uniprot:P49356 in Computationally mapped citations

11 results for uniprot:P49356 in Computationally mapped citations

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Multiple loci influence erythrocyte phenotypes in the CHARGE Consortium. Ganesh S.K., Zakai N.A., van Rooij F.J., Soranzo N., Smith A.V., Nalls M.A., Chen M.H., Kottgen A., Glazer N.L., Dehghan A. et al. Nat. Genet. 41:1191-1198(2009) GAD 597646 · Mapped (146) Associated with HEMATOLOGICAL: mean corpuscular volume; GAD 597646
Evaluation of farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models. Lobell R.B., Omer C.A., Abrams M.T., Bhimnathwala H.G., Brucker M.J., Buser C.A., Davide J.P., deSolms S.J., Dinsmore C.J., Ellis-Hutchings M.S. et al. Cancer Res. 61:8758-8768(2001) GeneRIF 2342 · Mapped (4) farnesyl:protein transferase and geranylgeranyl:protein transferase inhibitor combinations in preclinical models. GeneRIF 2342
Polymorphisms of the lamina maturation pathway and their association with the metabolic syndrome: the DESIR prospective study. Fontaine-Bisson B., Alessi M.C., Saut N., Fumeron F., Marre M., Dutour A., Badens C., Levy N., Tichet J., Juhan-Vague I. et al. J. Mol. Med. 88:193-201(2010) GeneRIF 2342 · Mapped (14) Observational study of gene-disease association and gene-gene interaction. (HuGE Navigator) GeneRIF 2342
Expression of farnesyltransferase in primary liver cancer. Sui G.D., Zhang G.Y., Niu Z.J., Hu S.Y. Chin. Med. J. 125:2427-2431(2012) GeneRIF 2342 · Mapped (4) The level of FTase mRNA expression in cancer tissues is much higher than in normal tissues. FTase may play an important role in the genesis and development of PLC and may be one of the markers for the metastatic activity gained by liver tumor cells. GeneRIF 2342
Expansion of protein farnesyltransferase specificity using "tunable" active site interactions: development of bioengineered prenylation pathways. Hougland J.L., Gangopadhyay S.A., Fierke C.A. J. Biol. Chem. 287:38090-38100(2012) GeneRIF 2342 · Mapped (4) Data show that protein farnesyltransferase (FTase) specificity can be "tuned" using a small number of active site contacts that play essential roles in discriminating against non-substrates in the wild-type enzyme. GeneRIF 2342
Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity. Reid T.S., Beese L.S. Biochemistry 43:6877-6884(2004) PDB 1SA4 · Mapped (4)
Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes. Reid T.S., Long S.B., Beese L.S. Biochemistry 43:9000-9008(2004) PDB 1S63 · Mapped (6)
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. Reid T.S., Terry K.L., Casey P.J., Beese L.S. J. Mol. Biol. 343:417-433(2004) PDB 1TN6 · Mapped (6)
Conversion of protein farnesyltransferase to a geranylgeranyltransferase. Terry K.L., Casey P.J., Beese L.S. Biochemistry 45:9746-9755(2006) PDB 2H6I PDB 2H6H PDB 2H6G PDB 2H6F · Mapped (2)
Resistance mutations at the lipid substrate binding site of Plasmodium falciparum protein farnesyltransferase. Eastman R.T., White J., Hucke O., Yokoyama K., Verlinde C.L., Hast M.A., Beese L.S., Gelb M.H., Rathod P.K., Van Voorhis W.C. Mol. Biochem. Parasitol. 152:66-71(2007) PDB 2IEJ · UniProtKB (2) · Mapped (2)
Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase. Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A., Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D. et al. Chem. Biol. 16:181-192(2009) PDB 3E37 · Mapped (4)

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