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References from Influence of chemical denaturants on the activity, fold and zinc status of anthrax lethal factor. Local targets link to admitted publications; unresolved targets remain external evidence.
Anthrax
10.1146/annurev.micro.55.1.647 · 2001 · External reference
Anthrax toxin
10.1146/annurev.cellbio.19.111301.140655 · 2003 · External reference
Anthrax toxin: receptor binding, internalization, pore formation, and translocation
10.1146/annurev.biochem.75.103004.142728 · 2007 · External reference
Crystal structure of the anthrax toxin protective antigen
10.1038/385833a0 · 1997 · External reference
The unfolding story of anthrax toxin translocation
10.1111/j.1365-2958.2011.07614.x · 2011 · External reference
Ratcheting up protein translocation with anthrax toxin
10.1002/pro.2052 · 2012 · External reference
Membrane translocation by anthrax toxin
10.1016/j.mam.2009.06.003 · 2009 · External reference
Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
10.1038/415396a · 2002 · External reference
Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor
10.1126/science.280.5364.734 · 1998 · External reference
Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
10.1006/bbrc.1998.9040 · 1998 · External reference
Anthrax lethal factor cleavage of Nlrp1 is required for activation of the inflammasome
10.1371/journal.ppat.1002638 · 2012 · External reference
Anthrax lethal factor cleaves mouse nlrp1b in both toxin-sensitive and toxin-resistant macrophages
10.1371/journal.pone.0049741 · 2012 · External reference
Direct proteolytic cleavage of NLRP1B is necessary and sufficient for inflammasome activation by anthrax lethal factor
10.1371/journal.ppat.1003452 · 2013 · External reference
Crystal structure of the anthrax lethal factor
10.1038/n35101998 · 2001 · External reference
Recent advances in zinc enzymology
10.1021/cr950042j · 1996 · External reference
Acid-induced unfolding of the amino-terminal domains of the lethal and edema factors of anthrax toxin
10.1016/j.jmb.2004.09.067 · 2004 · External reference
A phenylalanine clamp catalyzes protein translocation through the anthrax toxin pore
10.1126/science.1113380 · 2005 · External reference
Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation
10.1073/pnas.0905880106 · 2009 · External reference
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
10.1038/nsmb.1923 · 2010 · External reference
Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor
10.1016/j.febslet.2012.11.035 · 2013 · External reference
Preparation and characterization of cobalt-substituted anthrax lethal factor
10.1016/j.bbrc.2011.11.005 · 2011 · External reference
Alkaline earth metals are not required for the restoration of the apoform of anthrax lethal factor to its holoenzyme state
10.1016/j.bbrc.2010.11.009 · 2010 · External reference
High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue
10.1016/j.jinorgbio.2014.06.009 · 2014 · External reference
Screening inhibitors of anthrax lethal factor
10.1038/418386a · 2002 · External reference
The stability of globular proteins
10.3109/10409237509102551 · 1975 · External reference
Determination and analysis of urea and guanidine hydrochloride denaturation curves
10.1016/0076-6879(86)31045-0 · 1986 · External reference
Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
10.1021/bi00421a014 · 1988 · External reference
Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase
10.1073/pnas.90.6.2107 · 1993 · External reference
Tyrosine-728 and glutamic acid-735 are essential for the metalloproteolytic activity of the lethal factor of Bacillus anthracis
10.1016/j.bbrc.2003.11.134 · 2004 · External reference
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding
10.1002/pro.5560041020 · 1995 · External reference
Unresolved reference
2000 · External reference
The stability of 2-state, 3-state and more-state proteins from simple spectroscopic techniques… plus the structure of the equilibrium intermediates at the same time
10.1016/j.abb.2012.10.014 · 2013 · External reference
The metalloproteolytic activity of the anthrax lethal factor is substrate-inhibited
10.1074/jbc.m306466200 · 2003 · External reference
Mechanisms of tryptophan fluorescence shifts in proteins
10.1016/s0006-3495(01)76183-8 · 2001 · External reference
Purification and biophysical characterization of the core protease domain of anthrax lethal factor
10.1016/j.bbrc.2010.04.144 · 2010 · External reference
Conformational dynamics of the anthrax lethal factor catalytic center
10.1021/bi1017792 · 2010 · External reference
The structure of Mlc titration factor A (MtfA/YeeI) reveals a prototypical zinc metallopeptidase related to anthrax lethal factor
10.1128/jb.00038-12 · 2012 · External reference
The how׳s and why׳s of protein folding intermediates
10.1016/j.abb.2012.10.006 · 2013 · External reference
Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back
10.1146/annurev-physchem-032210-103531 · 2011 · External reference
Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding
10.1073/pnas.0808427105 · 2008 · External reference
Kinetic evidence for a two-stage mechanism of protein denaturation by guanidinium chloride
10.1073/pnas.1315453111 · 2014 · External reference
Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
10.1073/pnas.0812588106 · 2009 · External reference
The structural basis of urea-induced protein unfolding in β-catenin
2014 · External reference
Toward an atomistic description of the urea-denatured state of proteins
10.1073/pnas.1216589110 · 2013 · External reference
Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals
10.1006/abio.2000.4706 · 2000 · External reference
The use of 4-(2-pyridylazo)resorcinol in studies of zinc release from Escherichia coli aspartate transcarbamoylase
10.1016/0003-2697(85)90409-9 · 1985 · External reference
IMP-1 metallo-β-lactamase: effect of chelators and assessment of metal requirement by electrospray mass spectrometry
10.1016/s0304-4165(02)00258-1 · 2002 · External reference
A direct spectrophotometric method for the simultaneous determination of zinc and cobalt in metalloproteins using 4-(2-pyridylazo)resorcinol
10.1016/j.ab.2009.05.007 · 2009 · External reference
Denaturational stress induces formation of zinc-deficient monomers of Cu,Zn superoxide dismutase: implications for pathogenesis in amyotrophic lateral sclerosis
10.1016/j.jmb.2008.08.024 · 2008 · External reference
Cytosolic zinc buffering and muffling: their role in intracellular zinc homeostasis
10.1039/b926662c · 2010 · External reference
Zinc-buffering capacity of a eukaryotic cell at physiological pZn
10.1007/s00775-006-0150-5 · 2006 · External reference
