Search Results - "Schnier, Paul"
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Palmitoylation of TEAD Transcription Factors Is Required for Their Stability and Function in Hippo Pathway Signaling
Published in Structure (London) (05-01-2016)“…The Hippo signaling pathway is responsible for regulating the function of TEAD family transcription factors in metazoans. TEADs, with their co-activators…”
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Proximity-enhanced SuFEx chemical cross-linker for specific and multitargeting cross-linking mass spectrometry
Published in Proceedings of the National Academy of Sciences - PNAS (30-10-2018)“…Chemical cross-linking mass spectrometry (CXMS) is being increasingly used to study protein assemblies and complex protein interaction networks. Existing CXMS…”
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Genetically Introducing Biochemically Reactive Amino Acids Dehydroalanine and Dehydrobutyrine in Proteins
Published in Journal of the American Chemical Society (15-05-2019)“…Expansion of the genetic code with unnatural amino acids (Uaas) has significantly increased the chemical space available to proteins for exploitation. Due to…”
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Reliable Determinations of Protein–Ligand Interactions by Direct ESI-MS Measurements. Are We There Yet?
Published in Journal of the American Society for Mass Spectrometry (01-03-2012)“…The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules,…”
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On the Analytical Superiority of 1D NMR for Fingerprinting the Higher Order Structure of Protein Therapeutics Compared to Multidimensional NMR Methods
Published in Analytical chemistry (Washington) (02-06-2015)“…An important aspect in the analytical characterization of protein therapeutics is the comprehensive characterization of higher order structure (HOS). Nuclear…”
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Fibril treatment changes protein interactions of tau and α-synuclein in human neurons
Published in The Journal of biological chemistry (01-03-2023)“…In several neurodegenerative disorders, the neuronal proteins tau and α-synuclein adopt aggregation-prone conformations capable of replicating within and…”
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Hepcidin Revisited, Disulfide Connectivity, Dynamics, and Structure
Published in The Journal of biological chemistry (04-09-2009)“…Hepcidin is a tightly folded 25-residue peptide hormone containing four disulfide bonds, which has been shown to act as the principal regulator of iron…”
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Resolving Disulfide Structural Isoforms of IgG2 Monoclonal Antibodies by Ion Mobility Mass Spectrometry
Published in Analytical chemistry (Washington) (15-08-2010)“…Recombinant monoclonal antibodies are an important class of therapeutic agents that have found widespread use for the treatment of many human diseases. Here,…”
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Profiling formulated monoclonal antibodies by (1)H NMR spectroscopy
Published in Analytical chemistry (Washington) (15-10-2013)“…Nuclear magnetic resonance (NMR) is arguably the most direct methodology for characterizing the higher-order structure of proteins in solution. Structural…”
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Gas-Phase Proton-Transfer Chemistry Coupled with TOF Mass Spectrometry and Ion Mobility-MS for the Facile Analysis of Poly(ethylene glycols) and PEGylated Polypeptide Conjugates
Published in Analytical chemistry (Washington) (01-04-2008)“…Gas-phase ion/molecule chemistry has been combined with ion mobility separation and time-of-flight mass spectrometry to enable the characterization of large…”
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Native MS Analysis of Bacteriorhodopsin and an Empty Nanodisc by Orthogonal Acceleration Time-of-Flight, Orbitrap and Ion Cyclotron Resonance
Published in Analytical chemistry (Washington) (20-12-2016)“…Over the past two decades, orthogonal acceleration time-of-flight has been the de facto analyzer for solution and membrane-soluble protein native mass…”
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Hydrophobic Protein−Ligand Interactions Preserved in the Gas Phase
Published in Journal of the American Chemical Society (11-11-2009)“…The results of time-resolved thermal dissociation measurements and molecular dynamic simulations are reported for gaseous deprotonated ions of the specific…”
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13
Ordering of the N‑Terminus of Human MDM2 by Small Molecule Inhibitors
Published in Journal of the American Chemical Society (17-10-2012)“…Restoration of p53 function through the disruption of the MDM2-p53 protein complex is a promising strategy for the treatment of various types of cancer. Here,…”
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Structural and Functional Analysis of the Native Peripherin-ROM1 Complex Isolated from Photoreceptor Cells
Published in The Journal of biological chemistry (20-12-2013)“…Peripherin and its homologue ROM1 are retina-specific members of the tetraspanin family of integral membrane proteins required for morphogenesis and…”
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Energetics of Lipid Binding in a Hydrophobic Protein Cavity
Published in Journal of the American Chemical Society (15-02-2012)“…Hydrophobic bonding is central to many biochemical processes, such as protein folding and association. However, a complete description of the forces underlying…”
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Reduced Amino Acid Specificity of Mammalian Tyrosyl-tRNA Synthetase Is Associated with Elevated Mistranslation of Tyr Codons
Published in The Journal of biological chemistry (20-06-2014)“…Quality control operates at different steps in translation to limit errors to approximately one mistranslated codon per 10,000 codons during mRNA-directed…”
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PADLOC: A Powerful Tool to Assign Disulfide Bond Connectivities in Peptides and Proteins by NMR Spectroscopy
Published in Analytical chemistry (Washington) (03-01-2012)“…The determination of the disulfide bond connectivity in a peptide or protein represents a significant challenge. It is notoriously difficult to use NMR…”
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Gas Phase Stabilization of Noncovalent Protein Complexes Formed by Electrospray Ionization
Published in Analytical chemistry (Washington) (15-09-2009)“…The use of gas phase additives to stabilize noncovalent protein complexes in electrospray ionization mass spectrometry (ES-MS) is demonstrated for two…”
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Evidence that Water Can Reduce the Kinetic Stability of Protein−Hydrophobic Ligand Interactions
Published in Journal of the American Chemical Society (22-12-2010)“…The first quantitative comparison of the thermal dissociation rate constants measured for protein−ligand complexes in their hydrated and dehydrated states is…”
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