The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold
about
Cloning and characterization of a novel RING finger protein that interacts with class V myosinsHuman beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein IbalphaStructure of three tandem filamin domains reveals auto-inhibition of ligand bindingEvolutionarily conserved human targets of adenosine to inosine RNA editingIdentification of novel families and classification of the C2 domain superfamily elucidate the origin and evolution of membrane targeting activities in eukaryotesDifferent splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunitsExploring the energy landscape of GFP by single-molecule mechanical experiments.Filamin structure, function and mechanics: are altered filamin-mediated force responses associated with human disease?Transcript diversification in the nervous system: a to I RNA editing in CNS function and disease developmentSingle-molecule protein unfolding and translocation by an ATP-fueled proteolytic machine.Expression, crystallization and preliminary crystallographic data analysis of filamin A repeats 14-16.Interaptin, an actin-binding protein of the alpha-actinin superfamily in Dictyostelium discoideum, is developmentally and cAMP-regulated and associates with intracellular membrane compartments.Structural basis of filamin A functionsA dual phenotype of periventricular nodular heterotopia and frontometaphyseal dysplasia in one patient caused by a single FLNA mutation leading to two functionally different aberrant transcriptsThe filamins: organizers of cell structure and functionProtein unfolding under force: crack propagation in a network.Cytoplasmic Ig-domain proteins: cytoskeletal regulators with a role in human diseaseProtein folding on the ribosome studied using NMR spectroscopy.The folding pathway of a fast-folding immunoglobulin domain revealed by single-molecule mechanical experiments.Diverse phenotypic consequences of mutations affecting the C-terminus of FLNA.Filamin-regulated F-actin assembly is essential for morphogenesis and controls phototaxis in Dictyostelium.Scanning the available Dictyostelium discoideum proteome for O-linked GlcNAc glycosylation sites using neural networks.Dictyostelium Sun-1 connects the centrosome to chromatin and ensures genome stability.Distinguishing native conformations of proteins from decoys with an effective free energy estimator based on the OPLS all-atom force field and the Surface Generalized Born solvent model
P2860
Q22010202-51655CC1-4B6F-4779-9F7B-EC2F3884A95CQ24311451-F9E4FE79-0D0F-4A8F-89D2-936D1CA0D06FQ24337150-3F1ED207-3F8D-4F9E-8BCE-418EF0F517C9Q24556614-A35A742A-F0CA-4C62-8F2B-896D17959E0EQ24623162-25F41D77-1F8F-45A6-9618-0EC16B6E7153Q24652710-DA998D59-A9C2-4F3B-876F-3B81BE2B9081Q30160409-E6AD676E-064D-4340-B941-370B7DE27A15Q30402039-8BC07E97-D0DC-4DCC-9713-CF9253974EE6Q30465782-32EA9032-4BAB-4A3B-B90F-4EA56B004A29Q30473723-29687E12-DDE3-4E1A-9C08-68881689B4D4Q31107811-A3C02B93-775B-49E1-859B-64C5DD1FFD2DQ32040709-1BA87883-EA68-4FF5-8EBF-9F2FC82D8979Q33308469-AD2A70A8-2E10-4655-AE27-0EB1612AC9D2Q33909739-C3B9535E-9D53-466C-B233-BAC12124FDB5Q34891266-8610E2D5-EF13-4FEC-B07F-F3066D37EE2AQ35132782-1B725739-FC45-4F07-8A90-F0885E525F02Q37494624-B5F70A79-DDA1-44FD-BE58-45A6E6B54562Q37710489-0EA432F6-F2B0-49FD-AADD-18EF8835341FQ40108154-A74C84CD-8AA0-490C-8451-A62E8EA18F1DQ41428426-68C1946E-1892-411A-9C8A-9BC3E25665AFQ50707343-34B22D16-6E52-4334-81A9-F5D5465C076FQ52141888-2BEDE650-2383-4704-AE41-430DE55AA0C9Q53498909-2DBBB197-7729-4A57-B893-831E7D52739EQ57134711-C3C5F6BE-FC2D-48BC-9697-DD2E8DA5D45E
P2860
The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold
description
1997 nî lūn-bûn
@nan
1997 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի մարտին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The repeating segments of the ...... ve an immunoglobulin-like fold
@ast
The repeating segments of the ...... ve an immunoglobulin-like fold
@en
The repeating segments of the ...... ve an immunoglobulin-like fold
@nl
type
label
The repeating segments of the ...... ve an immunoglobulin-like fold
@ast
The repeating segments of the ...... ve an immunoglobulin-like fold
@en
The repeating segments of the ...... ve an immunoglobulin-like fold
@nl
prefLabel
The repeating segments of the ...... ve an immunoglobulin-like fold
@ast
The repeating segments of the ...... ve an immunoglobulin-like fold
@en
The repeating segments of the ...... ve an immunoglobulin-like fold
@nl
P2093
P2860
P356
P1476
The repeating segments of the ...... ve an immunoglobulin-like fold
@en
P2093
A A Noegel
C Herberhold
P2860
P304
P356
10.1038/NSB0397-223
P50
P577
1997-03-01T00:00:00Z