| + |
MSH4 | form complex 
binding
|
MutSgamma meiotic recombination complex |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281104 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38348856 |
Msh4 and Msh5, collectively known as MutSγ, form a heterodimer that is structurally and functionally akin to the bacterial DNA mismatch repair factor MutS, which is characterised by its ring-like structure [118]. In vitro, studies demonstrate MutSγ’s preference for binding to double Holliday junctions (dHJs), though it generally exhibits high affinity for a variety of DNA repair intermediates [119,120]. This binding is believed to physically entrap two duplexes of double-stranded DNA, thereby stabilising the recombination intermediate. However, super-resolution microscopy data suggest that the Msh4/5 complex may only embrace one dsDNA in the recombination intermediate |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MSH5 | form complex
binding
|
MutSgamma meiotic recombination complex |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281105 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38348856 |
Msh4 and Msh5, collectively known as MutSγ, form a heterodimer that is structurally and functionally akin to the bacterial DNA mismatch repair factor MutS, which is characterised by its ring-like structure [118]. In vitro, studies demonstrate MutSγ’s preference for binding to double Holliday junctions (dHJs), though it generally exhibits high affinity for a variety of DNA repair intermediates [119,120]. This binding is believed to physically entrap two duplexes of double-stranded DNA, thereby stabilising the recombination intermediate. However, super-resolution microscopy data suggest that the Msh4/5 complex may only embrace one dsDNA in the recombination intermediate |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MutSgamma meiotic recombination complex | up-regulates 
|
Meiotic_recombination |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281106 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 38348856 |
Msh4 and Msh5, collectively known as MutSγ, form a heterodimer that is structurally and functionally akin to the bacterial DNA mismatch repair factor MutS, which is characterised by its ring-like structure [118]. In vitro, studies demonstrate MutSγ’s preference for binding to double Holliday junctions (dHJs), though it generally exhibits high affinity for a variety of DNA repair intermediates [119,120]. This binding is believed to physically entrap two duplexes of double-stranded DNA, thereby stabilising the recombination intermediate. However, super-resolution microscopy data suggest that the Msh4/5 complex may only embrace one dsDNA in the recombination intermediate |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
MutSgamma meiotic recombination complex
CPX-9881