Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes.
about
Structural mass spectrometry of proteins using hydroxyl radical based protein footprintingHigh-resolution structure prediction and the crystallographic phase problemThe Use of Advanced Mass Spectrometry to Dissect the Life-Cycle of Photosystem IITopological mapping methods for α-helical bacterial membrane proteins--an update and a guideOxidized amino acid residues in the vicinity of Q(A) and Pheo(D1) of the photosystem II reaction center: putative generation sites of reducing-side reactive oxygen speciesProtein Structural Analysis via Mass Spectrometry-Based ProteomicsActivation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth.Mass spectrometry coupled experiments and protein structure modeling methods.Characterizing monoclonal antibody structure by carbodiimide/GEE footprintingQuantitative protein topography analysis and high-resolution structure prediction using hydroxyl radical labeling and tandem-ion mass spectrometry (MS)Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.Probing protein structure by amino acid-specific covalent labeling and mass spectrometry.Pulsed electron beam water radiolysis for submicrosecond hydroxyl radical protein footprintingAliphatic peptidyl hydroperoxides as a source of secondary oxidation in hydroxyl radical protein footprinting.Structural waters define a functional channel mediating activation of the GPCR, rhodopsin.Hydroxyl Radical Dosimetry for High Flux Hydroxyl Radical Protein Footprinting Applications Using a Simple Optical Detection Method.Integrated algorithms for high-throughput examination of covalently labeled biomolecules by structural mass spectrometry.Visualizing water molecules in transmembrane proteins using radiolytic labeling methods.Future directions of structural mass spectrometry using hydroxyl radical footprinting.Structural analysis of a highly glycosylated and unliganded gp120-based antigen using mass spectrometry.Protein Footprinting Comes of Age: Mass Spectrometry for Biophysical Structure Assessment.Mass spectrometry-based carboxyl footprinting of proteins: method evaluation.Structure and dynamics of protein waters revealed by radiolysis and mass spectrometryComparative informatics analysis to evaluate site-specific protein oxidation in multidimensional LC-MS/MS dataThree-dimensional structure of cofilin bound to monomeric actin derived by structural mass spectrometry data.Synchrotron X-ray footprinting as a method to visualize water in proteins.Modeling of protein binary complexes using structural mass spectrometry data.Radiation-induced oxidative damage to the DNA-binding domain of the lactose repressor.Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1.Multiple glycosaminoglycan-binding epitopes of monocyte chemoattractant protein-3/CCL7 enable it to function as a non-oligomerizing chemokine.Conformational changes in guanylate cyclase-activating protein 1 induced by Ca2+ and N-terminal fatty acid acylation.Structural characterization of semen coagulum-derived SEM1(86-107) amyloid fibrils that enhance HIV-1 infection.Fast photochemical oxidation of proteins for comparing structures of protein-ligand complexes: the calmodulin-peptide model system.Quantitative Protein Topography Measurements by High Resolution Hydroxyl Radical Protein Footprinting Enable Accurate Molecular Model SelectionMass spectrometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification?Oxidative protein labeling in mass-spectrometry-based proteomics.The ClpP N-terminus coordinates substrate access with protease active site reactivity.Visualizing the kinetic power stroke that drives proton-coupled zinc(II) transportImpact of limited oxidation on protein ion mobility and structure of importance to footprinting by radical probe mass spectrometry.Fast photochemical oxidation of proteins and mass spectrometry follow submillisecond protein folding at the amino-acid level.
P2860
Q24635319-17C069C0-F21A-43CC-8D94-2BDB51D0AD54Q24646937-6B51D092-BE84-4E00-A2CD-CD115B357B82Q26744607-D328FFD5-C495-4CA1-9F76-C47534A08863Q26863116-71F72F5F-4378-47F2-AAF9-77905F47ED75Q28487238-E0E9E822-60CA-4E73-A2BE-F750F274FD1BQ28818005-FA388E36-D346-4368-8B93-981B38B409B2Q30252408-E114ADD3-8757-4AA6-B433-D0DDAEB60FADQ30354609-57A120A2-9445-43CA-A89E-0CD2E1036A11Q30369478-4D62BDBB-33EE-4302-9A0F-20D9FA445953Q30371810-8BA39AA2-F543-42B1-A574-00BCB41B40C7Q30372486-7CB1C5B2-F345-4352-B957-99FA814A4931Q30373368-84AD77F5-F395-463E-9624-CD5C6D6C91DBQ30375367-BFCA753B-AFCE-45A4-9EA8-C3E1F55941F1Q30375486-07C38AA4-83D0-456F-BAFE-85463CC1E00BQ30380117-7BEC3E58-F3F4-43F4-A6B8-E18C09DAE8A7Q30380151-9B41249F-E307-403F-8E1B-8932E0587E15Q30381158-503FFEAB-65AC-4B95-BABE-DD70BF437D34Q30384065-94683CDF-8AAF-4D04-AC14-FD456BCCADAEQ30393257-8A25D882-2C27-4649-8B9C-B174BC473C2DQ30393415-02D177EC-6C9C-46E5-9C5F-6F51AE952047Q30399662-7691D251-2C88-4C8E-97B5-AF08354A8B3AQ30414169-A221D3D1-E9D6-454B-A29E-3424242CEDA9Q30559588-8F79F466-F420-4A8C-9324-42E1F41A56C8Q30653444-E4992792-947B-4F7F-AEDE-21470CAF1A36Q31110989-CBCE1AEE-E6F7-4C9E-A48D-4F322DEA8393Q31125696-2BF64878-CF7D-49DD-9A4F-59E01B103E32Q31137952-AEC3BDFA-98FB-41E0-8CE5-E37241DC0B02Q33270937-6F02FFF6-E460-413E-A2AB-B231E4B6ACBEQ33360642-A88CB0AB-4F87-4BF7-A1C1-19D0EB821F4CQ33652172-D5FB61FA-4C19-4613-A50A-3215B91FBC6FQ33657140-E3132D0A-23DC-4E57-A11A-303C8CD46D15Q33689504-497CB09E-5A81-45D9-B846-ECFF7EFCE4CDQ33766071-B06D9E37-A358-4480-9AFC-6E199BB23FD6Q33866908-A630F78D-4E5A-470F-90AB-E5CC7BF3CB3BQ33976657-9D874E2A-7E5B-477A-9149-DE4BB3066AA1Q34026210-55948E68-7B21-4131-81EB-8AB8AA8037B8Q34061068-59B16CD5-10CF-4C3C-8633-644CD8580903Q34087059-DC719872-5E88-431D-8268-B2D79D5D0F04Q34245065-33AA34BA-AD61-4829-8BE7-E18CF31EBE3DQ34449755-F1F54B4C-21E1-4988-819A-D5E5514AAC01
P2860
Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Radiolytic protein footprintin ...... e of macromolecular complexes.
@ast
Radiolytic protein footprintin ...... e of macromolecular complexes.
@en
type
label
Radiolytic protein footprintin ...... e of macromolecular complexes.
@ast
Radiolytic protein footprintin ...... e of macromolecular complexes.
@en
prefLabel
Radiolytic protein footprintin ...... e of macromolecular complexes.
@ast
Radiolytic protein footprintin ...... e of macromolecular complexes.
@en
P1476
Radiolytic protein footprintin ...... e of macromolecular complexes.
@en
P2093
Keiji Takamoto
Mark R Chance
P304
P356
10.1146/ANNUREV.BIOPHYS.35.040405.102050
P577
2006-01-01T00:00:00Z