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Practice Editing Here (Nov 23rd in-class Wiki session work)

 * This is a place to practice clicking the "edit" button and practice adding references (via the citation button).

Amyloidosis this is my article.

Assignment # 3

 * Note: You will be emailing your assignment # 3 directly to your tutor, however, please paste a version here that excludes your personal information. This will allow us to support your efforts on Wikipedia prior to editing "live" in the article.

Wikipedia Assignment 3 Amyloidosis Section: Pathogenesis

Proposed Changes:

Original: The cells in the body have two different ways of making proteins. Some proteins are made of one single piece or sequence of amino acids; in other cases, protein fragments are produced, and the fragments come and join together to form the whole protein. But such a protein can sometimes fall apart into the original protein fragments. This process of "flip flopping" happens frequently for certain protein types, especially the ones that cause amyloidosis.

Change to: The cells in the body have two different ways of making proteins. Some proteins are made of one single piece or sequence of amino acids; in other cases, protein fragments are produced, and the fragments come and join together to form the whole protein. But such a protein can sometimes fall apart into the original protein fragments. This process of "flip flopping" happens frequently for certain protein types, especially the ones that cause amyloidosis. The vast majority of proteins that have been found to form amyloid deposits are secreted proteins, so the misfolding and formation of the amyloid occurs outside cells, in the extracellular space. There is currently no evidence of any structural or functional similarities between the different types of proteins vulnerable to misfold into amyloid. Thirty-seven proteins have been identified as being vulnerable to amyloid formation, and only four are cytosolic. One third of amyloid disease is hereditary, in which case there is normally an early age of onset. Half of amyloid-related diseases are sporadic and have a late age of onset – in these cases, the protein aggregation is due to a progressive loss of the body’s ability to regulate protein formation, with aging. A small number of amyloid disorders occur as a result of medical treatment. [Underlined words indicate terms that would have to be hyperlinked and defined].

The information for the above changes came from recent review articles:

Dogan A. Amyloidosis: Insights from Proteomics. Annu Rev Pathol. 2017 Jan 24;12:277-304. doi: 10.1146/annurev-pathol-052016-100200. Epub 2016 Dec 5. PMID: 27959636.

Chiti F, Dobson CM. Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. Annu Rev Biochem. 2017 Jun 20;86:27-68. doi: 10.1146/annurev-biochem-061516-045115. Epub 2017 May 12. PMID: 28498720.

Rationale for proposed change:

I propose adding the above text to give readers more context about the origin of amyloidosis in terms of risk factors – I think it could be helpful to someone who’s just been diagnosed with amyloidosis to know that there is often little rhyme or reason to who gets the disease, in case they’re having feelings of guilt or fears around risk factors they could have been exposed to. Also, I talked a little bit about where things happen spatially, which I hope could be helpful for people trying to visualize these processes, as histological processes are often hard to picture or conceptualize.

Controversies:

I’ve mentioned in my addition to this section that there are currently 37 identified amyloid-forming proteins that are associated with human disease. This is in conflict with the introduction section and the classification section of the existing article, which list that there are 30 and 36, respectively. The articles quoted for those figures were published in 2014 and 2008, so the source I’ve cited, published in 2017, reflects an evolution of current knowledge around amyloidosis.

Critique of Source:

The source I’ve chosen was published recently (2017), and is a secondary source, so there’s no worry of bias associated with the authors having conducted primary research. Also, the article was published in a reputable journal (Annual Review of Biochemistry). However, because of the breadth of material covered by the main article I used for my addition (Chiti and Dobson, 2017) covers amyloidosis pathogenesis very broadly and at a cellular level, this article and my addition would not be very useful to people looking to learn about specific types of amyloidosis. Also, the review I’ve chosen is a narrative one as opposed to a systematic review, making it less rigorous and more prone to bias.

What to post on the Wikipedia article talk page?

 * This will also be covered on Nov 23rd in class. Your group should use the below template to share an outline of your proposed improvements (including your new wording and citations). Article talk pages are not places to share your assignment answers. The Wikipedia community will be more interested in viewing your exact article improvement suggestions including where you plan to improve the article (which section), what wording you suggest, and the exact citation (Note: all citations must meet WP:MEDRS)
 * You will not be able to paste citations directly from your sandbox to talk pages (unless you are interested in editing/learning Wiki-code in the "source editing" mode). We suggest re-adding your citations on the talk page manually (using the cite button and populating the citation by pasting in the DOI, website, or PMID). You will have to repeat this process yet again when you edit the actual article live.
 * Talk Page Template: CARL Medical Editing Initiative/Fall 2020/Talk Page Template