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Glutathione S-transferase, C-terminal domain (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Glutathione S-transferase, C-terminal domain" in English language version.

refsWebsite
Global rank English rank
7nih.gov
4th place
4th place
6doi.org
2nd place
2nd place

doi.org

  • Armstrong RN (1997). "Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases". Chemical Research in Toxicology. 10 (1): 2–18. doi:10.1021/tx960072x. PMID 9074797.
  • Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J (2000). "Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases". Journal of Biological Chemistry. 275 (32): 24798–24806. doi:10.1074/jbc.M001706200. PMID 10783391.
  • Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P (2000). "The Glutathione Transferase Structural Family Includes a Nuclear Chloride Channel and a Ryanodine Receptor Calcium Release Channel Modulator". Journal of Biological Chemistry. 276 (5): 3319–3323. doi:10.1074/jbc.M007874200. PMID 11035031.
  • Eaton DL, Bammler TK; Bammler (1999). "Concise review of the glutathione S-transferases and their significance to toxicology". Toxicological Sciences. 49 (2): 156–164. doi:10.1093/toxsci/49.2.156. PMID 10416260.
  • Polekhina G, Board PG, Blackburn AC, Parker MW (2001). "Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity". Biochemistry. 40 (6): 1567–1576. doi:10.1021/bi002249z. PMID 11327815.
  • Vuilleumier S (1997). "Bacterial glutathione S-transferases: What are they good for?". Journal of Bacteriology. 179 (5): 1431–1441. doi:10.1128/jb.179.5.1431-1441.1997. PMC 178850. PMID 9045797.

nih.gov

pubmed.ncbi.nlm.nih.gov

  • Armstrong RN (1997). "Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases". Chemical Research in Toxicology. 10 (1): 2–18. doi:10.1021/tx960072x. PMID 9074797.
  • Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J (2000). "Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases". Journal of Biological Chemistry. 275 (32): 24798–24806. doi:10.1074/jbc.M001706200. PMID 10783391.
  • Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P (2000). "The Glutathione Transferase Structural Family Includes a Nuclear Chloride Channel and a Ryanodine Receptor Calcium Release Channel Modulator". Journal of Biological Chemistry. 276 (5): 3319–3323. doi:10.1074/jbc.M007874200. PMID 11035031.
  • Eaton DL, Bammler TK; Bammler (1999). "Concise review of the glutathione S-transferases and their significance to toxicology". Toxicological Sciences. 49 (2): 156–164. doi:10.1093/toxsci/49.2.156. PMID 10416260.
  • Polekhina G, Board PG, Blackburn AC, Parker MW (2001). "Crystal structure of maleylacetoacetate isomerase/glutathione transferase zeta reveals the molecular basis for its remarkable catalytic promiscuity". Biochemistry. 40 (6): 1567–1576. doi:10.1021/bi002249z. PMID 11327815.
  • Vuilleumier S (1997). "Bacterial glutathione S-transferases: What are they good for?". Journal of Bacteriology. 179 (5): 1431–1441. doi:10.1128/jb.179.5.1431-1441.1997. PMC 178850. PMID 9045797.

ncbi.nlm.nih.gov