Gene Review:
METAP1 - methionyl aminopeptidase 1
Homo sapiens
Synonyms:
KIAA0094, MAP 1, MAP1A, MetAP 1, MetAP1A, ...
- Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Arfin, S.M., Kendall, R.L., Hall, L., Weaver, L.H., Stewart, A.E., Matthews, B.W., Bradshaw, R.A. Proc. Natl. Acad. Sci. U.S.A. (1995)
- The 1.15A crystal structure of the Staphylococcus aureus methionyl-aminopeptidase and complexes with triazole based inhibitors. Oefner, C., Douangamath, A., D'Arcy, A., Häfeli, S., Mareque, D., Mac Sweeney, A., Padilla, J., Pierau, S., Schulz, H., Thormann, M., Wadman, S., Dale, G.E. J. Mol. Biol. (2003)
- Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal. Solbiati, J., Chapman-Smith, A., Miller, J.L., Miller, C.G., Cronan, J.E. J. Mol. Biol. (1999)
- Characterization of full length and truncated type I human methionine aminopeptidases expressed from Escherichia coli. Li, J.Y., Chen, L.L., Cui, Y.M., Luo, Q.L., Gu, M., Nan, F.J., Ye, Q.Z. Biochemistry (2004)
- Molecular characterization of a 28 kDa surface antigen gene family of the tribe Ehrlichiae. Reddy, G.R., Sulsona, C.R., Barbet, A.F., Mahan, S.M., Burridge, M.J., Alleman, A.R. Biochem. Biophys. Res. Commun. (1998)
- Structure of human methionine aminopeptidase-2 complexed with fumagillin. Liu, S., Widom, J., Kemp, C.W., Crews, C.M., Clardy, J. Science (1998)
- Methionine aminopeptidase-1: the MAP of the mitochondrion? Keeling, P.J., Doolittle, W.F. Trends Biochem. Sci. (1996)
- Regulation of microtubule protein levels during cellular morphogenesis in nerve growth factor-treated PC12 cells. Drubin, D., Kobayashi, S., Kellogg, D., Kirschner, M. J. Cell Biol. (1988)
- PC12 cells express juvenile microtubule-associated proteins during nerve growth factor-induced neurite outgrowth. Brugg, B., Matus, A. J. Cell Biol. (1988)
- The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. D'souza, V.M., Holz, R.C. Biochemistry (1999)
- Small molecule inhibitors of methionine aminopeptidase type 2 (MetAP-2). Garrabrant, T., Tuman, R.W., Ludovici, D., Tominovich, R., Simoneaux, R.L., Galemmo, R.A., Johnson, D.L. Angiogenesis (2004)
- Structural basis for the functional differences between type I and type II human methionine aminopeptidases. Addlagatta, A., Hu, X., Liu, J.O., Matthews, B.W. Biochemistry (2005)
- Methionine aminopeptidases type I and type II are essential to control cell proliferation. Bernier, S.G., Taghizadeh, N., Thompson, C.D., Westlin, W.F., Hannig, G. J. Cell. Biochem. (2005)
- Selective inhibition of amino-terminal methionine processing by TNP-470 and ovalicin in endothelial cells. Turk, B.E., Griffith, E.C., Wolf, S., Biemann, K., Chang, Y.H., Liu, J.O. Chem. Biol. (1999)
- High expression of methionine aminopeptidase type 2 in germinal center B cells and their neoplastic counterparts. Kanno, T., Endo, H., Takeuchi, K., Morishita, Y., Fukayama, M., Mori, S. Lab. Invest. (2002)
- The phosphorylated isoform of microtubule associated protein 1B (MAP1B) is expressed in the visual system of the tench (Tinca tinca, L) during optic nerve regeneration. Vecino, E., Ulloa, L., Avila, J. Neurosci. Lett. (1998)
- Human methionine aminopeptidase type 2 in complex with L- and D-methionine. Nonato, M.C., Widom, J., Clardy, J. Bioorg. Med. Chem. Lett. (2006)
- Methionine aminopeptidase 2 is a new target for the metastasis-associated protein, S100A4. Endo, H., Takenaga, K., Kanno, T., Satoh, H., Mori, S. J. Biol. Chem. (2002)
- A single amino acid residue defines the difference in ovalicin sensitivity between type I and II methionine aminopeptidases. Brdlik, C.M., Crews, C.M. J. Biol. Chem. (2004)
- Two continuous spectrophotometric assays for methionine aminopeptidase. Zhou, Y., Guo, X.C., Yi, T., Yoshimoto, T., Pei, D. Anal. Biochem. (2000)
- The human spiral ganglion. Anniko, M., Arnold, W., Stigbrand, T., Ström, A. ORL J. Otorhinolaryngol. Relat. Spec. (1995)
- Human extravillous trophoblasts express laeverin, a novel protein that belongs to membrane-bound gluzincin metallopeptidases. Fujiwara, H., Higuchi, T., Yamada, S., Hirano, T., Sato, Y., Nishioka, Y., Yoshioka, S., Tatsumi, K., Ueda, M., Maeda, M., Fujii, S. Biochem. Biophys. Res. Commun. (2004)
- Expression of soluble human beta-globin chains in bacteria and assembly in vitro with alpha-globin chains. Yamaguchi, T., Pang, J., Reddy, K.S., Witkowska, H.E., Surrey, S., Adachi, K. J. Biol. Chem. (1996)
- A new approach to the design of uniquely folded thermally stable proteins. Jiang, X., Farid, H., Pistor, E., Farid, R.S. Protein Sci. (2000)
- Nerve growth factor regulates both the phosphorylation and steady-state levels of microtubule-associated protein 1.2 (MAP1.2). Aletta, J.M., Lewis, S.A., Cowan, N.J., Greene, L.A. J. Cell Biol. (1988)
- Microtubule-associated proteins in adult human sensory organs. Anniko, M., Arnold, W. ORL J. Otorhinolaryngol. Relat. Spec. (1995)