Mass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA.
about
Interaction and colocalization of Rad9/Rad1/Hus1 checkpoint complex with replication protein A in human cellsInvestigation of stable and transient protein-protein interactions: Past, present, and futureMass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductaseProbing protein structure by amino acid-specific covalent labeling and mass spectrometry.Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites.Modulation of replication protein A function by its hyperphosphorylation-induced conformational change involving DNA binding domain B.Analysis of protein-protein interaction surfaces using a combination of efficient lysine acetylation and nanoLC-MALDI-MS/MS applied to the E9:Im9 bacteriotoxin--immunity protein complex.Structural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Quantifying protein interface footprinting by hydroxyl radical oxidation and molecular dynamics simulation: application to galectin-1.Mass spectrometry-based footprinting of protein-protein interactionsCheckpoint kinase ATR promotes nucleotide excision repair of UV-induced DNA damage via physical interaction with xeroderma pigmentosum group A.'Fixed charge' chemical derivatization and data dependant multistage tandem mass spectrometry for mapping protein surface residue accessibility.Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA bindingProtein modification by adenine propenalA new structural insight into XPA-DNA interactions.Mapping protein surface accessibility via an electron transfer dissociation selectively cleavable hydrazone probeDynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein.Probing conformational changes of human DNA polymerase lambda using mass spectrometry-based protein footprintingProgress and outlook in structural biology of large viral RNAs.Domain structure and DNA binding regions of beta protein from bacteriophage lambda.DNA-dependent conformational changes in the Ku heterodimer.High resolution footprinting of the hepatitis C virus polymerase NS5B in complex with RNA.
P2860
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P2860
Mass spectrometric identification of lysines involved in the interaction of human replication protein a with single-stranded DNA.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Mass spectrometric identificat ...... in a with single-stranded DNA.
@ast
Mass spectrometric identificat ...... in a with single-stranded DNA.
@en
type
label
Mass spectrometric identificat ...... in a with single-stranded DNA.
@ast
Mass spectrometric identificat ...... in a with single-stranded DNA.
@en
prefLabel
Mass spectrometric identificat ...... in a with single-stranded DNA.
@ast
Mass spectrometric identificat ...... in a with single-stranded DNA.
@en
P2093
P2860
P356
P1433
P1476
Mass spectrometric identificat ...... in a with single-stranded DNA.
@en
P2093
Sonja Hess
Steven M Shell
P2860
P304
P356
10.1021/BI048208A
P407
P577
2005-01-01T00:00:00Z