DOI,IST REx ID,Research Group,Title of publication
10.15479/AT:ISTA:12497,12497,"GradSch,PaSc",Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues
10.1002/anie.202219314,12675,"GradSch,PaSc","The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues"
10.15479/AT:ISTA:12820,12820,PaSc,"Research data of the publication ""Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR"""
10.1021/jacs.3c01200,13095,PaSc,Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR
10.1038/s41586-023-05991-z,13096,PaSc,Structural basis of NINJ1-mediated plasma membrane rupture in cell death
10.1002/ange.202219314,14835,PaSc,"Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten"
10.1039/bk9781839165986-00136,14847,PaSc,"Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies"
10.1002/anie.202304138,14861,PaSc,"Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues"
10.1016/j.sbi.2023.102660,14036,PaSc,Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
10.1016/j.yjsbx.2022.100079,12114,PaSc,Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
10.1038/s41467-022-29423-0,11179,PaSc,Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
10.3389/fmolb.2021.762005,10323,PaSc,How do chaperones bind (partly) unfolded client proteins?
10.1186/s12915-019-0733-6,8402,,The mitochondrial carrier pathway transports non-canonical substrates with an odd number of transmembrane segments
10.1101/2020.06.08.140772,8403,,Structural basis of client specificity in mitochondrial membrane-protein chaperones
10.1101/2020.03.13.990150,8404,,Architecture and subunit dynamics of the mitochondrial TIM9·10·12 chaperone
10.1038/s41467-019-10490-9,8405,,Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex
10.1126/sciadv.aaw3818,8406,,Mechanism of the allosteric activation of the ClpP protease machinery by substrates and active-site inhibitors
10.1016/j.jmr.2019.07.025,8407,,"Relaxing with liquids and solids – A perspective on biomolecular dynamics"
10.1021/jacs.9b04219,8408,,"Aromatic ring dynamics, thermal activation, and transient conformations of a 468 kDa enzyme by specific 1H–13C labeling and fast magic-angle spinning NMR"
10.1016/j.jsb.2018.07.009,8409,,"Studying intact bacterial peptidoglycan by proton-detected NMR spectroscopy at 100 kHz MAS frequency"