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Intracellular Trafficking and Translocation of Pertussis Toxin

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1006/jmbi.1996.0277openalex-snapshot

Crystal Structure of the Pertussis Toxin–ATP Complex: A Molecular Sensor

inferredcites →https://doi.org/10.1007/82_2016_14openalex-snapshot

Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins

inferredcites →https://doi.org/10.1007/978-3-319-21687-4openalex-snapshot

Physical Biology of Proteins and Peptides

inferredcites →https://doi.org/10.1007/s00210-010-0581-yopenalex-snapshot

Exploring the role of host cell chaperones/PPIases during cellular up-take of bacterial ADP-ribosylating toxins as basis for novel pharmacological strategies to protect mammalian cells against these virulence factors

inferredcites →https://doi.org/10.1016/0006-291x(89)91660-4openalex-snapshot

Domain-specific bias in arginine/lysine usage by protein toxins

inferredcites →https://doi.org/10.1016/0014-5793(94)80122-3openalex-snapshot

Structure and stability of pertussis toxin studied by in situ atomic force microscopy

inferredcites →https://doi.org/10.1016/0092-8674(84)90008-4openalex-snapshot

Inhibition of receptor-mediated release of arachidonic acid by pertussis toxin

inferredcites →https://doi.org/10.1016/j.bbamcr.2013.06.031openalex-snapshot

Protein quality control and elimination of protein waste: The role of the ubiquitin–proteasome system

inferredcites →https://doi.org/10.1016/j.bbamem.2010.06.025openalex-snapshot

Protein dislocation from the ER

inferredcites →https://doi.org/10.1016/j.cellsig.2004.11.008openalex-snapshot

Pertussis toxin-sensitive Gi/o proteins are involved in nerve growth factor-induced pro-survival Akt signaling cascade in PC12 cells

inferredcites →https://doi.org/10.1016/j.febslet.2009.10.075openalex-snapshot

Multiple routes of protein transport from endosomes to the trans Golgi network

inferredcites →https://doi.org/10.1016/j.jmb.2007.12.075openalex-snapshot

Order–Disorder–Order Transitions Mediate the Activation of Cholera Toxin

inferredcites →https://doi.org/10.1016/j.semcdb.2014.04.011openalex-snapshot

The role of the cytoskeleton and molecular motors in endosomal dynamics

inferredcites →https://doi.org/10.1016/s0006-3495(93)81035-xopenalex-snapshot

Cellular motions and thermal fluctuations: the Brownian ratchet

inferredcites →https://doi.org/10.1016/s0021-9258(17)31296-6openalex-snapshot

Role of Cysteine 41 of the A Subunit of Pertussis Toxin

inferredcites →https://doi.org/10.1016/s0021-9258(17)35664-8openalex-snapshot

Adenine nucleotides promote dissociation of pertussis toxin subunits.

inferredcites →https://doi.org/10.1016/s0021-9258(17)36219-1openalex-snapshot

Amino acid-specific ADP-ribosylation. Sensitivity to hydroxylamine of [cysteine(ADP-ribose)]protein and [arginine(ADP-ribose)]protein linkages.

inferredcites →https://doi.org/10.1016/s0021-9258(17)43911-1openalex-snapshot

Pertussis toxin. Affinity purification of a new ADP-ribosyltransferase.

inferredcites →https://doi.org/10.1016/s0021-9258(17)44314-6openalex-snapshot

Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein).

inferredcites →https://doi.org/10.1016/s0021-9258(18)32285-3openalex-snapshot

A role of the B-oligomer moiety of islet-activating protein, pertussis toxin, in development of the biological effects on intact cells.

inferredcites →https://doi.org/10.1016/s0021-9258(18)68358-9openalex-snapshot

Use of glycosyltransferases to restore pertussis toxin receptor activity to asialoagalactofetuin.

inferredcites →https://doi.org/10.1016/s0021-9258(18)68870-2openalex-snapshot

Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein.

inferredcites →https://doi.org/10.1016/s0021-9258(18)83361-0openalex-snapshot

Alkylation of Cysteine 41, but Not Cysteine 200, Decreases the ADP-ribosytransferase Activity of the S1 Subunit of Pertussis Toxin

inferredcites →https://doi.org/10.1016/s0021-9258(19)50622-6openalex-snapshot

Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94.

inferredcites →https://doi.org/10.1016/s0021-9258(19)81393-5openalex-snapshot

Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum.

inferredcites →https://doi.org/10.1016/s0171-9335(98)80067-8openalex-snapshot

At reduced temperature, endocytic membrane traffic is blocked in multivesicular carrier endosomes in rat cardiac myocytes

inferredcites →https://doi.org/10.1016/s0969-2126(00)00007-1openalex-snapshot

The crystal structure of pertussis toxin

inferredcites →https://doi.org/10.1016/s1438-4221(00)80053-3openalex-snapshot

Intracellular trafficking and membrane translocation of pertussis toxin into host cells

inferredcites →https://doi.org/10.1021/bi00053a022openalex-snapshot

Effects of temperature on ADP-ribosylation factor stimulation of cholera toxin activity

inferredcites →https://doi.org/10.1021/bi00255a010openalex-snapshot

Effect of Temperature and Host Factors on the Activities of Pertussis Toxin and Bordetella Adenylate Cyclase

inferredcites →https://doi.org/10.1021/bi00265a021openalex-snapshot

Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model

inferredcites →https://doi.org/10.1021/bi00357a066openalex-snapshot

Stimulation of the thiol-dependent ADP-ribosyltransferase and NAD glycohydrolase activities of Bordetella pertussis toxin by adenine nucleotides, phospholipids, and detergents

inferredcites →https://doi.org/10.1021/bi00375a018openalex-snapshot

Structure-activity analysis of the activation of pertussis toxin

inferredcites →https://doi.org/10.1021/bi00388a031openalex-snapshot

Sulfhydryl-alkylating reagents inactivate the NAD glycohydrolase activity of pertussis toxin

inferredcites →https://doi.org/10.1021/bi061175+openalex-snapshot

The Pertussis Toxin S1 Subunit Is a Thermally Unstable Protein Susceptible to Degradation by the 20S Proteasome

inferredcites →https://doi.org/10.1021/bi971383popenalex-snapshot

Accumulating Evidence Suggests That Several AB-Toxins Subvert the Endoplasmic Reticulum-Associated Protein Degradation Pathway To Enter Target Cells

inferredcites →https://doi.org/10.1038/356260a0openalex-snapshot

Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

inferredcites →https://doi.org/10.1038/nrmicro3235openalex-snapshot

Bordetella pertussis pathogenesis: current and future challenges

inferredcites →https://doi.org/10.1038/nsb0994-591openalex-snapshot

Structure of a pertussis toxin–sugar complex as a model for receptor binding

inferredcites →https://doi.org/10.1042/ba20030089openalex-snapshot

The use of microcalorimetry to characterize tetanus neurotoxin, pertussis toxin and filamentous haemagglutinin

inferredcites →https://doi.org/10.1046/j.1462-5822.2001.00092.xopenalex-snapshot

Expression, activity and cytotoxicity of pertussis toxin S1 subunit in transfected mammalian cells

inferredcites →https://doi.org/10.1073/pnas.0809013105openalex-snapshot

Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum

inferredcites →https://doi.org/10.1073/pnas.83.13.4631openalex-snapshot

Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication.

inferredcites →https://doi.org/10.1074/jbc.m110.148981openalex-snapshot

Hsp90 Is Required for Transfer of the Cholera Toxin A1 Subunit from the Endoplasmic Reticulum to the Cytosol

inferredcites →https://doi.org/10.1074/jbc.m112.385575openalex-snapshot

Lipid Rafts Alter the Stability and Activity of the Cholera Toxin A1 Subunit

inferredcites →https://doi.org/10.1074/jbc.m114.609800openalex-snapshot

Co- and Post-translocation Roles for HSP90 in Cholera Intoxication

inferredcites →https://doi.org/10.1074/jbc.m300402200openalex-snapshot

Intra-Golgi Protein Transport Depends on a Cholesterol Balance in the Lipid Membrane

inferredcites →https://doi.org/10.1074/jbc.ra119.008568openalex-snapshot

HSC70 and HSP90 chaperones perform complementary roles in translocation of the cholera toxin A1 subunit from the endoplasmic reticulum to the cytosol

inferredcites →https://doi.org/10.1083/jcb.114.5.869openalex-snapshot

Stage-specific assays for coated pit formation and coated vesicle budding in vitro.

inferredcites →https://doi.org/10.1083/jcb.140.4.733openalex-snapshot

Toxin Entry: Retrograde Transport through the Secretory Pathway

inferredcites →https://doi.org/10.1083/jcb.200302028openalex-snapshot

Caveolae/raft-dependent endocytosis

inferredcites →https://doi.org/10.1083/jcb.201312042openalex-snapshot

ER-associated degradation: Protein quality control and beyond

inferredcites →https://doi.org/10.1086/514776openalex-snapshot

Changing Epidemiology of Pertussis in the United States: Increasing Reported Incidence Among Adolescents and Adults, 1990‐1996

inferredcites →https://doi.org/10.1093/femspd/ftv073openalex-snapshot

Contribution of pertussis toxin to the pathogenesis of pertussis disease: Graphical Abstract Figure.

inferredcites →https://doi.org/10.1093/femspd/ftw065openalex-snapshot

Intracellular disassembly and activity of pertussis toxin require interaction with ATP

inferredcites →https://doi.org/10.1096/fasebj.6.9.1612292openalex-snapshot

Pertussis toxin and target eukaryotic cells: binding, entry, and activation

inferredcites →https://doi.org/10.1111/cmi.12948openalex-snapshot

Humanised monoclonal antibodies neutralise pertussis toxin by receptor blockade and reduced retrograde trafficking

inferredcites →https://doi.org/10.1111/cmi.13074openalex-snapshot

A binding motif for Hsp90 in the A chains of ADP‐ribosylating toxins that move from the endoplasmic reticulum to the cytosol

inferredcites →https://doi.org/10.1111/j.1462-5822.2006.00813.xopenalex-snapshot

Pertussis toxin transiently affects barrier integrity, organelle organization and transmigration of monocytes in a human brain microvascular endothelial cell barrier model

inferredcites →https://doi.org/10.1111/j.1462-5822.2007.01115.xopenalex-snapshot

Retrograde transport of pertussis toxin in the mammalian cell

inferredcites →https://doi.org/10.1111/j.1742-4658.2011.08237.xopenalex-snapshot

The ins and outs of pertussis toxin

inferredcites →https://doi.org/10.1111/mmi.12807openalex-snapshot

ADP ‐ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A 1 polypeptide

inferredcites →https://doi.org/10.1126/science.3704651openalex-snapshot

Pertussis Toxin Gene: Nucleotide Sequence and Genetic Organization

inferredcites →https://doi.org/10.1128/cmr.18.2.326-382.2005openalex-snapshot

Molecular Pathogenesis, Epidemiology, and Clinical Manifestations of Respiratory Infections Due to Bordetella pertussis and Other Bordetella Subspecies

inferredcites →https://doi.org/10.1128/iai.00732-16openalex-snapshot

Thermal Unfolding of the Pertussis Toxin S1 Subunit Facilitates Toxin Translocation to the Cytosol by the Mechanism of Endoplasmic Reticulum-Associated Degradation

inferredcites →https://doi.org/10.1128/iai.02011-06openalex-snapshot

Evading the Proteasome: Absence of Lysine Residues Contributes to Pertussis Toxin Activity by Evasion of Proteasome Degradation

inferredcites →https://doi.org/10.1128/iai.57.11.3324-3330.1989openalex-snapshot

Binding of pertussis toxin to eucaryotic cells and glycoproteins

inferredcites →https://doi.org/10.1128/iai.63.3.825-832.1995openalex-snapshot

Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism

inferredcites →https://doi.org/10.1128/iai.64.2.593-599.1996openalex-snapshot

Pertussis toxin-catalyzed ADP-ribosylation of Gi-2 and Gi-3 in CHO cells is modulated by inhibitors of intracellular trafficking

inferredcites →https://doi.org/10.1128/iai.67.1.433-435.1999openalex-snapshot

Nonrestricted Differential Intoxication of Cells by Pertussis Toxin

inferredcites →https://doi.org/10.1128/iai.70.11.6172-6179.2002openalex-snapshot

Inhibition of Endoplasmic Reticulum-Associated Degradation in CHO Cells Resistant to Cholera Toxin, Pseudomonas aeruginosa Exotoxin A, and Ricin

inferredcites →https://doi.org/10.1146/annurev.biochem.78.081307.110540openalex-snapshot

Mechanisms of Endocytosis

inferredcites →https://doi.org/10.1167/iovs.04-0963openalex-snapshot

Interaction between mGluR8 and Calcium Channels in Photoreceptors Is Sensitive to Pertussis Toxin and Occurs Via G Protein βγ Subunit Signaling

inferredcites →https://doi.org/10.1186/1743-422x-3-26openalex-snapshot

Retrograde transport pathways utilised by viruses and protein toxins

inferredcites →https://doi.org/10.1203/00006450-200212000-00004openalex-snapshot

Chemical Chaperones: A Pharmacological Strategy for Disorders of Protein Folding and Trafficking

inferredcites →https://doi.org/10.2147/chc.s57108openalex-snapshot

Cytoskeleton and Golgi-apparatus interactions: a two-way road of function and structure

inferredcites →https://doi.org/10.2217/fmb.09.133openalex-snapshot

Pertussis Toxin and Adenylate Cyclase Toxin: Key Virulence Factors of Bordetella Pertussis and Cell Biology Tools

inferredcites →https://doi.org/10.3390/biom4030862openalex-snapshot

Regulating the 20S Proteasome Ubiquitin-Independent Degradation Pathway

inferredcites →https://doi.org/10.3390/toxins10050181openalex-snapshot

Pharmacological Cyclophilin Inhibitors Prevent Intoxication of Mammalian Cells with Bordetella pertussis Toxin

inferredcites →https://doi.org/10.3390/toxins11060350openalex-snapshot

Intracellular Transport and Cytotoxicity of the Protein Toxin Ricin

inferredcites →https://doi.org/10.3390/toxins11070373openalex-snapshot

Association of Pertussis Toxin with Severe Pertussis Disease

inferredcites →https://doi.org/10.3390/toxins3070787openalex-snapshot

Ricin Trafficking in Plant and Mammalian Cells

inferredcites →https://doi.org/10.3390/toxins3070884openalex-snapshot

Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX)

inferredcites →https://doi.org/10.3390/toxins7072674openalex-snapshot

A Conformational Shift in the Dissociated Cholera Toxin A1 Subunit Prevents Reassembly of the Cholera Holotoxin

inferredcites →https://doi.org/10.4161/pri.28938openalex-snapshot

The therapeutic potential of chemical chaperones in protein folding diseases

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4604133openalex-extracted

Larixol is Not an Inhibitor of Gα i Containing G Proteins and Lacks Effect on Signaling Mediated by Human Neutrophil Expressed Formyl Peptide Receptors

inferred← citeshttps://doi.org/10.1002/2211-5463.70329openalex-snapshot

Salmonella enterica serovar typhi limits the potency of typhoid toxin and ADP ‐ribosylating toxin AB to establish a persistent infection

inferred← citeshttps://doi.org/10.1007/s00204-026-04372-5openalex-snapshot

Novel endogenous protein-based strategies to inhibit clinically relevant bacterial AB-type toxins including pertussis toxin

inferred← citeshttps://doi.org/10.1007/s40259-023-00580-yopenalex-snapshot

Targeting the Inside of Cells with Biologicals: Toxin Routes in a Therapeutic Context

inferred← citeshttps://doi.org/10.1016/j.bcp.2023.115919openalex-snapshot

WITHDRAWN: Larixol is not an inhibitor of Gαi containing G proteins and lacks effect on signaling mediated by human neutrophil expressed formyl peptide receptors

inferred← citeshttps://doi.org/10.1016/j.bcp.2023.115995openalex-snapshot

Larixol is not an inhibitor of Gαi containing G proteins and lacks effect on signaling mediated by human neutrophil expressed formyl peptide receptors

inferred← citeshttps://doi.org/10.1016/j.colsurfb.2024.114321openalex-snapshot

Advances in the transport of oral nanoparticles in gastrointestinal tract

inferred← citeshttps://doi.org/10.1016/j.engmic.2023.100104openalex-snapshot

The diverse landscape of AB5-type toxins

inferred← citeshttps://doi.org/10.1039/d6an00215copenalex-snapshot

HDX-MS epitope characterization for evaluating antibody suitability for ELISA-based in vitro potency testing of vaccines

inferred← citeshttps://doi.org/10.1073/pnas.2419457122openalex-snapshot

Structural basis for neutralizing antibody binding to pertussis toxin

inferred← citeshttps://doi.org/10.1098/rsob.190147openalex-snapshot

Cellular functions and molecular mechanisms of non-lysine ubiquitination

inferred← citeshttps://doi.org/10.1101/2024.09.23.614357openalex-snapshot

Structural Basis for Antibody Neutralization of Pertussis Toxin

inferred← citeshttps://doi.org/10.1128/iai.00300-24openalex-snapshot

ER-transiting bacterial toxins amplify STING innate immune responses and elicit ER stress

inferred← citeshttps://doi.org/10.1371/journal.ppat.1010577openalex-snapshot

Pertussis toxin suppresses dendritic cell-mediated delivery of B. pertussis into lung-draining lymph nodes

inferred← citeshttps://doi.org/10.20944/preprints202302.0416.v1openalex-snapshot

Diphtheria and the AB Toxin Group

inferred← citeshttps://doi.org/10.3389/fcimb.2022.938015openalex-snapshot

Requirement of Peptidyl-Prolyl Cis/Trans isomerases and chaperones for cellular uptake of bacterial AB-type toxins

inferred← citeshttps://doi.org/10.3390/ijms22169064openalex-snapshot

Bordetella Adenylate Cyclase Toxin Elicits Airway Mucin Secretion through Activation of the cAMP Response Element Binding Protein

inferred← citeshttps://doi.org/10.3390/pharmaceutics15030987openalex-snapshot

Prospects of Using Protein Engineering for Selective Drug Delivery into a Specific Compartment of Target Cells

inferred← citeshttps://doi.org/10.3390/toxins12040223openalex-snapshot

Impact of Bacterial Toxins in the Lungs

inferred← citeshttps://doi.org/10.3390/toxins14010062openalex-snapshot

AB5 Enterotoxin-Mediated Pathogenesis: Perspectives Gleaned from Shiga Toxins

inferred← citeshttps://doi.org/10.3390/toxins14030187openalex-snapshot

Novel Strategies to Inhibit Pertussis Toxin

inferred← citeshttps://doi.org/10.3390/toxins15070412openalex-snapshot

Domperidone Inhibits Clostridium botulinum C2 Toxin and Bordetella pertussis Toxin

inferred← citeshttps://doi.org/10.3390/toxins16010036openalex-snapshot

The Chaperonin TRiC/CCT Inhibitor HSF1A Protects Cells from Intoxication with Pertussis Toxin

inferred← citeshttps://doi.org/10.3390/toxins18040189openalex-snapshot

Purification and Characterization of His-Tagged Recombinant Bacteroides fragilis Toxin-2 Variants In Vitro and In Vivo

inferred← citeshttps://doi.org/10.3390/toxins18050208openalex-snapshot

The Battle Against Pertussis: Discovery of Endogenous Human Proteins and Peptides as Toxin-Inhibitors

inferred← citeshttps://doi.org/10.70675/347d22f5zff8cz4653z9c3ez156cb378e146openalex-snapshot

Intéraction de toxines amphitropiques avec les membranes lors des étapes initiales de translocation

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