Mutation-Prone Positions Within the Estrogen Receptor

Taiwanese Journal of Obstetrics and Gynecology

Volumn 48, Issue 2, 2009, Pages 130-132

  Wiwanitkit, Viroj ^a  

^a NONE   (Thailand)

Author keywords

estrogen; mutation; receptor; weak linkage

Indexed keywords

ESTROGEN RECEPTOR;

AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; BIOINFORMATICS; GENE MUTATION; GENETIC LINKAGE; PREDICTION; PROTEIN MOTIF;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; COMPUTATIONAL BIOLOGY; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; FEMALE; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN STRUCTURE, TERTIARY; PROTEOMICS; RNA SPLICE SITES;

EID: 67749130912     PISSN: None     EISSN: 10284559     Source Type: Journal    
DOI: 10.1016/S1028-4559(09)60272-2     Document Type: Article

References (20)

1. Leclercq G., Lacroix M., Laios I., and Laurent G. Estrogen receptor alpha: impact of ligands on intracellular shuttling and turnover rate in breast cancer cells. Curr Cancer Drug Targets 6 (2006) 39-64
2. Cordera F., and Jordan V.C. Steroid receptors and their role in the biology and control of breast cancer growth. Semin Oncol 33 (2006) 631-641
3. Ikeda K., and Inoue S. Estrogen receptors and their downstream targets in cancer. Arch Histol Cytol 67 (2004) 435-442
4. Schneider H.P., and Bocker W. Hormones and progeny of breast tumor cells. Climacteric 9 (2006) 88-107
5. Herynk M.H., and Fuqua S.A. Estrogen receptor mutations in human disease. Endocr Rev 25 (2004) 869-898
6. Lee C., and Wang Q. Bioinformatics analysis of alternative splicing. Brief Bioinform 6 (2005) 23-33
7. Levin J.M., Penland R.C., Stamps A.T., and Cho C.R. Using in silico biology to facilitate drug development. Novartis Found Symp 247 (2002) 222-238
8. Gasteiger E., Gattiker A., Hoogland C., Ivanyi I., Appel R.D., and Bairoch A. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31 (2003) 3784-3788
9. Linding R., Russell R.B., Neduva V., and Gibson T.J. GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res 31 (2003) 3701-3708
10. Pearce S.T., and Jordan V.C. The biological role of estrogen receptors alpha and beta in cancer. Crit Rev Oncol Hematol 50 (2004) 3-22
11. Murphy L.C., Dotzlaw H., Leygue E., Douglas D., Coutts A., and Watson P.H. Estrogen receptor variants and mutations. J Steroid Biochem Mol Biol 62 (1997) 363-372
12. Gogarten J.P., and Olendzenski L. Orthologs, paralogs and genome comparisons. Curr Opin Genet Dev 9 (1999) 630-636
13. Golaz O., Wilkins M.R., Sanchez J.C., Appel R.D., Hochstrasser D.F., and Williams K.L. Identification of proteins by their amino acid composition: an evaluation of the method. Electrophoresis 17 (1996) 573-579
14. Wiwanitkit V. Where is the weak linkage in the globin chain?. Int J Nanomedicine 1 (2006) 109-110
15. Wiwanitkit V. Mutation-prone points in thrombin receptor. J Thromb Thrombolysis 25 (2008) 190-192
16. Wiwanitkit V. Weak linkage in androgen receptor: identification of mutation-prone points. Fertil Steril 91 (2009) e1-e3
17. Wiwanitkit V. Identification of weak points prone for mutation in ferredoxin of Trichomonas vaginalis. Indian J Med Microbiol 26 (2008) 158-159
18. Wiwanitkit V. Identification of mutation-prone points in bile salt export pump. HPB (Oxford) 9 (2007) 444-446
19. Azuaje F., Al-Shahrour F., and Dopazo J. Ontology-driven approaches to analyzing data in functional genomics. Methods Mol Biol 316 (2006) 67-86
20. Khan S., Situ G., Decker K., and Schmidt C.J. GoFigure: automated Gene Ontology annotation. Bioinformatics 19 (2003) 2484-2485