Výsledky vyhledávání - "Lorenza Pacini"

Akademický článek

GCAT: A network model of mutational influences between amino acid positions in PSD95pdz3

Publikováno v: Frontiers in Molecular Biosciences, Vol 9 (2022)

Proteins exist for more than 3 billion years: proof of a sustainable design. They have mechanisms coping with internal perturbations (e.g., amino acid mutations), which tie genetic backgrounds to diseases or drug therapy failure. One difficulty to gr

Externí odkaz: https://doaj.org/article/1ca46b5e498d4d689c90a4a53eba4fe3

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Akademický článek

A protocol to measure slow protein dynamics of the cholera toxin B pentamers using broadband dielectric spectroscopy

Autor: Laetitia Bourgeat, Lorenza Pacini, Anatoli Serghei, Claire Lesieur

Publikováno v: STAR Protocols, Vol 3, Iss 3, Pp 101561- (2022)

Summary: The present protocol describes how to measure experimentally the slow protein dynamics that take place upon the thermal unfolding of the B subunit cholera toxin pentamers using broadband dielectric spectroscopy (BDS) in weakly hydrated and n

Externí odkaz: https://doaj.org/article/e1cc37b2772c40f79acd5315f079b33a

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Akademický článek

Mapping Function from Dynamics: Future Challenges for Network-Based Models of Protein Structures

Autor: Lorenza Pacini, Rodrigo Dorantes-Gilardi, Laurent Vuillon, Claire Lesieur

Publikováno v: Frontiers in Molecular Biosciences, Vol 8 (2021)

Proteins fulfill complex and diverse biological functions through the controlled atomic motions of their structures (functional dynamics). The protein composition is given by its amino-acid sequence, which was assumed to encode the function. However,

Externí odkaz: https://doaj.org/article/08ba68e56aac4e09b7f4f98c51890492

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Complementarity and drivers of thermal and physical soil organic carbon fractions at the scale of mainland France

Autor: Amicie Delahaie, Lauric Cécillon, Claire Chenu, Dominique Arrouays, Line Boulonne, Claudy Jolivet, Céline Ratié, Nicolas Saby, Marija Stojanova, Antonio Bispo, Manuel Martin, Pierre Arbelet, Jussi Heinonsalo, Christopher Poeplau, Kristiina Karhu, Pierre Roudier, Samuel Abiven, Lorenza Pacini, Pierre Barré

Assessing soil organic carbon biogeochemical stability is critical for estimating future changes in soil carbon stocks. Several methods for the assessment of soil organic carbon (SOC) biogeochemical stability have been proposed but very few can be im

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::80dcffa8c7dfaa1760551ac3c85c639e
https://doi.org/10.5194/egusphere-egu23-6849

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A computational methodology to diagnose sequence-variant dynamic perturbations by comparing atomic protein structures

Autor: Claire Lesieur, Lorenza Pacini

Publikováno v: Bioinformatics
Bioinformatics, 2021, ⟨10.1093/bioinformatics/btab736⟩
Bioinformatics, Oxford University Press (OUP), 2021, ⟨10.1093/bioinformatics/btab736⟩

Motivation The objective is to diagnose dynamics perturbations caused by amino-acid mutations as prerequisite to assess protein functional health or drug failure, simply using network models of protein X-ray structures. Results We find that the diffe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::374832b461e2e33c94397a4fa94c040a
https://doi.org/10.1093/bioinformatics/btab736

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Experimental diagnostic of sequence-variant dynamic perturbations revealed by broadband dielectric spectroscopy

Autor: Claire Lesieur, Laëtitia Bourgeat, Anatoli Serghei, Lorenza Pacini

Publikováno v: Structure
Structure, Elsevier (Cell Press), 2021, ⟨10.1016/j.str.2021.05.005⟩

Summary Genetic diversity leads to protein robustness, adaptability, and failure. Some sequence variants are structurally robust but functionally disturbed because mutations bring the protein onto unfolding/refolding routes resulting in misfolding di

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c203e5b39829f32740f6b0788ba336ab
https://hal.archives-ouvertes.fr/hal-03428657

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Induced Perturbation Network and tiling for modeling the L55P Transthyretin amyloid fiber

Autor: Lorenza Pacini, Laurent Vuillon, Claire Lesieur

Publikováno v: Procedia Computer Science
Procedia Computer Science, Elsevier, 2020, 178, pp.8-17. ⟨10.1016/j.procs.2020.11.002⟩
Procedia Computer Science, 2020, 178, pp.8-17. ⟨10.1016/j.procs.2020.11.002⟩

Protein structures are complex spatial systems, formed by the three-dimensional arrangement of amino acids, that interact through atomic contacts. It is fundamental to understand the perturbation mechanisms associated with the amino acid mutations th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::772942a8d825e39bb7a23cbf794a850b
https://hal.archives-ouvertes.fr/hal-03428679

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Analysis of Nanoconfined Protein Dielectric Signals Using Charged Amino Acid Network Models

Autor: Lorenza Pacini, Laëtitia Bourgeat, Anatoli Serghei, Claire Lesieur

Publikováno v: Australian Journal of Chemistry
Australian Journal of Chemistry, CSIRO Publishing, 2020, 73 (8), pp.803. ⟨10.1071/CH19502⟩
Australian Journal of Chemistry, 2020, 73 (8), pp.803. ⟨10.1071/CH19502⟩

International audience; Protein slow motions involving collective molecular fluctuations on the timescale of microseconds to seconds are difficult to measure and not well understood despite being essential to sustain protein folding and protein funct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5ad6073de30e13ba5efe33e80e5acf8
https://hal.archives-ouvertes.fr/hal-03060094

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Exploring Allosteric Pathways of a V-Type Enzyme with Dynamical Perturbation Networks

Autor: Ivan Rivalta, Laurent Vuillon, Lorenza Pacini, Aria Gheeraert, Victor S. Batista, Claire Lesieur

Publikováno v: Journal of Physical Chemistry B
Journal of Physical Chemistry B, American Chemical Society, 2019, 123 (16), pp.3452-3461. ⟨10.1021/acs.jpcb.9b01294⟩
Journal of Physical Chemistry B, 2019, 123 (16), pp.3452-3461. ⟨10.1021/acs.jpcb.9b01294⟩

International audience; Elucidation of the allosteric pathways in proteins is a computational challenge that strongly benefits from combination of atomistic molecular dynamics (MD) simulations and coarse-grained analysis of the complex dynamical netw

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c3dd14ec93ed888d2cbfdbd65651e23
https://hal.archives-ouvertes.fr/hal-02134286

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In proteins, the structural responses of a position to mutation rely on the Goldilocks principle: not too many links, not too few

Autor: Rodrigo Dorantes-Gilardi, Claire Lesieur, Lorenza Pacini, Laurent Vuillon, Laëtitia Bourgeat

Publikováno v: Physical Chemistry Chemical Physics
Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2018, 20 (39), pp.25399-25410. ⟨10.1039/C8CP04530E⟩
Physical Chemistry Chemical Physics, 2018, 20 (39), pp.25399-25410. ⟨10.1039/C8CP04530E⟩

International audience; A disease has distinct genetic and molecular hallmarks such as sequence variants that are likely to produce the alternative protein structures accountable for individual responses to drugs and disease development. Thus, to set

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::decf170118f3d1eaf4cf351b61d6cb87
https://hal.archives-ouvertes.fr/hal-01921198

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