Talk:PPIB

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Untitled

Content

Overall organization of the article is strong. Content discussed under the "function" headline gives a good overview of PpiB. The oresentation is understandable to a wide audience and is not too specific. In terms of the topic, the article gives a comprehensive review of human PpiB but should include more about how PpiB works in other organisms. Discussion of the collagen interaction is specific to human cyclophilin and if the article is titled strictly "PPIB" it should be more generalized and encompass how diverse PpiB is among life.
The quality of the evidence in this article is strong with supporting references and additional reading. All information presented is factual and the photos on protein structure and chromosome location are nice visuals. Assumptions were not made and opinions were excluded. Great presentation of true facts.
Improvement to the organization of this article would help to explain it. Right now the function is great but the introduction again only speaks of human PpiB. If the article is to remain that way it should be renamed. Addition of bacterial PpiB which has been identified in many species such as Staphylococcus aureus, Escherichia coli and Bacillus subtilis would assist in showing the diverse roles of the protein as well as its conservation in both prokaryotes and eukaryotes.

Quality

The article has an introduction but again is specific to human PpiB and not "PPIB" which is the title. While the introduction is understandable, it should be more broad and encompassing of the protein's diversity. The line about regulating the protein folding of type I collagen can be moved to another section. Perhaps subheadings should be created to cover different families or domains of life. Again the information that is there is good, factual and has supporting images that aid the reader. Footnotes are properly placed and I enjoy the further readings. Coverage is neutral but does present from a clinical perspective and again favors human PpiB. All references are from reliable sources and have functional links to the article.

Peptidyl-prolyl cis-trans isomerase B is an enzyme that is widely conserved in both prokaryotes and eukaryotes. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds which are often the rate-limiting step in protein folding[6][7] PPIB is a member of the cyclophilin family of PPIase enzymes which are inhibited by cyclosporin A. ^[1] Rk145815 (talk) 15:41, 24 October 2017 (UTC)[reply]

References

^ Microbial cyclophilins: specialized functions in virulence and beyond.

Wiki Education Foundation-supported course assignment

This article is or was the subject of a Wiki Education Foundation-supported course assignment. Further details are available on the course page. Student editor(s): Rk145815.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 10:45, 18 January 2022 (UTC)[reply]

[1] Microbial cyclophilins: specialized functions in virulence and beyond.

[1]