Succinylome analysis reveals the involvement of lysine succinylation in the extreme resistance of Deinococcus radiodurans
10.1002/pmic.201900158 · doi-reference
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans
10.1038/s41467-019-09153-6 · doi-reference
10.1016/j.biocel.2013.08.011
10.1016/j.biocel.2013.08.011 · doi-reference
10.1016/j.cell.2013.02.037
10.1016/j.cell.2013.02.037 · doi-reference
10.1016/j.str.2017.06.004
10.1016/j.str.2017.06.004 · doi-reference
Structural and functional studies of MutS2 from Deinococcus radiodurans
10.1016/j.dnarep.2014.04.012 · doi-reference
Deinococcus radiodurans DR2231 is a two-metal-ion mechanism hydrolase with exclusive activity on dUTP
10.1111/febs.13923 · doi-reference
Structures and activities of widely conserved small prokaryotic aminopeptidases-P clarify classification of M24B peptidases
10.1002/prot.25641 · doi-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 · doi-reference
A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs
10.1016/s0969-2126(01)00613-x · doi-reference
10.1074/jbc.m809342200
10.1074/jbc.m809342200 · doi-reference
10.1016/j.bbrc.2019.03.209
10.1016/j.bbrc.2019.03.209 · doi-reference
10.1038/sj.emboj.7601760
10.1038/sj.emboj.7601760 · doi-reference
10.1038/sj.emboj.7600222
10.1038/sj.emboj.7600222 · doi-reference
10.1038/sj.emboj.7600582
10.1038/sj.emboj.7600582 · doi-reference
10.1016/j.str.2004.08.006
10.1016/j.str.2004.08.006 · doi-reference
10.1074/jbc.m111.247999
10.1074/jbc.m111.247999 · doi-reference
10.1093/nar/gkv444
10.1093/nar/gkv444 · doi-reference
10.1038/nsmb754
10.1038/nsmb754 · doi-reference
10.1074/jbc.r116.742494
10.1074/jbc.r116.742494 · doi-reference
Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter
10.7554/elife.41124 · doi-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 · doi-reference
10.1016/j.jmb.2006.11.032
10.1016/j.jmb.2006.11.032 · doi-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 · doi-reference
10.1016/j.jmb.2006.06.010
10.1016/j.jmb.2006.06.010 · doi-reference
10.1016/j.bbapap.2014.09.022
10.1016/j.bbapap.2014.09.022 · doi-reference
Cryo-trapping the six-coordinate, distorted-octahedral active site of manganese superoxide dismutase
10.1006/jmbi.1999.3506 · doi-reference
drFrnE represents a hitherto unknown class of eubacterial cytoplasmic disulfide oxido-reductases
10.1089/ars.2016.6960 · doi-reference
Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms
10.1107/s1744309106008402 · doi-reference
10.1111/febs.12895
10.1111/febs.12895 · doi-reference
Crystal structure of the IrrE protein, a central regulator of DNA damage repair in deinococcaceae
10.1016/j.jmb.2008.12.062 · doi-reference
10.1016/s0006-291x(03)00965-3
10.1016/s0006-291x(03)00965-3 · doi-reference
10.1096/fj.201801506r
10.1096/fj.201801506r · doi-reference
10.1139/o10-075
10.1139/o10-075 · doi-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 · doi-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 · doi-reference
Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage
10.1073/pnas.0401331101 · doi-reference
Mechanism for accurate, protein-assisted DNA annealing by Deinococcus radiodurans DdrB
10.1073/pnas.1520847113 · doi-reference
10.1093/nar/gkt759
10.1093/nar/gkt759 · doi-reference
10.1093/nar/gkq036
10.1093/nar/gkq036 · doi-reference
