Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant

Autor: Stepan Timr, Fabio Sterpone

Publikováno v: Biology, Vol 10, Iss 12, p 1240 (2021)

In this work, we investigate the β-barrel of superoxide dismutase 1 (SOD1) in a mutated form, the isoleucine 35 to alanine (I35A) mutant, commonly used as a model system to decipher the role of the full-length apoSOD1 protein in amyotrophic lateral

Externí odkaz: https://doaj.org/article/d0f6d92be7834fde9b7e6a5ae77451f6

Diffusive Dynamics of Bacterial Proteome as a Proxy of Cell Death

Autor: Daniele Di Bari, Stepan Timr, Marianne Guiral, Marie-Thérèse Giudici-Orticoni, Tilo Seydel, Christian Beck, Caterina Petrillo, Philippe Derreumaux, Simone Melchionna, Fabio Sterpone, Judith Peters, Alessandro Paciaroni

Publikováno v: ACS Central Science
ACS Central Science, 2023, ⟨10.1021/acscentsci.2c01078⟩

International audience; Temperature variations have a big impact on bacterial metabolism and death, yet an exhaustive molecular picture of these processes is still missing. For instance, whether thermal death is determined by the deterioration of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::115c76ce1889ef51d9f03e49809a0c85
https://doi.org/10.1021/acscentsci.2c01078

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

Autor: Ruth Nussinov, Pritam Ganguly, Son Tung Ngo, Carol K. Hall, John E. Straub, Laura Dominguez, Alfonso De Simone, Guanghong Wei, Bikash R. Sahoo, Brianna Hnath, Ayyalusamy Ramamoorthy, Sylvain Lesné, Fabio Sterpone, Simone Melchionna, Nikolay V. Dokholyan, Yiming Wang, Jie Zheng, Rakez Kayed, Jiaxing Chen, Birgit Habenstein, Peter Faller, Philippe Derreumaux, Antoine Loquet, Mara Chiricotto, Birgit Strodel, Buyong Ma, Stepan Timr, James McCarty, Phuong H. Nguyen, Mai Suan Li, Andrew J. Doig, Joan-Emma Shea, Saeed Najafi, Yifat Miller

Publikováno v: Chemical Reviews
Chemical Reviews, American Chemical Society, 2021
Chemical Reviews, American Chemical Society, 2021, 121 (4), pp.2545-2647. ⟨10.1021/acs.chemrev.0c01122⟩
Chemical reviews (2021): 2545–2647. doi:10.1021/acs.chemrev.0c01122
info:cnr-pdr/source/autori:Nguyen P.H.; Ramamoorthy A.; Sahoo B.R.; Zheng J.; Faller P.; Straub J.E.; Dominguez L.; Shea J.-E.; Dokholyan N.V.; De Simone A.; Ma B.; Nussinov R.; Najafi S.; Ngo S.T.; Loquet A.; Chiricotto M.; Ganguly P.; McCarty J.; Li M.S.; Hall C.; Wang Y.; Miller Y.; Melchionna S.; Habenstein B.; Timr S.; Chen J.; Hnath B.; Strodel B.; Kayed R.; Lesne S.; Wei G.; Sterpone F.; Doig A.J.; Derreumaux P./titolo:Amyloid Oligomers: A Joint Experimental%2FComputational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis/doi:10.1021%2Facs.chemrev.0c01122/rivista:Chemical reviews/anno:2021/pagina_da:2545/pagina_a:2647/intervallo_pagine:2545–2647/volume
Chemical reviews 121(4), 2545-2647 (2021). doi:10.1021/acs.chemrev.0c01122
Chem Rev

International audience; Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9bcb0310fc32a8257da65e0ea9a275e
http://hdl.handle.net/11588/839306

Computational Insights into the Unfolding of a Destabilized Superoxide Dismutase 1 Mutant

Autor: Fabio Sterpone, Stepan Timr

Publikováno v: Biology, Vol 10, Iss 1240, p 1240 (2021)
Biology; Volume 10; Issue 12; Pages: 1240
Biology

Simple Summary To function correctly, most proteins need to fold into well-defined three-dimensional structures. Destabilization of these structures may not only lead to the loss of function, but also to toxic aggregation and fibril formation. These

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0acc30f3ef44b0c195195e3c00f858b6
https://www.mdpi.com/2079-7737/10/12/1240

Protein thermal stability

Autor: Stepan, Timr, Dominique, Madern, Fabio, Sterpone

Publikováno v: Progress in molecular biology and translational science. 170

Proteins, in general, fold to a well-organized three-dimensional structure in order to function. The stability of this functional shape can be perturbed by external environmental conditions, such as temperature. Understanding the molecular factors un

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6b88129815cce8599f0f47951ccc91f3
https://pubmed.ncbi.nlm.nih.gov/32145947