Latrunculin alters the actin-monomer subunit interface to prevent polymerization - Wikidata - wikimedia - TriplyDB

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

http://www.wikidata.org/entity/Q27624918

about

An actin-regulated importin α/β-dependent extended bipartite NLS directs nuclear import of MRTF-A Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL Spatiotemporal regulation of chloride intracellular channel protein CLIC4 by RhoA.Small GTP-binding protein TC10 differentially regulates two distinct populations of filamentous actin in 3T3L1 adipocytes.A mutation of beta -actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia Identification of a novel sequence in PDZ-RhoGEF that mediates interaction with the actin cytoskeleton Molecular identification of a malaria merozoite surface sheddase Cytoskeleton-Dependent Transport as a Potential Target for Interfering with Post-transcriptional HuR mRNA Regulons Spatiotemporal quantification of subcellular ATP levels in a single HeLa cell during changes in morphology.Turnover of the actomyosin complex in zebrafish embryos directs geometric remodelling and the recruitment of lipid droplets.A dynamic formin-dependent deep F-actin network in axons.PI(3,5)P2 controls endosomal branched actin dynamics by regulating cortactin-actin interactions.aPKC regulates apical localization of Lgl to restrict elongation of microridges in developing zebrafish epidermis Cellular development associated with induced mycotoxin synthesis in the filamentous fungus Fusarium graminearum Structural differences explain diverse functions of Plasmodium actins Tubule-guided cell-to-cell movement of a plant virus requires class XI myosin motors Oxidized Hemoglobin Is an Endogenous Proinflammatory Agonist That Targets Vascular Endothelial Cells Polylysine induces an antiparallel actin dimer that nucleates filament assembly: crystal structure at 3.5-A resolution Mechanism of actin filament pointed-end capping by tropomodulin A role for the dynamin-like protein Vps1 during endocytosis in yeast Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis.The connection of cytoskeletal network with plasma membrane and the cell wall Actin-interacting protein 1 controls assembly and permeability of intestinal epithelial apical junctions Functional reconstitution of mammalian 'chloride intracellular channels' CLIC1, CLIC4 and CLIC5 reveals differential regulation by cytoskeletal actin Participation of actin on Giardia lamblia growth and encystation STARS, a striated muscle activator of Rho signaling and serum response factor-dependent transcription Latrunculin B or ATP depletion induces cofilin-dependent translocation of actin into nuclei of mast cells Stress-induced sensitization to cocaine: actin cytoskeleton remodeling within mesocorticolimbic nuclei Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension Osmotic stress signaling and osmoadaptation in yeasts.Flexible nets. The roles of intrinsic disorder in protein interaction networks.The chloride-channel blocker 9-anthracenecarboxylic acid reduces the nonlinear capacitance of prestin-associated charge movement.Functional effects of mutations in the tropomyosin-binding sites of tropomodulin1 and tropomodulin3.α-Actinin-4/FSGS1 is required for Arp2/3-dependent actin assembly at the adherens junction The actin-driven movement and formation of acetylcholine receptor clusters Disparities in voltage-sensor charge and electromotility imply slow chloride-driven state transitions in the solute carrier SLC26a5.Subsecond reorganization of the actin network in cell motility and chemotaxis.Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis.Mobile actin clusters and traveling waves in cells recovering from actin depolymerization.Identification of a distal GLUT4 trafficking event controlled by actin polymerization

P2860

Q24298695-1AC29AB1-D237-4B8C-A92A-735D99CFA4F8 Q24314708-3B704C6A-9961-4B44-9A1E-4131A4DE8F3F Q24318266-5339A44D-0FAA-4116-BFB4-87FC147D3565 Q24530193-7878F21B-8B8C-436E-9B74-54E67A19855C Q24546532-6FA7AF61-5011-4FA4-8462-23899CD1012C Q24610248-4DDBCD69-09FD-47AF-812E-91B5801343D0 Q24811597-20DE4A62-2980-414E-9C07-691432A27F77 Q26827136-44B8C0DA-DF60-44BB-BDD5-730F14F9BDCD Q27305640-397A9BB7-BF24-4F97-9644-CB95DAD1D4E2 Q27308699-B7E02EED-5FA5-4E17-8DE2-E4FD79B11149 Q27309123-87439F70-A5F6-4CD0-8510-7019D77B9D64 Q27310309-11BE1771-1627-4BB2-ADF6-3DE81EE53ADB Q27316263-C2230A7C-249F-4FB4-8002-C898E004C52D Q27321258-98701405-127E-48EA-9789-E22B68683AD5 Q27327176-1EA23B99-C563-4561-BFE7-C15F7C6CDFE0 Q27348727-09915F9C-C4BE-4BC4-AA31-82439911BAB3 Q27490449-B9544B1E-93C5-4E47-86A4-FEBCE233236D Q27638724-53BC7C2A-1818-4CA0-A04B-86C1A2CE4E72 Q27684814-3B1D6A21-66B8-4C83-9CB1-92C7F80B8367 Q27939694-A5357CB0-68FB-4A63-B858-E0A9710772F2 Q27939868-AB6AEC61-1F32-4F46-BB8B-2F8D77801B99 Q28081889-AE556C87-00FB-4A0B-BC9C-BFF71D0BB107 Q28117474-7FC1D7A8-221D-4D16-9906-E239542112D0 Q28258203-DBB497AB-87F9-46C7-876F-932E857F06B3 Q28476198-B64F378C-44D6-4387-88F1-D6C4D58A0C4B Q28512614-0B6C1A91-8553-49A4-93B0-661EEEB4AECA Q28570802-DC7418D7-DEA8-427A-B1FD-45F218A5E724 Q28573964-8C29B116-B17B-4331-95E6-09C0FF0DC3B8 Q28591494-7700D906-7F08-4433-B7B1-42F8F7627593 Q29617597-8452FDB9-7FD6-42C3-8177-2EB01F6013EA Q30351593-BAF574F4-64ED-4279-86BD-E853CE1E0DC8 Q30369744-3BD77D13-B6FE-4DDC-BE07-B19E04010505 Q30407577-F9D26684-8BAC-452F-80AC-A9156EC3737A Q30426063-540C9D81-EDF1-4E93-90AF-22D080EB4CB3 Q30442025-7BDE7BF8-22C5-4E42-A8B2-E353B0143C7F Q30449706-1EDAD1EB-E076-4891-A253-4142CFD8A955 Q30475911-E63E3DF7-86DF-4896-8FB6-A07946D54851 Q30476106-B2155D79-9C5C-4334-818C-54114C571C19 Q30476460-8286DEC5-CDB2-4465-8B14-FC446DB9D75A Q30489900-67B22D1D-96F7-4508-89CA-E7D778846640

P2860

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

http://www.wikidata.org/entity/Q27624918

description

2000 nî lūn-bûn

@nan

2000 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@ast

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@en

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@nl

type

label

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@ast

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@en

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@nl

prefLabel

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@ast

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@en

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@nl

P1433

Q27624918-5E0B64FC-C002-4F72-BA14-3425080E11E9

P1476

Q27624918-5E8D99F2-9785-4CBC-9FBC-6DAE892DCEAE

P2093

Q27624918-439C5465-6073-4A8F-9F2F-DAEE6175B60C

Q27624918-71DEA9A1-33A6-4F09-8F70-5EFAE83B1F2A

Q27624918-B5D53E7A-A804-46AE-8072-E1DBB5252548

P2860

Q27624918-180863BC-6732-4C4A-BFE3-00EC8CF0D806

Q27624918-1BD3EFAD-76F8-4841-B978-16042A78420C

Q27624918-3A379206-BD39-44A4-A330-40780E4D9065

Q27624918-4676AB85-EF45-40A2-839B-9318A78A2DD5

Q27624918-4B374F04-55A3-4C6E-A707-2825DA5BD87D

Q27624918-7B325CEE-3012-4149-B752-45D7B375EA86

Q27624918-8562ACCA-F2C5-4482-AA8E-A5D3A8864790

Q27624918-9689880F-F401-44B7-A58E-F3A25BE08012

Q27624918-AA680861-207C-4406-AB8B-27B77DC5B15A

Q27624918-ECA237D6-338B-4236-AEFB-24D63D014B96

P2888

Q27624918-978492A8-DCE7-4BE6-96AD-4C69491B5F5F

P304

Q27624918-0D677BA3-4A09-415C-9996-64328CB5AF28

P31

Q27624918-D9091756-5F76-4CDE-B53E-2ACD30400C8D

P3181

Q27624918-D577E3CA-3ABD-43D3-B4A8-937781E44A7C

P356

Q27624918-744B8C42-62ED-4510-B8F0-69E01B39C41C

P433

Q27624918-5094956D-CFD8-4B56-ADCE-CB8D4564BA82

P478

Q27624918-032C28AC-1EB2-44CC-8542-77923736437E

P577

Q27624918-01EA03A1-7035-47C6-BCEE-1418AD969AAE

P5875

Q27624918-C0B2E92C-45A9-4239-ADD1-7638650B0156

P6179

Q27624918-E5E49734-C6D0-439B-BB58-3AE9EDBE8069

P698

Q27624918-D91ABD0D-3029-4F89-9618-009E7C84CE93

P3181

P356

P1433

Nature Cell Biology

P1476

Latrunculin alters the actin-monomer subunit interface to prevent polymerization

@en

P2093

K R Ayscough

http://www.w3.org/2001/XMLSchema#string

P J McLaughlin

http://www.w3.org/2001/XMLSchema#string

W M Morton

http://www.w3.org/2001/XMLSchema#string

P2860

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Structure of gelsolin segment 1-actin complex and the mechanism of filament severing

Raster3D: photorealistic molecular graphics

An extensively modified version of MolScript that includes greatly enhanced coloring capabilities

Refinement of macromolecular structures by the maximum-likelihood method

High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A.

Inhibition of actin polymerization by latrunculin A.

Domain motions in actin.

Latrunculin, a new 2-thiazolidinone macrolide from the marine sponge

Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells

P2888

P304

376-8

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1132117

http://www.w3.org/2001/XMLSchema#string

P356

10.1038/35014075

http://www.w3.org/2001/XMLSchema#string

P433

6

http://www.w3.org/2001/XMLSchema#string

P478

2

http://www.w3.org/2001/XMLSchema#string

P577

2000-06-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

12464899

http://www.w3.org/2001/XMLSchema#string

P6179

1047936452

http://www.w3.org/2001/XMLSchema#string

P698

10854330

http://www.w3.org/2001/XMLSchema#string