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IRED specifications

Information


Unique identifier OMICS_27030
Name IRED
Alternative name Imine Reductase Engineering Database
Restrictions to use None
Community driven No
Data access File download, Browse
User data submission Not allowed
Version 3
Maintained Yes

Maintainer


  • person_outline Jurgen Pleiss

Publication for Imine Reductase Engineering Database

IRED citations

 (5)
library_books

A histone mimicking interdomain linker in a multidomain protein modulates multivalent histone binding

2017
PMCID: 5663869
PMID: 28864776
DOI: 10.1074/jbc.M117.801464

[…] °C. The intensity ratio of the oxidized and reduced (50 mm ascorbic acid) BAZ2B(PHD-BRD)–H3(1–21) complex was measured. Ratios of cross-peaks between oxidized and reduced states were calculated (Iox/Ired) and depicted as a temperature coding using home-written routines based on NMRPipe (). […]

library_books

Combining NMR and small angle X ray scattering for the study of biomolecular structure and dynamics

2017
PMCID: 5553349
PMID: 28501583
DOI: 10.1016/j.abb.2017.05.005

[…] data. These ensembles were subsequently used to develop a model describing the overall rotational diffusion of the dimer and the motional coupling between domains. Reorientational Eigenmode Dynamics (iRED) analysis was employed to extract eigenmodes from the selected ensemble and determine optimized correlation times in good agreement with experimental 15N spin relaxation data. This thorough anal […]

library_books

Age effects on voluntary and automatic adjustments in anti pointing tasks

2015
PMCID: 4731427
PMID: 26497989
DOI: 10.1007/s00221-015-4459-6

[…] uter screen. The start button was where the index finger rested at the beginning of each trial (i.e., starting position). That is, before each trial, the participants pressed on the start button (and IRED) with their right index finger. The starting button was released the moment the participant started reaching. This generated a signal, which was fed into the Optotrak and the E-prime systems. The […]

library_books

A Relationship between the Transient Structure in the Monomeric State and the Aggregation Propensities of α Synuclein and β Synuclein

2014
Biochemistry
PMCID: 4245978
PMID: 25389903
DOI: 10.1021/bi5009326

[…] rotein with MTSL attached in 10 mM sodium phosphate (pH 7.4), 100 mM NaCl, and 10% D2O. Control samples contained 100 μM 15N-labeled protein and 100 μM spin-labeled protein. The uniformity of the Iox/Ired calculated from the control spectra showed that there were no complications arising from the reduction method and that aggregation did not occur. Backbone NMR assignments for αS and βS were obtai […]

library_books

BAX Activation is Initiated at a Novel Interaction Site

2008
Nature
PMCID: 2597110
PMID: 18948948
DOI: 10.1038/nature07396

[…] cquired at 32°C on a Bruker 600 MHz NMR spectrometer, processed using NMRPipe and analyzed with NMRView (see Supplementary Notes for software references). Two 1H-15N HSQC spectra for PRE NMR were acquired using a 1:1 ratio of BAX to MTSL-labeled SAHB in the oxidized and reduced state. The reduced compound was generated by exposure to five molar excess ascorbic acid for one hour. PRE effects were m […]

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IRED institution(s)
Institute of Technical Biochemistry, University of Stuttgart, Stuttgart, Germany
IRED funding source(s)
Supported by the Ministry for Science, Research and the Arts of Baden-Wurttemberg, Germany [MWK; Baden-Wurttemberg Biosynthesis netWork (BW2)]; the Innovative Medicines Initiative Grant number: 115360; the European Union’s Seventh Framework Programme Grant number: FP7/2007–2013; and the EFPIA companies.

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