Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins.
about
Mechanism of mismatch recognition revealed by human MutSβ bound to unpaired DNA loopsFunctional studies and homology modeling of Msh2-Msh3 predict that mispair recognition involves DNA bending and strand separationInteraction between the Msh2 and Msh6 nucleotide-binding sites in the Saccharomyces cerevisiae Msh2-Msh6 complexDNA mismatch repair: molecular mechanism, cancer, and ageingPostreplicative mismatch repair.New insights into the mechanism of DNA mismatch repairDNA repair mechanisms and the bypass of DNA damage in Saccharomyces cerevisiaeA conserved MutS homolog connector domain interface interacts with MutL homologs.Nuclear reorganization of DNA mismatch repair proteins in response to DNA damage.Schizosaccharomyces pombe MutSα and MutLα Maintain Stability of Tetra-Nucleotide Repeats and Msh3 of Hepta-Nucleotide Repeats.Functional analysis of human mismatch repair gene mutations identifies weak alleles and polymorphisms capable of polygenic interactions.Probing DNA- and ATP-mediated conformational changes in the MutS family of mispair recognition proteins using deuterium exchange mass spectrometry.Msh6 protects mature B cells from lymphoma by preserving genomic stability.The nucleotide binding dynamics of human MSH2-MSH3 are lesion dependentDifferent roles of eukaryotic MutS and MutL complexes in repair of small insertion and deletion loops in yeast.Mlh2 is an accessory factor for DNA mismatch repair in Saccharomyces cerevisiae.Hijacking of the mismatch repair system to cause CAG expansion and cell death in neurodegenerative disease.Activation of Saccharomyces cerevisiae Mlh1-Pms1 Endonuclease in a Reconstituted Mismatch Repair System.Long-Range Signaling in MutS and MSH Homologs via Switching of Dynamic Communication PathwaysEngineered disulfide-forming amino acid substitutions interfere with a conformational change in the mismatch recognition complex Msh2-Msh6 required for mismatch repair.Dynamic DNA binding licenses a repair factor to bypass roadblocks in search of DNA lesions.Mispair-specific recruitment of the Mlh1-Pms1 complex identifies repair substrates of the Saccharomyces cerevisiae Msh2-Msh3 complex.Multiple factors insulate Msh2-Msh6 mismatch repair activity from defects in Msh2 domain I.Distinct requirements within the Msh3 nucleotide binding pocket for mismatch and double-strand break repair.
P2860
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P2860
Chimeric Saccharomyces cerevisiae Msh6 protein with an Msh3 mispair-binding domain combines properties of both proteins.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Chimeric Saccharomyces cerevis ...... s properties of both proteins.
@ast
Chimeric Saccharomyces cerevis ...... s properties of both proteins.
@en
type
label
Chimeric Saccharomyces cerevis ...... s properties of both proteins.
@ast
Chimeric Saccharomyces cerevis ...... s properties of both proteins.
@en
prefLabel
Chimeric Saccharomyces cerevis ...... s properties of both proteins.
@ast
Chimeric Saccharomyces cerevis ...... s properties of both proteins.
@en
P2860
P356
P1476
Chimeric Saccharomyces cerevis ...... es properties of both proteins
@en
P2093
Richard D Kolodner
Scarlet S Shell
P2860
P304
10956-10961
P356
10.1073/PNAS.0704148104
P407
P577
2007-06-15T00:00:00Z