Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry.
about
Structural mass spectrometry of proteins using hydroxyl radical based protein footprintingVisualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprintingDynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionMultiple proteases to localize oxidation sitesElectrospray-assisted modification of proteins: a radical probe of protein structure.Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry.Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry.Structural analysis of gelsolin using synchrotron protein footprinting.Improved identification and relative quantification of sites of peptide and protein oxidation for hydroxyl radical footprinting.Quantitative mapping of protein structure by hydroxyl radical footprinting-mediated structural mass spectrometry: a protection factor analysis.Using hydroxyl radical footprinting to explore the free energy landscape of protein folding.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.Structure and dynamics of protein waters revealed by radiolysis and mass spectrometryFast photochemical oxidation of proteins for comparing solvent-accessibility changes accompanying protein folding: data processing and application to barstarQuantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1.Controlling gas-phase reactions for efficient charge reduction electrospray mass spectrometry of intact proteins.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 SelectionOxidative protein labeling in mass-spectrometry-based proteomics.Sulfate radical anion as a new reagent for fast photochemical oxidation of proteins.Radiolysis of lac repressor by gamma-rays and heavy ions: a two-hit model for protein inactivation.Homology-modelled structure of the βB2B3-crystallin heterodimer studied by ion mobility and radical probe MS.Impact of limited oxidation on protein ion mobility and structure of importance to footprinting by radical probe mass spectrometry.Fast Fenton footprinting: a laboratory-based method for the time-resolved analysis of DNA, RNA and proteinsStructural NMR of protein oligomers using hybrid methods.Hydroxyl radical footprinting in vivo: mapping macromolecular structures with synchrotron radiation.A synchrotron-based hydroxyl radical footprinting analysis of amyloid fibrils and prefibrillar intermediates with residue-specific resolution.Studies of biomolecular conformations and conformational dynamics by mass spectrometry.Modeling of the DNA-binding site of yeast Pms1 by mass spectrometry.Reactivity and selectivity of charged phenyl radicals toward amino acids in a Fourier transform ion cyclotron resonance mass spectrometerAdvances in radical probe mass spectrometry for protein footprinting in chemical biology applications.Structural analysis of RNA in living cells by in vivo synchrotron X-ray footprinting.Fast photochemical oxidation of proteins for epitope mappingHigh structural resolution hydroxyl radical protein footprinting reveals an extended Robo1-heparin binding interface.Myosin binding surface on actin probed by hydroxyl radical footprinting and site-directed labelsDosimetry determines the initial OH radical concentration in fast photochemical oxidation of proteins (FPOP)
P2860
Q24635319-46614B41-E178-460E-8F44-E8D268474734Q24683589-BB18BB54-949B-4CEE-A3BB-82CCD1105F85Q26772129-B3D1536A-4967-4B65-B4C2-C2F4D6612F0FQ28544396-8108D9D8-D333-4E53-A61A-C2D53DD88401Q30323310-3AECE68D-44F7-448A-8991-A04FB92B6973Q30329157-65FFAED2-37CF-4B39-B55F-9E812369D7D1Q30329285-E898CB89-930C-4A9C-9B52-3E3C3E50D2CFQ30333455-0FF8FC2E-6348-4AA0-BA87-9575165439E3Q30353429-0C98B496-5F20-4A15-82AB-2AA18036A394Q30370483-ADC5CF65-85E3-4FC4-9A19-B2B3956D2736Q30372486-477A345A-3499-446D-93F5-9646AD9AC5FCQ30380117-DDF4C5E8-301F-4DC4-AA40-DCEA3EF8B45BQ30380151-07BE924E-D808-4557-87DB-56DB7F1FAD20Q30381158-DA5249DA-5A02-41F4-9677-0B67DC955F8FQ30384065-799CC090-7B13-43E7-9153-86110F517A05Q30393257-A10D6A5E-397A-41B6-A8E4-9E83E288456FQ30559588-6ACF8708-2A3A-4DA8-B95D-CCFB70598E71Q30597713-28CE4533-5369-40AF-9460-4DE3FDE2A157Q33360642-E06A35DF-9FAE-43F1-ACD6-D8A5ED4F1F3CQ33434078-10CD0CDB-66FB-40B9-8FC9-4CBC7C970F48Q33766071-6A9E12E9-5B34-4A8B-9F06-AFFD23EC2ED4Q33866908-D9DE8501-0641-4469-8FFF-3FB02B410929Q34026210-29324D4C-D056-4DBD-B545-61B0902C27EBQ34126967-D21466D5-2F84-46F5-9330-7680E4EBEA1FQ34177781-30DAE7AE-53C6-4E14-9AC1-670FFF49D5F2Q34208610-10542DC1-C2C9-4C80-A994-64AF2262168CQ34245065-CB896E1B-0118-4412-907E-08036237515FQ34499439-F68CBD01-C7A6-4E60-A5F6-0B39831C6E45Q34579372-BBE690B2-7E7E-412D-A037-29C426F257B5Q34595394-7BA524CF-5538-4526-ACF3-8BAAEEF21B4EQ34731594-503F100F-EE76-4C8C-AC15-1FF28A6C0F80Q34811742-B37E6208-6FE3-42A4-B14C-790D1F7E14A1Q34884364-3708BE19-83F1-44DE-9378-AEEAB08075D7Q35090521-EA8B06FF-01C8-45B4-B74F-B82EC182AFD8Q35109674-2BB8FB89-0600-4305-81AB-16E97B9933BDQ35131195-16B432A1-A943-41E1-B995-F3E7E6A5C699Q35349699-FB057636-2B51-4E1A-9D01-D38476BC16ADQ35536243-4C77108F-2F5C-41BB-ABAE-17375872491AQ35566451-B6D9DF25-9CB3-42D1-8C2C-6B99D3D749D0Q35567269-12C55D75-6BA3-4370-AABB-CE97831A6318
P2860
Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry.
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Millisecond radiolytic modific ...... entified by mass spectrometry.
@ast
Millisecond radiolytic modific ...... entified by mass spectrometry.
@en
type
label
Millisecond radiolytic modific ...... entified by mass spectrometry.
@ast
Millisecond radiolytic modific ...... entified by mass spectrometry.
@en
prefLabel
Millisecond radiolytic modific ...... entified by mass spectrometry.
@ast
Millisecond radiolytic modific ...... entified by mass spectrometry.
@en
P2093
P356
P1433
P1476
Millisecond radiolytic modific ...... entified by mass spectrometry.
@en
P2093
Brenowitz M
Maleknia SD
P304
P356
10.1021/AC990500E
P407
P577
1999-09-01T00:00:00Z