Structure of Human Methionine Aminopeptidase-2 Complexed with Fumagillin

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616

Angiogenesis in cancer, vascular, rheumatoid and other disease

Folkman, J. (1995) · Nature Medicine · doi:10.1038/nm0195-27 · Cited by 7,627

LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions

Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · Protein Engineering Design and Selection · doi:10.1093/protein/8.2.127 · Cited by 5,731

AMoRe: an automated package for molecular replacement

Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941

Crystallographic R Factor Refinement by Molecular Dynamics

Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,950

Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth

Ingber, D. E., Fujita, T., KISHIMOTO, S., Sudo, K., KANAMARU, T., Brem, H., & Folkman, J. (1990) · Nature · doi:10.1038/348555a0 · Cited by 1,301

Serine Proteases: Structure and Mechanism of Catalysis

Kraut, J. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.001555 · Cited by 1,253

ALSCRIPT: a tool to format multiple sequence alignments

Barton, G. J. (1993) · Protein Engineering Design and Selection · doi:10.1093/protein/6.1.37 · Cited by 1,144

Catalytic Mechanisms for Metallopeptidases

Auld, D. S. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382219-2.00078-8 · Cited by 26

The intriguing realm of protein biogenesis: Facing the green co-translational protein maturation networks

Breiman, A., Fieulaine, S., Meinnel, T., & Giglione, C. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.11.002 · Cited by 23

Non-peptide secondary metabolites from poisonous mushrooms: overview of chemistry, bioactivity, and biosynthesis

Lee, S., Yu, J. S., Lee, S. R., & Kim, K. H. (2021) · Natural Product Reports · doi:10.1039/d1np00049g · Cited by 24

Methionine aminopeptidase 2 over-expressed in cholangiocarcinoma: Potential for drug target

Sawanyawisuth, K., Wongkham, C., Pairojkul, C., Saeseow, O.-T., Riggins, G. J., Araki, N., & Wongkham, S. (2006) · Acta Oncologica · doi:10.1080/02841860600871061 · Cited by 23

Structural and functional highlights of methionine aminopeptidase 2 from Leishmania donovani

Bhat, S. Y., Dey, A., & Qureshi, I. A. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.04.090 · Cited by 23

Residue Preference Mapping of Ligand Fragments in the Protein Data Bank

Wang, L., Xie, Z., Wipf, P., & Xie, X. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100386y · Cited by 23

Synthesis and biological evaluation of novel fumagillin and ovalicin analogues

Mazitschek, R., Huwe, A., & Giannis, A. (2005) · Organic & Biomolecular Chemistry · doi:10.1039/b503163j · Cited by 23

Investigation of novel fumagillin analogues as angiogenesis inhibitors

Pyun, H., Fardis, M., Tario, J., Yang, C. Y., Ruckman, J., Henninger, D. D., Jin, H., & Kim, C. U. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2003.10.008 · Cited by 23

Methionine aminopeptidase 2 is required for HSC initiation and proliferation

Ma, A. C. H., Fung, T. K., Lin, R. H. C., Chung, M., Yang, D., Ekker, S. C., & Leung, A. Y. H. (2011) · Blood · doi:10.1182/blood-2011-04-350173 · Cited by 22

An Array of Bengamide E Analogues Modified at the Terminal Olefinic Position: Synthesis and Antitumor Properties

Martín‐Gálvez, F., García‐Ruiz, C., Sánchez‐Ruiz, A., Valeriote, F. A., & Sarabia, F. (2013) · ChemMedChem · doi:10.1002/cmdc.201300033 · Cited by 22

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Lanza, G. M., Caruthers, S. D., Winter, P. M., Hughes, M. S., Schmieder, A. H., Hu, G., & Wickline, S. A. (2010) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-010-1502-5 · Cited by 22

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Piggott, A. M., & Karuso, P. (2005) · Marine Drugs · doi:10.3390/md302036 · Cited by 22

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Fardis, M., Pyun, H., Tario, J., Jin, H., Kim, C. U., Ruckman, J., Lin, Y., Green, L., & Hicke, B. J. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2003.08.031 · Cited by 22

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Asami, Y., Kakeya, H., Okada, G., Toi, M., & Osada, H. (2006) · The Journal of Antibiotics · doi:10.1038/ja.2006.97 · Cited by 22

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Bhaskar, V., Desogus, J., Graff-Meyer, A., Schenk, A. D., Cavadini, S., & Chao, J. A. (2021) · RNA · doi:10.1261/rna.077602.120 · Cited by 23

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Hassan, A. H. E., Mahmoud, K., Phan, T.-N., Shaldam, M. A., Lee, C. H., Kim, Y. J., Cho, S. B., Bayoumi, W. A., El‐Sayed, S. M., Choi, Y., et al. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115211 · Cited by 21

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Theriot, C. M., Tove, S. R., & Grunden, A. M. (2009) · Advances in applied microbiology · doi:10.1016/s0065-2164(09)01203-9 · Cited by 21

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Calvo, E., Barasoaı́n, I., Matesanz, R., Pera, B., Camafeita, E., Pineda, O., Hamel, E., Vanderwal, C. D., Andreu, J. M., López, J. A., et al. (2011) · Biochemistry · doi:10.1021/bi201380p · Cited by 20

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Winter, P. M. (2014) · Scientifica · doi:10.1155/2014/746574 · Cited by 21

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Govender, P. P., Navizet, I., Perry, C. B., & Marques, H. M. (2013) · The Journal of Physical Chemistry A · doi:10.1021/jp311788t · Cited by 21

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Kwon, J., Jeong, H.-W., Kim, H., Kang, K., Chang, Y., Bae, K., Choi, J.-D., Lee, U. C., Son, K., & Kwon, B. (2000) · The Journal of Antibiotics · doi:10.7164/antibiotics.53.799 · Cited by 21

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Shimizu, K., Asai, T., & Oku, N. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.1.63 · Cited by 21

Chapter 29. Structure-Based Drug Design

Murcko, M. A., Caron, P. R., & Charifson, P. S. (1999) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(08)60591-6 · Cited by 21

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Weako, J., Uba, A. İ., Keskin, Ö., Gürsoy, A., & Yelekçi, K. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107244 · Cited by 20

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Poręba, M., Gajda, A., Pícha, J., Jiráček, J., Marschner, A., Klein, C. D. P., Salvesen, G. S., & Drąg, M. (2011) · Biochimie · doi:10.1016/j.biochi.2011.10.014 · Cited by 20

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Kodama, T., Narula, N., Agozzino, M., & Arbustini, E. (2012) · Journal of Cardiovascular Medicine · doi:10.2459/jcm.0b013e328356a5f2 · Cited by 20

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Brummond, K. M., & Dunn, J. M. M. (2006) · Tetrahedron · doi:10.1016/j.tet.2006.06.115 · Cited by 20

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Kass, D. J., Bridges, R. S., Borczuk, A., & Greenberg, S. (2007) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2006-0352oc · Cited by 20

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Hannig, G., Lazarus, D. D., Bernier, S. G., Karp, R., Lorusso, J., Qiu, D., Labenski, M., Wakefield, J., Thompson, C. D., & Westlin, W. (2006) · International Journal of Oncology · doi:10.3892/ijo.28.4.955 · Cited by 20

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Jeyakanthan, J., Takada, K., Sawano, M., Ogasahara, K., Mizutani, H., KUNISHIMA, N., Yokoyama, S., & Yutani, K. (2009) · Journal of Biophysics · doi:10.1155/2009/434038 · Cited by 19

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Halász, J., Podányi, B., VASVARI‐DEBRECZY, L., Szabó, A., Hajdú, F., Böcskei, Z., Hegedűs-Vajda, J., Győrbı́ró, A., & Hermecz, I. (2000) · Tetrahedron · doi:10.1016/s0040-4020(00)00979-0 · Cited by 19

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Datta, B., Datta, R., Ghosh, A., & Majumdar, A. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.06.009 · Cited by 19

Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions

Datta, B., Datta, R., Ghosh, A., & Majumdar, A. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.04.002 · Cited by 18

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Shimizu, H., Yamagishi, S., Chiba, H., & Ghazizadeh, M. (2015) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/60715 · Cited by 18

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Ghisalberti, E. L. (2002) · Studies in natural products chemistry · doi:10.1016/s1572-5995(02)80013-8 · Cited by 18

Pyridinylquinazolines Selectively Inhibit Human Methionine Aminopeptidase-1 in Cells

Zhang, F., Bhat, S., Gabelli, S. B., Chen, X., Miller, M. S., Nacev, B. A., Cheng, Y. L., Meyers, D. J., Tenney, K., Shim, J. S., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400227z · Cited by 18

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Xie, S.-X., Huang, W.-J., Ma, Z.-Q., Huang, M., Hanzlik, R. P., & Ye, Q.-Z. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906003878 · Cited by 18

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Klein, C. D. P., Schiffmann, R., Folkers, G., Piana, S., & Röthlisberger, U. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m305325200 · Cited by 18

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Texier, C., Brosson, D., Alaoui, H. E., Méténier, G., & Vivarès, C. P. (2005) · Folia Parasitologica · doi:10.14411/fp.2005.003 · Cited by 17

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Olaleye, O. A., Bishai, W. R., & Liu, J. O. (2009) · Tuberculosis · doi:10.1016/s1472-9792(09)70013-7 · Cited by 17

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Musil, D., Heinrich, T., & Lehmann, M. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6qej/pdb · Cited by 17

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Xie, J., Rice, M. A., Chen, Z., Cheng, Y., Hsu, E., Chen, M., Song, G., Cui, L., Zhou, K., Castillo, J. B., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-2969 · Cited by 16

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Núñez, C., Bastida, R., Macías, A., Valencia, L., Neuman, N. I., Rizzi, A. C., Brondino, C. D., González, P. J., Capelo, J. L., & Lodeiro, C. (2010) · Dalton Transactions · doi:10.1039/c0dt00692k · Cited by 16

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Bose, S., Datta, A., Ganguly, R., & Banerjee, M. K. (2013) · Journal of Nanotechnology in Engineering and Medicine · doi:10.1115/1.4026839 · Cited by 16

Kinetic and Spectroscopic Analysis of the Catalytic Role of H79 in the Methionine Aminopeptidase from Escherichia coli

Watterson, S. J., Mitra, S., Swierczek, S. I., Bennett, B., & Holz, R. C. (2008) · Biochemistry · doi:10.1021/bi801499g · Cited by 16

Pyridinylpyrimidines selectively inhibit human methionine aminopeptidase-1

Zhang, P., Yang, X., Zhang, F., Gabelli, S. B., Wang, R., Zhang, Y., Bhat, S., Chen, X., Furlani, M., Amzel, L. M., et al. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.02.023 · Cited by 16

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Esser, A. K., Schmieder, A. H., Ross, M. H., Xiang, J., Su, X., Cui, G., Zhang, H., Yang, X., Allen, J. S., Williams, T. A., et al. (2015) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2015.10.003 · Cited by 16

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Larrabee, J. A., Schenk, G., Mitić, N., & Riley, M. J. (2015) · European Biophysics Journal · doi:10.1007/s00249-015-1053-6 · Cited by 16

Negative regulation of the protection of eIF2α phosphorylation activity by a unique acidic domain present at the N-terminus of p67

Datta, R., Tammali, R., & Datta, B. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00042-3 · Cited by 16

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Klein, M. A., Wild, K., Kišonaitė, M., & Sinning, I. (2024) · Nature Communications · doi:10.1038/s41467-024-44862-7 · Cited by 15

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Zhou, G., Liu, F., Wan, J., Wang, J., Wang, D., Wei, P., & Ouyang, P. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.10.033 · Cited by 15

The stability of eukaryotic initiation factor 2-associated glycoprotein, p67, increases during skeletal muscle differentiation and that inhibits the phosphorylation of extracellular signal-regulated kinases 1 and 2

Datta, B., Datta, R., MAJUMDAR, A., & GHOSH, A. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.09.018 · Cited by 15

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SPENCER, J. M., & Walsh, T. R. (2006) · Angewandte Chemie · doi:10.1002/ange.200502984 · Cited by 15

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Talma, M., & Mucha, A. (2020) · Biomolecules · doi:10.3390/biom10040659 · Cited by 15

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Lam, A. Y. F., Vuong, D., Jex, A. R., Piggott, A. M., Lacey, E., & Emery‐Corbin, S. J. (2021) · International Journal for Parasitology Drugs and Drug Resistance · doi:10.1016/j.ijpddr.2021.01.001 · Cited by 14

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Ren, M., Li, Z., Wang, Z., Han, W., Wang, F., Li, Y., Zhang, W., Liu, X., Zhang, J., & Luo, D. (2024) · Journal of Natural Products · doi:10.1021/acs.jnatprod.4c00539 · Cited by 14

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Son, K., Kwon, J., Jeong, H.-W., Kim, H., Kim, C., Chang, Y., Choi, J.-D., & Kwon, B. (2002) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(01)00268-1 · Cited by 14

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Hartley, M. J., & Bennett, B. (2009) · Protein Expression and Purification · doi:10.1016/j.pep.2009.02.011 · Cited by 14

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Atanassova, A., Sugita, M., Sugiura, M., Pajpanova, T. I., & Ivanov, I. (2003) · Archives of Microbiology · doi:10.1007/s00203-003-0576-x · Cited by 14

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Weijers, C. A. G. M., Könst, P., Franssen, M. C. R., & Sudhölter, E. J. R. (2007) · Organic & Biomolecular Chemistry · doi:10.1039/b709742e · Cited by 14

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Alaoui, H. E., Bata, J., Bauchart, D., Doré, J., & Vivarès, C. P. (2001) · Journal of Parasitology · doi:10.1645/0022-3395(2001)087[0554:lotmsa]2.0.co;2 · Cited by 14

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Jørgensen, A. T., Norrby, P., & Liljefors, T. (2002) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1020119527789 · Cited by 14

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D’souza, V. M., Brown, R. S., Bennett, B., & Holz, R. C. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0611-7 · Cited by 14

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Watanabe, N., Saito‐Nakano, Y., Kurisawa, N., Otomo, K., Suenaga, K., Nakano, K., & Nozaki, T. (2023) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00560-23 · Cited by 13

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Fuentes-Terrón, A., Latter, R., Madden, S. R., Manrique-Gil, I., Estrada, J., Arteaga, N., Sánchez-Vicente, I., Lorenzo, Ó., & Flashman, E. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae667 · Cited by 13

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Siddik, M. A. B., Das, B. C., Weiss, L. M., Dhurandhar, N. V., & Hegde, V. K. (2019) · Adipocyte · doi:10.1080/21623945.2019.1636627 · Cited by 13

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Mitra, S., Dygas-Holz, A. M., Jiráček, J., Žertová, M., Žáková, L., & Holz, R. C. (2006) · Analytical Biochemistry · doi:10.1016/j.ab.2006.06.012 · Cited by 13

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Hou, Y. J., Li, Q., Chen, M., Wu, H., Yang, J., Sun, Z., Xu, X., & Ma, G. (2022) · Fitoterapia · doi:10.1016/j.fitote.2022.105251 · Cited by 12

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Minkwitz, S., Fassbender, M., Kronbach, Z., & Wildemann, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124217 · Cited by 12

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Nonato, M. C., Widom, J. M., & Clardy, J. (2006) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2006.02.047 · Cited by 12

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Kass, D. J., Rattigan, E. M., Kahloon, R. A., Loh, K. S., Yu, L., Savir, A., Markowski, M. C., Saqi, A., Rajkumar, R., Ahmad, F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0035388 · Cited by 12

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Ma, Z.-Q., Xie, S.-X., Huang, Q., Nan, F.-J., Hurley, T. D., & Ye, Q.-Z. (2007) · BMC Structural Biology · doi:10.1186/1472-6807-7-84 · Cited by 12

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Ciampini, M., Perlmutter, P., & Watson, K. (2007) · Tetrahedron Asymmetry · doi:10.1016/j.tetasy.2006.12.018 · Cited by 12

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Blanchet, É., Vansteelandt, M., Bot, R. L., Egorov, M., Guitton, Y., Pouchus, Y. F., & Grovel, O. (2014) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2014.04.012 · Cited by 12

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Weiss, L. M., Zhou, G., & Zhang, H. (2003) · Journal of Eukaryotic Microbiology · doi:10.1111/j.1550-7408.2003.tb00643.x · Cited by 12

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Lee, H. W., Cho, C. S., Kang, S. K., Yoo, Y. S., Shin, J. S., & Ahn, S. K. (2007) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.55.1024 · Cited by 12

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Smith, S. J., Hadler, K. S., Schenk, G., Hanson, G. R., & Mitić, N. (2009) · Biological magnetic resonance · doi:10.1007/978-1-4419-1139-1_9 · Cited by 12

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Sikora, S., & Godzik, A. (2004) · Protein Science · doi:10.1110/ps.03454904 · Cited by 12

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Bontems, F., Floch, P. L., Duffieux, F., Biderre‐Petit, C., Peyret, P., & Lallemand, J. (2003) · Biophysical Chemistry · doi:10.1016/s0301-4622(03)00056-5 · Cited by 12

(−)‐FR182877 Is a Potent and Selective Inhibitor of Carboxylesterase‐1

Adam, G. C., Vanderwal, C. D., Sorensen, E. J., & Cravatt, B. F. (2003) · Angewandte Chemie · doi:10.1002/ange.200352576 · Cited by 12

Molecular characterization of Nosema bombycis methionine aminopeptidase 2 (MetAP2) gene and evaluation of anti-microsporidian activity of Fumagilin-B in silkworm Bombyx mori

Esvaran, V. G., Gupta, T., Nayaka, A. R. N., Sivaprasad, V., & Ponnuvel, K. M. (2018) · 3 Biotech · doi:10.1007/s13205-018-1411-z · Cited by 11

Discovery and Preclinical Development of Antigiardiasis Fumagillol Derivatives

Padia, J. K., Kulakova, L., Galkin, A. G., & Herzberg, O. (2020) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00582-20 · Cited by 11

Structural insights into N-terminal methionine cleavage by the human mitochondrial methionine aminopeptidase, MetAP1D

Lee, Y. J., Kim, H., Lee, E., Hahn, H., Heo, Y., Jang, D. M., Kwak, K., Kim, H. S., & Kim, H. S. (2023) · Scientific Reports · doi:10.1038/s41598-023-49332-6 · Cited by 11

Effect of fumagillin on adipocyte differentiation and adipogenesis

Scroyen, I., Christiaens, V., & LIJNEN, H. R. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.11.015 · Cited by 11

Metabolites of PPI-2458, a Selective, Irreversible Inhibitor of Methionine Aminopeptidase-2: Structure Determination and In Vivo Activity

Arico-Muendel, C. C., Belanger, B., Benjamin, D. R., Blanchette, H., Caiazzo, T., DeLorey, J. L., Doyle, E., Gradhand, U., Griffin, S. T., Hill, S. E., et al. (2013) · Drug Metabolism and Disposition · doi:10.1124/dmd.112.048355 · Cited by 11

Discovery of natural product ovalicin sensitive type 1 methionine aminopeptidases: molecular and structural basis

Pillalamarri, V., Arya, T., Haque, N., Bala, S., Marapaka, A. K., & Addlagatta, A. (2019) · Biochemical Journal · doi:10.1042/bcj20180874 · Cited by 11

MetAP2 inhibition reduces food intake and body weight in a ciliopathy mouse model of obesity

Pottorf, T. S., Fagan, M. P., Burkey, B. F., Cho, D. J., Vath, J. E., & Tran, P. V. (2019) · JCI Insight · doi:10.1172/jci.insight.134278 · Cited by 11

Co- and Posttranslational Processing: The Removal of Methionine

Bradshaw, R. A., Hope, C. J., Yi, E., & Walker, K. W. (2002) · The Enzymes · doi:10.1016/s1874-6047(02)80015-4 · Cited by 11

Molecular Discrimination of Type-I over Type-II Methionyl Aminopeptidases

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Covalent Probes To Capture Legionella pneumophila Dup Effector Enzymes

Kloet, M. S., Mukhopadhyay, R., Mukherjee, R., Misra, M., Jeong, M., Ormeño, C. M. P. T., Moutsiopoulou, A., Tjokrodirijo, R. T. N., van Veelen, P. A., Shin, D., et al. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c08168 · Cited by 10

Broad‐range metalloprotease profiling in plants uncovers immunity provided by defence‐related metalloenzyme

Morimoto, K., Krahn, D., Kaschani, F., Hopkinson‐Woolley, D., Gee, A., Buscaill, P., Mohammed, S., Sieber, S. A., Cravatt, B. F., Schofield, C. J., et al. (2022) · New Phytologist · doi:10.1111/nph.18200 · Cited by 10

Two New Picoline-Derived Meroterpenoids with Anti-Acetylcholinesterase Activity from Ascidian-Derived Fungus Amphichorda felina

Jiang, M., Guo, H., Wu, Q., Yuan, S., & Liu, L. (2022) · Molecules · doi:10.3390/molecules27165076 · Cited by 11

Novel Antibacterial Targets in Protein Biogenesis Pathways

Potteth, U. S., Upadhyay, T., Saini, S., & Saraogi, I. (2021) · ChemBioChem · doi:10.1002/cbic.202100459 · Cited by 12

Computational Approaches to Enzyme Inhibition by Marine Natural Products in the Search for New Drugs

Gago, F. (2023) · Marine Drugs · doi:10.3390/md21020100 · Cited by 13

Monitoring of mitotic index and frequency of micronuclei in evaluation of genotoxic potential of fumagillin (dicyclohexylamine) in vivo

Stevanović, J., Stanimirović, Z., Ivana, P., & Lazarevic, M. (2006) · Acta veterinaria · doi:10.2298/avb0606437s · Cited by 10

Total synthesis and antiangiogenic activity of cyclopentane analogues of fumagillol

Jeong, B., Choi, N. S., Ahn, S. K., Bae, H., Kim, H. S., & Kim, D. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.05.065 · Cited by 10

Encephalitozoon cuniculi (Microspora): Characterization of a Phospholipid Metabolic Pathway Potentially Linked to Therapeutics

Alaoui, H. E., Bata, J., Peyret, P., & Vivarès, C. P. (2001) · Experimental Parasitology · doi:10.1006/expr.2001.4635 · Cited by 10

Crystal structure of a methionine aminopeptidase (TM1478) from Thermotoga maritima at 1.9 Å resolution

Spraggon, G., Schwarzenbacher, R., Kreusch, A., McMullan, D., Brinen, L. S., Cánaves, J. M., Dai, X., Deacon, A. M., Elsliger, M., Eshagi, S., et al. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20084 · Cited by 10

Identification of a Cryptic Pocket in Methionine Aminopeptidase-II Using Adaptive Bandit Molecular Dynamics Simulations and Markov State Models

Rubina, R., Moin, S. T., & Haider, S. M. (2024) · ACS Omega · doi:10.1021/acsomega.4c02516 · Cited by 10

The nascent polypeptide-associated complex (NAC) as regulatory hub on ribosomes

Rabl, L., & Deuerling, E. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0114 · Cited by 9

Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2.

Griffith, E. C., Su, Z., Niwayama, S., Ramsay, C. A., Chang, Y.-H., & Liu, J. O. (1998) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.95.26.15183 · Cited by 238

Understanding the Selectivity of Fumagillin for the Methionine Aminopeptidase Type II

Klein, C. D. P., & Folkers, G. (2003) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.3727/000000003108748036 · Cited by 18

Design and synthesis of highly potent fumagillin analogues from homology modeling for a human MetAP-2

Han, C. K., Ahn, S. K., Choi, N. S., Hong, R. K., Moon, S. K., Chun, H. S., Lee, S. J., Kim, J. W., Hong, C. I., Kim, D., et al. (2000) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(99)00577-6 · Cited by 58

Carbamate Analogues of Fumagillin as Potent, Targeted Inhibitors of Methionine Aminopeptidase-2

Arico-Muendel, C. C., Benjamin, D. R., Caiazzo, T., Centrella, P. A., Contonio, B. D., Cook, C. M., Doyle, E., Hannig, G., Labenski, M., Searle, L. L., et al. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm901260k · Cited by 29

Spiroepoxytriazoles Are Fumagillin-like Irreversible Inhibitors of MetAP2 with Potent Cellular Activity

Morgen, M., Jöst, C., Malz, M., Janowski, R., Niessing, D., Klein, C. D. P., Gunkel, N., & Miller, A. K. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00755 · Cited by 38