Contact and support
Need help, have a question, or want to contact the ResearchHub team?
© 2026 ResearchHub. Built for responsible scholarly connection.
Research graph
References from Structure, function and evolution of the bacterial DinG-like proteins. Local targets link to admitted publications; unresolved targets remain external evidence.
Structure, function and evolution of the XPD family of iron-sulfur-containing 5′-> 3′ DNA helicases
10.1042/bst0370547 · 2009 · External reference
10.1016/j.cell.2008.04.029
10.1016/j.cell.2008.04.029 · External reference
Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD
10.1371/journal.pbio.0060149 · 2008 · External reference
10.1038/emboj.2011.374
10.1038/emboj.2011.374 · External reference
10.1016/j.cell.2008.04.030
10.1016/j.cell.2008.04.030 · External reference
10.1002/mlf2.12137
10.1002/mlf2.12137 · External reference
10.1128/jb.174.10.3377-3385.1992
10.1128/jb.174.10.3377-3385.1992 · External reference
10.1128/jb.183.19.5496-5505.2001
10.1128/jb.183.19.5496-5505.2001 · External reference
The DinG protein from Escherichia coli is a structure-specific helicase
10.1074/jbc.m700376200 · 2007 · External reference
10.1093/genetics/158.1.41
10.1093/genetics/158.1.41 · External reference
Genetic Analysis of DinG Family Helicase YoaA and Its Interaction with Replication Clamp Loader Protein HolC in Escherichia coli
10.1128/jb.00228-21 · 2021 · External reference
10.1016/j.dnarep.2020.103006
10.1016/j.dnarep.2020.103006 · External reference
Characterization of the Escherichia coli XPD/Rad3 iron-sulfur helicase YoaA in complex with the DNA polymerase III clamp loader subunit chi (χ)
10.1016/j.jbc.2022.102786 · 2023 · External reference
10.1016/j.molcel.2023.05.036
10.1016/j.molcel.2023.05.036 · External reference
CasDinG is a 5′-3′ dsDNA and RNA/DNA helicase with three accessory domains essential for type IV CRISPR immunity
10.1093/nar/gkad546 · 2023 · External reference
10.1126/science.adi1910
10.1126/science.adi1910 · External reference
DNA translocation mechanism of an XPD family helicase
10.7554/elife.42400 · 2018 · External reference
10.1038/s41586-024-07487-w
10.1038/s41586-024-07487-w · External reference
10.1093/nar/gkac963
10.1093/nar/gkac963 · External reference
10.1093/nar/gkae241
10.1093/nar/gkae241 · External reference
10.1093/nar/gkad359
10.1093/nar/gkad359 · External reference
10.1146/annurev.biochem.74.082803.133518
10.1146/annurev.biochem.74.082803.133518 · External reference
10.1128/jb.00807-06
10.1128/jb.00807-06 · External reference
10.1074/jbc.m301188200
10.1074/jbc.m301188200 · External reference
10.1371/journal.pgen.1005651
10.1371/journal.pgen.1005651 · External reference
10.1038/emboj.2009.308
10.1038/emboj.2009.308 · External reference
10.1371/journal.pone.0187900
10.1371/journal.pone.0187900 · External reference
Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster
10.1074/jbc.m807943200 · 2009 · External reference
Mycobacterium tuberculosis DinG is a structure-specific helicase that unwinds G4 DNA: implications for targeting G4 DNA as a novel therapeutic approach
10.1074/jbc.m114.563569 · 2014 · External reference
10.1074/jbc.m113.496463
10.1074/jbc.m113.496463 · External reference
Stimulation of Escherichia coli DNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB
10.1016/j.febslet.2012.09.032 · 2012 · External reference
10.1021/ja501973c
10.1021/ja501973c · External reference
10.1080/10409230802341296
10.1080/10409230802341296 · External reference
Systematic identification of synthetic lethal mutations with reduced-genome Escherichia coli: synthetic genetic interactions among yoaA, xthA and holC related to survival from MMS exposure
10.1266/ggs.15-00068 · 2016 · External reference
10.1038/emboj.2011.305
10.1038/emboj.2011.305 · External reference
10.1098/rstb.2018.0087
10.1098/rstb.2018.0087 · External reference
Positioning diverse Type IV structures and functions within Class 1 CRISPR-Cas Systems
10.3389/fmicb.2021.671522 · 2021 · External reference
10.1038/s41564-022-01229-2
10.1038/s41564-022-01229-2 · External reference
10.1089/crispr.2019.0048
10.1089/crispr.2019.0048 · External reference
The N-terminal domain of Type IV-A1 CRISPR-associated DinG is vulnerable to proteolysis
2024 · External reference
10.1016/j.tibs.2020.07.002
10.1016/j.tibs.2020.07.002 · External reference
10.1002/pro.4519
10.1002/pro.4519 · External reference
10.1126/science.abq7220
10.1126/science.abq7220 · External reference
Activity and structure of EcoKMcrA
10.1093/nar/gky731 · 2018 · External reference
10.1016/j.molcel.2024.06.033
10.1016/j.molcel.2024.06.033 · External reference
10.1093/nar/gkx924
10.1093/nar/gkx924 · External reference
10.1128/jb.01464-06
10.1128/jb.01464-06 · External reference
Genetic composition of the Bacillus subtilis SOS system
10.1128/jb.187.22.7655-7666.2005 · 2005 · External reference
Staphylococcus aureus DinG, a helicase that has evolved into a nuclease
10.1042/bj20111903 · 2012 · External reference
10.1017/s0033583510000181
10.1017/s0033583510000181 · External reference
10.1093/nar/gkt278
10.1093/nar/gkt278 · External reference
How an exonuclease decides where to stop in trimming of nucleic acids: crystal structures of RNase T-product complexes
10.1093/nar/gks548 · 2012 · External reference
10.1002/pro.4374
10.1002/pro.4374 · External reference
10.1038/nsmb.3348
10.1038/nsmb.3348 · External reference
10.1073/pnas.95.21.12562
10.1073/pnas.95.21.12562 · External reference
Structural characterization of NrnC identifies unifying features of dinucleotidases
10.7554/elife.70146 · 2021 · External reference
10.1073/pnas.2018156117
10.1073/pnas.2018156117 · External reference
10.1093/nar/gks382
10.1093/nar/gks382 · External reference
10.1016/j.str.2009.03.008
10.1016/j.str.2009.03.008 · External reference
10.1016/j.molcel.2021.05.027
10.1016/j.molcel.2021.05.027 · External reference
10.1038/s41586-021-03951-z
10.1038/s41586-021-03951-z · External reference
10.1038/nature13037
10.1038/nature13037 · External reference
The iron-sulphur cluster in human DNA2 is required for all biochemical activities of DNA2
10.1038/s42003-020-1048-4 · 2020 · External reference
10.1074/jbc.m808526200
10.1074/jbc.m808526200 · External reference
Insights into Chi recognition from the structure of an AddAB-type helicase-nuclease complex
10.1038/emboj.2012.9 · 2012 · External reference
10.1128/jb.00425-08
10.1128/jb.00425-08 · External reference
10.1016/j.str.2017.04.002
10.1016/j.str.2017.04.002 · External reference
Rpn11-mediated ubiquitin processing in an ancestral archaeal ubiquitination system
10.1038/s41467-018-05198-1 · 2018 · External reference
10.1093/nar/gks741
10.1093/nar/gks741 · External reference
10.1093/nar/gkx547
10.1093/nar/gkx547 · External reference
10.1002/prot.24754
10.1002/prot.24754 · External reference
10.1016/j.tig.2003.08.005
10.1016/j.tig.2003.08.005 · External reference
10.1093/nar/gkw102
10.1093/nar/gkw102 · External reference
Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins
10.1007/s00018-008-8580-6 · 2009 · External reference
10.1016/j.cell.2008.08.016
10.1016/j.cell.2008.08.016 · External reference
10.1534/genetics.166.1.33
10.1534/genetics.166.1.33 · External reference