trimester, Second ; Proteins ; Radiography ; Sequence Homology, Amino Acid ; skeletogenesis</subject><ispartof>Journal of medical genetics, 2005-07, Vol.42 (7), p.e43-e43</ispartof><rights>Copyright 2005 Journal of Medical Genetics</rights><rights>Copyright: 2005 Copyright 2005 Journal of Medical Genetics</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b527t-fa6a2ecf7386ad9fd7cdf5c089a7c558cdbace914e99c51ecfdf7eacc4b7bc7f3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1736093/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1736093/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15994868$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bicknell, L S</creatorcontrib><creatorcontrib>Morgan, T</creatorcontrib><creatorcontrib>Bonafé, L</creatorcontrib><creatorcontrib>Wessels, M W</creatorcontrib><creatorcontrib>Bialer, M G</creatorcontrib><creatorcontrib>Willems, P J</creatorcontrib><creatorcontrib>Cohn, D H</creatorcontrib><creatorcontrib>Krakow, D</creatorcontrib><creatorcontrib>Robertson, S P</creatorcontrib><title>Mutations in FLNB cause boomerang dysplasia</title><title>Journal of medical genetics</title><addtitle>J Med Genet</addtitle><description>Boomerang dysplasia (BD) is a perinatal lethal osteochondrodysplasia, characterised by absence or underossification of the limb bones and vertebrae. The BD phenotype is similar to a group of disorders including atelosteogenesis I, atelosteogenesis III, and dominantly inherited Larsen syndrome that we have recently shown to be associated with mutations in FLNB, the gene encoding the actin binding cytoskeletal protein, filamin B. We report the identification of mutations in FLNB in two unrelated individuals with boomerang dysplasia. The resultant substitutions, L171R and S235P, lie within the calponin homology 2 region of the actin binding domain of filamin B and occur at sites that are evolutionarily well conserved. These findings expand the phenotypic spectrum resulting from mutations in FLNB and underline the central role this protein plays during skeletogenesis in humans.</description><subject>Abnormalities, Multiple - genetics</subject><subject>Aborted Fetus - diagnostic imaging</subject><subject>actin binding</subject><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Binding Sites - genetics</subject><subject>boomerang dysplasia</subject><subject>Conserved Sequence - genetics</subject><subject>Contractile Proteins - genetics</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Mutational Analysis</subject><subject>Electronic Letter</subject><subject>Enzymes</subject><subject>Female</subject><subject>Fetuses</subject><subject>filamin</subject><subject>Filamins</subject><subject>Heterozygote</subject><subject>Humans</subject><subject>Microfilament Proteins - genetics</subject><subject>Mutation</subject><subject>Osteochondrodysplasias - genetics</subject><subject>Phenotype</subject><subject>Pregnancy</subject><subject>Pregnancy Trimester, Second</subject><subject>Proteins</subject><subject>Radiography</subject><subject>Sequence Homology, Amino Acid</subject><subject>skeletogenesis</subject><issn>0022-2593</issn><issn>1468-6244</issn><issn>1468-6244</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFkD1PwzAURS0EoqUws6FIbKC0dhLb8YIEEQWkUEB8jZbjOCWliYudIPrvcZWqwMT0hnfufU8HgEMEhwiFZDSrpsMAwmgIA8YI3QJ9FJHYJ0EUbYM-hEHgB5iFPbBn7QxCFFJEdkEPYcaimMR9cHrbNqIpdW29svbG6eTCk6K1ysu0rpQR9dTLl3YxF7YU-2CnEHOrDtZzAJ7Hl0_JtZ_eXd0k56mf4YA2fiGICJQsaBgTkbMipzIvsIQxE1RiHMs8E1IxFCnGJEaOzAuqhJRRRjNJi3AAzrreRZtVKpeqboyY84UpK2GWXIuS_93U5Ruf6k-OaEggC13B8brA6I9W2YbPdGtq97NDYoRwTCF01KijpNHWGlVsLiDIV3a5s8tXdnln1yWOfj_2w691OsDvgNI26muzF-aduzjFfPKS8CRKX-8f4YQ_OP6k47Nq9u_1b9N6k-E</recordid><startdate>20050701</startdate><enddate>20050701</enddate><creator>Bicknell, L S</creator><creator>Morgan, T</creator><creator>Bonafé, L</creator><creator>Wessels, M W</creator><creator>Bialer, M G</creator><creator>Willems, P J</creator><creator>Cohn, D H</creator><creator>Krakow, D</creator><creator>Robertson, S P</creator><general>BMJ Publishing Group Ltd</general><general>BMJ Publishing Group LTD</general><general>BMJ Group</general><scope>BSCLL</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BTHHO</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope></search><sort><creationdate>20050701</creationdate><title>Mutations in FLNB cause boomerang dysplasia</title><author>Bicknell, L S ; Morgan, T ; Bonafé, L ; Wessels, M W ; Bialer, M G ; Willems, P J ; Cohn, D H ; Krakow, D ; Robertson, S P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b527t-fa6a2ecf7386ad9fd7cdf5c089a7c558cdbace914e99c51ecfdf7eacc4b7bc7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Abnormalities, Multiple - genetics</topic><topic>Aborted Fetus - diagnostic imaging</topic><topic>actin binding</topic><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Binding Sites - genetics</topic><topic>boomerang dysplasia</topic><topic>Conserved Sequence - genetics</topic><topic>Contractile Proteins - genetics</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA Mutational Analysis</topic><topic>Electronic Letter</topic><topic>Enzymes</topic><topic>Female</topic><topic>Fetuses</topic><topic>filamin</topic><topic>Filamins</topic><topic>Heterozygote</topic><topic>Humans</topic><topic>Microfilament Proteins - genetics</topic><topic>Mutation</topic><topic>Osteochondrodysplasias - genetics</topic><topic>Phenotype</topic><topic>Pregnancy</topic><topic>Pregnancy Trimester, Second</topic><topic>Proteins</topic><topic>Radiography</topic><topic>Sequence Homology, Amino Acid</topic><topic>skeletogenesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bicknell, L S</creatorcontrib><creatorcontrib>Morgan, T</creatorcontrib><creatorcontrib>Bonafé, L</creatorcontrib><creatorcontrib>Wessels, M W</creatorcontrib><creatorcontrib>Bialer, M G</creatorcontrib><creatorcontrib>Willems, P J</creatorcontrib><creatorcontrib>Cohn, D H</creatorcontrib><creatorcontrib>Krakow, D</creatorcontrib><creatorcontrib>Robertson, S P</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>ProQuest_Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>BMJ Journals</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of medical genetics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bicknell, L S</au><au>Morgan, T</au><au>Bonafé, L</au><au>Wessels, M W</au><au>Bialer, M G</au><au>Willems, P J</au><au>Cohn, D H</au><au>Krakow, D</au><au>Robertson, S P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mutations in FLNB cause boomerang dysplasia</atitle><jtitle>Journal of medical genetics</jtitle><addtitle>J Med Genet</addtitle><date>2005-07-01</date><risdate>2005</risdate><volume>42</volume><issue>7</issue><spage>e43</spage><epage>e43</epage><pages>e43-e43</pages><issn>0022-2593</issn><issn>1468-6244</issn><eissn>1468-6244</eissn><coden>JMDGAE</coden><abstract>Boomerang dysplasia (BD) is a perinatal lethal osteochondrodysplasia, characterised by absence or underossification of the limb bones and vertebrae. The BD phenotype is similar to a group of disorders including atelosteogenesis I, atelosteogenesis III, and dominantly inherited Larsen syndrome that we have recently shown to be associated with mutations in FLNB, the gene encoding the actin binding cytoskeletal protein, filamin B. We report the identification of mutations in FLNB in two unrelated individuals with boomerang dysplasia. The resultant substitutions, L171R and S235P, lie within the calponin homology 2 region of the actin binding domain of filamin B and occur at sites that are evolutionarily well conserved. These findings expand the phenotypic spectrum resulting from mutations in FLNB and underline the central role this protein plays during skeletogenesis in humans.</abstract><cop>England</cop><pub>BMJ Publishing Group Ltd</pub><pmid>15994868</pmid><doi>10.1136/jmg.2004.029967</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Abnormalities, Multiple - genetics Aborted Fetus - diagnostic imaging actin binding Amino Acid Substitution Animals Binding Sites - genetics boomerang dysplasia Conserved Sequence - genetics Contractile Proteins - genetics Deoxyribonucleic acid DNA DNA Mutational Analysis Electronic Letter Enzymes Female Fetuses filamin Filamins Heterozygote Humans Microfilament Proteins - genetics Mutation Osteochondrodysplasias - genetics Phenotype Pregnancy Pregnancy Trimester, Second Proteins Radiography Sequence Homology, Amino Acid skeletogenesis |
| title | Mutations in FLNB cause boomerang dysplasia |
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