Research graph
References from Disulphide maintenance systems and proteostasis. Local targets link to admitted publications; unresolved targets remain external evidence.
Disulfide interchange and the three-dimensional structure of proteins
10.1073/pnas.53.3.676 · 1965 · External reference
Cysteine reactivity across the subcellular universe
10.1016/j.cbpa.2018.11.002 · 2019 · External reference
Three approaches to one problem: protein folding in the periplasm, the endoplasmic reticulum, and the intermembrane space
10.1089/ars.2014.5841 · 2014 · External reference
Defining roles of specific reactive oxygen species (ROS) in cell biology and physiology
10.1038/s41580-022-00456-z · 2022 · External reference
Maintaining a healthy proteome during oxidative stress
10.1016/j.molcel.2017.12.021 · 2018 · External reference
Ero1 and redox homeostasis in the endoplasmic reticulum
10.1016/j.bbamcr.2007.12.011 · 2008 · External reference
Thioredoxin and thioredoxin reductase: current research with special reference to human disease
10.1016/j.bbrc.2010.03.083 · 2010 · External reference
The protein disulfide isomerase family: from proteostasis to pathogenesis
10.1016/j.bbagen.2019.04.003 · 2020 · External reference
Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead
10.1089/ars.2012.4864 · 2013 · External reference
Microbial antioxidant defense enzymes
10.1016/j.micpath.2017.06.015 · 2017 · External reference
The basics of thiols and cysteines in redox biology and chemistry
10.1016/j.freeradbiomed.2014.11.013 · 2015 · External reference
The role of thiols in antioxidant systems
10.1016/j.freeradbiomed.2019.05.035 · 2019 · External reference
Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery
10.1021/cr300163e · 2013 · External reference
Analysis and functional prediction of reactive cysteine residues
10.1074/jbc.r111.275578 · 2012 · External reference
Diverse functional roles of reactive cysteines
10.1021/cb3005269 · 2013 · External reference
Thioredoxins and glutaredoxins: unifying elements in redox biology
10.1146/annurev-genet-102108-134201 · 2009 · External reference
How proteins form disulfide bonds
10.1089/ars.2010.3575 · 2011 · External reference
Disulfide bond formation network in the three biological kingdoms, bacteria, fungi and mammals
10.1111/j.1742-4658.2012.08593.x · 2012 · External reference
Experimental approaches for investigating disulfide-based redox relays in cells
10.1021/acs.chemrestox.2c00123 · 2022 · External reference
Thioredoxin—a fold for all reasons
10.1016/s0969-2126(01)00154-x · 1995 · External reference
Thioredoxins and glutaredoxins as facilitators of protein folding
10.1016/j.bbamcr.2008.02.003 · 2008 · External reference
Balancing oxidative protein folding: the influences of reducing pathways on disulfide bond formation
10.1016/j.bbapap.2014.02.004 · 2014 · External reference
Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide
10.1016/s0969-2126(01)00153-8 · 1995 · External reference
Structure, function, and mechanism of thioredoxin proteins
10.1089/ars.2010.3114 · 2010 · External reference
Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase
10.1021/cr100006x · 2011 · External reference
Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B
10.1016/s0969-2126(01)00159-9 · 1995 · External reference
The solution structure of human thioredoxin complexed with its target from ref-1 reveals peptide chain reversal
10.1016/s0969-2126(96)00065-2 · 1996 · External reference
Structural basis for target protein recognition by the protein disulfide reductase thioredoxin
10.1016/j.str.2006.09.012 · 2006 · External reference
Crystal structures of barley thioredoxin h isoforms HvTrxh1 and HvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity
10.1110/ps.083460308 · 2008 · External reference
The specificity of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity
10.1039/c5sc01501d · 2015 · External reference
A universal entropy-driven mechanism for thioredoxin-target recognition
10.1073/pnas.1504376112 · 2015 · External reference
Thioredoxin reductase two modes of catalysis have evolved
10.1046/j.1432-1327.2000.01702.x · 2000 · External reference
Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation
10.1089/ars.2008.2291 · 2009 · External reference
Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes
10.1016/j.bbagen.2012.09.018 · 2013 · External reference
Molecular mechanisms of glutaredoxin enzymes: versatile hubs for thiol-disulfide exchange between protein thiols and glutathione
10.1016/j.jmb.2018.12.006 · 2019 · External reference
A single glutaredoxin or thioredoxin gene is essential for viability in the yeast Saccharomyces cerevisiae
10.1046/j.1365-2958.2000.01948.x · 2000 · External reference
One cysteine is enough: a monothiol Grx can functionally replace all cytosolic Trx and dithiol Grx
10.1016/j.redox.2020.101598 · 2020 · External reference
Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins
10.1038/s41467-020-17323-0 · 2020 · External reference
Oxidative protein folding fidelity and redoxtasis in the endoplasmic reticulum
10.1016/j.tibs.2022.06.011 · 2023 · External reference
Critical roles of protein disulfide isomerases in balancing proteostasis in the nervous system
10.1016/j.jbc.2022.102087 · 2022 · External reference
Mechanisms of productive folding and endoplasmic reticulum-associated degradation of glycoproteins and non-glycoproteins
10.1016/j.bbagen.2020.129812 · 2021 · External reference
The essential functions of molecular chaperones and folding enzymes in maintaining endoplasmic reticulum homeostasis
10.1016/j.jmb.2023.168418 · 2024 · External reference
The human PDI family: versatility packed into a single fold
10.1016/j.bbamcr.2007.11.010 · 2008 · External reference
The human protein disulfide isomerase gene family
10.1186/1479-7364-6-6 · 2012 · External reference
The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond
10.1155/2013/742923 · 2013 · External reference
The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis
10.1021/acs.accounts.5b00150 · 2015 · External reference
Oxidative folding in the mitochondrial intermembrane space: a regulated process important for cell physiology and disease
10.1016/j.bbamcr.2016.03.023 · 2016 · External reference
CHCHD4 (MIA40) and the mitochondrial disulfide relay system
10.1042/bst20190232 · 2021 · External reference
Novel mitochondrial intermembrane space proteins as substrates of the MIA import pathway
10.1016/j.jmb.2006.10.038 · 2007 · External reference
Systematic analysis of the twin cx(9)c protein family
10.1016/j.jmb.2009.08.041 · 2009 · External reference
Genome-wide analysis of eukaryotic twin CX9C proteins
10.1039/c0mb00058b · 2010 · External reference
Cyclophilin D is a new non-canonical substrate of the mitochondrial intermembrane space assembly pathway
10.1016/j.jbc.2025.110883 · 2025 · External reference
Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria
10.1016/j.jmb.2014.10.022 · 2014 · External reference
Mia40 is a facile oxidant of unfolded reduced proteins but shows minimal isomerase activity
10.1016/j.abb.2015.05.005 · 2015 · External reference
DSB proteins and bacterial pathogenicity
10.1038/nrmicro2087 · 2009 · External reference
Protein disulfide exchange by the intramembrane enzymes DsbB, DsbD, and CcdA
10.1016/j.jmb.2020.04.008 · 2020 · External reference
Reducing systems protecting the bacterial cell envelope from oxidative damage
10.1016/j.febslet.2015.04.057 · 2015 · External reference
Disulfide-bond-forming pathways in gram-positive bacteria
10.1128/jb.00769-15 · 2015 · External reference
The CXXC motif is more than a redox rheostat
10.1074/jbc.m705291200 · 2007 · External reference
Functional metagenomics of the thioredoxin superfamily
10.1074/jbc.ra120.016350 · 2021 · External reference
Broader than expected tolerance for substitutions in the WCGPCK catalytic motif of yeast thioredoxin 2
10.1016/j.freeradbiomed.2021.09.009 · 2022 · External reference
Methods to identify the substrates of thiol-disulfide oxidoreductases
10.1002/pro.3530 · 2019 · External reference
Identification of PDI substrates by mechanism-based kinetic trapping
10.1007/978-1-4939-9187-7_10 · 2019 · External reference
Bifunctional electrophiles cross-link thioredoxins with redox relay partners in cells
10.1021/tx4000123 · 2013 · External reference
Trapping redox partnerships in oxidant-sensitive proteins with a small, thiol-reactive cross-linker
10.1016/j.freeradbiomed.2016.10.506 · 2016 · External reference
A crosslinker-based identification of redox relay targets
10.1016/j.ab.2016.12.025 · 2017 · External reference
Identifying interaction partners of yeast protein disulfide isomerases using a small thiol-reactive cross-linker: implications for secretory pathway proteostasis
10.1021/acs.chemrestox.1c00376 · 2022 · External reference
A redox-active crosslinker reveals an essential and inhibitable oxidative folding network in the endoplasmic reticulum of malaria parasites
10.1371/journal.ppat.1009293 · 2021 · External reference
Mapping protein direct interactome of oxidoreductases with small molecular chemical cross-linkers in live cells
10.1016/j.redox.2023.102642 · 2023 · External reference
Expanding the crosslinking mass spectrometry toolbox with vinyl sulfone crosslinkers
10.1016/j.mcpro.2025.101315 · 2025 · External reference
Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
10.1242/jcs.059154 · 2009 · External reference
Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin
10.1016/j.molcel.2010.11.010 · 2010 · External reference
Adapting proteostasis for disease intervention
10.1126/science.1141448 · 2008 · External reference
Functional modules of the proteostasis network
10.1101/cshperspect.a033951 · 2020 · External reference
Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
10.1101/gad.12.24.3788 · 1998 · External reference
Small molecule activators of the heat shock response: chemical properties, molecular targets, and therapeutic promise
10.1021/tx300264x · 2012 · External reference
Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
10.1101/gad.13.10.1211 · 1999 · External reference
Cytoplasmic redox imbalance in the thioredoxin system activates Hsf1 and results in hyperaccumulation of the sequestrase Hsp42 with misfolded proteins
10.1091/mbc.e23-07-0296 · 2024 · External reference
Nonnative disulfide bond formation activates the sigma32-dependent heat shock response in Escherichia coli
10.1128/jb.00127-13 · 2013 · External reference
Redox regulation of proteostasis
10.1016/j.jbc.2024.107977 · 2024 · External reference
The thioredoxin system protects ribosomes against stress-induced aggregation
10.1091/mbc.e05-06-0520 · 2006 · External reference
Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
10.1074/jbc.m206626200 · 2002 · External reference
Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
10.1126/science.1080273 · 2003 · External reference
Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function
10.1016/j.cell.2004.05.002 · 2004 · External reference
Irreversible oxidation of the active-site cysteine of peroxiredoxin to cysteine sulfonic acid for enhanced molecular chaperone activity
10.1074/jbc.m804087200 · 2008 · External reference
Lifespan control by redox-dependent recruitment of chaperones to misfolded proteins
10.1016/j.cell.2016.05.006 · 2016 · External reference
Reversal of 2-cys peroxiredoxin oligomerization by sulfiredoxin
10.1016/j.bbrc.2013.01.114 · 2013 · External reference
ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
10.1038/nature02075 · 2003 · External reference
Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine
10.1074/jbc.m409482200 · 2004 · External reference
Catalytic mechanism of sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin
10.1074/jbc.m109.035352 · 2009 · External reference
From guide to guard-activation mechanism of the stress-sensing chaperone Get3
10.1016/j.molcel.2022.06.015 · 2022 · External reference
Identification of a redox-regulated chaperone network
10.1038/sj.emboj.7600016 · 2004 · External reference
Activation of RidA chaperone function by N-chlorination
10.1038/ncomms6804 · 2014 · External reference
Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase
10.1042/bj20030093 · 2003 · External reference
Heat-shock and redox-dependent functional switching of an h-type arabidopsis thioredoxin from a disulfide reductase to a molecular chaperone
10.1104/pp.109.135426 · 2009 · External reference
Chaperone-like properties of tobacco plastid thioredoxins f and m
10.1093/jxb/err282 · 2012 · External reference
An essential thioredoxin-type protein of Trypanosoma brucei acts as redox-regulated mitochondrial chaperone
10.1371/journal.ppat.1008065 · 2019 · External reference
Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin
10.1038/s41467-024-54892-w · 2024 · External reference
Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome
10.1074/jbc.m900016200 · 2009 · External reference
Thioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle
10.1074/jbc.m109.002121 · 2009 · External reference
Structure of the TXNL1-bound proteasome
10.1038/s41594-025-01639-w · 2025 · External reference
Structural landscape of the degrading 26S proteasome reveals conformation-specific binding of TXNL1
10.1038/s41594-025-01695-2 · 2025 · External reference
Protein disulfide isomerase is both an enzyme and a chaperone
10.1096/fasebj.7.15.7903263 · 1993 · External reference
Protein disulfide isomerase exhibits chaperone and anti-chaperone activity in the oxidative refolding of lysozyme
10.1016/s0021-9258(17)37352-0 · 1994 · External reference
Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation
10.1089/ars.2009.2466 · 2009 · External reference
Is protein disulfide isomerase a redox-dependent molecular chaperone?
10.1093/emboj/cdf685 · 2002 · External reference
Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress
10.15252/embj.2019103841 · 2020 · External reference
Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation
10.1091/mbc.e11-08-0722 · 2012 · External reference
BiP and PDI cooperate in the oxidative folding of antibodies in vitro
10.1074/jbc.m002655200 · 2000 · External reference
Interactions among yeast protein-disulfide isomerase proteins and endoplasmic reticulum chaperone proteins influence their activities
10.1074/jbc.m503377200 · 2005 · External reference
A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
10.1091/mbc.e02-05-0311 · 2002 · External reference
A multichaperone condensate enhances protein folding in the endoplasmic reticulum
10.1038/s41556-025-01730-w · 2025 · External reference
Ca(2+)-driven PDIA6 biomolecular condensation ensures proinsulin folding
10.1038/s41556-025-01794-8 · 2025 · External reference
Protein disulfide isomerase
10.1016/s1570-9639(04)00063-9 · 2004 · External reference
Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates
10.1091/mbc.e11-08-0704 · 2012 · External reference
Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
10.1083/jcb.200809198 · 2009 · External reference
A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum
10.1016/j.molcel.2011.04.027 · 2011 · External reference
A complex of Htm1 and the oxidoreductase Pdi1 accelerates degradation of misfolded glycoproteins
10.1074/jbc.m115.703256 · 2016 · External reference
Htm1p-Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation
10.1073/pnas.1608795113 · 2016 · External reference
Initiation of ERAD by the bifunctional complex of Mnl1/Htm1 mannosidase and protein disulfide isomerase
10.1038/s41594-025-01491-y · 2025 · External reference
ER-resident protein 46 (ERp46) triggers the mannose-trimming activity of ER degradation-enhancing alpha-mannosidase-like protein 3 (EDEM3)
10.1074/jbc.ra118.003129 · 2018 · External reference
In vitro mannosidase activity of EDEM3 against asparagine-linked oligomannose-type glycans
10.1016/j.bbrc.2022.04.094 · 2022 · External reference
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
10.1126/science.1159293 · 2008 · External reference
Glycosylation-independent ERAD pathway serves as a backup system under ER stress
10.1091/mbc.e13-03-0138 · 2013 · External reference
Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5
10.1016/j.molcel.2011.01.021 · 2011 · External reference
Characterization of early EDEM1 protein maturation events and their functional implications
10.1074/jbc.m111.243998 · 2011 · External reference
Mechanistic characterization of disulfide bond reduction of an ERAD substrate mediated by cooperation between ERdj5 and BiP
10.1016/j.jbc.2023.105274 · 2023 · External reference
The oxidative folding of nascent polypeptides provides electrons for reductive reactions in the ER
10.1016/j.celrep.2023.112742 · 2023 · External reference
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria
10.1038/nsmb.1553 · 2009 · External reference
A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding
10.1083/jcb.200905134 · 2009 · External reference
Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import
10.1073/pnas.1010095107 · 2010 · External reference
Mia40 targets cysteines in a hydrophobic environment to direct oxidative protein folding in the mitochondria
10.1038/ncomms4041 · 2014 · External reference
Mia40 is a trans-site receptor that drives protein import into the mitochondrial intermembrane space by hydrophobic substrate binding
10.7554/elife.16177 · 2016 · External reference
Atp23 biogenesis reveals a chaperone-like folding activity of Mia40 in the IMS of mitochondria
10.1038/emboj.2012.263 · 2012 · External reference
Interaction with the cysteine-free protein HAX1 expands the substrate specificity and function of MIA40 beyond protein oxidation
10.1111/febs.17328 · 2024 · External reference
Structural basis of client specificity in mitochondrial membrane-protein chaperones
10.1126/sciadv.abd0263 · 2020 · External reference
The ubiquitin-proteasome system regulates mitochondrial intermembrane space proteins
10.1128/mcb.01579-12 · 2013 · External reference
Vectorial import via a metastable disulfide-linked complex allows for a quality control step and import by the mitochondrial disulfide relay
10.1016/j.celrep.2018.12.092 · 2019 · External reference
How the assembly and protection of the bacterial cell envelope depend on cysteine residues
10.1074/jbc.rev120.011201 · 2020 · External reference
Does DsbA have chaperone-like activity?
10.1006/abbi.1996.9783 · 1997 · External reference
Chaperone activity of DsbC
1999 · External reference
Genetic analysis of 15 protein folding factors and proteases of the Escherichia coli cell envelope
10.1128/jb.00221-12 · 2012 · External reference
The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner
10.1111/j.1365-2958.2007.06030.x · 2008 · External reference
The two faces of coenzyme A in cellular biology
10.1016/j.freeradbiomed.2025.03.025 · 2025 · External reference
Emerging chemical biology of protein persulfidation
10.1089/ars.2023.0352 · 2023 · External reference
An in vivo pathway for disulfide bond isomerization in Escherichia coli
10.1073/pnas.93.23.13048 · 1996 · External reference
Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
10.1128/jb.179.21.6602-6608.1997 · 1997 · External reference
Endoplasmic reticulum (ER) stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant
10.1074/jbc.ra118.001824 · 2018 · External reference
Cytosolic thioredoxin system facilitates the import of mitochondrial small Tim proteins
10.1038/embor.2012.116 · 2012 · External reference
