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The RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the Protein.

Frontiers in molecular neuroscience

Zacco E, Martin SR, Thorogate R, Pastore A.
PMID: 30356856
Front Mol Neurosci. 2018 Oct 09;11:372. doi: 10.3389/fnmol.2018.00372. eCollection 2018.

The TAR DNA-binding protein 43 (TDP-43) is a nucleic acid-binding protein implicated in gene regulation and RNA processing and shuffling. It is a ribonuclear protein that carries out most of its functions by binding specific nucleic acid sequences with...

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Zacco E, Martin SR, Thorogate R, et al. The RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the Protein. Front Mol Neurosci. 2018;11:372doi: 10.3389/fnmol.2018.00372.
Zacco, E., Martin, S. R., Thorogate, R., & Pastore, A. (2018). The RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the Protein. Frontiers in molecular neuroscience, 11372. https://doi.org/10.3389/fnmol.2018.00372
Zacco, Elsa, et al. "The RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the Protein." Frontiers in molecular neuroscience vol. 11 (2018): 372. doi: https://doi.org/10.3389/fnmol.2018.00372
Zacco E, Martin SR, Thorogate R, Pastore A. The RNA-Recognition Motifs of TAR DNA-Binding Protein 43 May Play a Role in the Aberrant Self-Assembly of the Protein. Front Mol Neurosci. 2018 Oct 09;11:372. doi: 10.3389/fnmol.2018.00372. eCollection 2018. PMID: 30356856; PMCID: PMC6190850.
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The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus.

Frontiers in molecular biosciences

Yalinca H, Gehin CJC, Oleinikovas V, Lashuel HA, Gervasio FL, Pastore A.
PMID: 31632982
Front Mol Biosci. 2019 Oct 01;6:95. doi: 10.3389/fmolb.2019.00095. eCollection 2019.

Huntington disease is a neurodegenerative disease characterized by a polymorphic tract of polyglutamine repeats in exon 1 of the huntingtin protein, which is thought to be responsible for protein aggregation and neuronal death. The polyglutamine tract is preceded by...

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Yalinca H, Gehin CJC, Oleinikovas V, et al. The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus. Front Mol Biosci. 2019;6:95doi: 10.3389/fmolb.2019.00095.
Yalinca, H., Gehin, C. J. C., Oleinikovas, V., Lashuel, H. A., Gervasio, F. L., & Pastore, A. (2019). The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus. Frontiers in molecular biosciences, 695. https://doi.org/10.3389/fmolb.2019.00095
Yalinca, Havva, et al. "The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus." Frontiers in molecular biosciences vol. 6 (2019): 95. doi: https://doi.org/10.3389/fmolb.2019.00095
Yalinca H, Gehin CJC, Oleinikovas V, Lashuel HA, Gervasio FL, Pastore A. The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus. Front Mol Biosci. 2019 Oct 01;6:95. doi: 10.3389/fmolb.2019.00095. eCollection 2019. PMID: 31632982; PMCID: PMC6779701.
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Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor.

Frontiers in molecular biosciences

Paoletti F, de Chiara C, Kelly G, Covaceuszach S, Malerba F, Yan R, Lamba D, Cattaneo A, Pastore A.
PMID: 28083536
Front Mol Biosci. 2016 Dec 26;3:83. doi: 10.3389/fmolb.2016.00083. eCollection 2016.

Nerve Growth Factor (NGF), the prototype of the neurotrophin family, is essential for maintenance and growth of different neuronal populations. The X-ray crystal structure of NGF has been known since the early '90s and shows a β-sandwich fold with...

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Paoletti F, de Chiara C, Kelly G, et al. Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor. Front Mol Biosci. 2016;3:83doi: 10.3389/fmolb.2016.00083.
Paoletti, F., de Chiara, C., Kelly, G., Covaceuszach, S., Malerba, F., Yan, R., Lamba, D., Cattaneo, A., & Pastore, A. (2016). Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor. Frontiers in molecular biosciences, 383. https://doi.org/10.3389/fmolb.2016.00083
Paoletti, Francesca, et al. "Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor." Frontiers in molecular biosciences vol. 3 (2016): 83. doi: https://doi.org/10.3389/fmolb.2016.00083
Paoletti F, de Chiara C, Kelly G, Covaceuszach S, Malerba F, Yan R, Lamba D, Cattaneo A, Pastore A. Conformational Rigidity within Plasticity Promotes Differential Target Recognition of Nerve Growth Factor. Front Mol Biosci. 2016 Dec 26;3:83. doi: 10.3389/fmolb.2016.00083. eCollection 2016. PMID: 28083536; PMCID: PMC5183593.
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The effect of crowding and confinement: a comparison of Yfh1 stability in different environments.

Physical biology

Sanfelice D, Politou A, Martin SR, De Los Rios P, Temussi P, Pastore A.
PMID: 23912905
Phys Biol. 2013 Aug;10(4):045002. doi: 10.1088/1478-3975/10/4/045002. Epub 2013 Aug 02.

Crowding and confinement can affect protein stability, favouring the more compact species amongst the folded and unfolded conformations. An unbiased assessment of the relative efficacy of crowded and confined environments has been hampered so far by the paucity of...

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Sanfelice D, Politou A, Martin SR, et al. The effect of crowding and confinement: a comparison of Yfh1 stability in different environments. Phys Biol. 2013;10(4):045002doi: 10.1088/1478-3975/10/4/045002.
Sanfelice, D., Politou, A., Martin, S. R., De Los Rios, P., Temussi, P., & Pastore, A. (2013). The effect of crowding and confinement: a comparison of Yfh1 stability in different environments. Physical biology, 10(4), 045002. https://doi.org/10.1088/1478-3975/10/4/045002
Sanfelice, Domenico, et al. "The effect of crowding and confinement: a comparison of Yfh1 stability in different environments." Physical biology vol. 10,4 (2013): 045002. doi: https://doi.org/10.1088/1478-3975/10/4/045002
Sanfelice D, Politou A, Martin SR, De Los Rios P, Temussi P, Pastore A. The effect of crowding and confinement: a comparison of Yfh1 stability in different environments. Phys Biol. 2013 Aug;10(4):045002. doi: 10.1088/1478-3975/10/4/045002. Epub 2013 Aug 02. PMID: 23912905.
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Analyzing the Effects of a G137V Mutation in the FXN Gene.

Frontiers in molecular neuroscience

Faggianelli N, Puglisi R, Veneziano L, Romano S, Frontali M, Vannocci T, Fortuni S, Testi R, Pastore A.
PMID: 26635519
Front Mol Neurosci. 2015 Nov 25;8:66. doi: 10.3389/fnmol.2015.00066. eCollection 2015.

Reduced levels of frataxin, an essential mitochondrial protein involved in the regulation of iron-sulfur cluster biogenesis, are responsible for the recessive neurodegenerative Friedreich Ataxia (FRDA). Expansion of a GAA triplet in the first intron of the FRDA is essential...

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Faggianelli N, Puglisi R, Veneziano L, et al. Analyzing the Effects of a G137V Mutation in the FXN Gene. Front Mol Neurosci. 2015;8:66doi: 10.3389/fnmol.2015.00066.
Faggianelli, N., Puglisi, R., Veneziano, L., Romano, S., Frontali, M., Vannocci, T., Fortuni, S., Testi, R., & Pastore, A. (2015). Analyzing the Effects of a G137V Mutation in the FXN Gene. Frontiers in molecular neuroscience, 866. https://doi.org/10.3389/fnmol.2015.00066
Faggianelli, Nathalie, et al. "Analyzing the Effects of a G137V Mutation in the FXN Gene." Frontiers in molecular neuroscience vol. 8 (2015): 66. doi: https://doi.org/10.3389/fnmol.2015.00066
Faggianelli N, Puglisi R, Veneziano L, Romano S, Frontali M, Vannocci T, Fortuni S, Testi R, Pastore A. Analyzing the Effects of a G137V Mutation in the FXN Gene. Front Mol Neurosci. 2015 Nov 25;8:66. doi: 10.3389/fnmol.2015.00066. eCollection 2015. PMID: 26635519; PMCID: PMC4658817.
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An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches.

Chemphyschem : a European journal of chemical physics and physical chemistry

Politou AS, Pastore A, Temussi PA.
PMID: 34549492
Chemphyschem. 2021 Sep 22; doi: 10.1002/cphc.202100520. Epub 2021 Sep 22.

Approximating protein unfolding by an all-or-none cooperative event is a convenient assumption that can provide precious global information on protein stability. It is however quickly emerging that the scenario is far more complex and that global denaturation curves often...

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Politou AS, Pastore A, Temussi PA. An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Chemphyschem. 2021;doi: 10.1002/cphc.202100520.
Politou, A. S., Pastore, A., & Temussi, P. A. (2021). An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Chemphyschem : a European journal of chemical physics and physical chemistry, . https://doi.org/10.1002/cphc.202100520
Politou, Anastasia S, et al. "An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches." Chemphyschem : a European journal of chemical physics and physical chemistry vol. (2021). doi: https://doi.org/10.1002/cphc.202100520
Politou AS, Pastore A, Temussi PA. An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Chemphyschem. 2021 Sep 22; doi: 10.1002/cphc.202100520. Epub 2021 Sep 22. PMID: 34549492.
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An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches.

Chemphyschem : a European journal of chemical physics and physical chemistry

Politou AS, Pastore A, Temussi PA.
PMID: 34549492
Chemphyschem. 2022 Jan 05;23(1):e202100520. doi: 10.1002/cphc.202100520. Epub 2021 Oct 13.

Approximating protein unfolding by an all-or-none cooperative event is a convenient assumption that can provide precious global information on protein stability. It is however quickly emerging that the scenario is far more complex and that global denaturation curves often...

Cite
Politou AS, Pastore A, Temussi PA. An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Chemphyschem. 2021;23(1):e202100520doi: 10.1002/cphc.202100520.
Politou, A. S., Pastore, A., & Temussi, P. A. (2022). An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Chemphyschem : a European journal of chemical physics and physical chemistry, 23(1), e202100520. https://doi.org/10.1002/cphc.202100520
Politou, Anastasia S, et al. "An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches." Chemphyschem : a European journal of chemical physics and physical chemistry vol. 23,1 (2022): e202100520. doi: https://doi.org/10.1002/cphc.202100520
Politou AS, Pastore A, Temussi PA. An "Onion-like" Model of Protein Unfolding: Collective versus Site Specific Approaches. Chemphyschem. 2022 Jan 05;23(1):e202100520. doi: 10.1002/cphc.202100520. Epub 2021 Oct 13. PMID: 34549492.
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Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012).

Physical biology

Foffi G, Pastore A, Piazza F, Temussi PA.
PMID: 23912807
Phys Biol. 2013 Aug;10(4):040301. doi: 10.1088/1478-3975/10/4/040301. Epub 2013 Aug 02.

More than 60 years of biochemical and biophysical studies have accustomed us to think of proteins as highly purified entities that act in isolation, more or less freely diffusing until they find their cognate partner to bind to. While...

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Foffi G, Pastore A, Piazza F, et al. Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012). Phys Biol. 2013;10(4):040301doi: 10.1088/1478-3975/10/4/040301.
Foffi, G., Pastore, A., Piazza, F., & Temussi, P. A. (2013). Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012). Physical biology, 10(4), 040301. https://doi.org/10.1088/1478-3975/10/4/040301
Foffi, G, et al. "Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012)." Physical biology vol. 10,4 (2013): 040301. doi: https://doi.org/10.1088/1478-3975/10/4/040301
Foffi G, Pastore A, Piazza F, Temussi PA. Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10-14 June 2012). Phys Biol. 2013 Aug;10(4):040301. doi: 10.1088/1478-3975/10/4/040301. Epub 2013 Aug 02. PMID: 23912807.
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Further insights into the ubiquitin pathway: understanding the scarlet letter code.

Structure (London, England : 1993)

Pastore A.
PMID: 20696387
Structure. 2010 Aug 11;18(8):891-2. doi: 10.1016/j.str.2010.07.004.

Understanding the machinery that decides proteins' fate by tagging them with ubiquitin is an important goal of structural biology. Benirschke et al. (2010) have solved the structure of human E4B (or UFD2a), a U-box-containing protein that functions both as...

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Pastore A. Further insights into the ubiquitin pathway: understanding the scarlet letter code. Structure. 2010;18(8):891-2doi: 10.1016/j.str.2010.07.004.
Pastore, A. (2010). Further insights into the ubiquitin pathway: understanding the scarlet letter code. Structure (London, England : 1993), 18(8), 891-2. https://doi.org/10.1016/j.str.2010.07.004
Pastore, Annalisa. "Further insights into the ubiquitin pathway: understanding the scarlet letter code." Structure (London, England : 1993) vol. 18,8 (2010): 891-2. doi: https://doi.org/10.1016/j.str.2010.07.004
Pastore A. Further insights into the ubiquitin pathway: understanding the scarlet letter code. Structure. 2010 Aug 11;18(8):891-2. doi: 10.1016/j.str.2010.07.004. PMID: 20696387.
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The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau.

Frontiers in molecular biosciences

Lyu C, Da Vela S, Al-Hilaly Y, Marshall KE, Thorogate R, Svergun D, Serpell LC, Pastore A, Hanger DP.
PMID: 34778381
Front Mol Biosci. 2021 Oct 28;8:779240. doi: 10.3389/fmolb.2021.779240. eCollection 2021.

Tau35 is a truncated form of tau found in human brain in a subset of tauopathies. Tau35 expression in mice recapitulates key features of human disease, including progressive increase in tau phosphorylation, along with cognitive and motor dysfunction. The...

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Lyu C, Da Vela S, Al-Hilaly Y, et al. The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau. Front Mol Biosci. 2021;8:779240doi: 10.3389/fmolb.2021.779240.
Lyu, C., Da Vela, S., Al-Hilaly, Y., Marshall, K. E., Thorogate, R., Svergun, D., Serpell, L. C., Pastore, A., & Hanger, D. P. (2021). The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau. Frontiers in molecular biosciences, 8779240. https://doi.org/10.3389/fmolb.2021.779240
Lyu, Chen, et al. "The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau." Frontiers in molecular biosciences vol. 8 (2021): 779240. doi: https://doi.org/10.3389/fmolb.2021.779240
Lyu C, Da Vela S, Al-Hilaly Y, Marshall KE, Thorogate R, Svergun D, Serpell LC, Pastore A, Hanger DP. The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau. Front Mol Biosci. 2021 Oct 28;8:779240. doi: 10.3389/fmolb.2021.779240. eCollection 2021. PMID: 34778381; PMCID: PMC8581542.
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Aggregation is a Context-Dependent Constraint on Protein Evolution.

Frontiers in molecular biosciences

Monti M, Armaos A, Fantini M, Pastore A, Tartaglia GG.
PMID: 34222334
Front Mol Biosci. 2021 Jun 18;8:678115. doi: 10.3389/fmolb.2021.678115. eCollection 2021.

Solubility is a requirement for many cellular processes. Loss of solubility and aggregation can lead to the partial or complete abrogation of protein function. Thus, understanding the relationship between protein evolution and aggregation is an important goal. Here, we...

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Monti M, Armaos A, Fantini M, et al. Aggregation is a Context-Dependent Constraint on Protein Evolution. Front Mol Biosci. 2021;8:678115doi: 10.3389/fmolb.2021.678115.
Monti, M., Armaos, A., Fantini, M., Pastore, A., & Tartaglia, G. G. (2021). Aggregation is a Context-Dependent Constraint on Protein Evolution. Frontiers in molecular biosciences, 8678115. https://doi.org/10.3389/fmolb.2021.678115
Monti, Michele, et al. "Aggregation is a Context-Dependent Constraint on Protein Evolution." Frontiers in molecular biosciences vol. 8 (2021): 678115. doi: https://doi.org/10.3389/fmolb.2021.678115
Monti M, Armaos A, Fantini M, Pastore A, Tartaglia GG. Aggregation is a Context-Dependent Constraint on Protein Evolution. Front Mol Biosci. 2021 Jun 18;8:678115. doi: 10.3389/fmolb.2021.678115. eCollection 2021. PMID: 34222334; PMCID: PMC8249573.
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Showing 1 to 11 of 11 entries