Research graph
References from Oligomerization of the Clostridioides difficile transferase B component proceeds through a stepwise mechanism. Local targets link to admitted publications; unresolved targets remain external evidence.
Burden of Clostridium difficile infection in the United States
10.1056/nejmoa1408913 · 2015 · External reference
Clostridioides difficile toxins: mechanisms of action and antitoxin therapeutics
10.1038/s41579-021-00660-2 · 2022 · External reference
Toxin B is essential for virulence of Clostridium difficile
10.1038/nature07822 · 2009 · External reference
The binary toxin CDT enhances Clostridium difficile virulence by suppressing protective colonic eosinophilia
10.1038/nmicrobiol.2016.108 · 2016 · External reference
Purified CDT toxins and a clean deletion within the CDT locus provide novel insights into the contribution of binary toxin in cellular inflammation and Clostridioides difficile infection
10.1371/journal.ppat.1012568 · 2024 · External reference
Binary toxin and death after Clostridium difficile infection
10.3201/eid/1706.101483 · 2011 · External reference
The prognostic value of toxin B and binary toxin in Clostridioides difficile infection
10.1080/19490976.2021.1884516 · 2021 · External reference
Clostridium perfringens iota toxin: synergism between two proteins
10.1016/0041-0101(86)90101-7 · 1986 · External reference
Purification of the Clostridium spiroforme binary toxin and activity of the toxin on HEp-2 cells
10.1128/iai.57.8.2462-2469.1989 · 1989 · External reference
Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196
10.1128/iai.65.4.1402-1407.1997 · 1997 · External reference
Clostridial binary toxins: iota and C2 family portraits
10.3389/fcimb.2011.00011 · 2011 · External reference
Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase toxin CDTa from Clostridium difficile
10.1074/jbc.m109.043018 · 2009 · External reference
The N-terminus of the Clostridioides difficile transferase A component directs toxin activity and potency
2024 · External reference
Structural insights into the transition of Clostridioides difficile binary toxin from prepore to pore
10.1038/s41564-019-0601-8 · 2020 · External reference
Cryo-EM structures reveal translocational unfolding in the clostridial binary iota toxin complex
10.1038/s41594-020-0388-6 · 2020 · External reference
Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a di-heptamer macromolecular assembly
10.1073/pnas.1919490117 · 2020 · External reference
Crystal structure of the anthrax toxin protective antigen
10.1038/385833a0 · 1997 · External reference
Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT)
10.1073/pnas.1109772108 · 2011 · External reference
Structural elucidation of the Clostridioides difficile transferase toxin reveals a single-site binding mode for the enzyme
10.1073/pnas.1920555117 · 2020 · External reference
Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile
10.1038/s41467-022-33888-4 · 2022 · External reference
Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification
10.1074/jbc.m000596200 · 2000 · External reference
Inhibition of Arp2/3 Complex after ADP-Ribosylation of Arp2 by Binary Clostridioides Toxins
10.3390/cells11223661 · 2022 · External reference
Anthrax toxin receptor drives protective antigen oligomerization and stabilizes the heptameric and octameric oligomer by a similar mechanism
10.1371/journal.pone.0013888 · 2010 · External reference
The protective antigen component of anthrax toxin forms functional octameric complexes
10.1016/j.jmb.2009.07.037 · 2009 · External reference
The ins and outs of anthrax toxin
10.3390/toxins8030069 · 2016 · External reference
Atomic Structures of Anthrax Prechannel Bound with Full-Length Lethal and Edema Factors
10.1016/j.str.2020.05.009 · 2020 · External reference
Atomic structures of anthrax toxin protective antigen channels bound to partially unfolded lethal and edema factors
10.1038/s41467-020-14658-6 · 2020 · External reference
10.1101/2024.10.10.617581
10.1101/2024.10.10.617581 · External reference
Structural basis for the unfolding of anthrax lethal factor by protective antigen oligomers
10.1038/nsmb.1923 · 2010 · External reference
Trainable Weka Segmentation: a machine learning tool for microscopy pixel classification
10.1093/bioinformatics/btx180 · 2017 · External reference
Fiji: an open-source platform for biological-image analysis
10.1038/nmeth.2019 · 2012 · External reference
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
10.1038/nmeth.4169 · 2017 · External reference
Real-space refinement in PHENIX for cryo-EM and crystallography
10.1107/s2059798318006551 · 2018 · External reference
Features and development of Coot
10.1107/s0907444910007493 · 2010 · External reference
MolProbity: More and better reference data for improved all-atom structure validation
10.1002/pro.3330 · 2018 · External reference
