ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4
about
The molecular and functional interaction between ICln and HSPC038 proteins modulates the regulation of cell volume.ICln: a new regulator of non-erythroid 4.1R localisation and functionBinding cavities and druggability of intrinsically disordered proteins.TIS7 induces transcriptional cascade of methylosome components required for muscle differentiation.Pleckstrin homology (PH) domains and phosphoinositides.A PH domain in the Arf GTPase-activating protein (GAP) ARAP1 binds phosphatidylinositol 3,4,5-trisphosphate and regulates Arf GAP activity independently of recruitment to the plasma membranes.Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans.The C-terminus of ICln is natively disordered but displays local structural preformationCharacterization and in vivo functional analysis of the Schizosaccharomyces pombe ICLN gene.Role of pICLn in methylation of Sm proteins by PRMT5.EGF stimulates IClswell by a redistribution of proteins involved in cell volume regulation.Crystallizing the 6S and 8S spliceosomal assembly intermediates: a complex project.
P2860
1510b2f46bc95db4f1df463ece05e713bd50bb49210492f92cfa260366d15628d79074416d65fd6d41cbdc7e582fb41b15dabbd49e166211f2c2bcfb6d1cd35a889b29fde887a999599b8e2d7f09bc5583c942ee8129018b237c579ab3b207735204c508b1a559f9ba0b00d5ee60d360772985d4a419fc99e1f957770c11626079e233afd7903b5ecee06d81f6ee605945e6b4579489d1b882ed77524888789b
P248
Q34216368-5EF0708A-4D3A-4481-A75D-11470B92BC92Q35312210-94AFCD94-984B-4EE1-9079-ECF2373A9C9DQ35571730-0A45CADC-1BDE-4728-AD32-74AE91406C66Q36174725-08D71C2C-FAB3-480A-9C50-C89451E1C39CQ36711258-7EE856F0-6A1A-4603-BF1B-2AD7617CDD9BQ37459921-86C69DD2-0EAB-4571-8D4B-3A277C8522ACQ38197052-F1AAAAFC-9154-4022-8DD0-CE655A770A70Q41120778-EEFEE6C6-77CF-4ED7-8F4A-D8E1FF83EE5BQ41908770-A2374DB6-EFCC-4A6C-A18A-E1A6022C6C19Q42575278-92D23426-786A-4267-9B63-959F1501E8C7Q42802010-84E31F59-BA4A-48C9-A09D-55E808D6C5DAQ50925647-4771A114-D1B1-4679-8883-021D6AFAD3D3
P2860
ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@ast
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@en
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@nl
type
label
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@ast
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@en
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@nl
prefLabel
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@ast
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@en
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@nl
P2093
P2860
P50
P921
P3181
P356
P1476
ICln159 folds into a pleckstri ...... s and the splicing factor LSm4
@en
P2093
Andreas Schedlbauer
Ben C Tilly
Bettina Sarg
Claudia Bazzini
Giuliano Meyer
Guido Botta
Herbert Lindner
Johannes Fürst
Maria Lisa Garavaglia
Markus Paulmichl
P2860
P304
P3181
P356
10.1074/JBC.M500541200
P407
P577
2005-09-02T00:00:00Z