Zobrazeno 1 - 10 of 75 pro vyhledávání: '"Carlo Travaglini-Allocatelli"'
1
Akademický článek
GRB2: A dynamic adaptor protein orchestrating cellular signaling in health and disease
Autor: Francesca Malagrinò, Elena Puglisi, Livia Pagano, Carlo Travaglini-Allocatelli, Angelo Toto
Publikováno v: Biochemistry and Biophysics Reports, Vol 39, Iss , Pp 101803- (2024)
GRB2, or Growth Factor Receptor-Bound Protein 2, is a pivotal adaptor protein in intracellular signal transduction pathways, particularly within receptor tyrosine kinase (RTK) signaling cascades. Its crystal structure reveals a modular architecture c
Externí odkaz: https://doaj.org/article/4d1e56f4755e4ccd9e4ff1db49f9c690
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2
Akademický článek
Unveiling the folding mechanism of the Bromodomains
Autor: Maria Petrosino, Daniela Bonetti, Alessandra Pasquo, Laura Lori, Roberta Chiaraluce, Valerio Consalvi, Carlo Travaglini-Allocatelli
Publikováno v: Biochemistry and Biophysics Reports, Vol 11, Iss C, Pp 99-104 (2017)
Bromodomains (BRDs) are small protein domains often present in large multidomain proteins involved in transcriptional regulation in eukaryotic cells. They currently represent valuable targets for the development of inhibitors of aberrant transcriptio
Externí odkaz: https://doaj.org/article/7301862b8af74c558bcd25801b07fa67
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3
Akademický článek
Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms
Autor: Carlo Travaglini-Allocatelli
Publikováno v: Scientifica, Vol 2013 (2013)
Cytochromes c (Cyt c) are ubiquitous heme-containing proteins, mainly involved in electron transfer processes, whose structure and functions have been and still are intensely studied. Surprisingly, our understanding of the molecular mechanism whereby
Externí odkaz: https://doaj.org/article/3ddabaa5eb714cf5979d6084578f2b9e
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5
Folding Mechanism and Aggregation Propensity of the KH0 Domain of FMRP and Its R138Q Pathological Variant
Autor: Daniele Santorelli, Francesca Troilo, Francesca Fata, Francesco Angelucci, Nicola Demitri, Giorgio Giardina, Luca Federici, Flavia Catalano, Adele Di Matteo, Carlo Travaglini-Allocatelli
Publikováno v: International Journal of Molecular Sciences; Volume 23; Issue 20; Pages: 12178
The K-homology (KH) domains are small, structurally conserved domains found in proteins of different origins characterized by a central conserved βααβ “core” and a GxxG motif in the loop between the two helices of the KH core. In the eukaryot
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96a17b061b086d33716bea705c521db6
https://pubmed.ncbi.nlm.nih.gov/36293035
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6
Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTP ase A (RsgA) from Pseudomonas aeruginosa
Autor: Francesco Malatesta, Daniele Santorelli, Adele Di Matteo, S. Rocchio, Carlo Travaglini-Allocatelli, Mimma Franceschini, Serena Rinaldo, Francesco Imperi, Luca Federici
Publikováno v: The FEBS journal
286 (2019): 4245–4260. doi:10.1111/febs.14959
info:cnr-pdr/source/autori:Rocchio, Serena; Santorelli, Daniele; Rinaldo, Serena; Franceschini, Mimma; Malatesta, Francesco; Imperi, Francesco; Federici, Luca; Travaglini-Allocatelli, Carlo; Di Matteo, Adele/titolo:Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTPase A (RsgA) from Pseudomonas aeruginosa/doi:10.1111%2Ffebs.14959/rivista:The FEBS journal (Print)/anno:2019/pagina_da:4245/pagina_a:4260/intervallo_pagine:4245–4260/volume:286
The Small Ribosomal Subunit Biogenesis GTPase A (RsgA) is a bacterial assembly factor involved in the late stages of the 30S subunit maturation. It is a multidomain GTPase in which the central circularly permutated GTPase domain is flanked by an OB d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfa2432c3bd8ce3a1598850620115d4b
https://doi.org/10.1111/febs.14959
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7
A glimpse into the structural properties of the intermediate and transition state in the folding of bromodomain 2 d2 by Φ value analysis
Autor: Roberta Chiaraluce, Maria Petrosino, Leonore Novak, Daniele Santorelli, Carlo Travaglini-Allocatelli, Valerio Consalvi, Alessandra Pasquo
Publikováno v: International Journal of Molecular Sciences, Vol 22, Iss 5953, p 5953 (2021)
International Journal of Molecular Sciences
Volume 22
Issue 11
Bromodomains (BRDs) are small protein interaction modules of about 110 amino acids that selectively recognize acetylated lysine in histones and other proteins. These domains have been identified in a variety of multi-domain proteins involved in trans
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7eae466b275833ac2801b9411de5563c
http://hdl.handle.net/11573/1549781
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8
Mutational analysis of the essential lipopolysaccharide-transport protein LptH of Pseudomonas aeruginosa to uncover critical oligomerization sites
Autor: Luca Federici, Romano Silvestri, Antonio Coluccia, Francesco Imperi, Adele Di Matteo, Paolo Visca, Carlo Travaglini-Allocatelli, Romina Scala, Alessandra Lo Sciuto
Publikováno v: Scientific Reports
Scientific Reports, Vol 10, Iss 1, Pp 1-15 (2020)
Lipopolysaccharide (LPS) is a critical component of the outer membrane (OM) of many Gram-negative bacteria. LPS is translocated to the OM by the LPS transport (Lpt) system. In the human pathogen Pseudomonas aeruginosa, the periplasmic Lpt component,
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3cca96078eaf9f303b48c0e63a088ed
http://hdl.handle.net/11573/1452337
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9
Unveiling the folding mechanism of the Bromodomains
Autor: Alessandra Pasquo, Daniela Bonetti, Valerio Consalvi, Laura Lori, Carlo Travaglini-Allocatelli, Maria Petrosino, Roberta Chiaraluce
Publikováno v: Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 11, Iss C, Pp 99-104 (2017)
Bromodomains (BRDs) are small protein domains often present in large multidomain proteins involved in transcriptional regulation in eukaryotic cells. They currently represent valuable targets for the development of inhibitors of aberrant transcriptio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5af67658c95d147767495320acbca6d2
http://europepmc.org/articles/PMC5614698
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10
Studies of cytochrome c-551 unfolding using fluorescence correlation spectroscopy and other biophysical techniques
Autor: Pallabi Sil, Carlo Travaglini-Allocatelli, Eva Di Silvio, Simanta Sarani Paul, Krishnananda Chattopadhyay
Publikováno v: Physical Chemistry Chemical Physics. 18:24537-24548
In this paper, we have studied the equilibrium unfolding transitions of cytochrome c from Pseudomonas aeruginosa (cytc551), a small bacterial protein. Similar to eukaryotic cytochrome c, cytc551 folds sequentially, although significant differences ex
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2f3082cf667d73f8067e25340834e21
https://doi.org/10.1039/c6cp04819f
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