Research graph
References from Structural features and functional implications of proteins enabling the robustness of Deinococcus radiodurans. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1093/femsre/fuy037
10.1093/femsre/fuy037 · External reference
Deinococcus geothermalis sp. nov. and Deinococcus murrayi sp. nov., two extremely radiation-resistant and slightly thermophilic species from hot springs
10.1099/00207713-47-4-939 · 1997 · External reference
10.1099/ijs.0.63717-0
10.1099/ijs.0.63717-0 · External reference
10.4056/sigs.2756060
10.4056/sigs.2756060 · External reference
10.1016/j.dnarep.2011.10.024
10.1016/j.dnarep.2011.10.024 · External reference
10.1016/j.csbj.2016.04.001
10.1016/j.csbj.2016.04.001 · External reference
The diversity and commonalities of the radiation-resistance mechanisms of Deinococcus and its up-to-date applications
10.1186/s13568-019-0862-x · 2019 · External reference
10.1016/j.resmic.2019.11.002
10.1016/j.resmic.2019.11.002 · External reference
In vivo damage and recA-dependent repair of plasmid and chromosomal DNA in the radiation-resistant bacterium Deinococcus radiodurans
10.1128/jb.176.12.3508-3517.1994 · 1994 · External reference
10.1016/j.cell.2009.01.018
10.1016/j.cell.2009.01.018 · External reference
Single-strand gap repair involves both RecF and RecBCD pathways
10.1007/s00294-016-0575-5 · 2016 · External reference
10.1371/journal.pgen.1000774
10.1371/journal.pgen.1000774 · External reference
10.1128/jb.01851-07
10.1128/jb.01851-07 · External reference
10.1073/pnas.1420009111
10.1073/pnas.1420009111 · External reference
Structural basis for DNA 5 -end resection by RecJ
10.7554/elife.14294 · 2016 · External reference
Radioresistance of Deinococcus radiodurans: functions necessary to survive ionizing radiation are also necessary to survive prolonged desiccation
10.1128/jb.178.3.633-637.1996 · 1996 · External reference
10.1534/genetics.104.029249
10.1534/genetics.104.029249 · External reference
Deinococcus geothermalis: the pool of extreme radiation resistance genes shrinks
10.1371/journal.pone.0000955 · 2007 · External reference
Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus
10.1093/nar/gkz883 · 2019 · External reference
Structure and DNA damage-dependent derepression mechanism for the XRE family member DG-DdrO
10.1093/nar/gkz720 · 2019 · External reference
10.1111/mmi.12774
10.1111/mmi.12774 · External reference
10.1371/journal.pone.0122071
10.1371/journal.pone.0122071 · External reference
10.1093/molbev/msv119
10.1093/molbev/msv119 · External reference
10.1093/molbev/msy134
10.1093/molbev/msy134 · External reference
Biology of extreme radiation resistance: the way of Deinococcus radiodurans
2013 · External reference
10.1128/mmbr.00015-10
10.1128/mmbr.00015-10 · External reference
10.1128/jb.01046-09
10.1128/jb.01046-09 · External reference
10.1042/bj20120902
10.1042/bj20120902 · External reference
The three catalases in Deinococcus radiodurans: only two show catalase activity
10.1016/j.bbrc.2015.12.017 · 2016 · External reference
Gamma radiation-induced proteome of Deinococcus radiodurans primarily targets DNA repair and oxidative stress alleviation
10.1074/mcp.m111.011734 · 2012 · External reference
10.1371/journal.pone.0012570
10.1371/journal.pone.0012570 · External reference
10.1016/j.tim.2010.07.007
10.1016/j.tim.2010.07.007 · External reference
The novel ncRNA OsiR positively regulates expression of katE2 and is required for oxidative stress tolerance in Deinococcus radiodurans
2020 · External reference
Transcriptional analysis of Deinococcus radiodurans reveals novel small RNAs that are differentially expressed under ionizing radiation
2015 · External reference
A genome-wide search for ionizing-radiation-responsive elements in Deinococcus radiodurans reveals a regulatory role for the DNA gyrase subunit A gene's 5' untranslated region in the radiation and desiccation response
10.1128/aem.00039-17 · 2017 · External reference
10.1126/science.1103185
10.1126/science.1103185 · External reference
10.1080/10409230802122274
10.1080/10409230802122274 · External reference
10.1093/nar/gkn143
10.1093/nar/gkn143 · External reference
10.1074/jbc.m113.502112
10.1074/jbc.m113.502112 · External reference
Crystal structure of Deinococcus radiodurans RecQ helicase catalytic core domain: the interdomain flexibility
2014 · External reference
Structural and mechanistic insight into DNA unwinding by Deinococcus radiodurans UvrD
10.1371/journal.pone.0077364 · 2013 · External reference
10.1371/journal.pbio.0020304
10.1371/journal.pbio.0020304 · External reference
DdrB stimulates single-stranded DNA annealing and facilitates RecA-independent DNA repair in Deinococcus radiodurans
10.1016/j.dnarep.2010.04.006 · 2010 · External reference
10.1111/j.1365-2958.2004.04272.x
10.1111/j.1365-2958.2004.04272.x · External reference
Complex oligomeric structure of a truncated form of DdrA: a protein required for the extreme radiotolerance of Deinococcus
10.1016/j.bbapap.2008.03.009 · 2008 · External reference
10.1074/jbc.m109.010454
10.1074/jbc.m109.010454 · External reference
The deinococcal DdrB protein is involved in an early step of DNA double strand break repair and in plasmid transformation through its single-strand annealing activity
10.1016/j.dnarep.2011.09.010 · 2011 · External reference
10.1093/nar/gkq036
10.1093/nar/gkq036 · External reference
10.1093/nar/gkt759
10.1093/nar/gkt759 · External reference
Mechanism for accurate, protein-assisted DNA annealing by Deinococcus radiodurans DdrB
10.1073/pnas.1520847113 · 2016 · External reference
Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage
10.1073/pnas.0401331101 · 2004 · External reference
A common core for binding single-stranded DNA: structural comparison of the single-stranded DNA-binding proteins (SSB) from E. coli and human mitochondria
10.1016/s0014-5793(97)00747-3 · 1997 · External reference
PprA protein is involved in chromosome segregation via its physical and functional interaction with DNA gyrase in irradiated Deinococcus radiodurans bacteria
10.1128/msphere.00036-15 · 2016 · External reference
10.1139/o10-075
10.1139/o10-075 · External reference
10.1096/fj.201801506r
10.1096/fj.201801506r · External reference
10.1016/s0006-291x(03)00965-3
10.1016/s0006-291x(03)00965-3 · External reference
Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae
10.1016/j.jmb.2008.12.062 · 2009 · External reference
10.1111/febs.12895
10.1111/febs.12895 · External reference
Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms
10.1107/s1744309106008402 · 2006 · External reference
drFrnE represents a hitherto unknown class of eubacterial cytoplasmic disulfide oxido-reductases
10.1089/ars.2016.6960 · 2018 · External reference
10.1371/journal.pone.0189261
10.1371/journal.pone.0189261 · External reference
Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase
10.1006/jmbi.1999.3506 · 2000 · External reference
10.1016/j.bbapap.2014.09.022
10.1016/j.bbapap.2014.09.022 · External reference
Structure, function, and mechanism of thioredoxin proteins, antioxid redox
2010 · External reference
10.1016/j.jmb.2006.06.010
10.1016/j.jmb.2006.06.010 · External reference
The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus
10.1007/s00775-006-0142-5 · 2006 · External reference
10.1016/j.jmb.2006.11.032
10.1016/j.jmb.2006.11.032 · External reference
SAXS structural studies of Dps from Deinococcus radiodurans highlights the conformation of the mobile N-terminal extensions
10.1016/j.jmb.2017.01.008 · 2017 · External reference
Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter
10.7554/elife.41124 · 2019 · External reference
10.1074/jbc.r116.742494
10.1074/jbc.r116.742494 · External reference
10.1038/nsmb754
10.1038/nsmb754 · External reference
10.1093/nar/gkv444
10.1093/nar/gkv444 · External reference
10.1074/jbc.m111.247999
10.1074/jbc.m111.247999 · External reference
10.1016/j.str.2004.08.006
10.1016/j.str.2004.08.006 · External reference
10.1038/sj.emboj.7600582
10.1038/sj.emboj.7600582 · External reference
10.1038/sj.emboj.7600222
10.1038/sj.emboj.7600222 · External reference
10.1038/sj.emboj.7601760
10.1038/sj.emboj.7601760 · External reference
10.1016/j.bbrc.2019.03.209
10.1016/j.bbrc.2019.03.209 · External reference
10.1074/jbc.m809342200
10.1074/jbc.m809342200 · External reference
A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs
10.1016/s0969-2126(01)00613-x · 2001 · External reference
Two-domain aminopeptidase of M1 family: structural features for substrate binding and gating in absence of C-terminal domain
10.1016/j.jsb.2019.07.010 · 2019 · External reference
Structures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidases
10.1002/prot.25641 · 2019 · External reference
Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP
10.1111/febs.13923 · 2016 · External reference
Structural and functional studies of MutS2 from Deinococcus radiodurans
10.1016/j.dnarep.2014.04.012 · 2014 · External reference
10.1016/j.str.2017.06.004
10.1016/j.str.2017.06.004 · External reference
10.1016/j.cell.2013.02.037
10.1016/j.cell.2013.02.037 · External reference
10.1016/j.biocel.2013.08.011
10.1016/j.biocel.2013.08.011 · External reference
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans
10.1038/s41467-019-09153-6 · 2019 · External reference
Succinylome analysis reveals the involvement of lysine succinylation in the extreme resistance of Deinococcus radiodurans
10.1002/pmic.201900158 · 2019 · External reference
