Talk:Glutathione S-transferase

message: I had just made several hours worth of corrections on this article, and Firefox went belly-up on me (of course).  Because of that, I am in no pleasant mood and will not likely be going through all that again for awhile.  I will get around to fixing this article, and replacing all those beautiful external links, sometime later.  Furthermore, as I have to include all the information (and around 20 times more) about GSTs in the introduction to my dissertation, I will not be entering anything under the GFDL (and/or the public domain) until I have published my dissertation and obtained a copyright on it. Sorry, but I can't put Wikipedia information in my intro and don't want to have one of my committee members read this article and accuse me of plagiarizing (myself).  I'll slowly add more to the article as I find time. FMephit 18:17, 7 April 2006 (UTC)
replies: text: Browsers do crash from time to time. Always better practise (as with any computer application) to save your work often (i.e. click "save page" and then click "edit this page" every fifteen minutes or so. --Seans Potato Business 22:48, 20 October 2007 (UTC)

text: Any movement on the thesis copyright? I'm debating whether or not I should heavily modify this article. As my dissertation was on aminotransferases, I'm not sure if I can wear an expert badge with respect to glutathione transferases, but I'm willing to give it a shot if no one else (any real experts out there?) feels like it. Pdcook (talk) 17:49, 29 September 2009 (UTC)

text: I agree that the article should be called glutathoine transferases (without the S-). Pdcook (talk) 17:43, 29 September 2009 (UTC)
thread_title: Comments

message: *The first thing I noticed was the sign at the top of the article stating that it needs attention from an expert in Molecular and Cellular Biology. Hopefully, they are referring to you and the help they are able to provide. There is a recommended template for how articles in the molecular and cellular biology genre should be structure. You can find the article structure here [].
**That's been up since before I started this project. I'm afraid to take it down, but I'm also not sure it really applies anymore, since I've been adding to the article.
**UPDATE: I have removed the template, in an effort to be bold. Jnims (talk) 22:11, 8 May 2013 (UTC)
thread_title: Comments from Flemingrjf

message: need adding it? --  —Preceding unsigned comment added by 24.248.198.18 (talk) 17:52, 23 December 2009 (UTC)
thread_title: zeta GSTZ1 is missing in the list of the enzymes

message: Can someone who understand please clarify and change this sentence which I do not understand:
"GSTs catalyse the conjugation of reduced glutathione — via a sulfhydryl group — toelectrophilic centers on a wide variety of substrates."
Maybe there should be an article for "conjugate" (in this sense)? Nopedia (talk) 14:18, 9 January 2013 (UTC)
thread_title: Please clarify "conjugation" and the sentence

message: *Great leading section!
**Thanks.
*More citations are needed in the classification and nomenclature sections. I think you use the one citation at the end to account for everything, but maybe you can just place them on several more sentences for clarification.
**Done.
*Structure section is very well done.
**Thanks.
*I deleted some words like "aforementioned." I think that this pulls it away from being an encyclopedic entry. The sentences stand fine on their own without it.
**Thank you.
*I don't suppose you could find an image from a public domain article showing a pull-down or tag assay and include it in that section? It would really help to show a visualization.
**I have had trouble finding public domain images related to GSTs in general, unfortunately.
*Are there any other uses for GST besides cancer development? What about other disease states or clinical implications? I wouldn't mind seeing a section including that information.
**I plan to include a section about other diseases. Thanks.
**UPDATE: I have added a Clinical significance section. Jnims (talk) 01:46, 9 May 2013 (UTC)
thread_title:  Comments from MChapman5 

message: *In the Role in Cell Signaling section you say there are "several GST isozymes..." do you know which specific GST isozymes? Or is the next paragraph explain which specific isozyme it is? If so then never mind 
**Yes, I mentioned them in subsequent paragraphs.
*GSTs rely on GSH from synthetic enzymes are there no natural enzymes? 
**I meant that the enzymes synthesize GSH, not that they are not naturally-occurring. 
*Really well organized
**Thanks.
*Are there any other diseases associated with GSTs, like super bugs because of GSTs working with multidrug resistance protein 1?
**Yes, I plan to add a few sentences about other diseases.
**UPDATE: I have added a Clinical significance section. Jnims (talk) 01:45, 9 May 2013 (UTC)
thread_title:  Peer Review: BreCaitlin 

message: * The section on GST-tags and the GST pull-down assay needs a citation urgently.
**I have added sources.
* You mention that GST is involved in cancer, but isn't it involved in other diseases?  For instance, this article  mentions that it is implicated in liver disease.
**Yes, I plan to add a few sentences about other diseases.
**UPDATE: I have added a Clinical significance section. Jnims (talk) 01:31, 9 May 2013 (UTC)
thread_title: Peer Review: Gpruett2

message: *How are cytosolic, mitochondrial and microsomal GSTs different. Is it simply a matter of structure?
**Structure, sequence, and location seem to be the differences between the GSTs. Also, not all organisms have all three superfamilies.
*You say that the helix a2 has the most variability, do you mean conservation? If you do mean variability, you should clarify the statement a little.
**I did mean variability, in that the residue that interacts with glutathione can be one of three possibilities.
*I'm a little confused about the Max All Species column in the table. Could you clarify?
**I never understood what that was supposed to mean, so I finally deleted it.
*I believe when you talk about domains, it should be N-terminal or C-terminal instead of N-terminus or C-terminus.
**Fixed.
*How do GSTs recognize xenobiotic substrates?
**I will attempt to find and add this information.
**UPDATE: I have added the following information, which I hope will suffice (I would have included more, but each enzyme class seems to have a different strategy/structure for binding nonsubstrate ligands, and I didn't find any specific information about "recognition"): "Both subunits of the GST dimer, whether hetero- or homodimeric in nature, contain a single nonsubstrate binding site, as well as a GSH-binding site. In heterodimeric GST complexes such as those formed by the cytosolic mu and alpha classes, however, the cleft between the two subunits is home to an additional high-affinity nonsubstrate xenobiotic binding site, which may account for the enzymes' ability to form heterodimers." Jnims (talk) 01:45, 9 May 2013 (UTC)
thread_title: Maximus155