Talk:Guanylate-binding protein

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Wiki Education assignment: Adv Molecular Bio Bass-FSU-Fa23[edit]

This article was the subject of a Wiki Education Foundation-supported course assignment, between 28 August 2023 and 15 December 2023. Further details are available on the course page. Student editor(s): Achait2023 (article contribs).

— Assignment last updated by Achait2023 (talk) 14:29, 21 September 2023 (UTC)[reply]

Are there mistakes in the images used? Achait2023 (talk) 20:37, 5 December 2023 (UTC)[reply]

I am adding two paragraphs to a section and three sources:

GBP1, the most widely studied GBP, has been studied for its antimicrobial properties. It can effectively polymerize and target the lipopolysaccharide cell wall of gram-negative bacteria. In said bacteria type, the GBP1 polymer coating alters the lipopolysaccharide membrane, allowing access to other parts of the membrane by other innate antimicrobial agents within the cell to cause pathogen cell death.^[1] Besides detecting pathogens and causing bacterial cell lysis, GBP1 can also cause host-programmed cell death.^[2]

The GBP family of proteins is highly conserved among many different phyla.^[3] They are believed to be a shared gene family that is used to fight off mostly viral, parasitic, and bacterial infections.^[1]^[3] On that note, the expression of GBPs is noted to increase in humans once the body detects many different types of diseases ranging from the infections listed above to cancer.^[3] Due to the similarity between murine and human GBPs, mouse knockout studies have been utilized to investigate the different roles GBPs have in fighting off other diseases^[3]. These studies have confirmed that knocking out different GBPs has different effects on combating different infections^[3]. Achait2023 (talk) 12:20, 7 December 2023 (UTC)[reply]

References

^ ^a ^b Kutsch, Miriam; Coers, Jörn (2021-10). "Human Guanylate Binding Proteins: nanomachines orchestrating host defense". The FEBS journal. 288 (20): 5826–5849. doi:10.1111/febs.15662. ISSN 1742-464X. PMC 8196077. PMID 33314740. {{cite journal}}: Check date values in: |date= (help)
^ Rivera-Cuevas, Yolanda; Clough, Barbara; Frickel, Eva-Maria (2023-10). "Human guanylate-binding proteins in intracellular pathogen detection, destruction, and host cell death induction". Current Opinion in Immunology. 84: 102373. doi:10.1016/j.coi.2023.102373. ISSN 1879-0372. PMID 37536111. {{cite journal}}: Check date values in: |date= (help)
^ ^a ^b ^c ^d ^e Tretina, Kyle; Park, Eui-Soon; Maminska, Agnieszka; MacMicking, John D. (2019-03-04). "Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease". The Journal of Experimental Medicine. 216 (3): 482–500. doi:10.1084/jem.20182031. ISSN 0022-1007. PMC 6400534. PMID 30755454.

[:0-1] Kutsch, Miriam; Coers, Jörn (2021-10). "Human Guanylate Binding Proteins: nanomachines orchestrating host defense". The FEBS journal. 288 (20): 5826–5849. doi:10.1111/febs.15662. ISSN 1742-464X. PMC 8196077. PMID 33314740. {{cite journal}}: Check date values in: |date= (help)

[2] Rivera-Cuevas, Yolanda; Clough, Barbara; Frickel, Eva-Maria (2023-10). "Human guanylate-binding proteins in intracellular pathogen detection, destruction, and host cell death induction". Current Opinion in Immunology. 84: 102373. doi:10.1016/j.coi.2023.102373. ISSN 1879-0372. PMID 37536111. {{cite journal}}: Check date values in: |date= (help)

[:1-3] Tretina, Kyle; Park, Eui-Soon; Maminska, Agnieszka; MacMicking, John D. (2019-03-04). "Interferon-induced guanylate-binding proteins: Guardians of host defense in health and disease". The Journal of Experimental Medicine. 216 (3): 482–500. doi:10.1084/jem.20182031. ISSN 0022-1007. PMC 6400534. PMID 30755454.

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