The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia.
about
Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severingCellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastinInteraction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenanceSPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis.Autolytic activity of human calpain 7 is enhanced by ESCRT-III-related protein IST1 through MIT-MIM interactionSPG20 protein spartin associates with cardiolipin via its plant-related senescence domain and regulates mitochondrial Ca2+ homeostasisInteractions of the human LIP5 regulatory protein with endosomal sorting complexes required for transportScyl1, mutated in a recessive form of spinocerebellar neurodegeneration, regulates COPI-mediated retrograde trafficAb initio protein modelling reveals novel human MIT domainsStructure and ESCRT-III protein interactions of the MIT domain of human VPS4A.The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradationTroyer syndrome protein spartin is mono-ubiquitinated and functions in EGF receptor traffickingRecycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1Drosophila spastin regulates synaptic microtubule networks and is required for normal motor functionOxidative Stress in Caenorhabditis elegans: Protective Effects of SpartinA Common Substrate Recognition Mode Conserved between Katanin p60 and VPS4 Governs Microtubule Severing and Membrane Skeleton ReorganizationCrystal structure of the human spastin AAA domainStructural and functional characterization of the microtubule interacting and trafficking domains of two oomycete chitin synthasesAtg38 is required for autophagy-specific phosphatidylinositol 3-kinase complex integrity.The Vps4 C-terminal helix is a critical determinant for assembly and ATPase activity and has elements conserved in other members of the meiotic clade of AAA ATPases.Gene organization, evolution and expression of the microtubule-associated protein ASAP (MAP9)Spg20-/- mice reveal multimodal functions for Troyer syndrome protein spartin in lipid droplet maintenance, cytokinesis and BMP signalingSpartin recruits PKC-ζ via the PKC-ζ-interacting proteins ZIP1 and ZIP3 to lipid dropletsSMART 4.0: towards genomic data integrationLack of spartin protein in Troyer syndrome: a loss-of-function disease mechanism?The PRESAT-vector: asymmetric T-vector for high-throughput screening of soluble protein domains for structural proteomics.Spastin and atlastin, two proteins mutated in autosomal-dominant hereditary spastic paraplegia, are binding partnersSpartin activates atrophin-1-interacting protein 4 (AIP4) E3 ubiquitin ligase and promotes ubiquitination of adipophilin on lipid droplets.Chitin synthases from Saprolegnia are involved in tip growth and represent a potential target for anti-oomycete drugs.Role of spastin and protrudin in neurite outgrowth.Vps4 stimulatory element of the cofactor Vta1 contacts the ATPase Vps4 α7 and α9 to stimulate ATP hydrolysis.ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegiaSPG20, a novel biomarker for early detection of colorectal cancer, encodes a regulator of cytokinesis.Distinct mechanisms of recognizing endosomal sorting complex required for transport III (ESCRT-III) protein IST1 by different microtubule interacting and trafficking (MIT) domainsStrumpellin and Spartin, Hereditary Spastic Paraplegia Proteins, are Binding Partners.BECLIN 1-VPS34 COMPLEX ARCHITECTURE: UNDERSTANDING THE NUTS AND BOLTS OF THERAPEUTIC TARGETS.Relief of autoinhibition enhances Vta1 activation of Vps4 via the Vps4 stimulatory elementA role for ubiquitin ligases and Spartin/SPG20 in lipid droplet turnoverSpartin regulates synaptic growth and neuronal survival by inhibiting BMP-mediated microtubule stabilization.Membrane protein targeting to the MVB/lysosome.
P2860
Q24295083-999DFBC4-A800-485A-987E-3AAAB649127BQ24295115-05E19F60-0F2A-4641-BFBD-D5E556431988Q24295258-032A1A00-D6C4-4130-889F-0C6C828E8591Q24296616-A828DC24-5FAD-4AF8-BE3C-DF9D0A70714DQ24300075-39C4726F-68FA-42B8-8315-3FD4893609A3Q24301953-6B216575-E179-4D19-8266-11D93751FAFFQ24302018-ABA891AC-9F6C-404F-8B93-4CE902B473ADQ24321860-536B9347-F1E6-48BF-A9CF-A2A74A220BE7Q24322870-837675E3-E4ED-4D29-B191-5225C02628ACQ24328880-60E52168-36EA-4789-8068-62B7AC0A4372Q24337922-F76E062E-9F53-4B08-A1BE-A0E8155C4CD5Q24681559-17F02A10-CEF4-4E77-8930-F0666092A434Q24683826-5A058341-F2AF-460B-A7AB-F1EAA849BC7AQ24798261-33712A37-6198-48B5-B660-22C4FB94DDF7Q27303983-F210AE08-0149-4107-B28D-407238F082ACQ27660328-05519C7C-C5C3-4C08-8E76-97EB90F12579Q27678193-00FEB787-FE00-4D94-B2A7-E7B63D6584FDQ27715381-E0C72D20-CBA5-4561-AC47-506DE701FE58Q27930870-58249012-ED3A-48EA-98AA-574E52CAF3D0Q27938195-97AA474F-8B62-44CD-8870-2B6F1FFA37B4Q28507364-AA96964A-0C55-43E4-B2C1-78B5B22E2171Q28511369-CDD853D2-3058-4685-9A5A-8AF97AC0BC06Q28589177-933D0BA3-EBEA-4CBB-A9F0-5165E53130C2Q29547824-4D4124D6-5774-4A80-B6A8-DAB76DFBB7A9Q31152681-46D4858A-4463-4B33-8641-2A2CF85A6CEEQ33198534-9938D327-A3F7-4FBD-B2BF-CECFF72D75F0Q33229002-D9D90FEF-6DEE-47EB-AFC4-6474E966EC7AQ33588020-01F6C853-4149-4689-9CDF-8D5C59AC2232Q33701812-5A110F8D-BDC7-40BF-A22B-87D85179BDDDQ34273874-DB4957AE-5030-464B-B118-4B9144F4C624Q34317515-9B9D554E-6372-4408-8A9F-441FA3BDDF24Q34545631-F07590C5-BC76-4CA9-ADC0-99F6B6586795Q35216353-1905DA31-777C-4F68-B2BD-043164C4EDC6Q35221588-C5EDF9D6-42FC-4B92-AA4D-BD0CE2A8FFDEQ35591871-208ABEC0-15FE-4479-8650-BD4C7EA7DD3FQ36379709-7E53613E-5B8A-4A09-BDF0-6C8637EA887DQ37151081-B21A29B7-4F48-4936-93F6-1DDA01EBBC90Q37234369-E1D30B9C-CEBD-41A1-AA5C-5BF595E436B7Q37273587-CAE059F7-0D13-4474-B026-ABBC69E4FE30Q37401247-2DFC4873-81C1-4A79-907E-5A85A9B0C4BF
P2860
The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The identification of a conser ...... hereditary spastic paraplegia.
@ast
The identification of a conser ...... hereditary spastic paraplegia.
@en
The identification of a conser ...... hereditary spastic paraplegia.
@nl
type
label
The identification of a conser ...... hereditary spastic paraplegia.
@ast
The identification of a conser ...... hereditary spastic paraplegia.
@en
The identification of a conser ...... hereditary spastic paraplegia.
@nl
prefLabel
The identification of a conser ...... hereditary spastic paraplegia.
@ast
The identification of a conser ...... hereditary spastic paraplegia.
@en
The identification of a conser ...... hereditary spastic paraplegia.
@nl
P2093
P50
P1433
P1476
The identification of a conser ...... hereditary spastic paraplegia.
@en
P2093
Andrew H Crosby
Harold Cross
Heema Patel
Michael A Patton
Shakil Azam
P304
P356
10.1016/S0888-7543(03)00011-9
P577
2003-04-01T00:00:00Z