about
Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein importAtomic-resolution monitoring of protein maturation in live human cells by NMRIn-cell NMR in E. coli to monitor maturation steps of hSOD1.Protein interaction patterns in different cellular environments are revealed by in-cell NMR.Sequential protein expression and selective labeling for in-cell NMR in human cells.Characterization of proteins by in-cell NMR spectroscopy in cultured mammalian cells.The Casein Kinase 2-Dependent Phosphorylation of NS5A Domain 3 from Hepatitis C Virus Followed by Time-Resolved NMR Spectroscopy.A molecular chaperone activity of CCS restores the maturation of SOD1 fALS mutants.In-cell NMR reveals potential precursor of toxic species from SOD1 fALS mutants.Solution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP.Identification of a novel nucleophosmin-interaction motif in the tumor suppressor p14arf.Intracellular metal binding and redox behavior of human DJ-1.15N isotopic labelling for in-cell protein studies by NMR spectroscopy and single-cell IR synchrotron radiation FTIR microscopy: a correlative study.Direct structural evidence of protein redox regulation obtained by in-cell NMR.Visualization of redox-controlled protein fold in living cells.The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation.Combining in-cell NMR and X-ray fluorescence microscopy to reveal the intracellular maturation states of human superoxide dismutase 1Algal autolysate medium to label proteins for NMR in mammalian cellsStructural insights of proteins in sub-cellular compartments: In-mitochondria NMRCadmium effects on superoxide dismutase 1 in human cells revealed by NMRIn-Cell NMR in Human Cells: Direct Protein Expression Allows Structural Studies of Protein Folding and MaturationDrug Screening in Human Cells by NMR Spectroscopy Allows the Early Assessment of Drug PotencyConformational characterization of full-length X-chromosome-linked inhibitor of apoptosis protein (XIAP) through an integrated approachReal-Time Insights into Biological Events: In-Cell Processes and Protein-Ligand InteractionsBackbone resonance assignment of human DJ-1 in the reduced state and in the cysteine sulfinic acid stateMethylglyoxal interaction with superoxide dismutase 1
P50
Q24306303-590AAE1A-60DC-4759-8845-C770E87C6D39Q33595355-36100C41-DC64-43DE-AF85-59F696341245Q34009391-EBEB695F-F837-4C69-ABE2-CA2646AA547AQ36099762-9623BF89-BE61-4987-A3C6-641818186976Q38807151-E3EB637F-5447-4825-ABA8-1F0F45153FBCQ39753090-4E3FBC91-B334-4226-9FAA-B413DC1467F0Q40193153-C3200AC4-9D33-4765-845F-477A6BC81A15Q46242593-49C8614E-27A5-4099-985F-2E8D657A9A18Q46809689-EC5A0E5D-AAC8-4E88-91A6-CCCFEF9F4861Q47114434-B8713E3E-C590-4701-9EA8-DDF0C16BF51CQ47239822-483D523F-4590-47A3-A312-E025C7641D75Q47316460-9CA91E8E-AE10-41E6-86F0-1227C87526BEQ48101921-52844387-C791-401C-8BF8-8508F30A8A58Q50769112-3102E4C9-F295-495D-85B6-14254B3A7197Q50888274-F0819892-8064-4245-B45D-08E87CE5ABBFQ54965091-04B4BC25-AC3A-4DDB-8ADA-6747C2AE2BBBQ57183062-8F485864-3201-474A-9B53-333842A6EE7BQ60451888-3DD86F2B-EA7F-4E59-8AF1-8594B12775A8Q60451890-F96B9F69-0A36-4BFF-AB84-32EFD6C55577Q61803739-7BDD8222-F75E-4CA4-9E59-97BCDB8165BFQ88992406-943FCF55-15B3-49E2-8AC6-87A4B41AF1E6Q89542672-B08191E2-EC35-4F8B-8CC1-3942DAB2EA33Q90428040-ECFD70BD-7C8A-40E1-A415-56ED5E677F33Q90726347-5BF7274F-D98F-46CC-8AF9-061D855F5E55Q92391826-2FFDB939-63A7-464C-9DD9-DF33F6DFDA12Q92601857-E0A83F7C-14C7-40F9-B412-B24657E6900D
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description
hulumtues
@sq
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Enrico Luchinat
@ast
Enrico Luchinat
@en
Enrico Luchinat
@es
Enrico Luchinat
@nl
Enrico Luchinat
@sl
type
label
Enrico Luchinat
@ast
Enrico Luchinat
@en
Enrico Luchinat
@es
Enrico Luchinat
@nl
Enrico Luchinat
@sl
prefLabel
Enrico Luchinat
@ast
Enrico Luchinat
@en
Enrico Luchinat
@es
Enrico Luchinat
@nl
Enrico Luchinat
@sl
P214
P1053
O-1776-2014
P106
P1153
37066145400
P21
P214
P2798
P31
P3829
P396
IT\ICCU\BVEV\193469
P496
0000-0003-4183-4311
P569
1985-01-01T00:00:00Z
P7859
viaf-307327112