Increased Arterial Stiffness Observed in Patients with Systemic Lupus Erythematosus Rheumatology Advisor
Augmentation index was linked to the atherogenic lipoproteins that were analyzed using nuclear magnetic resonance imaging. The immunologic variables associated with augmentation index included C4 (r=0.259; P =.046) and immunoglobulin M ...
Increased Arterial Stiffness Observed in Patients with Systemic Lupus Erythematosus - Rheumatology Advisor More...
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Ischemic Stroke, Myocardial Infarction Both Tied to Lipoproteins, Lipids - Neurology Advisor
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Ischemic Stroke, Myocardial Infarction Both Tied to Lipoproteins, Lipids
Neurology Advisor
HealthDay News ā?? Lipoproteins and lipids are similarly associated with risk of myocardial infarction (MI) and ischemic stroke (IS) but not intracerebral hemorrhage (ICH), according to a study published in the Journal of the American College of ...
Ischemic Stroke, Myocardial Infarction Both Tied to...
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[NMR paper] Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain.
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain.
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Angew Chem Int Ed Engl. 2017 Mar 23;:
Authors: Baumann C, Beil A, Jurt S, Niederwanger M, Palacios O, Capdevila M, Atrian S, Dallinger R, Zerbe O
Abstract
In this study, we present an NMR structure of the metallothionein (MT) from the snail...
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03-24-2017 10:14 PM
[NMR paper] Protein-Observed Fluorine NMR is a Complementary Ligand Discovery Method to 1H CPMG Ligand-Observed NMR.
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http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Protein-Observed Fluorine NMR is a Complementary Ligand Discovery Method to 1H CPMG Ligand-Observed NMR.
ACS Chem Biol. 2016 Sep 14;
Authors: Urick AK, Calle Jiménez LP, Espinosa JF, Hu H, Pomerantz WC
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To evaluate its potential as a ligand discovery tool, we compare a newly developed...
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Towards Increased Concentration Sensitivity for Continuous Wave EPR Investigations of Spin-Labeled Biological Macromolecules at High Fields
Towards Increased Concentration Sensitivity for Continuous Wave EPR Investigations of Spin-Labeled Biological Macromolecules at High Fields
Publication date: Available online 15 February 2016
Source:Journal of Magnetic Resonance</br>
Author(s): Likai Song, Zhanglong Liu, Pavanjeet Kaur, Jackie M. Esquiaqui, Robert I. Hunter, Stephen Hill, Graham M. Smith, Gail E. Fanucci</br>
High-field, high-frequency electron paramagnetic resonance (EPR) spectroscopy at W- (~95 GHz) and D-band (~140 GHz) is important for investigating the conformational dynamics...
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Increased resolution of aromatic cross peaks using alternate 13 C labeling and TROSY
Increased resolution of aromatic cross peaks using alternate 13 C labeling and TROSY
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For typical globular proteins, contacts involving aromatic side chains would constitute the largest number of distance constraints that could be used to define the structure of proteins and protein complexes based on NOE contacts. However, the 1H NMR signals of aromatic side chains are often heavily overlapped, which hampers extensive use of aromatic NOE cross peaks. Some of this overlap can be overcome by recording 13C-dispersed NOESY spectra. However, the...
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Systemic and characteristic metabolites in the serum of streptozotocin-induced diabetic rats at different stages as revealed by a (1)H-NMR based metabonomic approach.
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Diabetes mellitus is a typical heterogeneous metabolic disorder characterized by abnormal...
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Increased precision for analysis of proteinā??ligand dissociation constants determined from chemical shift titrations
Increased precision for analysis of proteinā??ligand dissociation constants determined from chemical shift titrations
Abstract NMR is ideally suited for the analysis of proteinā??protein and protein ligand interactions with dissociation constants ranging from ~2 Ī¼M to ~1 mM, and with kinetics in the fast exchange regime on the NMR timescale. For the determination of dissociation constants (K D ) of 1:1 proteinā??protein or proteinā??ligand interactions using NMR, the protein and ligand concentrations must necessarily be similar in magnitude to the K D , and nonlinear least squares...
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[NMR paper] Increased rigidity of eglin c at acidic pH: evidence from NMR spin relaxation and MD
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Biochemistry. 2003 Dec 2;42(47):13856-68
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To gain physical insights into how proteins respond to changes in pH, the picosecond to nanosecond time scale dynamics of the small serine protease inhibitor eglin c have been studied by NMR spin relaxation experiments and MD simulations under two...