The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding.
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Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinAThe early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitroLULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutationPrintor, a novel torsinA-interacting protein implicated in dystonia pathogenesisTorsins: not your typical AAA+ ATPasesThe BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Torsin ATPases: Harnessing Dynamic Instability for Function.Functional evidence implicating a novel TOR1A mutation in idiopathic, late-onset focal dystonia.TorsinA and the torsinA-interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast.Biochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1AA unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding.DYT1 knock-in mice are not sensitized against mitochondrial complex-II inhibition.Untethering the nuclear envelope and cytoskeleton: biologically distinct dystonias arising from a common cellular dysfunctionIntracellular complexes of the early-onset torsion dystonia-associated AAA+ ATPase TorsinA.How lamina-associated polypeptide 1 (LAP1) activates Torsin.Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum.A predictable worm: application of Caenorhabditis elegans for mechanistic investigation of movement disorders.Invertebrate models of dystonia.Site-specific Proteolysis Mobilizes TorsinA from the Membrane of the Endoplasmic Reticulum (ER) in Response to ER Stress and B Cell Stimulation.Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia.Disruption of Protein Processing in the Endoplasmic Reticulum of DYT1 Knock-in Mice Implicates Novel Pathways in Dystonia Pathogenesis.Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion.Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF).Early-onset torsion dystonia: a novel high-throughput yeast genetic screen for factors modifying protein levels of torsinAΔE.Torsin ATPases: structural insights and functional perspectives.TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement.Review: Progresses in understanding N-ethylmaleimide sensitive factor (NSF) mediated disassembly of SNARE complexes.Membrane defects and genetic redundancy: Are we at a turning point for DYT1 dystonia?Exploring the influence of torsinA expression on protein quality control.Transcriptional and proteomic profiling in a cellular model of DYT1 dystoniaConsequences of the DYT1 mutation on torsinA oligomerization and degradation.LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia.Biallelic TOR1A variants in an infant with severe arthrogryposis.Age-associated changes in gene expression and developmental competence of bovine oocytes, and a possible countermeasure against age-associated events.The ins and outs of endoplasmic reticulum-controlled lipid biosynthesis.
P2860
Q22001542-948C4615-AA23-4DB6-A6E9-45A9DC3CDFADQ24300223-75B308D5-19FA-432C-A943-FAF060642629Q24311570-2E98ECAF-6F07-4063-BA93-BDE3B47D07D8Q24338612-A0584A21-AD31-42B9-AD7F-DFA9630B83BFQ28087663-0028C47E-F987-4AC8-8AF9-9F6B54091936Q33556224-9E6B267C-FAB3-4C4B-8789-BE4484EF3068Q33658996-C172CDFE-446B-4AD1-8C17-333CB0788297Q33938827-ADB71577-85F7-4864-B1F3-1B8661705E5FQ33983398-965A3E6E-2F60-4FF2-B7D9-2093C96C45F9Q34052884-9E48815B-3667-4384-82F7-6E8D79DB4C7AQ34333556-D6178AC4-92DC-4301-8932-B1EA02A91F3EQ34374500-3F16DEDD-0E6B-42C2-8777-5BD0BA00183AQ34638417-A285693F-798C-4360-9B59-A2B2B71311ECQ35059239-D3B0DF12-0C26-44B4-B621-CEEB7E69B261Q35173159-5F779796-E730-4210-AC09-253B7564D725Q35178306-FA0F15EE-5AB5-4E97-8002-5879AE634286Q35913800-B57F9200-AECB-4290-88D8-001DC358DD83Q36634138-F710BD58-AD3A-472C-98F0-223F5EA9ED4CQ36849988-ADA70885-D6EB-4A47-91DF-706A6A057FE7Q37207770-30CF94C6-DAF3-4AD9-8514-E29B3125D4ECQ37310305-7E47769F-874C-441A-B77B-09D11DD45CD4Q37459854-EC1785B0-84FC-4CFA-A288-0FC3107AA615Q37892093-655F5307-C104-4971-94D6-21520D0331C7Q38646083-B951D32B-A737-4148-BD1A-16682506AB85Q38709393-50716D1F-1ED1-455E-9EDB-2EF5AF914F99Q38714582-B8D46E3D-9F5E-4013-BD85-9227423A5D49Q38803266-4BFD6308-D293-4A98-9A9A-90E50B01F804Q39026993-B350FE63-B1B2-4CF4-BC46-A20F7671FAC9Q39619556-C718D89E-B1BA-4D15-BA10-7D95615AB693Q39815077-AA07B9F7-9886-4E10-8A0B-EF506ED0312CQ39926996-9C15206A-878C-4E40-AFDF-2ECF026493B1Q41785405-74B32424-1013-46EA-BBA8-81655B9C3F6EQ42280431-49547C70-6A87-4575-83C8-3D6C96679B4EQ42710994-972174CA-C9CD-4F24-8ED6-CB471D091541Q46273814-D63ACAA2-9C22-467C-A9F4-775B6B06FEF6
P2860
The torsin-family AAA+ protein OOC-5 contains a critical disulfide adjacent to Sensor-II that couples redox state to nucleotide binding.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
The torsin-family AAA+ protein ...... x state to nucleotide binding.
@en
type
label
The torsin-family AAA+ protein ...... x state to nucleotide binding.
@en
prefLabel
The torsin-family AAA+ protein ...... x state to nucleotide binding.
@en
P2093
P2860
P356
P1476
The torsin-family AAA+ protein ...... x state to nucleotide binding.
@en
P2093
Adam P Hayashi
James O Wrabl
Lesilee S Rose
Philip J Thomas
P2860
P304
P356
10.1091/MBC.E08-01-0015
P577
2008-06-11T00:00:00Z