Mapping protein-protein interactions between MutL and MutH by cross-linking.
about
Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase.Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.Identifying an interaction site between MutH and the C-terminal domain of MutL by crosslinking, affinity purification, chemical coding and mass spectrometry.Human MutLalpha: the jack of all trades in MMR is also an endonuclease.Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteineCYP2C8 exists as a dimer in natural membranes.Mutations in the MutSalpha interaction interface of MLH1 can abolish DNA mismatch repair.Development of enhanced capacity affinity microcolumns by using a hybrid of protein cross-linking/modification and immobilizationElucidating the higher-order structure of biopolymers by structural probing and mass spectrometry: MS3DAtomic force microscopy captures the initiation of methyl-directed DNA mismatch repair.The sliding clamp tethers the endonuclease domain of MutL to DNAModern aspects of the structural and functional organization of the DNA mismatch repair system.Catch me if you can: challenges and applications of cross-linking approaches.Developments and recent advancements in the field of endogenous amino acid selective bond forming reactions for bioconjugation.Structural and functional analysis of the MutS C-terminal tetramerization domain.Predicting Protein-Protein Interactions Using BiGGER: Case Studies.Covalent capture of phospho-dependent protein oligomerization by site-specific incorporation of a diazirine photo-cross-linker.Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNAMutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA.Physical and functional interactions between Escherichia coli MutL and the Vsr repair endonuclease.Pseudomonas aeruginosa MutL protein functions in Escherichia coli.The DNA binding activity of MutL is required for methyl-directed mismatch repair in Escherichia coli.Maltose binding protein (MalE) interacts with periplasmic loops P2 and P1 respectively of the MalFG subunits of the maltose ATP binding cassette transporter (MalFGK(2)) from Escherichia coli/Salmonella during the transport cycle.Interdomain conformational changes in Akt activation revealed by chemical cross-linking and tandem mass spectrometry.A Hinged Signal Peptide Hairpin Enables Tat-Dependent Protein Translocation.
P2860
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P2860
Mapping protein-protein interactions between MutL and MutH by cross-linking.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@en
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@nl
type
label
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@en
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@nl
prefLabel
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@en
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@nl
P2093
P2860
P356
P1476
Mapping protein-protein interactions between MutL and MutH by cross-linking.
@en
P2093
Bernhard Spengler
Dieter Kirsch
Luis Giron-Monzon
Peter Friedhoff
Robert Ahrends
P2860
P304
49338-49345
P356
10.1074/JBC.M409307200
P407
P577
2004-09-14T00:00:00Z