{"doi":"10.1172/jci117747","title":"The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile.","abstract":null,"journal":"Journal of Clinical Investigation","year":1995,"id":678785,"datarank":0.7218276533058626,"base_score":4.812184355372417,"endowment":4.812184355372417,"self_citation_contribution":0.7218276533058626,"citation_network_contribution":0.0,"self_endowment_contribution":0.7218276533058626,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":122,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1773497,"name":"J Selzer","orcid":null,"position":1,"is_corresponding":false},{"id":1773499,"name":"C von Eichel-Streiber","orcid":null,"position":2,"is_corresponding":false},{"id":1773501,"name":"K Aktories","orcid":null,"position":3,"is_corresponding":false},{"id":1773495,"name":"I Just","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile.","abstract":"Enterotoxin A is one of the major virulence factors of Clostridium difficile, and the causative agent of antibiotic-associated pseudomembranous colitis. In cell culture (NIH-3T3, rat basophilic leukemia cells) toxin A inhibits Clostridium botulinum ADP-ribosyltransferase C3 (C3)-catalyzed ADP-ribosylation of the low molecular mass GTP-binding Rho proteins. Rho participates in the regulation of the microfilament cytoskeleton. Decrease in ADP-ribosylation of Rho occurs in a time- and concentration-dependent manner and precedes the toxin A-induced destruction of the actin cytoskeleton. Action of toxin A is not due to proteolytical degradation of Rho or to an inherent ADP-ribosyltransferase activity of toxin A. Toxin A-induced decrease in ADP-ribosylation is observed also in cell lysates and with recombinant RhoA protein. A heat stable low molecular mass cytosolic factor is essential for the toxin effect on Rho. Thus, the enterotoxin (toxin A) resembles the effects of the C. difficile cytotoxin (toxin B) on Rho proteins (Just, I., G. Fritz, K. Aktories, M. Giry, M. R. Popoff, P. Boquet, S. Hegenbath, and C. Von Eichel-Streiber. 1994. J. Biol. Chem. 269:10706-10712). The data indicate that despite different in vivo effects, toxin A and toxin B act on the same cellular target protein Rho to elicit their toxic effects.","is_dataset_classified":null,"base_score":4.812184355372417,"endowment":4.812184355372417,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"7883950","pmcid":"PMC441436","openalex_id":"https://openalex.org/W1999628378","authors":[],"funders":[],"total_grants":0,"fwci":5.5028,"citation_percentile":0.96139979,"influential_citations":0,"citation_trend":[{"year":2012,"count":2},{"year":2013,"count":5},{"year":2014,"count":7},{"year":2015,"count":5},{"year":2016,"count":8},{"year":2017,"count":5},{"year":2018,"count":2},{"year":2020,"count":6},{"year":2021,"count":1},{"year":2023,"count":4},{"year":2024,"count":1},{"year":2025,"count":1}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"http://www.jci.org/articles/view/117747/files/pdf","host_type":"journal"},{"url":"http://www.jci.org/articles/view/117747/files/pdf","host_type":"publisher"},{"url":"https://doi.org/10.1172/jci117747","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/7883950","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/441436","host_type":"repository"},{"url":"http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.836.1962","host_type":""}],"fields_of_study":["Clostridium difficile and Clostridium perfringens research","Toxin Mechanisms and Immunotoxins","Botulinum Toxin and Related Neurological Disorders","ADP Ribose Transferases","Adenosine Diphosphate Ribose","Animals","Bacterial Proteins","Bacterial Toxins","Botulinum Toxins","Colchicine","Cytochalasin D","Dose-Response Relationship, Drug","Enterotoxins","GTP-Binding Proteins","GTPase-Activating Proteins","Rats","Tumor Cells, Cultured"],"mesh_terms":["Adenosine Diphosphate Ribose","Animals","Bacterial Proteins","Bacterial Toxins","Botulinum Toxins","Colchicine","Dose-Response Relationship, Drug","Enterotoxins","Tumor Cells, Cultured","Cytochalasin D","GTP-Binding Proteins","GTPase-Activating Proteins","ADP Ribose Transferases","Rats"],"keywords":["Clostridium difficile toxin B","Clostridium difficile toxin A","Toxin","ADP-ribosylation","RHOA","Enterotoxin","Pseudomembranous colitis","ADP ribosylation factor","Biology","Anthrax toxin","Pertussis toxin","Microbiology","Clostridium botulinum","Clostridium difficile","G protein","Molecular biology","Biochemistry","Recombinant DNA","Escherichia coli","Cell","Receptor","Enzyme","Signal transduction"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T11:23:57.150261Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}