Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Fabio Lapenta"'
Autor:
Tjaša Plaper, Jana Aupič, Petra Dekleva, Fabio Lapenta, Mateja Manček Keber, Roman Jerala, Mojca Benčina
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
Abstract Coiled-coil (CC) dimer-forming peptides are attractive designable modules for mediating protein association. Highly stable CCs are desired for biological activity regulation and assay. Here, we report the design and versatile applications of
Externí odkaz:
https://doaj.org/article/24366d44f44440bd9d30fddabfebcaae
Autor:
Fabio Lapenta, Jana Aupič, Marco Vezzoli, Žiga Strmšek, Stefano Da Vela, Dmitri I. Svergun, José María Carazo, Roberto Melero, Roman Jerala
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Coiled-coil protein origami is a strategy for the de novo design of polypeptide nanostructures based on coiled-coil dimer forming peptides, where a single chain protein folds into a polyhedral cage. Here, the authors design a single-chain triangular
Externí odkaz:
https://doaj.org/article/59b662ee2eb34c1b9ef2ffa7c77f0b87
Autor:
Jana Aupič, Žiga Strmšek, Fabio Lapenta, David Pahovnik, Tomaž Pisanski, Igor Drobnak, Ajasja Ljubetič, Roman Jerala
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Coiled-coil protein origami (CCPO) is a strategy for the design of polyhedral cage-shaped protein folds based on coiled-coil (CC) dimer-forming peptides. Here, the authors show that CCPO proteins fold in a multistep process governed by the spatial di
Externí odkaz:
https://doaj.org/article/fa4fbd33eafd4cd298224a301d7d0ce4
Autor:
Fabio Lapenta, Jana Aupič, Marco Vezzoli, Žiga Strmšek, Stefano Da Vela, Dmitri I. Svergun, José María Carazo, Roberto Melero, Roman Jerala
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-1 (2021)
A Correction to this paper has been published: https://doi.org/10.1038/s41467-021-21969-9
Externí odkaz:
https://doaj.org/article/9d1e44a13f874e7e8e4e186d66ceb0fa
Autor:
Fabio Lapenta, Alejandro Montón Silva, Renato Brandimarti, Massimiliano Lanzi, Fabio Lino Gratani, Perceval Vellosillo Gonzalez, Sofia Perticarari, Alejandro Hochkoeppler
Publikováno v:
PLoS ONE, Vol 11, Iss 4, p e0152915 (2016)
DNA Polymerases generate pyrophosphate every time they catalyze a step of DNA elongation. This elongation reaction is generally believed as thermodynamically favoured by the hydrolysis of pyrophosphate, catalyzed by inorganic pyrophosphatases. Howeve
Externí odkaz:
https://doaj.org/article/05861949adfd44bd87514b035285ac77
Publikováno v:
Proceedings of the National Academy of Sciences. 119
The function of many channels and transporters is enriched by the conformational plasticity of intrinsically disordered regions (IDRs). Copper transporter 1 (Ctr1) is the main entry point for Cu(I) ions in eukaryotes and contains IDRs both at its N-t
Autor:
Roman Jerala, Tjaša Plaper, Petra Dekleva, Mateja Manček, Fabio Lapenta, Jana Aupič, Mojca Benčina
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
Coiled-coil (CC) dimer-forming peptides are attractive designable modules for mediating protein association. Highly stable CCs are desired for biological activity regulation and assay. Here, we report the design and versatile applications of orthogon
Autor:
Marco Vezzoli, Stefano Da Vela, José María Carazo, Fabio Lapenta, Roberto Melero, Žiga Strmšek, Roman Jerala, Jana Aupič, Dmitri I. Svergun
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-1 (2021)
A Correction to this paper has been published: https://doi.org/10.1038/s41467-021-21969-9
Autor:
Fabio Lapenta, Roman Jerala, Žiga Strmšek, Ajasja Ljubetič, David Pahovnik, Jana Aupič, Igor Drobnak, Tomaž Pisanski
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications 12, 940 (2021). doi:10.1038/s41467-021-21185-5
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications 12, 940 (2021). doi:10.1038/s41467-021-21185-5
Natural proteins are characterised by a complex folding pathway defined uniquely for each fold. Designed coiled-coil protein origami (CCPO) cages are distinct from natural compact proteins, since their fold is prescribed by discrete long-range intera
Autor:
Roberto Melero, Žiga Strmšek, Roman Jerala, Marco Vezzoli, Fabio Lapenta, Jana Aupič, Stefano Da Vela, Dmitrii Ivanovich Svergun, José María Carazo
Publikováno v:
Nature Communications
Nature Communications 12(1), 939 (1-12) (2021). doi:10.1038/s41467-021-21184-6
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications 12(1), 939 (1-12) (2021). doi:10.1038/s41467-021-21184-6
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Coiled-coil protein origami (CCPO) is a modular strategy for the de novo design of polypeptide nanostructures. CCPO folds are defined by the sequential order of concatenated orthogonal coiled-coil (CC) dimer-forming peptides, where a single-chain pro