A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus (378 views)
Mol Biosyst (ISSN: 1742-206x), 2010; 6(12): 2498-2507.
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Paper type: Journal Article,
Impact factor: 3.825, 5-year impact factor: 3.986
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78149445520&partnerID=40&md5=01cd60e51bf58e7311f20af6182cfa4b
Keywords: Acylaminoacyl Peptidase, Acylaminoacyl-Peptidase, Peptide Hydrolase, Phosphatidylethanolamine Binding Protein, Proteinase Inhibitor, Amino Acid Sequence, Article, Chemical Structure, Chemistry, Drug Antagonism, Enzymology, Ic 50, Isolation And Purification, Kinetics, Metabolism, Molecular Genetics, Polyacrylamide Gel Electrophoresis, Protein Multimerization, Protein Transport, Sequence Alignment, Structural Homology, Sulfolobus Solfataricus, Inhibitory Concentration 50, Models, Molecular Sequence Data, Protease Inhibitors, Aeropyrum, Aeropyrum Pernix, Archaea, Mammalia, Pyrococcus Horikoshii,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, IBP-CNR, Napoli, Italy
Institute of Biostructures and Bioimaging, IBB-CNR, via Mezzocannone 16 80134, Napoli, Italy
Institute of Crystallography, IC-CNR, Bari, Italy
Department of Structural and Functional Biology, University of Naples Federico II, Napoli, Italy
References:
Hengst, U., Albrecht, H., Hess, D., Monard, D., (2001) J. Biol. Chem., 276, pp. 535-54
Mima, J., Narita, Y., Chiba, H., Hayashi, R., (2003) J. Biol. Chem., 278, pp. 29792-29800
Vallee, B.S., Tauc, P., Brochon, J.C., Maget-Dana, R., Lelievre, D., Metz-Boutigue, M.H., Bureaun, N., Schoentgen, F., (2001) Eur. J. Biochem., 268, pp. 5831-5841
Yeung, K., Seitz, T., Li, S., Janosch, P., McFerran, B., Kaiser, C., Fee, F., Koich, W., (1999) Nature, 401, pp. 173-177
Bruun, A.W., Svendsen, I., Sorensen, S.O., Kielland-Brandt, M.C., Winther, J.R., (1998) Biochemistry, 37, pp. 3351-3357
Palmieri, G., Catara, G., Saviano, M., Langella, E., Gogliettino, M., Rossi, M., (2009) J. Proteome Res., 8 (1), pp. 327-334
Polgar, L., (2002) Cell. Mol. Life Sci., 59, pp. 349-362
Rawlings, N.D., Polgar, L., Barrett, A.J., (1991) Biochem. J., 279, pp. 907-908
Jones, W.M., Scaloni, A., Manning, J.M., (1994) Methods Enzymol., 244, pp. 227-231
Fülöp, V., Böcskei, Z., Polgar, L., (1998) Cell, 94 (2), pp. 161-170
Rea, D., Fülöp, V., (2006) Cell Biochem. Biophys., 44, pp. 349-365
Kiss, A.L., Hornung, B., Rádi, K., Gengeliczki, Z., Sztáray, B., Juhász, T., Szeltner, Z., Polgár, L., (2007) J. Mol. Biol., 368, pp. 509-520
Bartlam, M., Wang, G., Yang, H., Gao, R., Zhao, X., Xie, G., Cao, S., Rao, Z., (2004) Structure, 12, pp. 1481-1488
Gade, W., Brown, J.L., (1978) J. Biol. Chem., 253, pp. 5012-5018
Sharma, K.K., Ortwerth, B.J., (1993) Eur. J. Biochem., 216, pp. 631-637
Ishikawa, K., Ishida, H., Koyama, Y., Kawarabayasi, Y., Kawahara, J., Matsui, E., Matsui, I., (1998) J. Biol. Chem., 273, pp. 17726-17731
Kobayashi, K., Smith, J.A., (1987) J. Biol. Chem., 262, pp. 11435-11445
Raphel, V., Giardina, T., Guevel, L., Perrier, J., Dupuis, L., Guo, X.-J., Puigserver, A., (1999) Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol., 1432, pp. 371-381
Scaloni, A., Jones, W.M., Barra, D., Pospischil, M., Sassa, S., Popowicz, A., Manning, L.R., Manning, J.M., (1992) J. Biol. Chem., 267, pp. 3811-3818
Erlandsson, R., Boldog, F., Persson, B., Zabarousky, E.R., Allikmets, R.L., Sümegi, J., Klein, G., Jörnvall, H., (1991) Oncogene, 6, pp. 1293-1295
Naylor, S.L., Marshall, A., Hensel, C., Martinez, P.F., Holley, B., Sakaguchi, A.Y., (1989) Genomics, 43, pp. 55-361
Richards, P.G., Johnson, M.K., Ray, D.R., (2000) Mol. Pharmacol., 58, pp. 577-583
Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V., Mann, M., (2006) Nat. Protoc., 1 (6), pp. 2856-2860
Elferink, M.G., Albers, S.V., Konings, W.N., Driessen, A., (2001) Mol. Microbiol., 39 (6), pp. 1494-1503
Kelley, L.A., Sternberg, M.J.E., (2009) Nat. Protoc., 4, pp. 363-371
Chen, R., Li, L., Weng, Z., (2003) Proteins: Struct., Funct., Genet., 52, pp. 80-87
Wiehe, K., Pierce, B., Tong, W.W., Hwang, H., Mintseris, J., Weng, Z., (2007) Proteins: Struct., Funct., Bioinf., 69, pp. 719-725
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graphics, 14, pp. 51-55
Reynolds, C., Damerell, D., Jones, S., (2009) Bioinformatics, 25, pp. 413-414
Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Higgins, D.G., (2007) Bioinformatics, 23, pp. 2947-2948
Kiss, A.L., Szeltnera, Z., Fulop, V., Polgar, L., (2004) FEBS Lett., 571, pp. 17-20
Yang, G., Bai, A., Gao, L., Zhang, Z., Zheng, B.M., Feng, Y., (2009) Biochim. Biophys. Acta, Proteins Proteomics, 1794, pp. 94-102
Kiss, A.L., Palló, A., Náray-Szabó, G., Harmat, V., Polgár, L., (2008) J. Struct. Biol., 162, pp. 312-323
Wang, Q., Yangm, G., Liu, Y., Feng, Y., (2006) J. Biol. Chem., 281, pp. 18618-18625
Rasmussen, H.B., Branner, S., Wiberg, F.C., Wagtmann, N., (2003) Nat. Struct. Biol., 10, pp. 19-25
Shan, L., Mathews, I.I., Khosla, C., (2005) Proc. Natl. Acad. Sci. U. S. A., 102, pp. 3599-604
Fuxreiter, M., Magyar, C., Juhász, T., Szeltner, Z., Polgár, L., Simon, I., (2005) Proteins: Struct., Funct., Bioinf., 60, pp. 504-512
Aertgeerts, K., Ye, S., Tennant, M.G., Kraus, M.L., Rogers, J., Sang, B.C., Skene, R.J., Prasad, G.S., (2004) Protein Sci., 13, pp. 412-21
Yamin, R., Zhao, C., O'Connor, P.B., McKee, A.C., Abraham, C.R., (2009) Mol. Neurodegener., 4, p. 33
Olmos, C., Sandoval, R., Rozas, C., Navarro, S., Wyneken, U., Zeise, M., Morales, B., Pancetti, F., (2009) Toxicol. Appl. Pharmacol., 238, pp. 37-46
Vallee, B. S., Tauc, P., Brochon, J. C., Maget-Dana, R., Lelievre, D., Metz-Boutigue, M. H., Bureaun, N., Schoentgen, F., (2001) Eur. J. Biochem., 268, pp. 5831-5841
Bruun, A. W., Svendsen, I., Sorensen, S. O., Kielland-Brandt, M. C., Winther, J. R., (1998) Biochemistry, 37, pp. 3351-3357
Rawlings, N. D., Polgar, L., Barrett, A. J., (1991) Biochem. J., 279, pp. 907-908
Jones, W. M., Scaloni, A., Manning, J. M., (1994) Methods Enzymol., 244, pp. 227-231
F l p, V., B cskei, Z., Polgar, L., (1998) Cell, 94 (2), pp. 161-170
Rea, D., F l p, V., (2006) Cell Biochem. Biophys., 44, pp. 349-365
Kiss, A. L., Hornung, B., R di, K., Gengeliczki, Z., Szt ray, B., Juh sz, T., Szeltner, Z., Polg r, L., (2007) J. Mol. Biol., 368, pp. 509-520
Sharma, K. K., Ortwerth, B. J., (1993) Eur. J. Biochem., 216, pp. 631-637
Naylor, S. L., Marshall, A., Hensel, C., Martinez, P. F., Holley, B., Sakaguchi, A. Y., (1989) Genomics, 43, pp. 55-361
Richards, P. G., Johnson, M. K., Ray, D. R., (2000) Mol. Pharmacol., 58, pp. 577-583
Elferink, M. G., Albers, S. V., Konings, W. N., Driessen, A., (2001) Mol. Microbiol., 39 (6), pp. 1494-1503
Kelley, L. A., Sternberg, M. J. E., (2009) Nat. Protoc., 4, pp. 363-371
Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Higgins, D. G., (2007) Bioinformatics, 23, pp. 2947-2948
Kiss, A. L., Szeltnera, Z., Fulop, V., Polgar, L., (2004) FEBS Lett., 571, pp. 17-20
Kiss, A. L., Pall, A., N ray-Szab, G., Harmat, V., Polg r, L., (2008) J. Struct. Biol., 162, pp. 312-323
Rasmussen, H. B., Branner, S., Wiberg, F. C., Wagtmann, N., (2003) Nat. Struct. Biol., 10, pp. 19-25
Mol Biosyst (ISSN: 1742-206x), 2010; 6(12): 2498-2507.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.825, 5-year impact factor: 3.986
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-78149445520&partnerID=40&md5=01cd60e51bf58e7311f20af6182cfa4b
Keywords: Acylaminoacyl Peptidase, Acylaminoacyl-Peptidase, Peptide Hydrolase, Phosphatidylethanolamine Binding Protein, Proteinase Inhibitor, Amino Acid Sequence, Article, Chemical Structure, Chemistry, Drug Antagonism, Enzymology, Ic 50, Isolation And Purification, Kinetics, Metabolism, Molecular Genetics, Polyacrylamide Gel Electrophoresis, Protein Multimerization, Protein Transport, Sequence Alignment, Structural Homology, Sulfolobus Solfataricus, Inhibitory Concentration 50, Models, Molecular Sequence Data, Protease Inhibitors, Aeropyrum, Aeropyrum Pernix, Archaea, Mammalia, Pyrococcus Horikoshii,
Affiliations:
*** IBB - CNR ***
Institute of Protein Biochemistry, IBP-CNR, Napoli, Italy
Institute of Biostructures and Bioimaging, IBB-CNR, via Mezzocannone 16 80134, Napoli, Italy
Institute of Crystallography, IC-CNR, Bari, Italy
Department of Structural and Functional Biology, University of Naples Federico II, Napoli, Italy
References:
Hengst, U., Albrecht, H., Hess, D., Monard, D., (2001) J. Biol. Chem., 276, pp. 535-54
Mima, J., Narita, Y., Chiba, H., Hayashi, R., (2003) J. Biol. Chem., 278, pp. 29792-29800
Vallee, B.S., Tauc, P., Brochon, J.C., Maget-Dana, R., Lelievre, D., Metz-Boutigue, M.H., Bureaun, N., Schoentgen, F., (2001) Eur. J. Biochem., 268, pp. 5831-5841
Yeung, K., Seitz, T., Li, S., Janosch, P., McFerran, B., Kaiser, C., Fee, F., Koich, W., (1999) Nature, 401, pp. 173-177
Bruun, A.W., Svendsen, I., Sorensen, S.O., Kielland-Brandt, M.C., Winther, J.R., (1998) Biochemistry, 37, pp. 3351-3357
Palmieri, G., Catara, G., Saviano, M., Langella, E., Gogliettino, M., Rossi, M., (2009) J. Proteome Res., 8 (1), pp. 327-334
Polgar, L., (2002) Cell. Mol. Life Sci., 59, pp. 349-362
Rawlings, N.D., Polgar, L., Barrett, A.J., (1991) Biochem. J., 279, pp. 907-908
Jones, W.M., Scaloni, A., Manning, J.M., (1994) Methods Enzymol., 244, pp. 227-231
Fülöp, V., Böcskei, Z., Polgar, L., (1998) Cell, 94 (2), pp. 161-170
Rea, D., Fülöp, V., (2006) Cell Biochem. Biophys., 44, pp. 349-365
Kiss, A.L., Hornung, B., Rádi, K., Gengeliczki, Z., Sztáray, B., Juhász, T., Szeltner, Z., Polgár, L., (2007) J. Mol. Biol., 368, pp. 509-520
Bartlam, M., Wang, G., Yang, H., Gao, R., Zhao, X., Xie, G., Cao, S., Rao, Z., (2004) Structure, 12, pp. 1481-1488
Gade, W., Brown, J.L., (1978) J. Biol. Chem., 253, pp. 5012-5018
Sharma, K.K., Ortwerth, B.J., (1993) Eur. J. Biochem., 216, pp. 631-637
Ishikawa, K., Ishida, H., Koyama, Y., Kawarabayasi, Y., Kawahara, J., Matsui, E., Matsui, I., (1998) J. Biol. Chem., 273, pp. 17726-17731
Kobayashi, K., Smith, J.A., (1987) J. Biol. Chem., 262, pp. 11435-11445
Raphel, V., Giardina, T., Guevel, L., Perrier, J., Dupuis, L., Guo, X.-J., Puigserver, A., (1999) Biochim. Biophys. Acta, Protein Struct. Mol. Enzymol., 1432, pp. 371-381
Scaloni, A., Jones, W.M., Barra, D., Pospischil, M., Sassa, S., Popowicz, A., Manning, L.R., Manning, J.M., (1992) J. Biol. Chem., 267, pp. 3811-3818
Erlandsson, R., Boldog, F., Persson, B., Zabarousky, E.R., Allikmets, R.L., Sümegi, J., Klein, G., Jörnvall, H., (1991) Oncogene, 6, pp. 1293-1295
Naylor, S.L., Marshall, A., Hensel, C., Martinez, P.F., Holley, B., Sakaguchi, A.Y., (1989) Genomics, 43, pp. 55-361
Richards, P.G., Johnson, M.K., Ray, D.R., (2000) Mol. Pharmacol., 58, pp. 577-583
Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V., Mann, M., (2006) Nat. Protoc., 1 (6), pp. 2856-2860
Elferink, M.G., Albers, S.V., Konings, W.N., Driessen, A., (2001) Mol. Microbiol., 39 (6), pp. 1494-1503
Kelley, L.A., Sternberg, M.J.E., (2009) Nat. Protoc., 4, pp. 363-371
Chen, R., Li, L., Weng, Z., (2003) Proteins: Struct., Funct., Genet., 52, pp. 80-87
Wiehe, K., Pierce, B., Tong, W.W., Hwang, H., Mintseris, J., Weng, Z., (2007) Proteins: Struct., Funct., Bioinf., 69, pp. 719-725
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graphics, 14, pp. 51-55
Reynolds, C., Damerell, D., Jones, S., (2009) Bioinformatics, 25, pp. 413-414
Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Higgins, D.G., (2007) Bioinformatics, 23, pp. 2947-2948
Kiss, A.L., Szeltnera, Z., Fulop, V., Polgar, L., (2004) FEBS Lett., 571, pp. 17-20
Yang, G., Bai, A., Gao, L., Zhang, Z., Zheng, B.M., Feng, Y., (2009) Biochim. Biophys. Acta, Proteins Proteomics, 1794, pp. 94-102
Kiss, A.L., Palló, A., Náray-Szabó, G., Harmat, V., Polgár, L., (2008) J. Struct. Biol., 162, pp. 312-323
Wang, Q., Yangm, G., Liu, Y., Feng, Y., (2006) J. Biol. Chem., 281, pp. 18618-18625
Rasmussen, H.B., Branner, S., Wiberg, F.C., Wagtmann, N., (2003) Nat. Struct. Biol., 10, pp. 19-25
Shan, L., Mathews, I.I., Khosla, C., (2005) Proc. Natl. Acad. Sci. U. S. A., 102, pp. 3599-604
Fuxreiter, M., Magyar, C., Juhász, T., Szeltner, Z., Polgár, L., Simon, I., (2005) Proteins: Struct., Funct., Bioinf., 60, pp. 504-512
Aertgeerts, K., Ye, S., Tennant, M.G., Kraus, M.L., Rogers, J., Sang, B.C., Skene, R.J., Prasad, G.S., (2004) Protein Sci., 13, pp. 412-21
Yamin, R., Zhao, C., O'Connor, P.B., McKee, A.C., Abraham, C.R., (2009) Mol. Neurodegener., 4, p. 33
Olmos, C., Sandoval, R., Rozas, C., Navarro, S., Wyneken, U., Zeise, M., Morales, B., Pancetti, F., (2009) Toxicol. Appl. Pharmacol., 238, pp. 37-46
Vallee, B. S., Tauc, P., Brochon, J. C., Maget-Dana, R., Lelievre, D., Metz-Boutigue, M. H., Bureaun, N., Schoentgen, F., (2001) Eur. J. Biochem., 268, pp. 5831-5841
Bruun, A. W., Svendsen, I., Sorensen, S. O., Kielland-Brandt, M. C., Winther, J. R., (1998) Biochemistry, 37, pp. 3351-3357
Rawlings, N. D., Polgar, L., Barrett, A. J., (1991) Biochem. J., 279, pp. 907-908
Jones, W. M., Scaloni, A., Manning, J. M., (1994) Methods Enzymol., 244, pp. 227-231
F l p, V., B cskei, Z., Polgar, L., (1998) Cell, 94 (2), pp. 161-170
Rea, D., F l p, V., (2006) Cell Biochem. Biophys., 44, pp. 349-365
Kiss, A. L., Hornung, B., R di, K., Gengeliczki, Z., Szt ray, B., Juh sz, T., Szeltner, Z., Polg r, L., (2007) J. Mol. Biol., 368, pp. 509-520
Sharma, K. K., Ortwerth, B. J., (1993) Eur. J. Biochem., 216, pp. 631-637
Naylor, S. L., Marshall, A., Hensel, C., Martinez, P. F., Holley, B., Sakaguchi, A. Y., (1989) Genomics, 43, pp. 55-361
Richards, P. G., Johnson, M. K., Ray, D. R., (2000) Mol. Pharmacol., 58, pp. 577-583
Elferink, M. G., Albers, S. V., Konings, W. N., Driessen, A., (2001) Mol. Microbiol., 39 (6), pp. 1494-1503
Kelley, L. A., Sternberg, M. J. E., (2009) Nat. Protoc., 4, pp. 363-371
Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Higgins, D. G., (2007) Bioinformatics, 23, pp. 2947-2948
Kiss, A. L., Szeltnera, Z., Fulop, V., Polgar, L., (2004) FEBS Lett., 571, pp. 17-20
Kiss, A. L., Pall, A., N ray-Szab, G., Harmat, V., Polg r, L., (2008) J. Struct. Biol., 162, pp. 312-323
Rasmussen, H. B., Branner, S., Wiberg, F. C., Wagtmann, N., (2003) Nat. Struct. Biol., 10, pp. 19-25
A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
This work describes the identification and characterization of a Sulfolobus solfataricus acylpeptide hydrolase, named APEHSs, recognised as a new protease target of the endogenous PEBP inhibitor, SsCEI. APEH is one of the four members of the prolyl oligopeptidase (POP) family, which removes acylated amino acid residues from the N terminus of oligopeptides. APEHSs is a cytosolic homodimeric protein with a molecular mass of 125 kDa. It displays a similar exopeptidase and endopeptidase activity to the homologous enzymes from Aeropyrum pernix and Pyrococcus horikoshii. Herein we demonstrate that SsCEI is the first PEBP protein found to efficiently inhibit APEH from both S. solfataricus and mammalian sources with IC50 values in the nanomolar range. The 3D model of APEHSs shows the typical structural features of the POP family including an N-terminal β-propeller and a C-terminal α/β hydrolase domain. Moreover, to gain insights into the binding mode of SsCEI toward APEHSs, a structural model of the inhibition complex is proposed, suggesting a mechanism of steric blockage on substrate access to the active site or on product release. Like other POP enzymes, APEH may constitute a new therapeutic target for the treatment of a number of pathologies and this study may represent a starting point for further medical research. © 2010 The Royal Society of Chemistry.
This work describes the identification and characterization of a Sulfolobus solfataricus acylpeptide hydrolase, named APEHSs, recognised as a new protease target of the endogenous PEBP inhibitor, SsCEI. APEH is one of the four members of the prolyl oligopeptidase (POP) family, which removes acylated amino acid residues from the N terminus of oligopeptides. APEHSs is a cytosolic homodimeric protein with a molecular mass of 125 kDa. It displays a similar exopeptidase and endopeptidase activity to the homologous enzymes from Aeropyrum pernix and Pyrococcus horikoshii. Herein we demonstrate that SsCEI is the first PEBP protein found to efficiently inhibit APEH from both S. solfataricus and mammalian sources with IC50 values in the nanomolar range. The 3D model of APEHSs shows the typical structural features of the POP family including an N-terminal β-propeller and a C-terminal α/β hydrolase domain. Moreover, to gain insights into the binding mode of SsCEI toward APEHSs, a structural model of the inhibition complex is proposed, suggesting a mechanism of steric blockage on substrate access to the active site or on product release. Like other POP enzymes, APEH may constitute a new therapeutic target for the treatment of a number of pathologies and this study may represent a starting point for further medical research. © 2010 The Royal Society of Chemistry.
A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
| ▼ Plant polypeptides as natural enhancers of biostimulation |
A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): A study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
Other filter: ([btitle,keywords] "Acylaminoacyl Peptid ...
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Impact Factor: 1.724
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Perrone-filardi P, Dellegrottaglie S, Rudd JH, Costanzo P, Marciano C, Vassallo E, Marsico F, Ruggiero D, Petretta MP, Chiariello M, Cuocolo A
* Molecular imaging of atherosclerosis in translational medicine (756 views)
Eur J Nucl Med (ISSN: 1619-7089, 1619-7070, 0340-6997), 2011 May; 38(5): 969-975.
Impact Factor: 4.991
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Palmieri G, Catara G, Saviano M, Langella E, Gogliettino M, Rossi M
* First archaeal PEPB-serine protease inhibitor from sulfolobus solfataricus with noncanonical amino acid sequence in the reactive-site loop (398 views)
J Proteome Res (ISSN: 1535-3893), 2009 Jan; 8(1): 327-334.
Impact Factor: 5.132
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Gioia M, Monaco S, Van Den Steen PE, Sbardella D, Grasso G, Marini S, Overall CM, Opdenakker G, Coletta M
* The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase (460 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
Impact Factor: 3.871
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Galdiero S, Falanga A, Vitiello M, Raiola L, Fattorusso R, Browne H, Pedone C, Isernia C, Galdiero M
* Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein (632 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 31; 283(44): 29993-30009.
Impact Factor: 5.52
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Marasco D, Perretta G, Sabatella M, Ruvo M
* Past and Future Perspectives of Synthetic Peptide Libraries (561 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Oct; 9(5): 447-467.
Impact Factor: 3.011
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Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
* A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111) (357 views)
Journal Of The American Society For Mass Spectrometry (ISSN: 1044-0305), 2007 May; 18(5): 961-969.
Impact Factor: 3.664
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Grasso G, D'Agata R, Rizzarelli E, Spoto G, D'Andrea LD, Pedone C, Picardi A, Romanelli A, Fragai M, Yeo KJ
* Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS (577 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2005 Dec; 40(12): 1565-1571.
Impact Factor: 3.574
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De Simone G, Menchise V, Omaggio S, Pedone C, Scozzafava A, Supuran CT
* Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: Molecular and X-ray crystallographic studies (354 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Sep 5; 42(30): 9013-9021.
Impact Factor: 3.922
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Spalletti-cernia D, Sorrentino R, Di Gaetano S, Arciello A, Garbi C, Piccoli R, D'Alessio G, Vecchio G, Laccetti P, Santoro M
* Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis (393 views)
Journal Of Clinical Endocrinology & Metabolism (ISSN: 0021-972x), 2003 Jun; 88(6): 2900-2907.
Impact Factor: 5.873
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De Falco S, Ruvoletto MG, Verdoliva A, Ruvo M, Raucci A, Marino M, Senatore S, Cassani G, Alberti A, Pontisso P, Fassina G
* Cloning and Expression of a Novel Hepatitis B Virus-binding Protein from HepG2 Cells (624 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2001 Sep 28; 276(39): 36613-36623.
Impact Factor: 7.258
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Lombardi A, De Simone G, Galdiero S, Staiano N, Nastri F, Pavone V
From natural to synthetic multisite thrombin inhibitors (349 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1999; 51(1): 19-39.
Impact Factor: 2.331
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Pavone V, De Simone G, Nastri F, Galdiero S, Staiano N, Lombardi A, Pedone C
Multiple binding mode of reversible synthetic thrombin inhibitors. A comparative structural analysis (590 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 1998 Sep; 379(8-9): 987-1006.
Impact Factor: 2.636
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* Selective inhibition of acylpeptide hydrolase in SAOS-2 osteosarcoma cells: is this enzyme a viable anticancer target? (21 views)
Mol Biol Rep (ISSN: 0301-4851linking), 2021 Feb; 48(2): 1505-1519.
Impact Factor: 2.316
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Palmieri G, Cocca E, Gogliettino M, Valentino R, Ruvo M, Cristofano G, Angiolillo A, Balestrieri M, Rossi M, Di Costanzo A
* Low Erythrocyte Levels of Proteasome and Acyl-Peptide Hydrolase (APEH) Activities in Alzheimer's Disease: A Sign of Defective Proteostasis? (350 views)
J Alzheimers Dis (ISSN: 1387-2877, 1387-2877linking), 2017; 60(3): 1097-1106.
Impact Factor: 3.476
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Palumbo R, Gogliettino M, Cocca E, Iannitti R, Sandomenico A, Ruvo M, Balestrieri M, Rossi M, Palmieri G
* APEH Inhibition Affects Osteosarcoma Cell Viability via Downregulation of the Proteasome (341 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2016 Sep 23; 17(10): N/D-N/D.
Impact Factor: 3.226
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Milardi D, Pappalardo M
* Molecular dynamics: New advances in drug discovery (433 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 0223-5234linking), 2015; 91: 1-3.
Impact Factor: 3.902
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Bergamo P, Cocca E, Palumbo R, Gogliettino M, Rossi M, Palmieri G
* RedOx status, proteasome and APEH: Insights into anticancer mechanisms of t10, c12-conjugated linoleic acid isomer on A375 melanoma cells (742 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2013 Nov 19; 8(11): N/D-N/D.
Impact Factor: 3.534
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Doti N, Raimondo D, Sabatella M, Ruvo M
* Identification of Protease Inhibitors by a Fast Fluorimetric Assay (653 views)
Mol Biotechnol (ISSN: 1073-6085, 1559-0305electronic, 1073-6085linking), 2013 Jun; 54(2): 283-291.
Impact Factor: 2.275
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Sandomenico A, Russo A, Palmieri G, Bergamo P, Gogliettino M, Falcigno L, Ruvo M
* Small peptide inhibitors of acetyl-peptide hydrolase having an uncommon mechanism of inhibition and a stable bent conformation (521 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2012 Mar 8; 55(5): 2102-2111.
Impact Factor: 5.614
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Palmieri G, Bergamo P, Luini A, Ruvo M, Gogliettino M, Langella E, Saviano M, Hegde RN, Sandomenico A, Rossi M
* Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation (492 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2011 Oct 10; 6(10): e25888-e25888.
Impact Factor: 4.092
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Cuocolo A
Current research in nuclear medicine and molecular imaging in Italy: Highlights of the 10th National Congress of the Italian Association of Nuclear Medicine and Molecular Imaging (466 views)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1824-4785linking), 2011 Jun; 55(3): 280-300.
Impact Factor: 1.724
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Perrone-filardi P, Dellegrottaglie S, Rudd JH, Costanzo P, Marciano C, Vassallo E, Marsico F, Ruggiero D, Petretta MP, Chiariello M, Cuocolo A
* Molecular imaging of atherosclerosis in translational medicine (756 views)
Eur J Nucl Med (ISSN: 1619-7089, 1619-7070, 0340-6997), 2011 May; 38(5): 969-975.
Impact Factor: 4.991
View Export to BibTeX Export to EndNote
Palmieri G, Catara G, Saviano M, Langella E, Gogliettino M, Rossi M
* First archaeal PEPB-serine protease inhibitor from sulfolobus solfataricus with noncanonical amino acid sequence in the reactive-site loop (398 views)
J Proteome Res (ISSN: 1535-3893), 2009 Jan; 8(1): 327-334.
Impact Factor: 5.132
View Export to BibTeX Export to EndNote
Gioia M, Monaco S, Van Den Steen PE, Sbardella D, Grasso G, Marini S, Overall CM, Opdenakker G, Coletta M
* The Collagen Binding Domain of Gelatinase A Modulates Degradation of Collagen IV by Gelatinase (460 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009; 386(2): 419-434.
Impact Factor: 3.871
View Export to BibTeX Export to EndNote
Galdiero S, Falanga A, Vitiello M, Raiola L, Fattorusso R, Browne H, Pedone C, Isernia C, Galdiero M
* Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein (632 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 31; 283(44): 29993-30009.
Impact Factor: 5.52
View Export to BibTeX Export to EndNote
Marasco D, Perretta G, Sabatella M, Ruvo M
* Past and Future Perspectives of Synthetic Peptide Libraries (561 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Oct; 9(5): 447-467.
Impact Factor: 3.011
View Export to BibTeX Export to EndNote
Grasso G, Fragai M, Rizzarelli E, Spoto G, Yeo KJ
* A new methodology for monitoring the activity of cdMMP-12 anchored and freeze-dried on Au (111) (357 views)
Journal Of The American Society For Mass Spectrometry (ISSN: 1044-0305), 2007 May; 18(5): 961-969.
Impact Factor: 3.664
View Export to BibTeX Export to EndNote
Grasso G, D'Agata R, Rizzarelli E, Spoto G, D'Andrea LD, Pedone C, Picardi A, Romanelli A, Fragai M, Yeo KJ
* Activity of anchored human matrix metalloproteinase-1 catalytic domain on Au(111) surfaces monitored by ESI-MS (577 views)
J Mass Spectrom (ISSN: 1076-5174, 1096-9888), 2005 Dec; 40(12): 1565-1571.
Impact Factor: 3.574
View Export to BibTeX Export to EndNote
De Simone G, Menchise V, Omaggio S, Pedone C, Scozzafava A, Supuran CT
* Design of weakly basic thrombin inhibitors incorporating novel P1 binding functions: Molecular and X-ray crystallographic studies (354 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2003 Sep 5; 42(30): 9013-9021.
Impact Factor: 3.922
View Export to BibTeX Export to EndNote
Spalletti-cernia D, Sorrentino R, Di Gaetano S, Arciello A, Garbi C, Piccoli R, D'Alessio G, Vecchio G, Laccetti P, Santoro M
* Antineoplastic ribonucleases selectively kill thyroid carcinoma cells via caspase-mediated induction of apoptosis (393 views)
Journal Of Clinical Endocrinology & Metabolism (ISSN: 0021-972x), 2003 Jun; 88(6): 2900-2907.
Impact Factor: 5.873
View Export to BibTeX Export to EndNote
De Falco S, Ruvoletto MG, Verdoliva A, Ruvo M, Raucci A, Marino M, Senatore S, Cassani G, Alberti A, Pontisso P, Fassina G
* Cloning and Expression of a Novel Hepatitis B Virus-binding Protein from HepG2 Cells (624 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2001 Sep 28; 276(39): 36613-36623.
Impact Factor: 7.258
View Export to BibTeX Export to EndNote
Lombardi A, De Simone G, Galdiero S, Staiano N, Nastri F, Pavone V
From natural to synthetic multisite thrombin inhibitors (349 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 1999; 51(1): 19-39.
Impact Factor: 2.331
View Export to BibTeX Export to EndNote
Pavone V, De Simone G, Nastri F, Galdiero S, Staiano N, Lombardi A, Pedone C
Multiple binding mode of reversible synthetic thrombin inhibitors. A comparative structural analysis (590 views)
Biol Chem Biological Chemistry (ISSN: 1431-6730, 1437-4315), 1998 Sep; 379(8-9): 987-1006.
Impact Factor: 2.636
View Export to BibTeX Export to EndNote
21 Records (20 excluding Abstracts).
Total impact factor: 81.942 (78.408 excluding Abstracts).
Total 5 year impact factor: 74.331 (70.316 excluding Abstracts).
Total impact factor: 81.942 (78.408 excluding Abstracts).
Total 5 year impact factor: 74.331 (70.316 excluding Abstracts).
378 views. Last view on Friday 26 May 2023, 20:06:11
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