ArticleInfection and immunity1994
Chlamydia trachomatis serovar L2 induces protein tyrosine phosphorylation during uptake by HeLa cells.
Article in Infection and immunity, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 77 citations in OpenAlex.
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- Proteomics and phosphoproteomics of freshwater mollusk carcasses reveal novel insights as potential food source.Frontiers in cellular and infection microbiology · 2025Article
- Vitamin D effects onFrontiers in cellular and infection microbiology · 2024Article
- Chlamydia repurposes the actin-binding protein EPS8 to disassemble epithelial tight junctions and promote infection.Cell host & microbe · 2022Article
- Bacteria-Mediated Oncogenesis and the Underlying Molecular Intricacies: What We Know So Far.Frontiers in oncology · 2022Review
- Infection-provoked psoriasis: Induced or aggravated (Review).Experimental and therapeutic medicine · 2021Review
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- Analysis of complement deposition and processing on Chlamydia trachomatis.Medical microbiology and immunology · 2021Article
- Pathogenic Puppetry: Manipulation of the Host Actin Cytoskeleton byInternational journal of molecular sciences · 2019Review
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- The Loss of Expression of a Single Type 3 Effector (CT622) Strongly ReducesFrontiers in cellular and infection microbiology · 2018Article
- Activation of epidermal growth factor receptor is required for Chlamydia trachomatis development.BMC microbiology · 2014Article
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- Specific chlamydial inclusion membrane proteins associate with active Src family kinases in microdomains that interact with the host microtubule network.Cellular microbiology · 2010Article
- Inflammasome-dependent caspase-1 activation in cervical epithelial cells stimulates growth of the intracellular pathogen Chlamydia trachomatis.The Journal of biological chemistry · 2009Article
- RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry.PLoS pathogens · 2008Article
- Chlamydia trachomatis species-specific induction of ezrin tyrosine phosphorylation functions in pathogen entry.Infection and immunity · 2007Article
- Chlamydophila pneumoniae PknD exhibits dual amino acid specificity and phosphorylates Cpn0712, a putative type III secretion YscD homolog.Journal of bacteriology · 2007Article
- Persistent infection of Chlamydia in reactive arthritis.Annals of the rheumatic diseases · 2006Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chlamydia trachomatis L2 is an obligate intracellular microorganism with a unique biphasic life cycle. The extracellular form, the elementary body (EB), is infectious but metabolically inactive. Attachment of EBs to host cells is medicated by a heparan sulfate-like glycosaminoglycan. Following attachment, the EB is internalized within a membrane-bound vesicle, and during the first 8 h of infection the vesicles are transported to a perinuclear location where they aggregate and fuse. By use of a monoclonal antibody against phosphotyrosine, we showed that three classes of proteins are tyrosine phosphorylated: a triple band of 68, 66, and 64 kDa, a 97-kDa band, and a 140-kDa band. The phosphorylation could be detected by immunoblotting from 15 min after infection of HeLa cells. We followed the movement of the EBs and the tyrosine phosphorylation of proteins by double-labelling immunofluorescence microscopy with the same monoclonal anti-phosphotyrosine antibody and a polyclonal antibody against the C. trachomatis L2 outer membrane complex. During the first 8 h of infection, the phosphorylation colocalized with EBs. Sixteen hours after infection, EBs have reorganized to the replicating reticulate bodies, forming an inclusion. At this time, phosphorylation was seen as dotted spots in the periphery of the inclusion.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.