Sort   by:  
 Page size 
UnknownSynthesis, crystal structure and antibacterial studies of dihydropyrimidines and their regioselectively oxidized products.
Not available
S-EPMC8694924 | biostudies-literature
UnknownHuman senataxin is a bona fide R-loop resolving enzyme and transcription termination factor.
Not available
S-EPMC10085699 | biostudies-literature
UnknownAssociation of CYP3A5*3, CYP3A4*18 & CYP2B6*6 polymorphisms with imatinib treatment outcome in Azerbaijani chronic myeloid leukaemia patients.
Not available
S-EPMC10645035 | biostudies-literature
UnknownDDX17 helicase promotes resolution of R-loop-mediated transcription-replication conflicts in human cells.
Not available
S-EPMC9757067 | biostudies-literature
ProteomicsDDX17 helicase promotes resolution of R-loop-mediated transcription-replication conflicts in human cells
R-loops are three-stranded nucleic acid structures composed of an RNA:DNA hybrid and displaced DNA strand. These structures can halt DNA replication when formed co- transcriptionally in the opposite orientation to replication fork progression. Recent studies have shown that replication forks stalled...
ORGANISM(S): Homo sapiens (Human) 
2022-11-02 | PXD034331 | Pride
Dna replication stress  r-loop  helicase  genomic instability  transcription 
UnknownRECQ4-MUS81 interaction contributes to telomere maintenance with implications to Rothmund-Thomson syndrome.
Not available
S-EPMC11791078 | biostudies-literature
ProteomicsSearching for binding partners of the SLX4 577-795 region and assessing the impact of the SLX4 D614G and L618P cancer patient-derived mutations on their association with SLX4
The project was aimed at identifying new binding partners of SLX4 that associate with a region spanning the conserved amphipathic helix of SLX4 and the downstream BTB domain. It was also aimed at assessing which of those partners might have their association with SLX4 abrogated by the cancer patient...
ORGANISM(S): Homo sapiens (Human) 
2020-03-05 | PXD012426 | Pride
Slx4 scaffold Protein-protein binding domain Cancer associated mutations Interactome 
ProteomicsSearching for new members of the SLX4 complex and for SLX4-complex members that are SUMOylated in vitro
The project was initially aimed at identifying new members of the SLX4 complex as well as members of the complex that are SUMOylated in vitro. The project was also aimed at assessing whether SUMOylation may change the compositon of the complex by reducing complex association of SUMOylated partners. ...
ORGANISM(S): Homo sapiens (Human) 
2020-03-05 | PXD012425 | Pride
Slx4 scaffold Protein sumoylation Interactome 
Sort   by:  
 Page size