Daniel Nietlispach

ORCID: 0000-0003-4364-9291
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Enzyme Structure and Function
  • NMR spectroscopy and applications
  • Protein Kinase Regulation and GTPase Signaling
  • Protein Structure and Dynamics
  • Receptor Mechanisms and Signaling
  • Lipid Membrane Structure and Behavior
  • Advanced NMR Techniques and Applications
  • RNA and protein synthesis mechanisms
  • Photoreceptor and optogenetics research
  • Neuroscience and Neuropharmacology Research
  • Advanced MRI Techniques and Applications
  • Mass Spectrometry Techniques and Applications
  • Microbial Natural Products and Biosynthesis
  • Neuropeptides and Animal Physiology
  • Microtubule and mitosis dynamics
  • Sparse and Compressive Sensing Techniques
  • RNA Research and Splicing
  • Glycosylation and Glycoproteins Research
  • Molecular spectroscopy and chirality
  • Metabolomics and Mass Spectrometry Studies
  • Organometallic Complex Synthesis and Catalysis
  • Cancer-related gene regulation
  • Enzyme Production and Characterization
  • Monoclonal and Polyclonal Antibodies Research
  • Cellular transport and secretion

University of Cambridge
2016-2025

University of Liège
2010

Institut Curie
2009

Inserm
2009

RIKEN
2002

University of Leicester
2002

European Molecular Biology Laboratory
1996

Merck (Germany)
1996

DuPont (United States)
1996

University of Zurich
1994

Make it snappy! The use of compressed sensing to reconstruct multidimensional NMR spectra enables significant reductions in recording time. Thus, 3D HNCA (blue) and HN(CO)CA (green) sufficient quality for rapid protein-backbone assignment were reconstructed from only 16 % the fully sampled data. generality method its robustness noise should make more broadly applicable, example, solid-state spectroscopy. Detailed facts importance specialist readers are published as ”Supporting Information”....

10.1002/anie.201100440 article EN Angewandte Chemie International Edition 2011-06-06

Abstract A complex conformational energy landscape determines G-protein-coupled receptor (GPCR) signalling via intracellular binding partners (IBPs), e.g., G s and β-arrestin. Using 13 C methyl methionine NMR for the β 1 -adrenergic receptor, we identify ligand efficacy-dependent equilibria between an inactive pre-active state and, in with -mimetic nanobody, more less active ternary complexes. Formation of a basal activity through ligand-free nanobody–receptor interaction reveals structural...

10.1038/s41467-017-02008-y article EN cc-by Nature Communications 2017-11-21

G-protein-coupled receptors (GPCRs) are allosteric signaling proteins that transmit an extracellular stimulus across the cell membrane. Using 19F NMR and site-specific labelling, we investigate response of cytoplasmic region transmembrane helices 6 7 β1-adrenergic receptor to agonist stimulation coupling a Gs-protein-mimetic nanobody. Agonist binding shows in equilibrium between two inactive states pre-active form, increasingly populated with higher ligand efficacy. Nanobody leads fully...

10.1038/s41467-020-14526-3 article EN cc-by Nature Communications 2020-02-03

Vinculin regulates both cell-cell and cell-matrix junctions anchors adhesion complexes to the actin cytoskeleton through its interactions with vinculin binding sites of α-actinin or talin. Activation requires a severing intramolecular between N- C-terminal domains, which is necessary for bind F-actin; yet how this occurs in cells not resolved. We tested hypothesis that talin activate their sites. Indeed, we show these have high affinity full-length vinculin, are sufficient sever head-tail...

10.1074/jbc.m510397200 article EN cc-by Journal of Biological Chemistry 2006-01-10

Abstract G protein-coupled receptors (GPCRs) bind to different protein α-subtypes with varying degrees of selectivity. The mechanism by which GPCRs achieve this selectivity is still unclear. Using 13 C methyl methionine and 19 F NMR, we investigate the agonist-bound active state β 1 AR its ternary complexes proteins in solution. We find receptor adopts very similar conformations. In contrast, full assumes a conformation differing from previously characterised activation intermediates or...

10.1038/s41467-024-45680-7 article EN cc-by Nature Communications 2024-02-13

A combination of simulation and experiment is used to demonstrate that the sensitivity a family 3D/4D NMR experiments assign resonances obtain structural restraints in proteins improved by partial random deuteration; improvement increases as correlation time protein becomes longer. The results suggest deuteration at level ∼50% optimizes which are sidechain 1H 13C correlating them with from backbone nuclei. In addition, this also good compromise for recording NOESY experiments. Using...

10.1021/ja952207b article EN Journal of the American Chemical Society 1996-01-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTGeneral route to the half-open ruthenium metallocenes C5Me5Ru(pentadienyl) and C5Me5Ru(diene)Cl. X-ray structures of an optically active metallocene a dimetallic ruthenabenzene complexH. William Bosch, Hans Ulrich Hung, Daniel Nietlispach, Albrecht SalzerCite this: Organometallics 1992, 11, 6, 2087–2098Publication Date (Print):June 1, 1992Publication History Published online1 May 2002Published inissue 1 June...

10.1021/om00042a025 article EN Organometallics 1992-06-01

Protein in motion: A solution-state NMR study on the seven-helix transmembrane protein pSRII (see picture) a detergent solution focused sequential backbone assignment, characterization of secondary structure, and dynamics. The structural integrity was confirmed, mobility loops (ps–ns timescale) slower motions helical core (μs–ms were identified. Supporting information for this article is available WWW under http://www.wiley-vch.de/contents/jc_2002/2008/z802783_s.pdf or from author. Please...

10.1002/anie.200802783 article EN Angewandte Chemie International Edition 2008-08-01

The partial unfolding of human lysozyme underlies its conversion from the soluble state into amyloid fibrils observed in a fatal hereditary form systemic amyloidosis. To understand molecular origins disease, it is critical to characterize structural and physicochemical properties amyloidogenic states protein. Here we provide high-resolution view process at low pH for three different variants, wild-type protein mutants I56T I59T, which show variable stabilities propensities aggregate vitro....

10.1021/ja103524m article EN publisher-specific-oa Journal of the American Chemical Society 2010-10-19

Klasse statt Masse: Durch die Anwendung des "Compressed-Sensing"-Verfahrens bei der Rekonstruktion mehrdimensionaler NMR-Spektren lassen sich Aufnahmezeiten beträchtlich verkürzen. So wurden 3D-HNCA- (blau) und 3D-HN(CO)CA-Spektren (grün) mit hinreichender Qualität für schnelle Zuordnung von Proteinrückgrat-Signalen aus nur 16 % aller gesammelten Daten rekonstruiert. Die allgemeine wenig rauschempfindliche Methode könnte auch Festkörper-NMR-Spektroskopie Nutzen sein. Detailed facts of...

10.1002/ange.201100440 article EN Angewandte Chemie 2011-06-06

Based on the saposin-A (SapA) scaffold protein, we demonstrate suitability of a size-adaptable phospholipid membrane-mimetic system for solution NMR studies membrane proteins (MPs) under close-to-native conditions. The Salipro nanoparticle size can be tuned over wide pH range by adjusting saposin-to-lipid stoichiometry, enabling maintenance sufficiently high amounts in to mimic realistic environment while controlling overall enable MPs. Three representative MPs, including one...

10.1021/jacs.7b06730 article EN cc-by Journal of the American Chemical Society 2017-10-09
Coming Soon ...