The bacterial toxin toolkit

Lipid rafts and signal transduction

Simons, K., & Toomre, D. K. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35036052 · Cited by 6,252 · see citing works

Structure of Staphylococcal α-Hemolysin, a Heptameric Transmembrane Pore

Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., & Gouaux, J. E. (1996) · Science · doi:10.1126/science.274.5294.1859 · Cited by 2,378 · see citing works

Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin

Schiavo, G., Benfenati, F., Poulain, B., Rossetto, O., de Laureto, P. P., DasGupta, B. R., & Montecucco, C. (1992) · Nature · doi:10.1038/359832a0 · Cited by 1,803 · see citing works

A bacterial two-hybrid system based on a reconstituted signal transduction pathway

Karimova, G., Pidoux, J., Ullmann, A., & Ladant, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.10.5752 · Cited by 1,664 · see citing works

Pathogenicity Islands and the Evolution of Microbes

Hacker, J. H., & Kaper, J. B. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.641 · Cited by 1,298 · see citing works

Neurotoxins Affecting Neuroexocytosis

Schiavo, G., Matteoli, M., & Montecucco, C. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.2.717 · Cited by 1,266 · see citing works

SNARE-mediated membrane fusion

Chen, Y. A., & Scheller, R. H. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35052017 · Cited by 1,133 · see citing works

Proteolytic Inactivation of MAP-Kinase-Kinase by Anthrax Lethal Factor

Duesbery, N. S., Webb, C. P., Leppla, S. H., Gordon, V. M., Klimpel, K. R., Copeland, T. D., Ahn, N. G., Oskarsson, M. K., Fukasawa, K., Paull, K. D., et al. (1998) · Science · doi:10.1126/science.280.5364.734 · Cited by 1,007 · see citing works

Targeted expression of tetanus toxin light chain in Drosophila specifically eliminates synaptic transmission and causes behavioral defects

Sweeney, S. T., Broadie, K., Keane, J., Niemann, H., & O'Kane, C. J. (1995) · Neuron · doi:10.1016/0896-6273(95)90290-2 · Cited by 938 · see citing works

G proteins

Hepler, J. R., & Gilman, A. G. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90005-t · Cited by 894 · see citing works

REGULATION OF CERAMIDE PRODUCTION AND APOPTOSIS

Kolesnick, R., & Krönke, M. (1998) · Annual Review of Physiology · doi:10.1146/annurev.physiol.60.1.643 · Cited by 803 · see citing works

The Comprehensive Sourcebook of Bacterial Protein Toxins

ALOUF, J. E., Ladant, D., & Popoff, M. R. (2015) · Elsevier eBooks · doi:10.1016/c2013-0-14258-4 · Cited by 612 · see citing works

A Bacterial Toxin That Controls Cell Cycle Progression as a Deoxyribonuclease I-Like Protein

Lara-Tejero, M., & Galán, J. E. (2000) · Science · doi:10.1126/science.290.5490.354 · Cited by 551 · see citing works

Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor

Naglich, J. G., Metherall, J. E., Russell, D. W., & Eidels, L. (1992) · Cell · doi:10.1016/0092-8674(92)90623-k · Cited by 550 · see citing works

Living dangerously: how Helicobacter pylori survives in the human stomach

Montecucco, C., & Rappuoli, R. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35073084 · Cited by 538 · see citing works

Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1

Schmidt, G., Sehr, P., Wilm, M., Selzer, J., Mann, M., & Aktories, K. (1997) · Nature · doi:10.1038/42735 · Cited by 530 · see citing works

Rapid Cycling of Lipid Raft Markers between the Cell Surface and Golgi Complex

Nichols, B. J., Kenworthy, A. K., Polishchuk, R., Lodge, R., Roberts, T. H., Hirschberg, K., Phair, R. D., & Lippincott‐Schwartz, J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.3.529 · Cited by 525 · see citing works

Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae.

Parton, R. G. (1994) · Journal of Histochemistry & Cytochemistry · doi:10.1177/42.2.8288861 · Cited by 507 · see citing works

Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine

Flatau, G., Lemichez, E., Gauthier, M., Chardin, P., Paris, S., Fiorentini, C., & Boquet, P. (1997) · Nature · doi:10.1038/42743 · Cited by 499 · see citing works

Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum

Sandvig, K., Garred, Ø., Prydz, K., Kozlov, J. V., Hansen, S. H., & van Deurs, B. (1992) · Nature · doi:10.1038/358510a0 · Cited by 429 · see citing works

Rab6 Coordinates a Novel Golgi to ER Retrograde Transport Pathway in Live Cells

White, J., Johannes, L., Mallard, F., Girod, A., Grill, S. W., Reinsch, S. S., Keller, P., Tzschaschel, B. D., Échard, A., Goud, B., et al. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.4.743 · Cited by 419 · see citing works

Bacteroides fragilis enterotoxin cleaves the zonula adherens protein, E-cadherin

Wu, S., Lim, K.-C., Huang, J. H. Y., Saidi, R. F., & Sears, C. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14979 · Cited by 410 · see citing works

Anthrax Lethal Factor Cleaves the N-Terminus of MAPKKs and Induces Tyrosine/Threonine Phosphorylation of MAPKs in Cultured Macrophages

Vitale, G., Pellizzari, R., Recchi, C., Napolitani, G., Mock, M., & Montecucco, C. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9040 · Cited by 402 · see citing works

The N‐terminal 34 kDa fragment of Helicobacter pylori vacuolating cytotoxin targets mitochondria and induces cytochrome c release

Galmiche, A., Rassow, J., Doye, A., Cagnol, S., Chambard, J., Contamin, S., de Thillot, V., Just, I., Ricci, V., Solcia, E., et al. (2000) · The EMBO Journal · doi:10.1093/emboj/19.23.6361 · Cited by 362 · see citing works

The Mechanism of Membrane Insertion for a Cholesterol-Dependent Cytolysin

Shatursky, O. Y., Heuck, A. P., Shepard, L. A., Rossjohn, J., Parker, M. W., Johnson, A. E., & Tweten, R. K. (1999) · Cell · doi:10.1016/s0092-8674(00)81660-8 · Cited by 358 · see citing works

Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor

Vitale, G., Bernardi, L., Napolitani, G., Mock, M., & Montecucco, C. (2000) · Biochemical Journal · doi:10.1042/bj3520739 · Cited by 355 · see citing works

Lysenin, a Novel Sphingomyelin-specific Binding Protein

Yamaji, A., Sekizawa, Y., Emoto, K., Sakuraba, H., Inoue, K., Kobayashi, H., & Umeda, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.9.5300 · Cited by 338 · see citing works

Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O

Walev, I., Bhakdi, S. C., Hofmann, F., Djonder, N., Valeva, A., Aktories, K., & Bhakdi, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051429498 · Cited by 329 · see citing works

DNase I homologous residues in CdtB are critical for cytolethal distending toxin‐mediated cell cycle arrest

Elwell, C. A., & Dreyfus, L. A. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02070.x · Cited by 301 · see citing works

Bordetella pertussis adenylate cyclase: a toxin with multiple talents

Ladant, D., & Ullmann, A. (1999) · Trends in Microbiology · doi:10.1016/s0966-842x(99)01468-7 · Cited by 293 · see citing works

Cholesterol modulates membrane traffic along the endocytic pathway in sphingolipid-storage diseases

Puri, V., Watanabe, R., Dominguez, M., Sun, X., Wheatley, C. L., Marks, D. L., & Pagano, R. E. (1999) · Nature Cell Biology · doi:10.1038/14084 · Cited by 289 · see citing works

Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins

Bhakdi, S., Bayley, H., Valeva, A., Walev, I., Walker, B., Weller, U., Kehoe, M., & Palmer, M. (1996) · Archives of Microbiology · doi:10.1007/s002030050300 · Cited by 288 · see citing works

Penetration of protein toxins into cells

Falnes, P. Ø., & Sandvig, K. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00109-5 · Cited by 264 · see citing works

Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria

Kenny, B., & Jepson, M. A. (2000) · Cellular Microbiology · doi:10.1046/j.1462-5822.2000.00082.x · Cited by 257 · see citing works

Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives

Sandvig, K., & van Deurs, B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.5943 · Cited by 256 · see citing works

Membrane traffic and the cellular uptake of cholera toxin

Lencer, W. I., Hirst, T. R., & Holmes, R. K. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00070-1 · Cited by 246 · see citing works

A Pore-forming Toxin Interacts with a GPI-anchored Protein and Causes Vacuolation of the Endoplasmic Reticulum

Abrami, L., Fivaz, M. L., Glauser, P.-E., Parton, R. G., & van der Goot, F. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.3.525 · Cited by 216 · see citing works

Ganglioside Structure Dictates Signal Transduction by Cholera Toxin and Association with Caveolae-like Membrane Domains in Polarized Epithelia

Wolf, A. A., Jobling, M. G., Wimer-Mackin, S., Ferguson-Maltzman, M., Madara, J., Holmes, R. K., & Lencer, W. I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.917 · Cited by 213 · see citing works

Glycosylphosphatidylinositol Anchors of Membrane Glycoproteins Are Binding Determinants for the Channel-forming Toxin Aerolysin

Diep, D. B., Nelson, K. L., Raja, S. M., Pleshak, E. N., & Buckley, J. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.2355 · Cited by 186 · see citing works

Cellular Microbiology Emerging

Cossart, P., Boquet, P., Normark, S. J., & Rappuoli, R. (1996) · Science · doi:10.1126/science.271.5247.315 · Cited by 172 · see citing works

[5] A bacterial two-hybrid system that exploits a cAMP signaling cascade in Escherichia coli

Karimova, G., Ullmann, A., & Ladant, D. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)28390-0 · Cited by 165 · see citing works

The N-Terminal Part of the Enzyme Component (C2I) of the Binary Clostridium botulinum C2 Toxin Interacts with the Binding Component C2II and Functions as a Carrier System for a Rho ADP-Ribosylating C3-Like Fusion Toxin

Barth, H., Hofmann, F., Olenik, C., Just, I., & Aktories, K. (1998) · Infection and Immunity · doi:10.1128/iai.66.4.1364-1369.1998 · Cited by 157 · see citing works

Expression of Neutral Sphingomyelinase Identifies a Distinct Pool of Sphingomyelin Involved in Apoptosis

Zhang, P., Liu, B., Jenkins, G. M., Hannun, Y. A., & Obeid, L. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9609 · Cited by 153 · see citing works

Pathogenesis and Immunity in Pertussis

Lenton, S. (1989) · Archives of Disease in Childhood · doi:10.1136/adc.64.4.640-b · Cited by 151 · see citing works

Targeting of the pro‐apoptotic VDAC‐like porin (PorB) of Neisseria gonorrhoeae to mitochondria of infected cells

Mueller, A., Günther, D., Brinkmann, V., Hurwitz, R., Meyer, T. F., & Rudel, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5332 · Cited by 137 · see citing works

Adventures of a pore-forming toxin at the target cell surface

Abrami, L., Fivaz, M. L., & BRINK, G. R. V. D. (2000) · Trends in Microbiology · doi:10.1016/s0966-842x(00)01722-4 · Cited by 136 · see citing works

The B Subunit of Shiga Toxin Fused to a Tumor Antigen Elicits CTL and Targets Dendritic Cells to Allow MHC Class I-Restricted Presentation of Peptides Derived from Exogenous Antigens

Haicheur, N., Bismuth, E., Bosset, S., Adotévi, O., Warnier, G., Lacabanne, V., Régnault, A., Desaymard, C., Amigorena, S., Ricciardi‐Castagnoli, P., et al. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.6.3301 · Cited by 131 · see citing works

Binding and Transcytosis of Botulinum Neurotoxin by Polarized Human Colon Carcinoma Cells

Maksymowych, A. B., & Simpson, L. L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21950 · Cited by 125 · see citing works

Pathogenesis and immunity in pertussis

Wardlaw, A. C., & Parton, R. (1988) · Wiley eBooks · Cited by 117 · see citing works

Activation of Rho through a cross‐link with polyamines catalyzed by Bordetella dermonecrotizing toxin

Masuda, M., Betancourt, L. H., Matsuzawa, T., Kashimoto, T., Takao, T., Shimonishi, Y., & Horiguchi, Y. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.521 · Cited by 113 · see citing works

Cellular Internalization of Cytolethal Distending Toxin fromHaemophilus ducreyi

Cortes-Bratti, X., Chaves‐Olarte, E., Lagergård, T., & Thelestam, M. (2000) · Infection and Immunity · doi:10.1128/iai.68.12.6903-6911.2000 · Cited by 109 · see citing works

Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho

Horiguchi, Y., Inoue, N., Masuda, M., Kashimoto, T., Katahira, J., Sugimoto, N., & Matsuda, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11623 · Cited by 107 · see citing works

The 27-kD diphtheria toxin receptor-associated protein (DRAP27) from vero cells is the monkey homologue of human CD9 antigen: expression of DRAP27 elevates the number of diphtheria toxin receptors on toxin-sensitive cells.

Mitamura, T., Iwamoto, R., Umata, T., Yomo, T., Urabe, I., Tsuneoka, M., & Mekada, E. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.118.6.1389 · Cited by 106 · see citing works

A Novel C3-like ADP-ribosyltransferase fromStaphylococcus aureus Modifying RhoE and Rnd3

Wilde, C., Chhatwal, G. S., Schmalzing, G., Aktories, K., & Just, I. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011035200 · Cited by 90 · see citing works

Targeting HIV proteins to the major histocompatibility complex class I processing pathway with a novel gp120-anthrax toxin fusion protein

Goletz, T. J., Klimpel, K. R., Arora, N., Leppla, S. H., Keith, J. M., & Berzofsky, J. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.12059 · Cited by 89 · see citing works

Postsynaptic expression of tetanus toxin light chain blocks synaptogenesis in Drosophila

Baines, R., Robinson, S. G., Fujioka, M., Jaynes, J. B., & Bate, M. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80510-7 · Cited by 88 · see citing works

Subcytocidal Attack by Staphylococcal Alpha-Toxin Activates NF-κB and Induces Interleukin-8 Production

Dragneva, Y., Anuradha, C. D., Valeva, A., Hoffmann, A., Bhakdi, S., & Husmann, M. (2001) · Infection and Immunity · doi:10.1128/iai.69.4.2630-2635.2001 · Cited by 80 · see citing works

Delivery of Recombinant Tetanus–Superoxide Dismutase Proteins to Central Nervous System Neurons by Retrograde Axonal Transport

Figueiredo, D. M. M., Hallewell, R. A., Chen, L. L., Fairweather, N. F., Gordon Dougan, B., Savitt, J. M., Parks, D. A., & Fishman, P. S. (1997) · Experimental Neurology · doi:10.1006/exnr.1997.6490 · Cited by 78 · see citing works

Aerolysin Induces G-protein Activation and Ca2+Release from Intracellular Stores in Human Granulocytes

Krause, K., Fivaz, M. L., Monod, A., & van der Goot, F. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18122 · Cited by 75 · see citing works

Identification of the C-terminal Part of BordetellaDermonecrotic Toxin as a Transglutaminase for Rho GTPases

Schmidt, G., Goehring, U.-M., Schirmer, J., Lerm, M., & Aktories, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.31875 · Cited by 74 · see citing works

Bacterial toxins : tools in cell biology and pharmacology

Aktories, K. (1997) · Chapman & Hall eBooks · Cited by 72 · see citing works

Direct Delivery of the Bordetella pertussis Adenylate Cyclase Toxin to the MHC Class I Antigen Presentation Pathway

Guermonprez, P., Ladant, D., Karimova, G., Ullmann, A., & Leclerc, C. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.4.1910 · Cited by 68 · see citing works

Microbial toxins and the glycosylation of Rho family GTPases

Busch, C., & Aktories, K. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00126-3 · Cited by 67 · see citing works

Toxins from anaerobic bacteria: specificity and molecular mechanisms of action

Boquet, P., Munro, P. M., Fiorentini, C., & Just, I. (1998) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(98)80144-6 · Cited by 51 · see citing works

Facing Inward from Compartment Shores: How Many Pathways were we Looking For?

Johannes, L., & Goud, B. (2000) · Traffic · doi:10.1034/j.1600-0854.2000.010204.x · Cited by 48 · see citing works

Intranuclear delivery of an antiviral peptide mediated by the B subunit of Escherichia coli heat-labile enterotoxin

Loregian, A., Papini, E., Satin, B., Marsden, H. S., Hirst, T. R., & Palù, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.5221 · Cited by 42 · see citing works

Phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis as a probe for the distribution of phosphatidylinositol in hepatocyte membranes

Higgins, J. A., HITCHIN, B. W., & Low, M. G. (1989) · Biochemical Journal · doi:10.1042/bj2590913 · Cited by 33 · see citing works

Receptor-mediated uptake of an extracellular Bcl-x L fusion protein inhibits apoptosis

Liu, X.-H., Castelli, J. C., & Youle, R. J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9563 · Cited by 21 · see citing works

Selection of Mammalian Cell Mutants in Sphingolipid Biosynthesis

Hanada, K., & Nishijima, M. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)12917-9 · Cited by 18 · see citing works

Clostridial Toxins and Endocrine Secretion: Their Use in Insulin‐Secreting Cells

Lang, J., Regazzi, R., & Wollheim, C. B. (1997) · doi:10.1002/9783527614615.ch16 · Cited by 15 · see citing works

Clostridial Neurotoxins

Schiavo, G., & Montecucco, C. (1997) · Wiley eBooks · doi:10.1002/9783527614615.ch14 · Cited by 12 · see citing works

Anti-virulence strategies to combat bacteria-mediated disease

Rasko, D. A., & Sperandio, V. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3013 · Cited by 1,383 · see citing works

Furin at the cutting edge: From protein traffic to embryogenesis and disease

Thomas, G. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm934 · Cited by 1,222 · see citing works

Pathogenicity Islands in BacterialPathogenesis

Schmidt, H., & Hensel, M. (2004) · Clinical Microbiology Reviews · doi:10.1128/cmr.17.1.14-56.2004 · Cited by 776 · see citing works

Helicobacter pylori VacA, a paradigm for toxin multifunctionality

Cover, T. L., & Blanke, S. R. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1095 · Cited by 569 · see citing works

Plasma Membrane Disruption: Repair, Prevention, Adaptation

McNeil, P. L., & Steinhardt, R. A. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.140101 · Cited by 489 · see citing works

Rab5 and Rab7 Control Endocytic Sorting along the Axonal Retrograde Transport Pathway

Deinhardt, K., Salinas, S., Verastegui, C., Watson, R., Worth, D. C., Hanrahan, S. J., Bucci, C., & Schiavo, G. (2006) · Neuron · doi:10.1016/j.neuron.2006.08.018 · Cited by 466 · see citing works

A mechanism of cell death involving an adenylyl cyclase/PKA signaling pathway is induced by the Cry1Ab toxin of Bacillus thuringiensis

Zhang, X., Candas, M., Griko, N. B., Taussig, R., & Bulla, L. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604017103 · Cited by 408 · see citing works

Interactions of Methicillin Resistant Staphylococcus aureus USA300 and Pseudomonas aeruginosa in Polymicrobial Wound Infection

Pastar, I., Nusbaum, A. G., Gil, J., Patel, S. B., Chen, J., Valdes, J., Stojadinovic, O., Plano, L. R., Tomic-Canic, M., & Davis, S. C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056846 · Cited by 391 · see citing works

Nanoparticle-based local antimicrobial drug delivery

Gao, W., Chen, Y., Zhang, Y., Zhang, Q., & Zhang, L. (2017) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2017.09.015 · Cited by 404 · see citing works

Antibiotic Adjuvants: Diverse Strategies for Controlling Drug‐Resistant Pathogens

Gill, E. E., Franco, O. L., & Hancock, R. E. W. (2014) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12478 · Cited by 322 · see citing works

Glycointeractions in bacterial pathogenesis

Poole, J., Day, C. J., von Itzstein, M., Paton, J. C., & Jennings, M. P. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0007-2 · Cited by 273 · see citing works

The journey of tetanus and botulinum neurotoxins in neurons

Lalli, G., Bohnert, S., Deinhardt, K., Verastegui, C., & Schiavo, G. (2003) · Trends in Microbiology · doi:10.1016/s0966-842x(03)00210-5 · Cited by 231 · see citing works

Large clostridial cytotoxins

Just, I., & Gerhard, R. (2004) · Springer eBooks · doi:10.1007/s10254-004-0033-5 · Cited by 219 · see citing works

Membrane Traffic Exploited by Protein Toxins

Sandvig, K., & van Deurs, B. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.011502.142107 · Cited by 218 · see citing works

Cytotoxicity of Bacillus thuringiensis Cry1Ab toxin depends on specific binding of the toxin to the cadherin receptor BT-R1 expressed in insect cells

Zhang, X., Candas, M., Griko, N. B., Rose-Young, L., & Bulla, L. A. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401675 · Cited by 200 · see citing works

Molecular and Cellular Mechanisms of Ectodomain Shedding

Hayashida, K., Bartlett, A. H., Chen, Y., & Park, P. W. (2010) · The Anatomical Record · doi:10.1002/ar.20757 · Cited by 198 · see citing works

PathoFact: a pipeline for the prediction of virulence factors and antimicrobial resistance genes in metagenomic data

de Nies, L., Lopes, S., Busi, S. B., Galata, V., Heintz‐Buschart, A., Laczny, C. C., May, P., & Wilmes, P. (2021) · Microbiome · doi:10.1186/s40168-020-00993-9 · Cited by 186 · see citing works

Protective role of autophagy against <i>Vibrio cholerae</i> cytolysin, a pore-forming toxin from <i>V. cholerae</i>

Gutierrez, M. G., Saka, H. A., Chinen, I., Zoppino, F. C. M., Yoshimori, T., Bocco, J. L., & Colombo, M. I. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601437104 · Cited by 174 · see citing works

Pore formation: An ancient yet complex form of attack

Iacovache, I., van der Goot, F. G., & Pernot, L. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.01.026 · Cited by 170 · see citing works

Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome

Hanakawa, Y., Schechter, N. M., Lin, C., Garza, L. A., Li, H., Yamaguchi, T., Fudaba, Y., Nishifuji, K., Sugai, M., Amagai, M., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215766 · Cited by 164 · see citing works

Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome

Hanakawa, Y., Schechter, N. M., Lin, C., Garza, L. A., Li, H., Yamaguchi, T., Fudaba, Y., Nishifuji, K., Sugai, M., Amagai, M., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15766 · Cited by 162 · see citing works

Probing the Endocytic Pathway in Live Cells Using Dual-Color Fluorescence Cross-Correlation Analysis

Bacia, K., Majoul, I. V., & Schwille, P. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75242-9 · Cited by 161 · see citing works

Clostridial Glucosylating Toxins Enter Cells via Clathrin-Mediated Endocytosis

Papatheodorou, P., Zamboglou, C., Genisyuerek, S., Guttenberg, G., & Aktories, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010673 · Cited by 160 · see citing works

GTPase activating proteins: structural and functional insights 18 years after discovery

Scheffzek, K., & Ahmadian, M. R. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5136-x · Cited by 154 · see citing works

Bacterial virulence factors targeting Rho GTPases: parasitism or symbiosis?

Boquet, P., & Lemichez, E. (2003) · Trends in Cell Biology · doi:10.1016/s0962-8924(03)00037-0 · Cited by 153 · see citing works

A Common Structural Motif in the Binding of Virulence Factors to Bacterial Secretion Chaperones

Lilić, M., Vujanac, M., & Stebbins, C. E. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.026 · Cited by 141 · see citing works

Pathways followed by protein toxins into cells

Sandvig, K., Spilsberg, B., Lauvrak, S. U., Torgersen, M. L., Iversen, T., & van Deurs, B. O. (2004) · International Journal of Medical Microbiology · doi:10.1078/1438-4221-00294 · Cited by 130 · see citing works

Reactive Oxygen Species Mediate Met Receptor Transactivation by G Protein-coupled Receptors and the Epidermal Growth Factor Receptor in Human Carcinoma Cells

Fischer, O. M., Giordano, S., Comoglio, P. M., & Ullrich, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402508200 · Cited by 126 · see citing works

CAT-8015: A Second-Generation Pseudomonas Exotoxin A–Based Immunotherapy Targeting CD22-Expressing Hematologic Malignancies

Alderson, R. F., Kreitman, R. J., Chen, T., Yeung, P., Herbst, R., Fox, J. A., & Pastan, I. H. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1456 · Cited by 104 · see citing works

Bacterial subversion of lipid rafts

Lafont, F. (2004) · Current Opinion in Microbiology · doi:10.1016/j.mib.2003.12.007 · Cited by 103 · see citing works

Sustainable Approaches to Controlling Plant Pathogenic Bacteria

Kannan, V. R., & Bastas, K. K. (2015) · CRC Press eBooks · doi:10.1201/b18892 · Cited by 99 · see citing works

Role of bacteria in carcinogenesis, with special reference to carcinoma of the gallbladder

Nath, G. (2010) · World Journal of Gastroenterology · doi:10.3748/wjg.v16.i43.5395 · Cited by 93 · see citing works

Cholera Toxin Entry into Pig Enterocytes Occurs via a Lipid Raft- and Clathrin-Dependent Mechanism

Hansen, G. H., Dalskov, S., Rasmussen, C. R., Immerdal, L., Niels-Christiansen, L.-L., & Danielsen, E. M. (2004) · Biochemistry · doi:10.1021/bi047959+ · Cited by 78 · see citing works

DBETH: A Database of Bacterial Exotoxins for Human

Chakraborty, A., Ghosh, S., Chowdhary, G., Maulik, U., & Chakrabarti, S. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr942 · Cited by 71 · see citing works

Opportunities and challenges in managing antibiotic resistance in bacteria using plant secondary metabolites

Kongkham, B., Duraivadivel, P., & Hariprasad, P. (2020) · Fitoterapia · doi:10.1016/j.fitote.2020.104762 · Cited by 71 · see citing works

Targeting Bacterial Toxins

Ivarsson, M. E., Leroux, J., & Castagner, B. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201104384 · Cited by 70 · see citing works

Discovery of novel bacterial toxins by genomics and computational biology

Doxey, A. C., Mansfield, M. J., & Montecucco, C. (2018) · Toxicon · doi:10.1016/j.toxicon.2018.02.002 · Cited by 67 · see citing works

Needle in the haystack: structure-based toxin discovery

Fieldhouse, R. J., & Merrill, A. R. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2008.08.003 · Cited by 64 · see citing works

A Novel Non-Lens βγ−Crystallin and Trefoil Factor Complex from Amphibian Skin and Its Functional Implications

Liu, S., He, Y., Zhang, Y., Lee, W.-H., Qian, J., Lai, R., & Jin, Y. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001770 · Cited by 64 · see citing works

Toxin secretion and trafficking by Mycobacterium tuberculosis

Pajuelo, D., Tak, U., Zhang, L., Danilchanka, O., Tischler, A. D., & Niederweis, M. (2021) · Nature Communications · doi:10.1038/s41467-021-26925-1 · Cited by 63 · see citing works

Hijacking Rho GTPases by protein toxins and apoptosis: molecular strategies of pathogenic bacteria

Fiorentini, C., Falzano, L., Travaglione, S., & Fabbri, A. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401151 · Cited by 63 · see citing works

Biology of Lysenin, a Protein in the Coelomic Fluid of the Earthworm Eisenia foetida

Kobayashi, H., Ohta, N., & Umeda, M. (2004) · International review of cytology · doi:10.1016/s0074-7696(04)36002-x · Cited by 63 · see citing works

Analysis of lectin binding to glycolipid complexes using combinatorial glycoarrays

Rinaldi, S., Brennan, K. M., Goodyear, C. S., O’Leary, C., Schiavo, G., Crocker, P. R., & Willison, H. J. (2009) · Glycobiology · doi:10.1093/glycob/cwp049 · Cited by 61 · see citing works

Pasteurella multocida toxin as a tool for studying Gq signal transduction

Wilson, B. A., & Ho, M. (2004) · Springer eBooks · doi:10.1007/s10254-004-0032-6 · Cited by 58 · see citing works

Cholera- and Anthrax-Like Toxins Are among Several New ADP-Ribosyltransferases

Fieldhouse, R. J., Turgeon, Z. J., White, D., & Merrill, A. R. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1001029 · Cited by 57 · see citing works

Exploring the potential of phytochemicals and nanomaterial: A boon to antimicrobial treatment

Yadav, H., Mahalvar, A., Pradhan, M., Yadav, D. K., Sahu, K. K., & Yadav, R. (2023) · Medicine in Drug Discovery · doi:10.1016/j.medidd.2023.100151 · Cited by 62 · see citing works

Exploitation of the endoplasmic reticulum by bacterial pathogens

Roy, C. R. (2002) · Trends in Microbiology · doi:10.1016/s0966-842x(02)02421-6 · Cited by 56 · see citing works

Putting on the brakes: Bacterial impediment of wound healing

Brothers, K. M., Stella, N. A., Hunt, K. M., Romanowski, E. G., Liu, X., Klarlund, J. K., & Shanks, R. M. Q. (2015) · Scientific Reports · doi:10.1038/srep14003 · Cited by 55 · see citing works

Evolutionary Features in the Structure and Function of Bacterial Toxins

Kumar, P., Feltrup, T. M., Kukreja, R. V., Patel, K. B., Cai, S., & Singh, B. R. (2019) · Toxins · doi:10.3390/toxins11010015 · Cited by 55 · see citing works

Getting muscles moving again after botulinum toxin: novel therapeutic challenges

Foran, P., Davletov, B. A., & Meunier, F. A. (2003) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(03)00113-8 · Cited by 55 · see citing works

ER-Golgi-localized proteins TMED2 and TMED10 control the formation of plasma membrane lipid nanodomains

Anwar, M. U., Sergeeva, O. A., Abrami, L., Mesquita, F. S., Lukonin, I., Amen, T., Chuat, A., Capolupo, L., Liberali, P., D’Angelo, G., et al. (2022) · Developmental Cell · doi:10.1016/j.devcel.2022.09.004 · Cited by 53 · see citing works

Anthrax toxin triggers the activation of src -like kinases to mediate its own uptake

Abrami, L., Kunz, B., & van der Goot, F. G. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910782107 · Cited by 53 · see citing works

Identification of Compounds with Bioactivity against the Nematode Caenorhabditis elegans by a Screen Based on the Functional Genomics of the Marine Bacterium Pseudoalteromonas tunicata D2

Ballestriero, F., Thomas, T., Burke, C., Egan, S., & Kjelleberg, S. J. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00695-10 · Cited by 53 · see citing works

The Rho-activating CNF1 toxin from pathogenic E. coli: A risk factor for human cancer development?

Travaglione, S., Fabbri, A., & Fiorentini, C. (2008) · Infectious Agents and Cancer · doi:10.1186/1750-9378-3-4 · Cited by 52 · see citing works

Regulation of SNARE-Mediated Membrane Fusion during Exocytosis

McNew, J. A. (2008) · Chemical Reviews · doi:10.1021/cr0782325 · Cited by 51 · see citing works

Why All the Fury over Furin?

Osman, E. E. A., Rehemtulla, A., & Neamati, N. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00518 · Cited by 51 · see citing works

Conformational dynamics of actin: Effectors and implications for biological function

Hild, G., Bugyi, B., & Nyitrai, M. (2010) · Cytoskeleton · doi:10.1002/cm.20473 · Cited by 46 · see citing works

Pore-forming Esx proteins mediate toxin secretion by Mycobacterium tuberculosis

Tak, U., Dokland, T., & Niederweis, M. (2021) · Nature Communications · doi:10.1038/s41467-020-20533-1 · Cited by 45 · see citing works

Caveolin-1 binding motif of α-hemolysin: its role in stability and pore formation

Pany, S., Vijayvargia, R., & Krishnasastry, M. V. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.07.073 · Cited by 45 · see citing works

Adhesion-related Kinase Repression of Gonadotropin-releasing Hormone Gene Expression Requires Rac Activation of the Extracellular Signal-regulated Kinase Pathway

Allen, M. P., Xu, M., Linseman, D. A., Pawlowski, J. E., Bokoch, G., Heidenreich, K. A., & Wierman, M. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200826200 · Cited by 45 · see citing works

The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics

Emery, G., Parton, R. G., Rojo, M., & Gruenberg, J. E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00802 · Cited by 44 · see citing works

Polymer antidotes for toxin sequestration

Weisman, A. C., Chou, B., O'Brien, J., & Shea, K. J. (2015) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.05.011 · Cited by 43 · see citing works

The Vibrio cholerae haemolysin anion channel is required for cell vacuolation and death

Moschioni, M., Tombola, F., de Bernard, M., Coelho, A., Zitzer, A. O., Zoratti, M., & Montecucco, C. (2002) · Cellular Microbiology · doi:10.1046/j.1462-5822.2002.00199.x · Cited by 42 · see citing works

The Elusive Compass of Clostridial Neurotoxins: Deciding When and Where to Go?

Bercsényi, K., Giribaldi, F., & Schiavo, G. (2012) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-33570-9_5 · Cited by 40 · see citing works

Knockin’ on heaven’s door: Molecular mechanisms of neuronal tau uptake

La‐Rocque, S. D., Moretto, E., Butnaru, I., & Schiavo, G. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15144 · Cited by 42 · see citing works

Shiga Toxins: Intracellular Trafficking to the ER Leading to Activation of Host Cell Stress Responses

Lee, M., Cherla, R. P., & Tesh, V. L. (2010) · Toxins · doi:10.3390/toxins2061515 · Cited by 38 · see citing works

Transport of Bacterial Toxins into Target Cells: Pathways Followed by Cholera Toxin and Botulinum Progenitor Toxin

Fujinaga, Y. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj161 · Cited by 36 · see citing works

Recent Insights into Pasteurella Multocida Toxin and Other G-Protein-Modulating Bacterial Toxins

Wilson, B. A., & Ho, M. (2010) · Future Microbiology · doi:10.2217/fmb.10.91 · Cited by 35 · see citing works

Entry of Oomycete and Fungal Effectors into Host Cells

Tyler, B. M. (2011) · doi:10.1002/9781119949138.ch10 · Cited by 33 · see citing works

Defense and death responses to pore forming toxins

Cancino-Rodezno, A., Porta, H., Soberón, M., & Bravo, A. (2009) · Biotechnology and Genetic Engineering Reviews · doi:10.5661/bger-26-65 · Cited by 32 · see citing works

Chromosomal and Plasmid-Encoded Factors of Shigella flexneri Induce Secretogenic Activity Ex Vivo

Faherty, C. S., Harper, J. M., Shea‐Donohue, T., Barry, E. M., Kaper, J. B., Fasano, A., & Nataro, J. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049980 · Cited by 32 · see citing works

The janus faces of botulinum neurotoxin: Sensational medicine and deadly biological weapon

Osborne, S. L., Latham, C. F., Wen, P. J., Cavaignac, S. M., Fanning, J. P., Foran, P., & Meunier, F. A. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21171 · Cited by 31 · see citing works

Identification and characterization of the Pasteurella multocida toxin translocation domain

Baldwin, M. R., Lakey, J. H., & Lax, A. J. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04264.x · Cited by 30 · see citing works

Macromolecular Nanotherapeutics and Antibiotic Adjuvants to Tackle Bacterial and Fungal Infections

Dey, R. K., Mukherjee, S., Barman, S., & Haldar, J. (2021) · Macromolecular Bioscience · doi:10.1002/mabi.202100182 · Cited by 28 · see citing works

Lipid Microdomain‐Dependent Macropinocytosis Determines Compartmentation of Afipia felis

Schneider, B. E., Schueller, C., Utermöhlen, O., & Haas, A. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00525.x · Cited by 28 · see citing works

Intracellular pathogens in membrane interactions and vacuole biogenesis

Gorvel, J. (2004) · Cited by 27 · see citing works

Bacillus anthracis lethal toxin negatively modulates ILC3 function through perturbation of IL-23-mediated MAPK signaling

Seshadri, S., Allan, D., Carlyle, J. R., & Zenewicz, L. A. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006690 · Cited by 26 · see citing works

Combinatorial Glycoarray

Rinaldi, S., Brennan, K. M., & Willison, H. J. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-373-8_28 · Cited by 25 · see citing works

Measurement of the Binding of Cholera Toxin to GM1 Gangliosides on Solid Supported Lipid Bilayer Vesicles and Inhibition by Europium (III) Chloride

Williams, T. L., & Jenkins, A. T. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja710543x · Cited by 25 · see citing works

Endocytosing the death sentence

Griffiths, G. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212143 · Cited by 25 · see citing works

Bacterial toxins induce non-canonical migracytosis to aggravate acute inflammation

Li, D., Yang, Q., Luo, J., Xu, Y., Li, J., & Tao, L. (2024) · Cell Discovery · doi:10.1038/s41421-024-00729-1 · Cited by 24 · see citing works

Heteromeric glycolipid complexes as modulators of autoantibody and lectin binding

Rinaldi, S., Brennan, K. M., & Willison, H. J. (2009) · Progress in Lipid Research · doi:10.1016/j.plipres.2009.09.001 · Cited by 23 · see citing works

Human α-Defensin-5 Efficiently Neutralizes Clostridioides difficile Toxins TcdA, TcdB, and CDT

Korbmacher, M., Fischer, S., Landenberger, M., Papatheodorou, P., Aktories, K., & Barth, H. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01204 · Cited by 22 · see citing works

The Draft Genome Sequence of the Yersinia entomophaga Entomopathogenic Type Strain MH96T

Hurst, C. J., Beattie, A. K., Altermann, E., Moraga, R., Harper, L., Calder, J., & Laugraud, A. (2016) · Toxins · doi:10.3390/toxins8050143 · Cited by 21 · see citing works

Targeting Gi/o protein–coupled receptor signaling blocks HER2-induced breast cancer development and enhances HER2-targeted therapy

Lyu, C., Ye, Y., Lensing, M., Wagner, K., Weigel, R. J., & Chen, S. (2021) · JCI Insight · doi:10.1172/jci.insight.150532 · Cited by 19 · see citing works

Bacillus cereus Certhrax ADP-ribosylates Vinculin to Disrupt Focal Adhesion Complexes and Cell Adhesion

Simon, N. C., & Barbieri, J. T. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.500710 · Cited by 19 · see citing works

Structural insights into bacterial modulation of the host cytoskeleton

Stebbins, C. E. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.09.011 · Cited by 19 · see citing works

Bordetella pertussis adenylate cyclase toxin: a versatile screening tool

Dautin, N., Karimova, G., & Ladant, D. (2002) · Toxicon · doi:10.1016/s0041-0101(02)00158-7 · Cited by 18 · see citing works

Interplay of bacterial toxins with host defence: Molecular mechanisms of immunomodulatory signalling

Backert, S., & König, W. (2005) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2005.06.011 · Cited by 18 · see citing works

Acute toxicity of βγ-CAT, a naturally existing non-lens βγ-crystallin and trefoil factor complex from frog Bombina maxima skin secretions

Qian, J., Liu, S., He, Y., Lee, W.-H., & Zhang, Y. (2008) · Toxicon · doi:10.1016/j.toxicon.2008.05.007 · Cited by 17 · see citing works

Peptide inhibitors of botulinum neurotoxin by mRNA display

Yiadom, K., Muhie, S. Y., & Yang, D. C. H. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.196 · Cited by 16 · see citing works

Discovery of Inhibitors of Shiga Toxin Type 2 by On‐Plate Generation and Screening of a Focused Compound Library

Dasgupta, S., Kitov, P. I., Sadowska, J. M., & Bundle, D. R. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201309436 · Cited by 15 · see citing works

Moving across membranes

Neale, E. A. (2002) · Nature Structural Biology · doi:10.1038/nsb0103-2 · Cited by 15 · see citing works

Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome

Hanakawa, Y., Schechter, N. M., Lin, C., Garza, L. A., Li, H., Yamaguchi, T., Fudaba, Y., Nishifuji, K., Sugai, M., Amagai, M., et al. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215766 · Cited by 15 · see citing works

Assessing the relationship between the gut microbiota and growth traits in Chinese indigenous pig breeds

Zhou, M., Wu, L., Sun, X., Liu, M., Wang, Y., Yang, B. J., Ai, H., Chen, C., & Huang, L. (2025) · BMC Veterinary Research · doi:10.1186/s12917-025-04739-3 · Cited by 13 · see citing works

ExoSloNano: multimodal nanogold labels for identification of macromolecules in live cells and cryo-electron tomograms

Young, L. N., Sherrard, A., Zhou, H., Shaikh, F., Hutchings, J., Riggi, M., Narasimhan, M., Flaherty, W. A., Bennett, E. J., Rosen, M. K., et al. (2025) · Nature Methods · doi:10.1038/s41592-025-02928-4 · Cited by 12 · see citing works

Transport of Toxins across Intracellular Membranes

Sandvig, K. (2014) · ASM Press eBooks · doi:10.1128/9781555817893.ch11 · Cited by 12 · see citing works

Microbial influences on hormesis, oncogenesis, and therapy: A review of the literature

Clanton, R., Saucier, D., Ford, J. R., & Akabani, G. (2015) · Environmental Research · doi:10.1016/j.envres.2015.06.026 · Cited by 11 · see citing works

Plant Pathogenic Bacteria: An Overview

Kannan, V. R., Baştaş, K. K., & Antony, R. (2015) · CRC Press eBooks · doi:10.1201/b18892-2 · Cited by 11 · see citing works

Structural features common to intracellularly acting toxins from bacteria

Ménétrey, J., Gillet, D., & Ménèz, A. (2004) · Toxicon · doi:10.1016/j.toxicon.2004.09.004 · Cited by 11 · see citing works

Bakterijski toksini i njihova primjena

Sukser, V. (2011)

Bacterial Protein Toxins as Tools in Cell Biology and Physiology

Lemichez, E., Paillares, E., Orth, K., & Kaval, K. G. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00224-8

Bacterial toxins: Offensive, defensive, or something else altogether?

Rudkin, J., McLoughlin, R. M., Preston, A., & Massey, R. C. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006452 · Cited by 82 · see citing works

Cellular microbiology: Bacterial toxin interference drives understanding of eukaryotic cell function

Lemichez, E., Popoff, M. R., & Satchell, K. J. F. (2020) · Cellular Microbiology · doi:10.1111/cmi.13178 · Cited by 5 · see citing works

Synopses Bacterial Toxins: Friends or Foes?

Schmitt, C. K., Meysick, K. C., & O’brien, A. D. (2013)