[NMR paper] NMR spectroscopy of macrophages loaded with native, oxidized or enzymatically degraded lipoproteins.
NMR spectroscopy of macrophages loaded with native, oxidized or enzymatically degraded lipoproteins.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.plosone.org-images-pone_120x30.png http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR spectroscopy of macrophages loaded with native, oxidized or enzymatically degraded lipoproteins.
PLoS One. 2013;8(2):e56360
Authors: Ramm Sander P, Peer M, Grandl M, Bogdahn U, Schmitz G, Kalbitzer...
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08-29-2013 01:53 PM
[NMR paper] NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
Related Articles NMR analysis of a novel enzymatically-active unlinked Dengue NS2B-NS3 protease complex.
J Biol Chem. 2013 Mar 19;
Authors: Kim YM, Gayen S, Kang C, Joy J, Huang Q, Chen AS, Wee JL, Ang MJ, Lim HA, Hung AW, Li R, Noble CG, Lee LT, Yip A, Wang QY, Chia CS, Hill J, Shi PY, Keller TH
Abstract
The dengue virus (DENV) is a mosquito-borne pathogen responsible for an estimated 100 million human infections annually. The viral genome encodes a...
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03-21-2013 02:58 PM
Low-field one-dimensional and direction-dependent relaxation imaging of bovine articular cartilage
Low-field one-dimensional and direction-dependent relaxation imaging of bovine articular cartilage
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 10 September 2011</br>
Erik*Rössler, Carlos*Mattea, Ayret*Mollova, Siegfried*Stapf</br>
The structure of articular cartilage is separated into three layers of differently oriented collagen fibers, which is accompanied by a gradient of increasing glycosaminoglycan (GAG) and decreasing water concentration from the top layer towards the bone interface. The combined effect of these structural variations results in...
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09-12-2011 09:00 PM
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
Protein Analysis by (31)P NMR Spectroscopy in Ionic Liquid: Quantitative Determination of Enzymatically Created Cross-Links.
J Agric Food Chem. 2011 Jan 10;
Authors: Monogioudi E, Permi P, Filpponen I, Lienemann M, Li B, Argyropoulos D, Buchert J, Mattinen ML
Cross-linking of ?-casein by Trichoderma reesei tyrosinase (TrTyr) and Streptoverticillium mobaraense transglutaminase (Tgase) was analyzed by (31)P nuclear magnetic...
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01-12-2011 11:11 AM
[NMR paper] 600 MHz NMR studies of human articular cartilage keratan sulfates.
600 MHz NMR studies of human articular cartilage keratan sulfates.
Related Articles 600 MHz NMR studies of human articular cartilage keratan sulfates.
Eur J Biochem. 1999 Dec;266(3):1174-83
Authors: Huckerby TN, Nieduszynski IA, Bayliss MT, Brown GM
The use of high-field two-dimensional 1H-correlation data is described for the detailed comparison of intact keratan sulfate polymer chains derived from human articular cartilage sources as a function of age. For fetal material the nonreducing chain termini are shown to be sparsely capped by sialyl...
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11-18-2010 08:31 PM
[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
Related Articles NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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08-22-2010 03:33 AM
[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
Related Articles NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...