revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases
Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated, branched-chain), bile acid-CoAs, CoA esters of prostaglandins, etc., to the corresponding free acid and CoA. However, there is significant confusion...
Saved in:
Published in | Journal of lipid research Vol. 46; no. 9; pp. 2029 - 2032 |
---|---|
Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier
01.09.2005
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated, branched-chain), bile acid-CoAs, CoA esters of prostaglandins, etc., to the corresponding free acid and CoA. However, there is significant confusion regarding the nomenclature of these genes. In agreement with the HUGO Gene Nomenclature Committee and the Mouse Genomic Nomenclature Committee, a revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases has been suggested for the 12 member family. The family root symbol is ACOT, with human genes named ACOT1-ACOT12, and rat and mouse genes named Acot1-Acot12. Several of the ACOT genes are the result of splicing events, and these splice variants are cataloged. |
---|---|
AbstractList | Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated, branched-chain), bile acid-CoAs, CoA esters of prostaglandins, etc., to the corresponding free acid and CoA. However, there is significant confusion regarding the nomenclature of these genes. In agreement with the HUGO Gene Nomenclature Committee and the Mouse Genomic Nomenclature Committee, a revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases has been suggested for the 12 member family. The family root symbol is ACOT, with human genes named ACOT1-ACOT12, and rat and mouse genes named Acot1-Acot12. Several of the ACOT genes are the result of splicing events, and these splice variants are cataloged. |
Author | Yamada, Junji Podesta, Ernesto J Wright, Mathew W Alexson, Stefan E. H Hunt, Mary C Maltais, Lois J |
Author_xml | – sequence: 1 fullname: Hunt, Mary C – sequence: 2 fullname: Yamada, Junji – sequence: 3 fullname: Maltais, Lois J – sequence: 4 fullname: Wright, Mathew W – sequence: 5 fullname: Podesta, Ernesto J – sequence: 6 fullname: Alexson, Stefan E. H |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/16103133$$D View this record in MEDLINE/PubMed http://kipublications.ki.se/Default.aspx?queryparsed=id:1952742$$DView record from Swedish Publication Index |
BookMark | eNp1kU9v1DAQxS1URLeFL8ABcuKWdsb_khyrpYWilZCAni3HGbdZknixd0H77eslCxUHfPHo6ffeSPPO2MkUJmLsNcIFYiMv10O8uFaQnyg_rb5wgGdsgUo0ZcU1P2ELAM5Lzit1ys5SWgOglBpfsFPUCAKFWLD3kX72ibpiCiNNbrDbXaTCh1iMdhzt0NupsG4_lMtwVWwf-kBpS9EmSpcP-y6G4TC-ZM-9HRK9Ov7n7O7m-tvyY7n6_OF2ebUqnWr0thQcpCNU0HHVtiBqjbXqAFGAt7Vzznea6lYQYFMjSuGEJqW8BM2bLItzdjvndsGuzSb2o417E2xvfgsh3hsbt70byAiPlkQLvCUnudQWGl05BO8EkPcqZ5VzVvpFm137T9pR-p4nMqpqpDzw1X_5TQzdk-mPERvFK8mz893szNiPXb6fGfvkaBjsRGGXjK5lrSpRZ5DPoIshpUj-7xIEc2jc5MbNsXEzN55Nb47pu3ak7slyrDgDb2fA22DsfeyTufvKIR8dgaOQjXgEvbOz4A |
CitedBy_id | crossref_primary_10_1002_cbdv_200790169 crossref_primary_10_3389_fphys_2020_580167 crossref_primary_10_1074_mcp_M700169_MCP200 crossref_primary_10_1530_JOE_11_0313 crossref_primary_10_1074_jbc_M508479200 crossref_primary_10_1152_ajpendo_00052_2013 crossref_primary_10_1074_jbc_RA120_015701 crossref_primary_10_1248_bpb_34_87 crossref_primary_10_1017_S0007114517002641 crossref_primary_10_1096_fj_06_6042com crossref_primary_10_1073_pnas_0700974104 crossref_primary_10_1155_2022_2669114 crossref_primary_10_1016_j_plipres_2013_01_001 crossref_primary_10_1016_j_jsbmb_2006_01_003 crossref_primary_10_3390_cancers15030946 crossref_primary_10_1016_j_bbrc_2009_05_122 crossref_primary_10_1016_j_febslet_2007_07_040 crossref_primary_10_1007_s00018_013_1422_1 crossref_primary_10_1186_1479_7364_4_6_411 crossref_primary_10_1016_j_mce_2006_12_026 crossref_primary_10_1038_cddis_2017_202 crossref_primary_10_1038_s41598_018_32354_w crossref_primary_10_1074_jbc_M703745200 crossref_primary_10_1194_jlr_M076489 crossref_primary_10_1080_21623945_2020_1776553 crossref_primary_10_1016_j_ymgme_2007_12_005 crossref_primary_10_1016_j_plipres_2010_04_001 crossref_primary_10_1039_C3OB42515K crossref_primary_10_1194_jlr_M030163 crossref_primary_10_1186_s12876_021_01750_4 crossref_primary_10_3389_fnagi_2024_1345668 crossref_primary_10_1007_s00418_013_1079_8 crossref_primary_10_1371_journal_pone_0050376 crossref_primary_10_2337_db15_1240 crossref_primary_10_1371_journal_pone_0051588 crossref_primary_10_1016_j_bbrc_2010_11_066 crossref_primary_10_1194_jlr_M700119_JLR200 crossref_primary_10_3390_cells11203236 crossref_primary_10_1002_cbdv_200890199 crossref_primary_10_1042_BJ20090039 crossref_primary_10_1016_j_bcp_2013_08_067 crossref_primary_10_1016_j_ijpara_2009_12_006 crossref_primary_10_1111_j_1742_4658_2006_05496_x crossref_primary_10_1016_j_bbadis_2012_03_009 crossref_primary_10_1038_s41467_021_27738_y crossref_primary_10_3892_or_2014_3155 crossref_primary_10_3389_fonc_2024_1374094 crossref_primary_10_1194_jlr_R005959 crossref_primary_10_3389_fcell_2015_00035 crossref_primary_10_1007_s11655_012_0964_7 crossref_primary_10_1172_jci_insight_160987 crossref_primary_10_1016_j_tem_2017_03_001 crossref_primary_10_14814_phy2_14474 crossref_primary_10_1007_s13762_013_0424_8 crossref_primary_10_1016_j_bbalip_2015_12_012 crossref_primary_10_1016_j_freeradbiomed_2019_04_020 crossref_primary_10_1002_jcb_25305 crossref_primary_10_4161_adip_21853 crossref_primary_10_1080_00498250601167091 |
Cites_doi | 10.1194/jlr.E400002-JLR200 10.1074/jbc.274.48.34317 10.1042/bj3600135 10.18388/abp.2002_3753 10.1074/jbc.272.21.13779 10.1016/S0006-291X(02)02587-1 10.1074/jbc.M313863200 10.1006/bbrc.1997.7217 10.1083/jcb.108.5.1657 10.1016/j.abb.2004.06.005 10.1006/bbrc.2001.6245 10.1074/jbc.M109040200 10.1093/oxfordjournals.jbchem.a022544 10.1046/j.1432-1327.1998.2560060.x 10.1074/jbc.M106458200 10.1111/j.1742-4658.2005.04616.x 10.1007/s00726-005-0181-1 10.1042/bj3290601 10.1074/jbc.274.27.19188 10.1006/abbi.1996.0053 10.1016/S0163-7827(01)00017-0 10.1046/j.1432-1327.2001.02162.x 10.1074/jbc.274.14.9216 10.1046/j.1432-1327.1998.2510631.x 10.1006/bbrc.2000.3285 |
ContentType | Journal Article |
DBID | FBQ CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 ADTPV AOWAS D8T ZZAVC DOA |
DOI | 10.1194/jlr.E500003-JLR200 |
DatabaseName | AGRIS Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic SwePub SwePub Articles SWEPUB Freely available online SwePub Articles full text Directory of Open Access Journals |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
DatabaseTitleList | MEDLINE |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 3 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 4 dbid: FBQ name: AGRIS url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN sourceTypes: Publisher |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Anatomy & Physiology Chemistry |
EISSN | 1539-7262 |
EndPage | 2032 |
ExternalDocumentID | oai_doaj_org_article_3f1ae3b02bec4246a0967c10fc30eff5 oai_swepub_ki_se_579445 oai_prod_swepub_kib_ki_se_1952742 10_1194_jlr_E500003_JLR200 16103133 US201301021349 |
Genre | Research Support, U.S. Gov't, P.H.S Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NHGRI NIH HHS grantid: HG-00330 |
GroupedDBID | --- -~X .55 .GJ 0SF 0VX 18M 29K 2WC 34G 39C 4.4 53G 5GY 5RE 5VS AAEDW AAFWJ AAXUO AAYOK ABCQX ABOCM ACCCW ACGFO ACKIV ACNCT ACPRK ADBBV AENEX AEXQZ AFFNX AFOSN AFPKN AI. ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS BAWUL BTFSW C1A CS3 D-I DIK DU5 E3Z EBS EJD F5P FBQ FDB FRP GROUPED_DOAJ GX1 H13 HH5 HYE H~9 J5H KQ8 L7B MVM OK1 P2P RHF RHI ROL RPM TBC TR2 TWZ VH1 W8F WH7 WOQ X7M XFK YHG YKV ZA5 ZGI ZXP ~KM 0R~ AALRI ADVLN AITUG AKRWK CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 ADTPV AOWAS D8T ZZAVC |
ID | FETCH-LOGICAL-c596t-3204ce150d25bb0386185d01130fa8cccfd6e8b3e01981143c36e55f40629b3e3 |
IEDL.DBID | DOA |
ISSN | 0022-2275 |
IngestDate | Tue Oct 22 15:02:46 EDT 2024 Mon Dec 16 03:35:59 EST 2024 Wed Oct 30 04:42:18 EDT 2024 Fri Oct 25 02:46:20 EDT 2024 Fri Dec 06 03:14:27 EST 2024 Wed Oct 16 00:44:11 EDT 2024 Wed Dec 27 18:54:49 EST 2023 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 9 |
Language | English |
License | http://creativecommons.org/licenses/by/4.0 https://www.elsevier.com/tdm/userlicense/1.0 |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c596t-3204ce150d25bb0386185d01130fa8cccfd6e8b3e01981143c36e55f40629b3e3 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://doaj.org/article/3f1ae3b02bec4246a0967c10fc30eff5 |
PMID | 16103133 |
PQID | 68485738 |
PQPubID | 23479 |
PageCount | 4 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_3f1ae3b02bec4246a0967c10fc30eff5 swepub_primary_oai_swepub_ki_se_579445 swepub_primary_oai_prod_swepub_kib_ki_se_1952742 proquest_miscellaneous_68485738 crossref_primary_10_1194_jlr_E500003_JLR200 pubmed_primary_16103133 fao_agris_US201301021349 |
PublicationCentury | 2000 |
PublicationDate | 2005-09-01 |
PublicationDateYYYYMMDD | 2005-09-01 |
PublicationDate_xml | – month: 09 year: 2005 text: 2005-09-01 day: 01 |
PublicationDecade | 2000 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States |
PublicationTitle | Journal of lipid research |
PublicationTitleAlternate | J Lipid Res |
PublicationYear | 2005 |
Publisher | Elsevier |
Publisher_xml | – name: Elsevier |
References | Gould (10.1194/jlr.E500003-JLR200_bib17) 1989; 108 Liu (10.1194/jlr.E500003-JLR200_bib21) 1997; 272 Jones (10.1194/jlr.E500003-JLR200_bib22) 1999; 274 Maloberti (10.1194/jlr.E500003-JLR200_bib19) 2005; 272 Hunt (10.1194/jlr.E500003-JLR200_bib10) 2002; 277 Suematsu (10.1194/jlr.E500003-JLR200_bib12) 2002; 49 Lindquist (10.1194/jlr.E500003-JLR200_bib4) 1998; 251 Hunt (10.1194/jlr.E500003-JLR200_bib14) 1999; 274 Mashek (10.1194/jlr.E500003-JLR200_bib3) 2004; 45 Yamada (10.1194/jlr.E500003-JLR200_bib7) 1999; 126 Svensson (10.1194/jlr.E500003-JLR200_bib15) 1998; 329 Watanabe (10.1194/jlr.E500003-JLR200_bib20) 1997; 238 Ofman (10.1194/jlr.E500003-JLR200_bib11) 2002; 290 Finkielstein (10.1194/jlr.E500003-JLR200_bib18) 1998; 256 Yamada (10.1194/jlr.E500003-JLR200_bib2) 2005; 28 Yamada (10.1194/jlr.E500003-JLR200_bib23) 2002; 299 Jones (10.1194/jlr.E500003-JLR200_bib16) 2000; 275 Huhtinen (10.1194/jlr.E500003-JLR200_bib5) 2002; 277 Takagi (10.1194/jlr.E500003-JLR200_bib25) 2004; 429 Yamada (10.1194/jlr.E500003-JLR200_bib8) 1996; 326 Poupon (10.1194/jlr.E500003-JLR200_bib9) 1999; 274 Adams (10.1194/jlr.E500003-JLR200_bib24) 2001; 360 Suematsu (10.1194/jlr.E500003-JLR200_bib13) 2001; 268 Westin (10.1194/jlr.E500003-JLR200_bib6) 2004; 279 Hunt (10.1194/jlr.E500003-JLR200_bib1) 2002; 41 |
References_xml | – volume: 45 start-page: 1958 year: 2004 ident: 10.1194/jlr.E500003-JLR200_bib3 article-title: Revised nomenclature for the mammalian long-chain acyl-CoA synthetase gene family publication-title: J. Lipid Res. doi: 10.1194/jlr.E400002-JLR200 contributor: fullname: Mashek – volume: 274 start-page: 34317 year: 1999 ident: 10.1194/jlr.E500003-JLR200_bib14 article-title: Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise a highly conserved novel multi-gene family involved in lipid metabolism publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.48.34317 contributor: fullname: Hunt – volume: 360 start-page: 135 year: 2001 ident: 10.1194/jlr.E500003-JLR200_bib24 article-title: BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose tissue: cloning, organization of the human gene and assessment of a potential link to obesity publication-title: Biochem. J. doi: 10.1042/bj3600135 contributor: fullname: Adams – volume: 49 start-page: 937 year: 2002 ident: 10.1194/jlr.E500003-JLR200_bib12 article-title: Mouse cytosolic acetyl-CoA hydrolase, a novel candidate for a key enzyme involved in fat metabolism: cDNA cloning, sequencing and functional expression publication-title: Acta Biochim. Pol. doi: 10.18388/abp.2002_3753 contributor: fullname: Suematsu – volume: 272 start-page: 13779 year: 1997 ident: 10.1194/jlr.E500003-JLR200_bib21 article-title: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.21.13779 contributor: fullname: Liu – volume: 299 start-page: 49 year: 2002 ident: 10.1194/jlr.E500003-JLR200_bib23 article-title: Human brain acyl-CoA hydrolase isoforms encoded by a single gene publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/S0006-291X(02)02587-1 contributor: fullname: Yamada – volume: 279 start-page: 21841 year: 2004 ident: 10.1194/jlr.E500003-JLR200_bib6 article-title: Molecular cloning and characterization of two mouse peroxisome proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal acyl-CoA thioesterases publication-title: J. Biol. Chem. doi: 10.1074/jbc.M313863200 contributor: fullname: Westin – volume: 238 start-page: 234 year: 1997 ident: 10.1194/jlr.E500003-JLR200_bib20 article-title: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.1997.7217 contributor: fullname: Watanabe – volume: 108 start-page: 1657 year: 1989 ident: 10.1194/jlr.E500003-JLR200_bib17 article-title: A conserved tripeptide sorts proteins to peroxisomes publication-title: J. Cell Biol. doi: 10.1083/jcb.108.5.1657 contributor: fullname: Gould – volume: 429 start-page: 100 year: 2004 ident: 10.1194/jlr.E500003-JLR200_bib25 article-title: A 50-kDa isoform of mouse brain acyl-CoA hydrolase: expression and molecular properties publication-title: Arch. Biochem. Biophys. doi: 10.1016/j.abb.2004.06.005 contributor: fullname: Takagi – volume: 290 start-page: 629 year: 2002 ident: 10.1194/jlr.E500003-JLR200_bib11 article-title: Demonstration of dimethylnonanoyl-CoA thioesterase activity in rat liver peroxisomes followed by purification and molecular cloning of the thioesterase involved publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.2001.6245 contributor: fullname: Ofman – volume: 277 start-page: 3424 year: 2002 ident: 10.1194/jlr.E500003-JLR200_bib5 article-title: The peroxisome proliferator-induced cytosolic type I acyl-CoA thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha/beta hydrolase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M109040200 contributor: fullname: Huhtinen – volume: 126 start-page: 1013 year: 1999 ident: 10.1194/jlr.E500003-JLR200_bib7 article-title: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase publication-title: J. Biochem. (Tokyo). doi: 10.1093/oxfordjournals.jbchem.a022544 contributor: fullname: Yamada – volume: 256 start-page: 60 year: 1998 ident: 10.1194/jlr.E500003-JLR200_bib18 article-title: An adrenocorticotropin-regulated phosphoprotein intermediary in steroid synthesis is similar to an acyl-CoA thioesterase enzyme publication-title: Eur. J. Biochem. doi: 10.1046/j.1432-1327.1998.2560060.x contributor: fullname: Finkielstein – volume: 277 start-page: 1128 year: 2002 ident: 10.1194/jlr.E500003-JLR200_bib10 article-title: Characterization of an acyl-CoA thioesterase that functions as a major regulator of peroxisomal lipid metabolism publication-title: J. Biol. Chem. doi: 10.1074/jbc.M106458200 contributor: fullname: Hunt – volume: 272 start-page: 1804 year: 2005 ident: 10.1194/jlr.E500003-JLR200_bib19 article-title: Silencing the expression of mitochondrial acyl-CoA thioesterase I and acyl-CoA synthetase 4 inhibits hormone-induced steroidogenesis publication-title: FEBS J. doi: 10.1111/j.1742-4658.2005.04616.x contributor: fullname: Maloberti – volume: 28 start-page: 273 year: 2005 ident: 10.1194/jlr.E500003-JLR200_bib2 article-title: Long-chain acyl-CoA hydrolase in the brain publication-title: Amino Acids. doi: 10.1007/s00726-005-0181-1 contributor: fullname: Yamada – volume: 329 start-page: 601 year: 1998 ident: 10.1194/jlr.E500003-JLR200_bib15 article-title: Molecular cloning and characterization of a mitochondrial peroxisome proliferator-induced acyl-CoA thioesterase from rat liver publication-title: Biochem. J. doi: 10.1042/bj3290601 contributor: fullname: Svensson – volume: 274 start-page: 19188 year: 1999 ident: 10.1194/jlr.E500003-JLR200_bib9 article-title: Molecular cloning and characterization of MT-ACT48, a novel mitochondrial acyl-CoA thioesterase publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.27.19188 contributor: fullname: Poupon – volume: 326 start-page: 106 year: 1996 ident: 10.1194/jlr.E500003-JLR200_bib8 article-title: Long-chain acyl-CoA hydrolase from rat brain cytosol: purification, characterization, and immunohistological localization publication-title: Arch. Biochem. Biophys. doi: 10.1006/abbi.1996.0053 contributor: fullname: Yamada – volume: 41 start-page: 99 year: 2002 ident: 10.1194/jlr.E500003-JLR200_bib1 article-title: The role acyl-CoA thioesterases play in mediating intracellular lipid metabolism publication-title: Prog. Lipid Res. doi: 10.1016/S0163-7827(01)00017-0 contributor: fullname: Hunt – volume: 268 start-page: 2700 year: 2001 ident: 10.1194/jlr.E500003-JLR200_bib13 article-title: Molecular cloning and functional expression of rat liver cytosolic acetyl-CoA hydrolase publication-title: Eur. J. Biochem. doi: 10.1046/j.1432-1327.2001.02162.x contributor: fullname: Suematsu – volume: 274 start-page: 9216 year: 1999 ident: 10.1194/jlr.E500003-JLR200_bib22 article-title: Identification of peroxisomal acyl-CoA thioesterases in yeast and human publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.14.9216 contributor: fullname: Jones – volume: 251 start-page: 631 year: 1998 ident: 10.1194/jlr.E500003-JLR200_bib4 article-title: Molecular cloning of the peroxisome proliferator-induced 46-kDa cytosolic acyl-CoA thioesterase from mouse and rat liver publication-title: Eur. J. Biochem. doi: 10.1046/j.1432-1327.1998.2510631.x contributor: fullname: Lindquist – volume: 275 start-page: 233 year: 2000 ident: 10.1194/jlr.E500003-JLR200_bib16 article-title: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase publication-title: Biochem. Biophys. Res. Commun. doi: 10.1006/bbrc.2000.3285 contributor: fullname: Jones |
SSID | ssj0014461 |
Score | 2.1409953 |
Snippet | Acyl-CoA thioesterases, also known as acyl-CoA hydrolases, are a group of enzymes that hydrolyze CoA esters such as acyl-CoAs (saturated, unsaturated,... |
SourceID | doaj swepub proquest crossref pubmed fao |
SourceType | Open Website Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 2029 |
SubjectTerms | Alternative Splicing Animals coenzyme A fatty acid metabolism Humans Medicin och hälsovetenskap Mice Multigene Family Palmitoyl-CoA Hydrolase - genetics peroxisomes Rats Terminology as Topic |
Title | revised nomenclature for mammalian acyl-CoA thioesterases/hydrolases |
URI | https://www.ncbi.nlm.nih.gov/pubmed/16103133 https://search.proquest.com/docview/68485738 http://kipublications.ki.se/Default.aspx?queryparsed=id:1952742 https://doaj.org/article/3f1ae3b02bec4246a0967c10fc30eff5 |
Volume | 46 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwEB6hcoALghZoKBQfUC8orONHEh_DqquqRRwKK3qzHMemhd2k2t0e9t8zdpJSUCUuHCJFlqM488XzsMffALwTJfWZZyblzLpUOFWkSkkWKER9oVBXWhfZPj_nJ3NxeiEv7pT6CjlhPT1wL7gJ95lxvKYMXyaYyA363IXNqLecOu979lLKxmBq2D_AICcbecIZK-R4XEaJyY_F6sNxKANAeXr66ZyFs213TFJk7kdD4013n9P5F6NotEKzp_BkcB9J1Q_7GTxw7S7sVS2GzsstOSIxoTOulO_Co-lYzG0PZhUJ-bxr15A2cC7YRST0JOiykqVZLuNqBzF2u0inXUU2l1ddpFBAG7eeXG6bFUbAePsc5rPjr9OTdCihkFqp8g0iQIV16PQ1TNY15WWO9rnBOc2pN6W11je5K2vu0NMrMTTiludOSo9mnils5i9gp-1atw-kyZlRmaiVYU4ojgpb1IXlRuWKWZ6JBN6PUtTXPVOGjhGGEhplrgeZ617mCXwMgr7tGViuYwNirwfs9b-wT2AfYdLmO-pDPf_Cwi5sKFXOhUrg7YidRlGHXRDTuu5mrfNSlLLgZQIve0h_jzYPNS84T4D2GP8xumDQ9ND-8ypceu10hj92IVgCR_c8cts79JSo-YR89T---wAeRwbZmOr2GnY2qxv3Bn2jTX0ID6uz829nh3E6_AKU8wrp |
link.rule.ids | 230,314,780,784,864,885,2102,27924,27925 |
linkProvider | Directory of Open Access Journals |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=A+revised+nomenclature+for+mammalian+acyl-CoA+thioesterases%2Fhydrolases&rft.jtitle=Journal+of+lipid+research&rft.au=Hunt%2C+Mary+C&rft.au=Yamada%2C+Junji&rft.au=Maltais%2C+Lois+J&rft.au=Wright%2C+Mathew+W&rft.date=2005-09-01&rft.issn=0022-2275&rft.volume=46&rft.issue=9&rft.spage=2029&rft.epage=2032&rft_id=info:doi/10.1194%2Fjlr.E500003-JLR200&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-2275&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-2275&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-2275&client=summon |