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Journal Article
Angewandte Chemie, ISSN 0044-8249, 09/2016, Volume 128, Issue 39, pp. 12149 - 12153
An approach to the de novo structure prediction of proteins is described that relies on surface accessibility data from NMR paramagnetic relaxation... 
Paramagnetische Relaxation | Strukturbiologie | Proteinstrukturbestimmung | NMR-Spektroskopie | CS-Rosetta | Proteins | Analysis | Algorithms | Accessibility | Computation | Mathematical models | Folding | Standards | Convergence
Journal Article
Acta Neuropathologica, ISSN 0001-6322, 4/2016, Volume 131, Issue 4, pp. 587 - 604
Deposition of the nuclear DNA/RNA-binding protein Fused in sarcoma (FUS) in cytosolic inclusions is a common hallmark of some cases of frontotemporal lobar... 
Pathology | Neurosciences | Protein arginine methyltransferase 1 (PRMT1) | Transportin-1 | Medicine & Public Health | Frontotemporal lobar degeneration (FTLD) | Amyotrophic lateral sclerosis (ALS) | Neurodegeneration | Fused in sarcoma (FUS) | Arginine methylation | NUCLEAR IMPORT | PROTEIN ARGININE METHYLTRANSFERASE | AMYOTROPHIC-LATERAL-SCLEROSIS | PATHOLOGY | FRONTOTEMPORAL LOBAR DEGENERATION | NEUROSCIENCES | MASS-SPECTROMETRY | CLINICAL NEUROLOGY | METHYLATION SITES | FET PROTEINS | LINKED MUTATIONS | IN-VIVO | SARCOMA EWS PROTEIN | Protein Binding - genetics | Embryo, Mammalian | Humans | Male | Cerebral Cortex - cytology | RNA-Binding Protein FUS - immunology | Frontotemporal Lobar Degeneration - metabolism | beta Karyopherins - immunology | Protein Binding - drug effects | Female | Neurons - metabolism | Protein-Arginine N-Methyltransferases - genetics | Inclusion Bodies - metabolism | Neurons - drug effects | Amyotrophic Lateral Sclerosis - genetics | Mice, Inbred C57BL | Cells, Cultured | Enzyme Inhibitors - pharmacology | Rats | Inclusion Bodies - drug effects | RNA-Binding Protein FUS - metabolism | Mice, Knockout | Protein-Arginine N-Methyltransferases - metabolism | Antibodies - pharmacology | Animals | Amyotrophic Lateral Sclerosis - metabolism | Mice | Embryonic Stem Cells | Frontotemporal Lobar Degeneration - genetics | beta Karyopherins - metabolism | Methylation | Arginine - metabolism | Monoclonal antibodies | Amyotrophic lateral sclerosis | Chemical properties | Sarcoma | Transferases | Protein binding | Index Medicus
Journal Article
BIOspektrum, ISSN 0947-0867, 3/2018, Volume 24, Issue 2, pp. 161 - 163
Nuclear magnetic resonance (NMR) spectroscopy is a well suited method for the analysis of biomolecules in solution and provides unique insights into their... 
Life Sciences | Biochemistry, general | Human Genetics | Life Sciences, general | Microbiology | Pharmacology/Toxicology | Spectroscopy | Nuclear magnetic resonance--NMR | Data acquisition | Structure-function relationships
Journal Article
Angewandte Chemie, ISSN 0044-8249, 11/2016, Volume 128, Issue 47, pp. 15069 - 15073
Die Erforschung von intrinsisch unstrukturierten Proteinen (IDPs) mit NMR‐spektroskopischen Methoden wird oftmals durch starke Überlagerung der Proteinsignale... 
Pseudo-chemische Verschiebung | Lanthanoide | Chemische Verschiebungsdispersion | Instrinsisch unstrukturierte Proteine | Kernspinresonanz
Journal Article
Journal of Physical Chemistry B, ISSN 1520-6106, 04/2009, Volume 113, Issue 13, pp. 4400 - 4406
Journal Article
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 02/2019, Volume 116, Issue 9, pp. 3604 - 3613
Journal Article
International Journal of Computer Assisted Radiology and Surgery, ISSN 1861-6410, 6/2018, Volume 13, Issue 6, pp. 759 - 767
Journal Article