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・ FIS Snowboarding World Championships 2013 – Men's halfpipe
・ FIS Snowboarding World Championships 2013 – Men's parallel giant slalom
・ FIS Snowboarding World Championships 2013 – Men's parallel slalom
・ FIS Snowboarding World Championships 2013 – Men's slopestyle
・ FIS Snowboarding World Championships 2013 – Men's snowboard cross
・ FIS Snowboarding World Championships 2013 – Women's halfpipe
・ FIS Snowboarding World Championships 2013 – Women's parallel giant slalom
・ FIS Snowboarding World Championships 2013 – Women's parallel slalom
・ FIS Snowboarding World Championships 2013 – Women's slopestyle
・ FIS Snowboarding World Championships 2013 – Women's snowboard cross
・ FIS Team Tour 2010
・ FIS Team Tour 2011
・ FIS Team Tour 2012
・ FIS Team Tour 2013
・ FIS World Cup
FIS1
・ FISA (disambiguation)
・ FISA Accountability and Privacy Protection Act of 2013
・ FISA Improvements Act
・ Fisaga
・ Fisantekraal
・ Fisantekraal Airfield
・ FISA–FOCA war
・ FISBA
・ Fisc
・ Fisc (disambiguation)
・ Fiscaglia
・ Fiscal
・ Fiscal (Amares)
・ Fiscal adjustment


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FIS1 : ウィキペディア英語版
FIS1

Mitochondrial fission 1 protein (FIS1) is a protein that in humans is encoded by the ''FIS1'' gene on chromosome 7.〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51024 )〕 This protein is a component of a mitochondrial complex, the ARCosome, that promotes mitochondrial fission.〔 Its role in mitochondrial fission thus implicates it in the regulation of mitochondrial morphology, the cell cycle, and apoptosis.〔〔〔 By extension, the protein is involved in associated diseases, including neurodegenerative diseases and cancers.

==Structure==
The protein encoded by this gene is a 16 kDa integral protein situated in the outer mitochondrial membrane (OMM).〔 It is composed of a transmembrane domain at the C-terminal and a cytosolic domain at the N-terminal.〔 The transmembrane domain anchors FIS1 in the OMM, though it has been observed to target different cellular compartments, such as the peroxisome, depending on its hydrophobicity, charge, and length.〔 Meanwhile, the cytosolic domain contains a bundle of six helices, four of which contain two tandem tetratricopeptide repeat (TPR)-like motifs. These motifs form a concave surface by their combined superhelical structure and potentially bind another FIS1 protein to form a dimer, or other proteins.〔〔 Moreover, the N-terminal arm can dock at, and thus obstruct, the TPR motifs, allowing the protein to exist in a dynamic equilibrium between “open” and “closed” states.〔

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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