Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ (297 views)
Oncogenesis (ISSN: 2157-9024), 2017; 6(9): N/D-N/D.
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Paper type: Journal Article,
Impact factor: 4.722, 5-year impact factor: 4.692
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032725431&doi=10.1038%2foncsis.2017.78&partnerID=40&md5=75a2dbef3e5944b1ef2c7a26491ee922
Keywords: Centromere Protein W, F Box Wd Repeat Containing Protein 7, F Box Wd Repeat Containing Protein 7 Gamma, Human Immunodeficiency Virus Protein, Nuclear Protein, Nucleophosmin, Transactivator Protein, Tumor Suppressor Protein, Unclassified Drug, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Controlled Study, Molecular Docking, Molecular Dynamics, Nucleolar Localization Signal, Priority Journal, Protein Domain, Protein Expression, Protein Protein Interaction, Protein Structure, Site Directed Mutagenesis, Structural Model,
Affiliations:
*** IBB - CNR ***
Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy
Dipartimento di Scienze Mediche, Orali e Biotecnologiche, Università di Chieti-Pescara G d'Annunzio, Via dei Vestini 31, Chieti, 66100, Italy
CeSI-Met, Università di Chieti-Pescara G d'Annunzio, Chieti, Italy
Dipartimento di Biologia e Biotecnologie C Darwin, Sapienza Università di Roma, Roma, Italy
CINECA Consorzio Interuniversitario, Sede di Roma, Roma, Italy
Dipartimento di Farmacia, Università di Napoli Federico II, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Napoli, Italy
References:
Grisendi, S., Mecucci, C., Falini, B., Pandolfi, P.P., Nucleophosmin and cancer (2006) Nat Rev Cancer, 6, pp. 493-50
Emmott, E., Hiscox, J.A., Nucleolar targeting: The hub of the matter (2009) EMBO Rep, 10, pp. 231-238
Mitrea, D.M., Cika, J.A., Guy, C.S., Ban, D., Banerjee, P.R., Stanley, C.B., Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA (2016) Elife, 5, p. e13571
Lindstrom, M.S., NPM1/B23: A multifunctional chaperone in ribosome biogenesis and chromatin remodeling (2011) Biochem Res Int, 2011, p. 195209
Colombo, E., Alcalay, M., Pelicci, P.G., Nucleophosmin and its complex network: A possible therapeutic target in hematological diseases (2011) Oncogene, 30, pp. 2595-2609
Federici, L., Falini, B., Nucleophosmin mutations in acute myeloid leukemia: A tale of protein unfolding and mislocalization (2013) Protein Sci, 22, pp. 545-556
Herrera, J.E., Savkur, R., Olson, M.O., The ribonuclease activity of nucleolar protein B23 (1995) Nucleic Acids Res, 23, pp. 3974-3979
Murano, K., Okuwaki, M., Hisaoka, M., Nagata, K., Transcription regulation of the rRNA gene by a multifunctional nucleolar protein, B23/nucleophosmin, through its histone chaperone activity (2008) Mol Cell Biol, 28, pp. 3114-3126
Scott, D.D., Oeffinger, M., Nucleolin and nucleophosmin: Nucleolar proteins with multiple functions in DNA repair (2016) Biochem Cell Biol, 94, pp. 419-432
Ziv, O., Zeisel, A., Mirlas-Neisberg, N., Swain, U., Nevo, R., Ben-Chetrit, N., Identification of novel DNA-damage tolerance genes reveals regulation of translesion DNA synthesis by nucleophosmin (2014) Nat Commun, 5, p. 5437
Okuwaki, M., Matsumoto, K., Tsujimoto, M., Nagata, K., Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone (2001) FEBS Lett, 506, pp. 272-276
Szebeni, A., Olson, M.O., Nucleolar protein B23 has molecular chaperone activities (1999) Protein Sci, 8, pp. 905-912
Okuda, M., The role of nucleophosmin in centrosome duplication (2002) Oncogene, 21, pp. 6170-6174
Wang, W., Budhu, A., Forgues, M., Wang, X.W., Temporal and spatial control of nucleophosmin by the Ran-Crm1 complex in centrosome duplication (2005) Nat Cell Biol, 7, pp. 823-830
Yang, K., Wang, M., Zhao, Y., Sun, X., Yang, Y., Li, X., A redox mechanism underlying nucleolar stress sensing by nucleophosmin (2016) Nat Commun, 7, p. 13599
Di Matteo, A., Franceschini, M., Chiarella, S., Rocchio, S., Travaglini-Allocatelli, C., Federici, L., Molecules that target nucleophosmin for cancer treatment: An update (2016) Oncotarget, 7, pp. 44821-44840
Yung, B.Y., Oncogenic role of nucleophosmin/B23 (2007) Chang Gung Med J, 30, pp. 285-293
Holmberg Olausson, K., Elsir, T., Moazemi Goudarzi, K., Nistér, M., Lindström, M.S., NPM1 histone chaperone is upregulated in glioblastoma to promote cell survival and maintain nucleolar shape (2015) Sci Rep, 5, p. 16495
Falini, B., Mecucci, C., Tiacci, E., Alcalay, M., Rosati, R., Pasqualucci, L., Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype (2005) N Engl J Med, 352, pp. 254-266
Scott, M.S., Troshin, P.V., Barton, G.J., NoD: A Nucleolar localization sequence detector for eukaryotic and viral proteins (2011) BMC Bioinformatics, 12, p. 317
Bonetti, P., Davoli, T., Sironi, C., Amati, B., Pelicci, P.G., Colombo, E., Nucleophosmin and its AML-associated mutant regulate c-Myc turnover through Fbw7 gamma (2008) J Cell Biol, 182, pp. 19-26
Davis, R.J., Welcker, M., Clurman, B.E., Tumor suppression by the Fbw7 ubiquitin ligase: Mechanisms and opportunities (2014) Cancer Cell, 26, pp. 455-464
Welcker, M., Orian, A., Grim, J.E., Eisenman, R.N., Clurman, B.E., A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size (2004) Curr Biol, 14, pp. 1852-1857
Colombo, E., Martinelli, P., Zamponi, R., Shing, D.C., Bonetti, P., Luzi, L., Delocalization and destabilization of the Arf tumour suppressor by the leukemiaassociated NPM mutant (2006) Cancer Res, 66, pp. 3044-3050
Bolli, N., De Marco, M.F., Martelli, M.P., Bigerna, B., Pucciarini, A., Rossi, R., A dosedependent tug of war involving the NPM1 leukaemic mutant, nucleophosmin, and ARF (2009) Leukemia, 23, pp. 501-509
Li, Y.P., Protein B23 is an important human factor for the nucleolar localization of the human immunodeficiency virus protein Tat (1997) J Virol, 71, pp. 4098-4102
Chun, Y., Park, B., Koh, W., Lee, S., Cheon, Y., Kim, R., New centromeric component CENP-W is an RNA-associated nuclear matrix protein that interacts with nucleophosmin/B23 protein (2011) J Biol Chem, 286, pp. 42758-42769
Foltz, D.R., Jansen, L.E., Black, B.E., Bailey, A.O., Yates, J.R., III, Cleveland, D.W., The human CENP-A centromeric nucleosome-associated complex (2006) Nat Cell Biol, 8, pp. 458-469
Mitrea, D.M., Grace, C.R., Buljan, M., Yun, M.K., Pytel, N.J., Satumba, J., Structural polymorphism in the N-terminal oligomerization domain of NPM1 (2014) Proc Natl Acad Sci USA, 111, pp. 4466-4471
Fantini, D., Vascotto, C., Marasco, D., D'Ambrosio, C., Romanello, M., Vitagliano, L., Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions (2010) Nucleic Acids Res, 38, pp. 8239-8256
Scaloni, F., Gianni, S., Federici, L., Falini, B., Brunori, M., Folding mechanism of the C-terminal domain of nucleophosmin: Residual structure in the denatured state and its pathophysiological significance (2009) FASEB J, 23, pp. 2360-2365
Scaloni, F., Federici, L., Brunori, M., Gianni, S., Deciphering the folding transition state structure and denatured state properties of Nucleophosmin C-terminal domain (2010) Proc Natl Acad Sci USA, 107, pp. 5447-5452
Scognamiglio, P.L., Di Natale, C., Leone, M., Cascella, R., Cecchi, C., Lirussi, L., Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia (2016) Oncotarget, 7, pp. 59129-59143
Di Natale, C., Scognamiglio, P.L., Cascella, R., Cecchi, C., Russo, A., Leone, M., Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions (2015) FASEB J, 29, pp. 3689-3701
Chiarella, S., De Cola, A., Scaglione, G.L., Carletti, E., Graziano, V., Barcaroli, D., Nucleophosmin mutations alter its nucleolar localization by impairing G-quadruplex binding at ribosomal DNA (2013) Nucleic Acids Res, 41, pp. 3228-3239
Federici, L., Arcovito, A., Scaglione, G.L., Scaloni, F., Lo Sterzo, C., Di Matteo, A., Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA (2010) J Biol Chem, 285, pp. 37138-37149
Gallo, A., Lo Sterzo, C., Mori, M., Di Matteo, A., Bertini, I., Banci, L., Structure of nucleophosmin DNA-binding domain and analysis of its complex with a G-quadruplex sequence from the c-MYC promoter (2012) J Biol Chem, 287, pp. 26539-26548
Leong, S.M., Tan, B.X., Bte Ahmad, B., Yan, T., Chee, L.Y., Ang, S.T., Mutant nucleophosmin deregulates cell death and myeloid differentiation through excessive caspase-6 and -8 inhibition (2010) Blood, 116, pp. 3286-3296
Noguera, N.I., Song, M.S., Divona, M., Catalano, G., Calvo, K.L., García, F., Nucleophosmin/B26 regulates PTEN through interaction with HAUSP in acute myeloid leukemia (2013) Leukemia, 27, pp. 1037-1043
Roboz, G.J., Current treatment of acute myeloid leukemia (2012) Curr Opin Oncol, 24, pp. 711-719
Falini, B., Gionfriddo, I., Cecchetti, F., Ballanti, S., Pettirossi, V., Martelli, M.P., Acute Myeloid Leukemia with mutated nucleophosmin (NPM1): Any hope for a targeted therapy? (2011) Blood Rev, 25, pp. 247-254
Di Silvio, E., Di Matteo, A., Malatesta, F., Travaglini-Allocatelli, C., Recognition and binding of apocytochrome c to P. Aeruginosa CcmI, a component of cytochrome c maturation machinery (2013) Biochim Biophys Acta, 1834, pp. 1554-1561
Tien, M.Z., Sydykova, D.K., Meyer, A.G., Wilke, C.O., PeptideBuilder: A simple Python library to generate model peptides (2013) PeerJ, 1, p. e80
Thomsen, R., Christensen, M.H., MolDock: A new technique for high-accuracy molecular docking (2006) J Med Chem, 49, pp. 3315-3321
Webb, B., Sali, A., Protein structure modeling with MODELLER (2014) Methods Mol Biol, 1137, pp. 1-15
Bramucci, E., Paiardini, A., Bossa, F., Pascarella, S., PyMod: Sequence similarity searches, multiple sequence-structure alignments, and homology modeling within PyMOL (2012) BMC Bioinformatics, 13, p. S2
Berendsen, H.J.C., Postma, J.P.M., Van Gunsteren, W.F., Hermans, J., Interaction models for water in relation to protein hydration (1981) Intermolecular Forces. Reidel: Dordrecht, pp. 331-342. , Pullman P. ed, The Netherlands
Darden, T., York, D., Pedersen, L., Particle mesh Ewald - An N·log (N) method for Ewald sums in large systems (1993) J Chem Phys, 98, pp. 10089-10092
Hess, B., Bekker, H., Berendsen, H.J.C., Fraaije, J.G.E.M., LINCS: A linear constraint solver for molecular simulations (1997) J Comput Chem, 18, pp. 1463-1472
Oncogenesis (ISSN: 2157-9024), 2017; 6(9): N/D-N/D.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.722, 5-year impact factor: 4.692
Url: https://www.scopus.com/inward/record.uri?eid=2-s2.0-85032725431&doi=10.1038%2foncsis.2017.78&partnerID=40&md5=75a2dbef3e5944b1ef2c7a26491ee922
Keywords: Centromere Protein W, F Box Wd Repeat Containing Protein 7, F Box Wd Repeat Containing Protein 7 Gamma, Human Immunodeficiency Virus Protein, Nuclear Protein, Nucleophosmin, Transactivator Protein, Tumor Suppressor Protein, Unclassified Drug, Amino Terminal Sequence, Article, Carboxy Terminal Sequence, Controlled Study, Molecular Docking, Molecular Dynamics, Nucleolar Localization Signal, Priority Journal, Protein Domain, Protein Expression, Protein Protein Interaction, Protein Structure, Site Directed Mutagenesis, Structural Model,
Affiliations:
*** IBB - CNR ***
Istituto di Biologia e Patologia Molecolari, Consiglio Nazionale delle Ricerche, Roma, Italy
Dipartimento di Scienze Mediche, Orali e Biotecnologiche, Università di Chieti-Pescara G d'Annunzio, Via dei Vestini 31, Chieti, 66100, Italy
CeSI-Met, Università di Chieti-Pescara G d'Annunzio, Chieti, Italy
Dipartimento di Biologia e Biotecnologie C Darwin, Sapienza Università di Roma, Roma, Italy
CINECA Consorzio Interuniversitario, Sede di Roma, Roma, Italy
Dipartimento di Farmacia, Università di Napoli Federico II, Napoli, Italy
Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Napoli, Italy
References:
Grisendi, S., Mecucci, C., Falini, B., Pandolfi, P.P., Nucleophosmin and cancer (2006) Nat Rev Cancer, 6, pp. 493-50
Emmott, E., Hiscox, J.A., Nucleolar targeting: The hub of the matter (2009) EMBO Rep, 10, pp. 231-238
Mitrea, D.M., Cika, J.A., Guy, C.S., Ban, D., Banerjee, P.R., Stanley, C.B., Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA (2016) Elife, 5, p. e13571
Lindstrom, M.S., NPM1/B23: A multifunctional chaperone in ribosome biogenesis and chromatin remodeling (2011) Biochem Res Int, 2011, p. 195209
Colombo, E., Alcalay, M., Pelicci, P.G., Nucleophosmin and its complex network: A possible therapeutic target in hematological diseases (2011) Oncogene, 30, pp. 2595-2609
Federici, L., Falini, B., Nucleophosmin mutations in acute myeloid leukemia: A tale of protein unfolding and mislocalization (2013) Protein Sci, 22, pp. 545-556
Herrera, J.E., Savkur, R., Olson, M.O., The ribonuclease activity of nucleolar protein B23 (1995) Nucleic Acids Res, 23, pp. 3974-3979
Murano, K., Okuwaki, M., Hisaoka, M., Nagata, K., Transcription regulation of the rRNA gene by a multifunctional nucleolar protein, B23/nucleophosmin, through its histone chaperone activity (2008) Mol Cell Biol, 28, pp. 3114-3126
Scott, D.D., Oeffinger, M., Nucleolin and nucleophosmin: Nucleolar proteins with multiple functions in DNA repair (2016) Biochem Cell Biol, 94, pp. 419-432
Ziv, O., Zeisel, A., Mirlas-Neisberg, N., Swain, U., Nevo, R., Ben-Chetrit, N., Identification of novel DNA-damage tolerance genes reveals regulation of translesion DNA synthesis by nucleophosmin (2014) Nat Commun, 5, p. 5437
Okuwaki, M., Matsumoto, K., Tsujimoto, M., Nagata, K., Function of nucleophosmin/B23, a nucleolar acidic protein, as a histone chaperone (2001) FEBS Lett, 506, pp. 272-276
Szebeni, A., Olson, M.O., Nucleolar protein B23 has molecular chaperone activities (1999) Protein Sci, 8, pp. 905-912
Okuda, M., The role of nucleophosmin in centrosome duplication (2002) Oncogene, 21, pp. 6170-6174
Wang, W., Budhu, A., Forgues, M., Wang, X.W., Temporal and spatial control of nucleophosmin by the Ran-Crm1 complex in centrosome duplication (2005) Nat Cell Biol, 7, pp. 823-830
Yang, K., Wang, M., Zhao, Y., Sun, X., Yang, Y., Li, X., A redox mechanism underlying nucleolar stress sensing by nucleophosmin (2016) Nat Commun, 7, p. 13599
Di Matteo, A., Franceschini, M., Chiarella, S., Rocchio, S., Travaglini-Allocatelli, C., Federici, L., Molecules that target nucleophosmin for cancer treatment: An update (2016) Oncotarget, 7, pp. 44821-44840
Yung, B.Y., Oncogenic role of nucleophosmin/B23 (2007) Chang Gung Med J, 30, pp. 285-293
Holmberg Olausson, K., Elsir, T., Moazemi Goudarzi, K., Nistér, M., Lindström, M.S., NPM1 histone chaperone is upregulated in glioblastoma to promote cell survival and maintain nucleolar shape (2015) Sci Rep, 5, p. 16495
Falini, B., Mecucci, C., Tiacci, E., Alcalay, M., Rosati, R., Pasqualucci, L., Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype (2005) N Engl J Med, 352, pp. 254-266
Scott, M.S., Troshin, P.V., Barton, G.J., NoD: A Nucleolar localization sequence detector for eukaryotic and viral proteins (2011) BMC Bioinformatics, 12, p. 317
Bonetti, P., Davoli, T., Sironi, C., Amati, B., Pelicci, P.G., Colombo, E., Nucleophosmin and its AML-associated mutant regulate c-Myc turnover through Fbw7 gamma (2008) J Cell Biol, 182, pp. 19-26
Davis, R.J., Welcker, M., Clurman, B.E., Tumor suppression by the Fbw7 ubiquitin ligase: Mechanisms and opportunities (2014) Cancer Cell, 26, pp. 455-464
Welcker, M., Orian, A., Grim, J.E., Eisenman, R.N., Clurman, B.E., A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size (2004) Curr Biol, 14, pp. 1852-1857
Colombo, E., Martinelli, P., Zamponi, R., Shing, D.C., Bonetti, P., Luzi, L., Delocalization and destabilization of the Arf tumour suppressor by the leukemiaassociated NPM mutant (2006) Cancer Res, 66, pp. 3044-3050
Bolli, N., De Marco, M.F., Martelli, M.P., Bigerna, B., Pucciarini, A., Rossi, R., A dosedependent tug of war involving the NPM1 leukaemic mutant, nucleophosmin, and ARF (2009) Leukemia, 23, pp. 501-509
Li, Y.P., Protein B23 is an important human factor for the nucleolar localization of the human immunodeficiency virus protein Tat (1997) J Virol, 71, pp. 4098-4102
Chun, Y., Park, B., Koh, W., Lee, S., Cheon, Y., Kim, R., New centromeric component CENP-W is an RNA-associated nuclear matrix protein that interacts with nucleophosmin/B23 protein (2011) J Biol Chem, 286, pp. 42758-42769
Foltz, D.R., Jansen, L.E., Black, B.E., Bailey, A.O., Yates, J.R., III, Cleveland, D.W., The human CENP-A centromeric nucleosome-associated complex (2006) Nat Cell Biol, 8, pp. 458-469
Mitrea, D.M., Grace, C.R., Buljan, M., Yun, M.K., Pytel, N.J., Satumba, J., Structural polymorphism in the N-terminal oligomerization domain of NPM1 (2014) Proc Natl Acad Sci USA, 111, pp. 4466-4471
Fantini, D., Vascotto, C., Marasco, D., D'Ambrosio, C., Romanello, M., Vitagliano, L., Critical lysine residues within the overlooked N-terminal domain of human APE1 regulate its biological functions (2010) Nucleic Acids Res, 38, pp. 8239-8256
Scaloni, F., Gianni, S., Federici, L., Falini, B., Brunori, M., Folding mechanism of the C-terminal domain of nucleophosmin: Residual structure in the denatured state and its pathophysiological significance (2009) FASEB J, 23, pp. 2360-2365
Scaloni, F., Federici, L., Brunori, M., Gianni, S., Deciphering the folding transition state structure and denatured state properties of Nucleophosmin C-terminal domain (2010) Proc Natl Acad Sci USA, 107, pp. 5447-5452
Scognamiglio, P.L., Di Natale, C., Leone, M., Cascella, R., Cecchi, C., Lirussi, L., Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia (2016) Oncotarget, 7, pp. 59129-59143
Di Natale, C., Scognamiglio, P.L., Cascella, R., Cecchi, C., Russo, A., Leone, M., Nucleophosmin contains amyloidogenic regions that are able to form toxic aggregates under physiological conditions (2015) FASEB J, 29, pp. 3689-3701
Chiarella, S., De Cola, A., Scaglione, G.L., Carletti, E., Graziano, V., Barcaroli, D., Nucleophosmin mutations alter its nucleolar localization by impairing G-quadruplex binding at ribosomal DNA (2013) Nucleic Acids Res, 41, pp. 3228-3239
Federici, L., Arcovito, A., Scaglione, G.L., Scaloni, F., Lo Sterzo, C., Di Matteo, A., Nucleophosmin C-terminal leukemia-associated domain interacts with G-rich quadruplex forming DNA (2010) J Biol Chem, 285, pp. 37138-37149
Gallo, A., Lo Sterzo, C., Mori, M., Di Matteo, A., Bertini, I., Banci, L., Structure of nucleophosmin DNA-binding domain and analysis of its complex with a G-quadruplex sequence from the c-MYC promoter (2012) J Biol Chem, 287, pp. 26539-26548
Leong, S.M., Tan, B.X., Bte Ahmad, B., Yan, T., Chee, L.Y., Ang, S.T., Mutant nucleophosmin deregulates cell death and myeloid differentiation through excessive caspase-6 and -8 inhibition (2010) Blood, 116, pp. 3286-3296
Noguera, N.I., Song, M.S., Divona, M., Catalano, G., Calvo, K.L., García, F., Nucleophosmin/B26 regulates PTEN through interaction with HAUSP in acute myeloid leukemia (2013) Leukemia, 27, pp. 1037-1043
Roboz, G.J., Current treatment of acute myeloid leukemia (2012) Curr Opin Oncol, 24, pp. 711-719
Falini, B., Gionfriddo, I., Cecchetti, F., Ballanti, S., Pettirossi, V., Martelli, M.P., Acute Myeloid Leukemia with mutated nucleophosmin (NPM1): Any hope for a targeted therapy? (2011) Blood Rev, 25, pp. 247-254
Di Silvio, E., Di Matteo, A., Malatesta, F., Travaglini-Allocatelli, C., Recognition and binding of apocytochrome c to P. Aeruginosa CcmI, a component of cytochrome c maturation machinery (2013) Biochim Biophys Acta, 1834, pp. 1554-1561
Tien, M.Z., Sydykova, D.K., Meyer, A.G., Wilke, C.O., PeptideBuilder: A simple Python library to generate model peptides (2013) PeerJ, 1, p. e80
Thomsen, R., Christensen, M.H., MolDock: A new technique for high-accuracy molecular docking (2006) J Med Chem, 49, pp. 3315-3321
Webb, B., Sali, A., Protein structure modeling with MODELLER (2014) Methods Mol Biol, 1137, pp. 1-15
Bramucci, E., Paiardini, A., Bossa, F., Pascarella, S., PyMod: Sequence similarity searches, multiple sequence-structure alignments, and homology modeling within PyMOL (2012) BMC Bioinformatics, 13, p. S2
Berendsen, H.J.C., Postma, J.P.M., Van Gunsteren, W.F., Hermans, J., Interaction models for water in relation to protein hydration (1981) Intermolecular Forces. Reidel: Dordrecht, pp. 331-342. , Pullman P. ed, The Netherlands
Darden, T., York, D., Pedersen, L., Particle mesh Ewald - An N·log (N) method for Ewald sums in large systems (1993) J Chem Phys, 98, pp. 10089-10092
Hess, B., Bekker, H., Berendsen, H.J.C., Fraaije, J.G.E.M., LINCS: A linear constraint solver for molecular simulations (1997) J Comput Chem, 18, pp. 1463-1472
Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ
Nucleophosmin (NPM1) is a multifunctional nucleolar protein implicated in ribogenesis, centrosome duplication, cell cycle control, regulation of DNA repair and apoptotic response to stress stimuli. The majority of these functions are played through the interactions with a variety of protein partners. NPM1 is frequently overexpressed in solid tumors of different histological origin. Furthermore NPM1 is the most frequently mutated protein in acute myeloid leukemia (AML) patients. Mutations map to the C-terminal domain and lead to the aberrant and stable localization of the protein in the cytoplasm of leukemic blasts. Among NPM1 protein partners, a pivotal role is played by the tumor suppressor Fbw7γ, an E3-ubiquitin ligase that degrades oncoproteins like c-MYC, cyclin E, Notch and c-jun. In AML with NPM1 mutations, Fbw7γ is degraded following its abnormal cytosolic delocalization by mutated NPM1. This mechanism also applies to other tumor suppressors and it has been suggested that it may play a key role in leukemogenesis. Here we analyse the interaction between NPM1 and Fbw7γ, by identifying the protein surfaces implicated in recognition and key aminoacids involved. Based on the results of computational methods, we propose a structural model for the interaction, which is substantiated by experimental findings on several site-directed mutants. We also extend the analysis to two other NPM1 partners (HIV Tat and CENP-W) and conclude that NPM1 uses the same molecular surface as a platform for recognizing different protein partners. We suggest that this region of NPM1 may be targeted for cancer treatment. © The Author(s) 2017.
Nucleophosmin (NPM1) is a multifunctional nucleolar protein implicated in ribogenesis, centrosome duplication, cell cycle control, regulation of DNA repair and apoptotic response to stress stimuli. The majority of these functions are played through the interactions with a variety of protein partners. NPM1 is frequently overexpressed in solid tumors of different histological origin. Furthermore NPM1 is the most frequently mutated protein in acute myeloid leukemia (AML) patients. Mutations map to the C-terminal domain and lead to the aberrant and stable localization of the protein in the cytoplasm of leukemic blasts. Among NPM1 protein partners, a pivotal role is played by the tumor suppressor Fbw7γ, an E3-ubiquitin ligase that degrades oncoproteins like c-MYC, cyclin E, Notch and c-jun. In AML with NPM1 mutations, Fbw7γ is degraded following its abnormal cytosolic delocalization by mutated NPM1. This mechanism also applies to other tumor suppressors and it has been suggested that it may play a key role in leukemogenesis. Here we analyse the interaction between NPM1 and Fbw7γ, by identifying the protein surfaces implicated in recognition and key aminoacids involved. Based on the results of computational methods, we propose a structural model for the interaction, which is substantiated by experimental findings on several site-directed mutants. We also extend the analysis to two other NPM1 partners (HIV Tat and CENP-W) and conclude that NPM1 uses the same molecular surface as a platform for recognizing different protein partners. We suggest that this region of NPM1 may be targeted for cancer treatment. © The Author(s) 2017.
Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ
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Structural investigation of Nucleophosmin interaction with the tumor suppressor Fbw7γ
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Scognamiglio PL, Di Natale C, Leone M, Cascella R, Cecchi C, Lirussi L, Antoniali G, Riccardi D, Morelli G, Tell G, Chiti F, Marasco D
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Impact Factor: 5.168
View Export to BibTeX Export to EndNote
Tornatore L, Sandomenico A, Raimondo D, Low C, Rocci A, Tralau-Stewart C, Capece D, D'Andrea D, Bua M, Boyle E, van Duin M, Zoppoli P, Jaxa-Chamiec A, Thotakura AK, Dyson J, Walker BA, Leonardi A, Chambery A, Driessen C, Sonneveld P, Morgan G, Palumbo A, Tramontano A, Rahemtulla A, Ruvo M, Franzoso G
* Cancer-selective targeting of the NF-kappaB survival pathway with GADD45beta/MKK7 inhibitors (623 views)
Cancer Cell (ISSN: 1535-6108), 2014 Oct 13; 26(4): 495-508.
Impact Factor: 23.523
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Scognamiglio PL, Di Natale C, Leone M, Poletto M, Vitagliano L, Tell G, Marasco D
* G-quadruplex DNA recognition by nucleophosmin: new insights from protein dissection (570 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2014 Jun; 1840(6): 2050-2059.
Impact Factor: 5.353
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Marasco D, Ruggiero A, Vascotto C, Poletto M, Scognamiglio PL, Tell G, Vitagliano L
* Role of mutual interactions in the chemical and thermal stability of nucleophosmin NPM1 domains (326 views)
Biochemical And Biophysical Research Communications (ISSN: 0006-291x), 2013 Jan 11; 430(2): 523-528.
Impact Factor: 2.281
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Musumeci D, Roviello GN, Montesarchio D, Sapio R, Valente M, Anr V, Bucci EM
* Hairpin ODN-based ligands as potential inhibitors of HMGB1 cytokine activity (436 views)
Rsc Adv (ISSN: 2046-2069), 2013; 3(30): 12176-12184.
Impact Factor: 3.708
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Poletto M, Vascotto C, Scognamiglio PL, Lirussi L, Marasco D, Tell G
* Role Of The Unstructured N-Terminal Domain Of The Human Apurinic/Apyrimidinic Endonuclease 1 (hape1) In The Modulation Of Its Interaction With Nucleic Acids And Nucleophosmin (npm1) (496 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2013; 452(3): 545-557.
Impact Factor: 4.779
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Lirussi L, Antoniali G, Vascotto C, D'Ambrosio C, Poletto M, Romanello M, Marasco D, Leone M, Quadrifoglio F, Bhakat KK, Scaloni A, Tell G
* Nucleolar accumulation of APE1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its BER activity in cells (790 views)
Mol Biol Cell (ISSN: 1059-1524), 2012 Oct 15; 23(20): 4079-4096.
Impact Factor: 4.803
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Tagliamonte M, Marasco D, Ruggiero A, de Stradis A, Tornesello ML, Totrov M, Buonaguro FM, Buonaguro L
* HIV p24 as Scaffold for Presenting Conformational HIV Env Antigens (468 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2012 Sep 17; 7(8): N/D-N/D.
Impact Factor: 3.73
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Vitagliano L, Fiume G, Scognamiglio PL, Doti N, Cannavo R, Puca A, Pedone C, Scala G, Quinto I, Marasco D
* Structural and functional insights into IkappaB-alpha/HIV-1 Tat interaction (603 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2011 Sep; 93(9): 1592-1600.
Impact Factor: 3.022
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Salvatore E, Di Maio L, Filla A, Ferrara AM, Rinaldi C, Sacca F, Peluso S, Macchia PE, Pappata S, De Michele G
* Benign hereditary chorea: Clinical and neuroimaging features in an Italian family (356 views)
Mov Disord (ISSN: 0885-3185, 1531-8257, 0885-3185linking), 2010 Jul 30; 25(10): 1491-1496.
Impact Factor: 4.48
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Malaguarnera R, Vella V, Pandini G, Sanfilippo M, Pezzino V, Vigneri R, Frasca F
* TAp73α increases p53 tumor suppressor activity in thyroid cancer cells via the inhibition of Mdm2-mediated degradation (420 views)
Mol Cancer Res (ISSN: 1541-7786), 2008; 6(1): 64-77.
Impact Factor: 4.533
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Minopoli G, Stante M, Napolitano F, Telese F, Aloia L, De Felice M, Di Lauro R, Pacelli R, Brunetti A, Zambrano N, Russo T
* Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in the cellular response to DNA damage (660 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2007 Jan 12; 282(2): 831-835.
Impact Factor: 5.581
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Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S-I
* Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex (407 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Oct 7; 280(40): 34278-34287.
Impact Factor: 5.854
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Criscuolo C, Mancini P, Menchise V, Sacca F, De Michele G, Banfi S, Filla A
* Very late onset in ataxia oculomotor apraxia type I [1] (330 views)
Ann Neurol (ISSN: 0364-5134), 2005 May; 57(5): 777-777.
Impact Factor: 7.571
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Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
* Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain (473 views)
J Pept Res (ISSN: 1397-002x), 2005 Feb; 65(2): 200-208.
Impact Factor: 1.741
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Borgatti M, Lampronti I, Romanelli A, Pedone C, Saviano M, Bianchi N, Mischiati C, Gambari R
* Transcription factor decoy molecules based on a peptide nucleic acid (PNA)-DNA chimera mimicking Sp1 binding sites (600 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2003 Feb 28; 278(9): 7500-7509.
Impact Factor: 6.482
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* Destabilisation, aggregation, toxicity and cytosolic mislocalisation of nucleophosmin regions associated with acute myeloid leukemia (396 views)
Oncotarget (ISSN: 1949-2553, 1949-2553electronic, 1949-2553linking), 2016 Sep 13; 7(37): 59129-59143.
Impact Factor: 5.168
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Tornatore L, Sandomenico A, Raimondo D, Low C, Rocci A, Tralau-Stewart C, Capece D, D'Andrea D, Bua M, Boyle E, van Duin M, Zoppoli P, Jaxa-Chamiec A, Thotakura AK, Dyson J, Walker BA, Leonardi A, Chambery A, Driessen C, Sonneveld P, Morgan G, Palumbo A, Tramontano A, Rahemtulla A, Ruvo M, Franzoso G
* Cancer-selective targeting of the NF-kappaB survival pathway with GADD45beta/MKK7 inhibitors (623 views)
Cancer Cell (ISSN: 1535-6108), 2014 Oct 13; 26(4): 495-508.
Impact Factor: 23.523
View Export to BibTeX Export to EndNote
Scognamiglio PL, Di Natale C, Leone M, Poletto M, Vitagliano L, Tell G, Marasco D
* G-quadruplex DNA recognition by nucleophosmin: new insights from protein dissection (570 views)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2014 Jun; 1840(6): 2050-2059.
Impact Factor: 5.353
View Export to BibTeX Export to EndNote
Marasco D, Ruggiero A, Vascotto C, Poletto M, Scognamiglio PL, Tell G, Vitagliano L
* Role of mutual interactions in the chemical and thermal stability of nucleophosmin NPM1 domains (326 views)
Biochemical And Biophysical Research Communications (ISSN: 0006-291x), 2013 Jan 11; 430(2): 523-528.
Impact Factor: 2.281
View Export to BibTeX Export to EndNote
Musumeci D, Roviello GN, Montesarchio D, Sapio R, Valente M, Anr V, Bucci EM
* Hairpin ODN-based ligands as potential inhibitors of HMGB1 cytokine activity (436 views)
Rsc Adv (ISSN: 2046-2069), 2013; 3(30): 12176-12184.
Impact Factor: 3.708
View Export to BibTeX Export to EndNote
Poletto M, Vascotto C, Scognamiglio PL, Lirussi L, Marasco D, Tell G
* Role Of The Unstructured N-Terminal Domain Of The Human Apurinic/Apyrimidinic Endonuclease 1 (hape1) In The Modulation Of Its Interaction With Nucleic Acids And Nucleophosmin (npm1) (496 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2013; 452(3): 545-557.
Impact Factor: 4.779
View Export to BibTeX Export to EndNote
Lirussi L, Antoniali G, Vascotto C, D'Ambrosio C, Poletto M, Romanello M, Marasco D, Leone M, Quadrifoglio F, Bhakat KK, Scaloni A, Tell G
* Nucleolar accumulation of APE1 depends on charged lysine residues that undergo acetylation upon genotoxic stress and modulate its BER activity in cells (790 views)
Mol Biol Cell (ISSN: 1059-1524), 2012 Oct 15; 23(20): 4079-4096.
Impact Factor: 4.803
View Export to BibTeX Export to EndNote
Tagliamonte M, Marasco D, Ruggiero A, de Stradis A, Tornesello ML, Totrov M, Buonaguro FM, Buonaguro L
* HIV p24 as Scaffold for Presenting Conformational HIV Env Antigens (468 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2012 Sep 17; 7(8): N/D-N/D.
Impact Factor: 3.73
View Export to BibTeX Export to EndNote
Vitagliano L, Fiume G, Scognamiglio PL, Doti N, Cannavo R, Puca A, Pedone C, Scala G, Quinto I, Marasco D
* Structural and functional insights into IkappaB-alpha/HIV-1 Tat interaction (603 views)
Biochimie (ISSN: 0300-9084, 1638-6183, 1638-6183electronic), 2011 Sep; 93(9): 1592-1600.
Impact Factor: 3.022
View Export to BibTeX Export to EndNote
Salvatore E, Di Maio L, Filla A, Ferrara AM, Rinaldi C, Sacca F, Peluso S, Macchia PE, Pappata S, De Michele G
* Benign hereditary chorea: Clinical and neuroimaging features in an Italian family (356 views)
Mov Disord (ISSN: 0885-3185, 1531-8257, 0885-3185linking), 2010 Jul 30; 25(10): 1491-1496.
Impact Factor: 4.48
View Export to BibTeX Export to EndNote
Malaguarnera R, Vella V, Pandini G, Sanfilippo M, Pezzino V, Vigneri R, Frasca F
* TAp73α increases p53 tumor suppressor activity in thyroid cancer cells via the inhibition of Mdm2-mediated degradation (420 views)
Mol Cancer Res (ISSN: 1541-7786), 2008; 6(1): 64-77.
Impact Factor: 4.533
View Export to BibTeX Export to EndNote
Minopoli G, Stante M, Napolitano F, Telese F, Aloia L, De Felice M, Di Lauro R, Pacelli R, Brunetti A, Zambrano N, Russo T
* Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in the cellular response to DNA damage (660 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2007 Jan 12; 282(2): 831-835.
Impact Factor: 5.581
View Export to BibTeX Export to EndNote
Santelli E, Leone M, Li C, Fukushima T, Preece NE, Olson AJ, Ely KR, Reed JC, Pellecchia M, Liddington RC, Matsuzawa S-I
* Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex (407 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Oct 7; 280(40): 34278-34287.
Impact Factor: 5.854
View Export to BibTeX Export to EndNote
Criscuolo C, Mancini P, Menchise V, Sacca F, De Michele G, Banfi S, Filla A
* Very late onset in ataxia oculomotor apraxia type I [1] (330 views)
Ann Neurol (ISSN: 0364-5134), 2005 May; 57(5): 777-777.
Impact Factor: 7.571
View Export to BibTeX Export to EndNote
Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
* Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain (473 views)
J Pept Res (ISSN: 1397-002x), 2005 Feb; 65(2): 200-208.
Impact Factor: 1.741
View Export to BibTeX Export to EndNote
Borgatti M, Lampronti I, Romanelli A, Pedone C, Saviano M, Bianchi N, Mischiati C, Gambari R
* Transcription factor decoy molecules based on a peptide nucleic acid (PNA)-DNA chimera mimicking Sp1 binding sites (600 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2003 Feb 28; 278(9): 7500-7509.
Impact Factor: 6.482
View Export to BibTeX Export to EndNote
16 Records (14 excluding Abstracts).
Total impact factor: 92.609 (81.308 excluding Abstracts).
Total 5 year impact factor: 99.363 (83.766 excluding Abstracts).
Total impact factor: 92.609 (81.308 excluding Abstracts).
Total 5 year impact factor: 99.363 (83.766 excluding Abstracts).
297 views. Last view on Thursday 01 June 2023, 22:53:52
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