ArticleThe Journal of biological chemistry2017
Deciphering Key Residues Involved in the Virulence-promoting Interactions between
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
The trial behind it
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
9 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- Pathogen Moonlighting Proteins: From Ancestral Key Metabolic Enzymes to Virulence Factors.Microorganisms · 2021Article
- Thermal stability and structure of glyceraldehyde-3-phosphate dehydrogenase from the coralRSC advances · 2021Article
- Lysine Residues in the MK-Rich Region Are Not Required for Binding of the PbsP Protein From Group B Streptococci to Plasminogen.Frontiers in cellular and infection microbiology · 2021Article
- Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding.Protein science : a publication of the Protein Society · 2020Article
- Epitopes for Multivalent Vaccines AgainstFrontiers in cellular and infection microbiology · 2020Article
- Partial catalytic Cys oxidation of human GAPDH to Cys-sulfonic acid.Wellcome open research · 2020Article
- Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases.Bioscience reports · 2018Review
- A cryoprotectant induces conformational change in glyceraldehyde-3-phosphate dehydrogenase.Acta crystallographica. Section F, Structural biology communications · 2018Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial pathogens recruit circulating proteins to their own surfaces, co-opting the host protein functions as a mechanism of virulence. Particular attention has focused on the binding of plasminogen (Plg) to bacterial surfaces, as it has been shown that this interaction contributes to bacterial adhesion to host cells, invasion of host tissues, and evasion of the immune system. Several bacterial proteins are known to serve as receptors for Plg including glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a cytoplasmic enzyme that appears on the cell surface in this moonlighting role. Although Plg typically binds to these receptors via several lysine-binding domains, the specific interactions that occur have not been documented in all cases. However, identification of the relevant residues could help define strategies for mitigating the virulence of important human pathogens, such as
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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.