Editing 4-Hydroxynonenal (section)

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GS-HNE is a potent inhibitor of the activity of glutathione S-transferase, and therefore must be shuttled out of the cell to allow conjugation to occur at a physiological rate.<ref>{{Cite journal |last=Singhal |first=Sharad S. |last2=Singh |first2=Sharda P. |last3=Singhal |first3=Preeti |last4=Horne |first4=David |last5=Singhal |first5=Jyotsana |last6=Awasthi |first6=Sanjay |date=2015-12-15 |title=Antioxidant role of glutathione S-transferases: 4-Hydroxynonenal, a key molecule in stress-mediated signaling |url=https://linkinghub.elsevier.com/retrieve/pii/S0041008X15301095 |journal=[[Toxicology and Applied Pharmacology]] |language=en |volume=289 |issue=3 |pages=361–370 |doi=10.1016/j.taap.2015.10.006 |pmc=4852854 |pmid=26476300}}</ref>  Ral-interacting GTPase activating protein (RLIP76, also known as Ral-binding protein 1), is a membrane-bound protein which has high activity towards the transport of GS-HNE from the cytoplasm to the extracellular space.  This protein accounts for approximately 70% of such transport in human cell lines, while the remainder appears to be accounted for by Multidrug Resistance Protein 1 (MRP1).<ref>{{Cite journal |last=Singhal |first=Sharad S. |last2=Yadav |first2=Sushma |last3=Roth |first3=Cherice |last4=Singhal |first4=Jyotsana |date=2009-03-01 |title=RLIP76: A novel glutathione-conjugate and multi-drug transporter |url=https://linkinghub.elsevier.com/retrieve/pii/S0006295208007156 |journal=[[Biochemical Pharmacology (journal)|Biochemical Pharmacology]] |language=en |volume=77 |issue=5 |pages=761–769 |doi=10.1016/j.bcp.2008.10.006 |pmc=2664079 |pmid=18983828}}</ref><ref>{{Cite journal |last=Fenwick |first=R. Brynmor |last2=Campbell |first2=Louise J. |last3=Rajasekar |first3=Karthik |last4=Prasannan |first4=Sunil |last5=Nietlispach |first5=Daniel |last6=Camonis |first6=Jacques |last7=Owen |first7=Darerca |last8=Mott |first8=Helen R. |date=2010-08-11 |title=The RalB-RLIP76 Complex Reveals a Novel Mode of Ral-Effector Interaction |url=https://linkinghub.elsevier.com/retrieve/pii/S0969212610002339 |journal=Structure |language=en |volume=18 |issue=8 |pages=985–995 |doi=10.1016/j.str.2010.05.013 |pmc=4214634 |pmid=20696399}}</ref>