Research graph
References from Unveiling the versatility of the thioredoxin framework: Insights from the structural examination of Francisella tularensis DsbA1. Local targets link to admitted publications; unresolved targets remain external evidence.
Structure, catalytic mechanism, and evolution of the glutathione transferases
10.1021/tx960072x · 1997 · External reference
10.1371/journal.pcbi.1000541
10.1371/journal.pcbi.1000541 · External reference
10.1073/pnas.181342398
10.1073/pnas.181342398 · External reference
A pathway for disulfide bond formation in vivo
10.1073/pnas.90.3.1038 · 1993 · External reference
10.1016/0092-8674(91)90532-4
10.1016/0092-8674(91)90532-4 · External reference
The Eps1p protein disulfide isomerase conserves classic thioredoxin superfamily amino acid motifs but not their functional geometries
10.1371/journal.pone.0113431 · 2014 · External reference
Unresolved reference
2016 · External reference
10.1128/jb.185.3.991-1000.2003
10.1128/jb.185.3.991-1000.2003 · External reference
Unresolved reference
External reference
Unresolved reference
External reference
10.1107/s0907444909042073
10.1107/s0907444909042073 · External reference
Unresolved reference
External reference
Tularemia as a biological weapon: medical and public health management
10.1001/jama.285.21.2763 · 2001 · External reference
10.1073/pnas.0804621105
10.1073/pnas.0804621105 · External reference
10.1107/s0907444910007493
10.1107/s0907444910007493 · External reference
The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
10.1111/j.1432-1033.1983.tb07429.x · 1983 · External reference
10.1007/978-1-59745-196-3_7
10.1007/978-1-59745-196-3_7 · External reference
10.1107/s090744491003982x
10.1107/s090744491003982x · External reference
A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
10.1038/ncomms16065 · 2017 · External reference
Breaking antimicrobial resistance by disrupting extracytoplasmic protein folding
10.7554/elife.57974 · 2022 · External reference
Crystal structures of reduced and oxidized DsbA: investigation of domain motion and thiolate stabilization
10.1016/s0969-2126(98)00077-x · 1998 · External reference
10.1002/pro.5560060910
10.1002/pro.5560060910 · External reference
10.1073/pnas.0402769101
10.1073/pnas.0402769101 · External reference
10.1038/nrmicro2087
10.1038/nrmicro2087 · External reference
10.1074/jbc.m110.101360
10.1074/jbc.m110.101360 · External reference
10.1073/pnas.1311592111
10.1073/pnas.1311592111 · External reference
Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product
10.1073/pnas.96.22.12333 · 1999 · External reference
10.1128/jb.01896-05
10.1128/jb.01896-05 · External reference
10.1002/pro.4519
10.1002/pro.4519 · External reference
10.1016/s0021-9258(19)83562-7
10.1016/s0021-9258(19)83562-7 · External reference
A single dipeptide sequence modulates the redox properties of a whole enzyme family
10.1016/s1359-0278(98)00024-8 · 1998 · External reference
PROMOTIF—A program to identify and analyze structural motifs in proteins
10.1002/pro.5560050204 · 1996 · External reference
Disulfide bond formation system in escherichia coli
10.1093/jb/mvp102 · 2009 · External reference
10.1016/j.cell.2006.10.034
10.1016/j.cell.2006.10.034 · External reference
PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA
10.1073/pnas.91.24.11552 · 1994 · External reference
10.1038/s41586-021-03819-2
10.1038/s41586-021-03819-2 · External reference
10.1107/s0907444909047374
10.1107/s0907444909047374 · External reference
10.1126/science.1091724
10.1126/science.1091724 · External reference
10.1016/0022-2836(90)90313-b
10.1016/0022-2836(90)90313-b · External reference
Comparative sequence, structure and redox analyses of Klebsiella pneumoniae DsbA show that anti-virulence target DsbA enzymes fall into distinct classes
10.1371/journal.pone.0080210 · 2013 · External reference
10.1089/ars.2008.2420
10.1089/ars.2008.2420 · External reference
10.1016/j.jmb.2009.07.056
10.1016/j.jmb.2009.07.056 · External reference
10.1038/s41564-017-0106-2
10.1038/s41564-017-0106-2 · External reference
10.1110/ps.0207702
10.1110/ps.0207702 · External reference
10.1021/ja047300r
10.1021/ja047300r · External reference
10.1074/jbc.m111.224865
10.1074/jbc.m111.224865 · External reference
10.1089/ars.2007.9.25
10.1089/ars.2007.9.25 · External reference
DOLOP- database of bacterial lipoproteins
10.1093/bioinformatics/18.4.641 · 2002 · External reference
Thioredoxin--a fold for all reasons
10.1016/s0969-2126(01)00154-x · 1995 · External reference
10.1038/365464a0
10.1038/365464a0 · External reference
10.1016/s0969-2126(01)00672-4
10.1016/s0969-2126(01)00672-4 · External reference
10.1016/0022-2836(68)90205-2
10.1016/0022-2836(68)90205-2 · External reference
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
10.1038/73295 · 2000 · External reference
10.1016/j.bbapap.2014.01.013
10.1016/j.bbapap.2014.01.013 · External reference
10.1038/s41592-022-01488-1
10.1038/s41592-022-01488-1 · External reference
Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from escherichia coli
10.1074/jbc.274.36.25254 · 1999 · External reference
10.1107/s0907444911001314
10.1107/s0907444911001314 · External reference
10.1006/jmbi.1998.1760
10.1006/jmbi.1998.1760 · External reference
10.1110/ps.062268106
10.1110/ps.062268106 · External reference
10.1074/jbc.m109.011502
10.1074/jbc.m109.011502 · External reference
Research progress of glutathione peroxidase family (GPX) in redoxidation [Review]
2023 · External reference
The suppressor of copper sensitivity protein C from Caulobacter crescentus is a trimeric disulfide isomerase that binds copper(I) with subpicomolar affinity
10.1107/s2059798322000729 · 2022 · External reference
10.1107/s0907444913017800
10.1107/s0907444913017800 · External reference
10.1002/prot.20329
10.1002/prot.20329 · External reference
Francisella tularensis subsp. tularensis Schu S4 disulfide bond formation protein B, but not an RND-type efflux pump, is required for virulence
10.1128/iai.00363-08 · 2008 · External reference
Identification of an essential Francisella tularensis subsp. tularensis virulence factor
10.1128/iai.01113-08 · 2009 · External reference
10.1128/jb.01359-13
10.1128/jb.01359-13 · External reference
Components of the type six secretion system are substrates of Francisella tularensis Schu S4 DsbA-like FipB protein
10.1080/21505594.2016.1168550 · 2016 · External reference
10.1074/jbc.m705291200
10.1074/jbc.m705291200 · External reference
10.1107/s0907444901012471
10.1107/s0907444901012471 · External reference
10.1111/mmi.12808
10.1111/mmi.12808 · External reference
10.1074/jbc.m809509200
10.1074/jbc.m809509200 · External reference
10.1128/jb.179.21.6602-6608.1997
10.1128/jb.179.21.6602-6608.1997 · External reference
Characterization of Francisella tularensis Schu S4 defined mutants as live-attenuated vaccine candidates
10.1093/femspd/ftv036 · 2015 · External reference
10.1016/j.csbj.2021.08.018
10.1016/j.csbj.2021.08.018 · External reference
10.1016/s0006-3495(02)75469-6
10.1016/s0006-3495(02)75469-6 · External reference
10.1089/ars.2012.4939
10.1089/ars.2012.4939 · External reference
10.1089/ars.2010.3344
10.1089/ars.2010.3344 · External reference
Two new classes of F-pili mutants of Escherichia coli resistant to infection by the male specific bacteriophage f2
10.1016/0042-6822(68)90125-6 · 1968 · External reference
Unresolved reference
2022 · External reference
10.1016/j.pep.2005.01.016
10.1016/j.pep.2005.01.016 · External reference
The Scs disulfide reductase system cooperates with the metallochaperone CueP in Salmonella copper resistance
10.1074/jbc.ra119.010164 · 2019 · External reference
10.1089/ars.2020.8218
10.1089/ars.2020.8218 · External reference
10.1089/ars.2017.7104
10.1089/ars.2017.7104 · External reference
10.1093/nar/gkab1061
10.1093/nar/gkab1061 · External reference
A high-throughput cell-based assay pipeline for the preclinical development of bacterial DsbA inhibitors as antivirulence therapeutics
10.1038/s41598-021-81007-y · 2021 · External reference
The 1.2 A resolution crystal structure of TcpG, the Vibrio cholerae DsbA disulfide-forming protein required for pilus and cholera-toxin production
10.1107/s0907444912026388 · 2012 · External reference
The atypical thiol-disulfide exchange protein [alpha]-DsbA2 from Wolbachia pipientis is a homotrimeric disulfide isomerase
10.1107/s2059798318018442 · 2019 · External reference
A buried water network modulates the activity of the escherichia coli disulphide catalyst DsbA
10.3390/antiox12020380 · 2023 · External reference
First-sphere and second-sphere electrostatic effects in the active site of a class mu glutathione transferase
10.1021/bi960189k · 1996 · External reference
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo
10.1021/bi00070a016 · 1993 · External reference
Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
10.1021/bi00015a019 · 1995 · External reference
10.1107/s0021889813011461
10.1107/s0021889813011461 · External reference
Dimerization by domain hybridization bestows chaperone and isomerase activities
10.1074/jbc.m306945200 · 2003 · External reference