PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7793976-1 1995 In this study, we have spin-labeled the lysine and cysteine residues of low-density lipoprotein (LDL) using N-4-(2,2,6,6-tetramethylpiperidinyl-1-oxyl-4-yl) maleimide (MAL-6) and succinimidyl-2,2,5,5-tetramethyl-3-pyrroline-1-oxyl-3-carboxylate (SSL), respectively. Cysteine 51-59 spindlin 1 Homo sapiens 23-27 11804734-2 2001 Spin labels (N-(1-oxyl-2,2,5,5-tetramethyl-3-pyrrolidinyl)iodoacetamide, IPSL) were introduced at cysteines, by site-directed mutagenesis at seven different positions in the protein. Cysteine 98-107 spindlin 1 Homo sapiens 0-4 10423365-2 1999 The peptide, which follows the single letter sequence, was reacted with the methanethiosulfonate spin label at the cysteine sulfur. Cysteine 115-123 spindlin 1 Homo sapiens 97-101 7639532-5 1995 The addition of glutathione or cysteine produces a large increase in the intensity of the .DMPO-OH spin adduct signal; experiments employing superoxide dismutase suggest that the increases in the amounts of .DMPO-OH adduct are produced from the decomposition of the spin adduct of the superoxide radical (.DMPO-OOH). Cysteine 31-39 spindlin 1 Homo sapiens 99-103 7639532-5 1995 The addition of glutathione or cysteine produces a large increase in the intensity of the .DMPO-OH spin adduct signal; experiments employing superoxide dismutase suggest that the increases in the amounts of .DMPO-OH adduct are produced from the decomposition of the spin adduct of the superoxide radical (.DMPO-OOH). Cysteine 31-39 spindlin 1 Homo sapiens 266-270 35490028-0 2022 Manipulating electron-spin polarization using cysteine-DNA chiral conjugates. Cysteine 46-54 spindlin 1 Homo sapiens 22-26 34776648-0 2021 Spin Labeling of Surface Cysteines Using a Bromoacrylaldehyde Spin Label. Cysteine 25-34 spindlin 1 Homo sapiens 0-4 34776648-0 2021 Spin Labeling of Surface Cysteines Using a Bromoacrylaldehyde Spin Label. Cysteine 25-34 spindlin 1 Homo sapiens 62-66 34776648-1 2021 Structural investigations of proteins and their biological complexes are now frequently complemented by distance constraints between spin labeled cysteines generated using double electron-electron resonance (DEER) spectroscopy, via site directed spin labeling (SDSL). Cysteine 146-155 spindlin 1 Homo sapiens 133-137 34776648-3 2021 In this article we introduce the use of bromoacrylaldehyde spin label (BASL) as a cysteine spin label, demonstrating an advantage over MTSSL due to its increased selectivity for surface cysteines, eliminating the need to "knock out" superfluous cysteine residues. Cysteine 82-90 spindlin 1 Homo sapiens 59-63 34776648-3 2021 In this article we introduce the use of bromoacrylaldehyde spin label (BASL) as a cysteine spin label, demonstrating an advantage over MTSSL due to its increased selectivity for surface cysteines, eliminating the need to "knock out" superfluous cysteine residues. Cysteine 82-90 spindlin 1 Homo sapiens 91-95 35490028-2 2022 We report a controlled spin-selective transmission of electrons through self-assembled monolayers of 15 base-paired double-stranded deoxyribonucleic acid functionalized with two enantiomeric cysteine molecules on gold explored through the quantum mechanical tunneling effect. Cysteine 191-199 spindlin 1 Homo sapiens 23-27 2458760-6 1988 The distance between the Glx and Cys moieties was estimated at greater than or equal to 10-25 A from double spin-labeling experiments. Cysteine 33-36 spindlin 1 Homo sapiens 108-112 30776218-2 2019 The spin label links to cysteines via a short thioether tether and has a narrow central transition indicative of small zero-field splitting (ZFS). Cysteine 24-33 spindlin 1 Homo sapiens 4-8 164224-4 1975 Selective modification of the active site cysteine residue (149) and determinations of total sulphydryl content implicate this residue as the site of the immobile spin-label. Cysteine 42-50 spindlin 1 Homo sapiens 163-167 31657498-0 2020 Isoindoline-Based Nitroxides as Bioresistant Spin Labels for Protein Labeling via Cysteines and Alkyne Bearing Noncanonical Amino Acids. Cysteine 82-91 spindlin 1 Homo sapiens 45-49 28933855-0 2017 Orthogonal Tyrosine and Cysteine Site-Directed Spin Labeling for Dipolar Pulse EPR Spectroscopy on Proteins. Cysteine 24-32 spindlin 1 Homo sapiens 47-51 30686862-1 2018 Site-directed spin labeling of proteins by chemical modification of engineered cysteine residues with the molecule MTSSL (1-Oxyl-2,2,5,5-tetramethylpyrroline-3-methyl methanethiosulfonate) has been an invaluable tool for conducting double electron electron resonance (DEER) spectroscopy experiments. Cysteine 79-87 spindlin 1 Homo sapiens 14-18 29369431-5 2018 To render a particular target molecule accessible for PELDOR, it can be engineered to contain only one or two surface-exposed cysteine residues, which can be efficiently spin-labelled using thiol-reactive nitroxide compounds. Cysteine 126-134 spindlin 1 Homo sapiens 170-174 29369431-9 2018 Here we describe the concept of "inhibitor-directed spin labelling" (IDSL) as an approach to spin label suitable cysteine-rich proteins in a site-directed and highly specific manner by employing bespoke spin-labelled inhibitors. Cysteine 113-121 spindlin 1 Homo sapiens 52-56 29369431-9 2018 Here we describe the concept of "inhibitor-directed spin labelling" (IDSL) as an approach to spin label suitable cysteine-rich proteins in a site-directed and highly specific manner by employing bespoke spin-labelled inhibitors. Cysteine 113-121 spindlin 1 Homo sapiens 93-97 29369431-9 2018 Here we describe the concept of "inhibitor-directed spin labelling" (IDSL) as an approach to spin label suitable cysteine-rich proteins in a site-directed and highly specific manner by employing bespoke spin-labelled inhibitors. Cysteine 113-121 spindlin 1 Homo sapiens 93-97 29278328-3 2018 Here we map the spin density distribution onto the cysteine ligands for the three major classes of the protein-bound, reduced [2Fe-2S](His)n(Cys)4-n (n = 0, 1, 2) cluster by selective cysteine-13Cbeta isotope labeling. Cysteine 51-59 spindlin 1 Homo sapiens 16-20 29278328-3 2018 Here we map the spin density distribution onto the cysteine ligands for the three major classes of the protein-bound, reduced [2Fe-2S](His)n(Cys)4-n (n = 0, 1, 2) cluster by selective cysteine-13Cbeta isotope labeling. Cysteine 141-144 spindlin 1 Homo sapiens 16-20 29278328-3 2018 Here we map the spin density distribution onto the cysteine ligands for the three major classes of the protein-bound, reduced [2Fe-2S](His)n(Cys)4-n (n = 0, 1, 2) cluster by selective cysteine-13Cbeta isotope labeling. Cysteine 184-192 spindlin 1 Homo sapiens 16-20 24231132-7 2013 Spin polarization with an unusual mirror symmetry on Ni- and Pd-doped graphene is induced by chemisorption of unprotonated l-cysteine, except for O-end adsorption on Pd-doped graphene. Cysteine 123-133 spindlin 1 Homo sapiens 0-4 27797176-3 2016 In this Account, we discuss new types of spin-dependent electrochemistry measurements and their use to probe the spin-dependent charge transport properties of nonmagnetic chiral conductive polymers and biomolecules, such as oligopeptides, L/D cysteine, cytochrome c, bacteriorhodopsin (bR), and oligopeptide-CdSe nanoparticles (NPs) hybrid structures. Cysteine 243-251 spindlin 1 Homo sapiens 41-45 27797176-3 2016 In this Account, we discuss new types of spin-dependent electrochemistry measurements and their use to probe the spin-dependent charge transport properties of nonmagnetic chiral conductive polymers and biomolecules, such as oligopeptides, L/D cysteine, cytochrome c, bacteriorhodopsin (bR), and oligopeptide-CdSe nanoparticles (NPs) hybrid structures. Cysteine 243-251 spindlin 1 Homo sapiens 113-117