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 (393 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:
Not available.
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:
Not available.
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
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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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View Export to BibTeX Export to EndNote
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View Export to BibTeX Export to EndNote
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* APEH Inhibition Affects Osteosarcoma Cell Viability via Downregulation of the Proteasome (343 views)
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View Export to BibTeX Export to EndNote
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* Molecular dynamics: New advances in drug discovery (456 views)
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Impact Factor: 3.902
View Export to BibTeX Export to EndNote
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* RedOx status, proteasome and APEH: Insights into anticancer mechanisms of t10, c12-conjugated linoleic acid isomer on A375 melanoma cells (754 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2013 Nov 19; 8(11): N/D-N/D.
Impact Factor: 3.534
View Export to BibTeX Export to EndNote
Doti N, Raimondo D, Sabatella M, Ruvo M
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Mol Biotechnol (ISSN: 1073-6085, 1559-0305electronic, 1073-6085linking), 2013 Jun; 54(2): 283-291.
Impact Factor: 2.275
View Export to BibTeX Export to EndNote
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 (549 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2012 Mar 8; 55(5): 2102-2111.
Impact Factor: 5.614
View Export to BibTeX Export to EndNote
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 (565 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2011 Oct 10; 6(10): e25888-e25888.
Impact Factor: 4.092
View Export to BibTeX Export to EndNote
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 (535 views)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1824-4785linking), 2011 Jun; 55(3): 280-300.
Impact Factor: 1.724
View Export to BibTeX Export to EndNote
Perrone-filardi P, Dellegrottaglie S, Rudd JH, Costanzo P, Marciano C, Vassallo E, Marsico F, Ruggiero D, Petretta MP, Chiariello M, Cuocolo A
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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 (439 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 (470 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 (668 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 (590 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) (393 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 (657 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 (368 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 (408 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 (670 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 (377 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 (612 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).
393 views. Last view on Tuesday 21 November 2023, 8:09:38
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