FNTB

FNTB

Farnesyltransferase, CAAX box, beta, also known as FNTB, is a human gene.cite web | title = Entrez Gene: FNTB farnesyltransferase, CAAX box, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2342| accessdate = ]

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References

Further reading

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*cite journal | author=Manne V, Roberts D, Tobin A, "et al." |title=Identification and preliminary characterization of protein-cysteine farnesyltransferase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 19 |pages= 7541–5 |year= 1990 |pmid= 2217184 |doi=
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Sinensky M, Fantle K, Trujillo M, "et al." |title=The processing pathway of prelamin A. |journal=J. Cell. Sci. |volume=107 ( Pt 1) |issue= |pages= 61–7 |year= 1994 |pmid= 8175923 |doi=
*cite journal | author=Andres DA, Milatovich A, Ozçelik T, "et al." |title=cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences. |journal=Genomics |volume=18 |issue= 1 |pages= 105–12 |year= 1994 |pmid= 8276393 |doi= 10.1006/geno.1993.1432
*cite journal | author=Omer CA, Kral AM, Diehl RE, "et al." |title=Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases. |journal=Biochemistry |volume=32 |issue= 19 |pages= 5167–76 |year= 1993 |pmid= 8494894 |doi=
*cite journal | author=Wang T, Danielson PD, Li BY, "et al." |title=The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling. |journal=Science |volume=271 |issue= 5252 |pages= 1120–2 |year= 1996 |pmid= 8599089 |doi=
*cite journal | author=Nantais DE, Schwemmle M, Stickney JT, "et al." |title=Prenylation of an interferon-gamma-induced GTP-binding protein: the human guanylate binding protein, huGBP1. |journal=J. Leukoc. Biol. |volume=60 |issue= 3 |pages= 423–31 |year= 1996 |pmid= 8830800 |doi=
*cite journal | author=Goalstone ML, Draznin B |title=Effect of insulin on farnesyltransferase activity in 3T3-L1 adipocytes. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27585–9 |year= 1996 |pmid= 8910345 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Long SB, Casey PJ, Beese LS |title=Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. |journal=Biochemistry |volume=37 |issue= 27 |pages= 9612–8 |year= 1998 |pmid= 9657673 |doi= 10.1021/bi980708e
*cite journal | author=Prakash B, Praefcke GJ, Renault L, "et al." |title=Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. |journal=Nature |volume=403 |issue= 6769 |pages= 567–71 |year= 2000 |pmid= 10676968 |doi= 10.1038/35000617
*cite journal | author=Zeng Q, Si X, Horstmann H, "et al." |title=Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and -3 with the plasma membrane and the early endosome. |journal=J. Biol. Chem. |volume=275 |issue= 28 |pages= 21444–52 |year= 2000 |pmid= 10747914 |doi= 10.1074/jbc.M000453200
*cite journal | author=Ashar HR, James L, Gray K, "et al." |title=Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules. |journal=J. Biol. Chem. |volume=275 |issue= 39 |pages= 30451–7 |year= 2000 |pmid= 10852915 |doi= 10.1074/jbc.M003469200
*cite journal | author=Guenzi E, Töpolt K, Cornali E, "et al." |title=The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines. |journal=EMBO J. |volume=20 |issue= 20 |pages= 5568–77 |year= 2001 |pmid= 11598000 |doi= 10.1093/emboj/20.20.5568
*cite journal | author=Long SB, Hancock PJ, Kral AM, "et al." |title=The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 23 |pages= 12948–53 |year= 2001 |pmid= 11687658 |doi= 10.1073/pnas.241407898
*cite journal | author=Lobell RB, Omer CA, Abrams MT, "et al." |title=Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models. |journal=Cancer Res. |volume=61 |issue= 24 |pages= 8758–68 |year= 2002 |pmid= 11751396 |doi=
*cite journal | author=Bell IM, Gallicchio SN, Abrams M, "et al." |title=3-Aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency. |journal=J. Med. Chem. |volume=45 |issue= 12 |pages= 2388–409 |year= 2002 |pmid= 12036349 |doi=
*cite journal | author=Long SB, Casey PJ, Beese LS |title=Reaction path of protein farnesyltransferase at atomic resolution. |journal=Nature |volume=419 |issue= 6907 |pages= 645–50 |year= 2002 |pmid= 12374986 |doi= 10.1038/nature00986
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=deSolms SJ, Ciccarone TM, MacTough SC, "et al." |title=Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents. |journal=J. Med. Chem. |volume=46 |issue= 14 |pages= 2973–84 |year= 2003 |pmid= 12825937 |doi= 10.1021/jm020587n

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  • FNTA — Farnesyltransferase, CAAX box, alpha, also known as FNTA, is a human gene.cite web | title = Entrez Gene: FNTA farnesyltransferase, CAAX box, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=2339|… …   Wikipedia

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