Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
about
Crystal structure of human coactosin-like protein at 1.9 A resolutionVisualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprintingStructural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilinSolution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factorStructure of the actin-depolymerizing factor homology domain in complex with actinStructure of the N Terminus of a Nonmuscle α-Tropomyosin in Complex with the C Terminus: Implications for Actin Binding † ‡Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1Solution structure and dynamics of ADF from Toxoplasma gondiiA Plasmodium actin-depolymerizing factor that binds exclusively to actin monomersStructural analysis of gelsolin using synchrotron protein footprinting.Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis.Pulsed electron beam water radiolysis for submicrosecond hydroxyl radical protein footprintingVisualizing water molecules in transmembrane proteins using radiolytic labeling methods.Future directions of structural mass spectrometry using hydroxyl radical footprinting.Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin.Fast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstarThree-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data.Modeling of protein binary complexes using structural mass spectrometry data.Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1.'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility.Conformational changes in guanylate cyclase-activating protein 1 induced by Ca2+ and N-terminal fatty acid acylation.Structural and functional dissection of the Abp1 ADFH actin-binding domain reveals versatile in vivo adapter functions.A potential yeast actin allosteric conduit dependent on hydrophobic core residues val-76 and trp-79.The ClpP N-terminus coordinates substrate access with protease active site reactivity.Dynamic protein ligand interactions--insights from MS.Mapping the cofilin binding site on yeast G-actin by chemical cross-linking.A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.Myosin binding surface on actin probed by hydroxyl radical footprinting and site-directed labelsVisualizing Arp2/3 complex activation mediated by binding of ATP and WASp using structural mass spectrometryStructural analysis of proinsulin hexamer assembly by hydroxyl radical footprinting and computational modelingThe effect of histidine oxidation on the dissociation patterns of peptide ions.Isotope-Coded Labeling for Accelerated Protein Interaction Profiling Using MS.Probing the pH-dependent prepore to pore transition of Bacillus anthracis protective antigen with differential oxidative protein footprintingCovalent labeling with isotopically encoded reagents for faster structural analysis of proteins by mass spectrometry.Regulation of actin cytoskeleton dynamics in cells.Chemokine oligomerization in cell signaling and migration.Radiolytic mapping of solvent-contact surfaces in Photosystem II of higher plants: experimental identification of putative water channels within the photosystem.Structural Analysis of Human Cofilin 2/Filamentous Actin Assemblies: Atomic-Resolution Insights from Magic Angle Spinning NMR Spectroscopy.Painting proteins with covalent labels: what's in the picture?
P2860
Q24645230-0B403D5E-E2A9-408F-BE2B-2CF3C8EF5F2EQ24683589-22CB917F-81C8-407E-BDE8-907F64DD61DCQ27639578-3C209939-841F-4F9D-AF16-D504C8BB0E06Q27642591-72E35C6A-5843-4BC9-8DAF-D2BDD4E74850Q27651195-8F9A6C52-D33B-450D-B5FD-EE5B41D8AF14Q27653518-CE81D934-E76C-4D10-8B90-8460E8855CE3Q27668107-64C82CE0-2EE0-436E-B71A-EA0A41035B27Q27671565-8DC9C2A1-C606-4FBC-AA65-F0FACA3D985FQ30042138-D3CEA863-B4EA-41C7-B23B-595143487E3BQ30333455-FC9FA2E0-4213-4654-8F6B-11299F37EFD2Q30370483-3D1B76CC-BE4A-46FB-A1B8-8427434B6671Q30375367-97AF8864-D373-42A0-B0F3-D3A1C25F6496Q30384065-32ED1690-82C2-490C-83CB-588841A1C746Q30393257-96079B96-BAAA-4729-B184-24AAE044E479Q30493280-D78B525D-B8DA-4E7A-96B8-8739723C70C8Q30597713-31E77014-5DCE-49C9-8B79-E09EE6E425D8Q31110989-EBA9DB75-56B5-4D8D-AC9A-C8AA8F584249Q31137952-7533F812-6496-4FC0-AD17-A49093F2A367Q33360642-2663EFBE-C5F1-4651-81CD-A39DE91617ADQ33572511-5C5A6F1B-6C35-47E9-BF8D-7340C22C6840Q33657140-60759834-E0CE-4A4A-9483-DB485BFDB8E6Q33877002-2BA899E6-0689-4EA9-89FB-4A8BDC3607B2Q33966824-7D6DB1FF-88E5-40E7-9488-519FD100407FQ34061068-860C0C00-0A79-48D1-96E3-24026D6A3EA5Q34132743-C7C47397-9386-4562-B673-E1A7092F2851Q34639865-AA93D9E6-DF35-4A83-BFAE-B99512AC7FD3Q34731594-C43171C9-6BE1-4FCC-8AA9-E2D9F90A2736Q35226230-E15548CD-AB7B-4A99-B366-A2CD9007B97BQ35566451-2EC5007C-7519-4A94-978F-AE42E9C9604BQ35616418-847B2AAA-97B8-4DDC-8527-7DA467EBE6C0Q35626221-AF8657E6-D256-4B4D-9C07-1DCFACF43A66Q35728815-A8EA414E-22BB-443A-AD98-BF7D99DA1730Q35950122-1BF3361C-9E4E-4AD1-A78F-16105E4503C2Q37104130-75BDCA43-85EE-4BAC-AECD-0C155191AE3CQ37286388-C3A99BFA-7133-4897-A0E4-E1282FDE3895Q37542009-C05E1B2D-B140-417C-A0D8-AD865B8D7966Q37608845-3531F041-DAB8-458B-876F-C529857F3DFEQ37629791-B3C2AB76-8332-4512-A9E3-B30EBDBB4515Q37707893-678594FC-31AE-404A-8D14-240E7CED905FQ38451471-11C278B7-DD37-41F4-BA7F-962AD80DDC36
P2860
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@ast
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@en
type
label
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@ast
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@en
prefLabel
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@ast
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@en
P2093
P356
P1433
P1476
Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting.
@en
P2093
Jing-Qu Guan
Mark R Chance
Sergeui Vorobiev
Steven C Almo
P304
P356
10.1021/BI0121104
P407
P577
2002-05-01T00:00:00Z