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Showing 1–13 of 13 results

Advanced filters: Author: Enrico Luchinat Clear advanced filters

In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants

Mutations in the enzyme superoxide dismutase 1 (SOD1) underlie a form of neurodegenerative disease called amyotrophic lateral sclerosis. Here the authors employ in-cell NMR to show that SOD1 mutants adopt unstructured conformations that are unable to bind zinc and may form toxic SOD1 aggregates.

Enrico Luchinat
Letizia Barbieri
Lucia Banci
Research27 Nov 2014
Nature Communications

Volume: 5, P: 1-10
The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation

Mutations in superoxide dismutase-1 (SOD1) cause amyotrophic lateral sclerosis (ALS). Here the authors present the SOD1 crystal structure bound to the small cysteine-reactive molecule ebselen and show that ebselen is a chaperone for SOD1.

Michael J. Capper
Gareth S. A. Wright
S. Samar Hasnain
ResearchOpen Access27 Apr 2018
Nature Communications

Volume: 9, P: 1-9
The competitive world of RAS biology

System-wide approaches are gaining popularity over traditional studies of individual molecular components. A new NMR approach unravels the interaction hierarchy of these different components by placing them in direct competition for the same target.

Claudio Luchinat
Giacomo Parigi
Enrico Ravera
News & Views14 Feb 2014
Nature Chemical Biology

Volume: 10, P: 173-174
Atomic-resolution monitoring of protein maturation in live human cells by NMR

Analysis of proteins within their native environment can confirm and extend in vitro–derived conclusions. NMR analysis of superoxide dismutase 1 in live human cells now corroborates previously identified steps on the maturation pathway and demonstrates copper-independent function of the chaperone CCS.

Lucia Banci
Letizia Barbieri
A Radu Aricescu
Research03 Mar 2013
Nature Chemical Biology

Volume: 9, P: 297-299
Structural characterization of a protein adsorbed on aluminum hydroxide adjuvant in vaccine formulation

Linda Cerofolini
Stefano Giuntini
Marco Fragai
ResearchOpen Access28 May 2019
npj Vaccines

Volume: 4, P: 1-5
Atomic structural details of a protein grafted onto gold nanoparticles

Stefano Giuntini
Linda Cerofolini
Claudio Luchinat
ResearchOpen Access20 Dec 2017
Scientific Reports

Volume: 7, P: 1-6
Protein interaction patterns in different cellular environments are revealed by in-cell NMR

Letizia Barbieri
Enrico Luchinat
Lucia Banci
ResearchOpen Access24 Sept 2015
Scientific Reports

Volume: 5, P: 1-9
¹H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization

Enrico Ravera
Linda Cerofolini
Claudio Luchinat
ResearchOpen Access09 Jun 2016
Scientific Reports

Volume: 6, P: 1-7
Interhelical interactions within the STIM1 CC1 domain modulate CRAC channel activation

The helical bundle structure of the CC1 domain of STIM1 of the store-activated calcium channel CRAC is crucial to maintaining the channel resting state, and helix–helix interactions can be manipulated to normalize a disease-linked STIM1 mutant.

Petr Rathner
Marc Fahrner
Norbert Müller
Research26 Oct 2020
Nature Chemical Biology

Volume: 17, P: 196-204
Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models

Inducible protein overexpression in stably transfected cells enables the acquisition of atomically resolved NMR spectra of proteins in human cells during specific cell cycle phases and in 3D human tissue models.

Jan Rynes
Eva Istvankova
Lukas Trantirek
ResearchOpen Access07 Feb 2025
Communications Biology

Volume: 8, P: 1-9
Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP

Meng-Meng Hou
Panagis Polykretis
Xun-Cheng Su
ResearchOpen Access30 Nov 2017
Scientific Reports

Volume: 7, P: 1-11
Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells

In-cell NMR provides detailed structural information about proteins in their native environment in living cells. This in-cell NMR protocol allows the study of protein folding and maturation in the presence of cofactors in cultured mammalian cells.

Letizia Barbieri
Enrico Luchinat
Lucia Banci
Protocols19 May 2016
Nature Protocols

Volume: 11, P: 1101-1111
A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants

Enrico Luchinat
Letizia Barbieri
Lucia Banci
ResearchOpen Access12 Dec 2017
Scientific Reports

Volume: 7, P: 1-8