Related ArticlesA Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.
J Med Chem. 2013 Jan 30;
Authors: Dal Piaz F, Vassallo A, Temraz A, Cotugno R, Belisario MA, Bifulco G, Chini MG, Pisano C, De Tommasi N, Braca A
Abstract
The potential of Heat Shock Protein 90 (Hsp90) as a therapeutic target for numerous diseases has made the identification and optimization of novel Hsp90 inhibitors an emerging therapeutic strategy. A Surface Plasmon Resonance (SPR) approach was adopted to screen some iridoids for their Hsp90 ? binding capability. Twenty-four iridoid derivatives, including 13 new natural compounds, were isolated from the leaves of Tabebuia argentea and petioles of Catalpa bignonioides. Their structures were elucidated by NMR, ESIMS and chemical methods. By means of a panel of chemical and biological approaches, four iridoids were demonstrated to bind Hsp90 ?. In particular, the dimeric iridoid argenteoside A was shown to efficiently inhibit the chaperone in biochemical and cellular assays. Our results disclose C9-type iridoids as a novel class of Hsp90 inhibitors.
PMID: 23362862 [PubMed - as supplied by publisher]
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Probing Dynamic Conformationsof the High-Molecular-Weight?B-Crystallin Heat Shock Protein Ensemble by NMR Spectroscopy
Andrew J. Baldwin, Patrick Walsh, D. Flemming Hansen, Gillian R. Hilton, Justin L. P. Benesch, Simon Sharpe and Lewis E. Kay
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja307874r/aop/images/medium/ja-2012-07874r_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja307874r
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qcs9RnHBiBY
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1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
1H NMR-based metabolic profiling reveals inherent biological variation in yeast and nematode model systems
Abstract The application of metabolomics to human and animal model systems is poised to provide great insight into our understanding of disease etiology and the metabolic changes that are associated with these conditions. However, metabolomic studies have also revealed that there is significant, inherent biological variation in human samples and even in samples from animal model systems where the animals are housed under carefully controlled conditions. This inherent biological...
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03-03-2011 02:06 AM
[NMR paper] NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding
NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
Related Articles NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.
Chembiochem. 2003 Sep 5;4(9):870-7
Authors: Dehner A, Furrer J, Richter K, Schuster I, Buchner J, Kessler H
Hsp90 is one of the most abundant chaperone proteins in the cytosol. In an ATP-dependent manner it plays an essential role in the folding and activation of a...
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[NMR paper] Interaction of a type II myosin with biological membranes studied by 2H solid state N
Interaction of a type II myosin with biological membranes studied by 2H solid state NMR.
Related Articles Interaction of a type II myosin with biological membranes studied by 2H solid state NMR.
Biochemistry. 1998 Apr 21;37(16):5582-8
Authors: Arêas JA, Gröbner G, Glaubitz C, Watts A
Deuterium nuclear magnetic resonance spectroscopy (2H NMR) has been employed to investigate the interaction of lung type II myosin protein with neutral bilayers containing dimyristoylphosphatidylcholine (DMPC) as the only constituent and mixed bilayers containing...
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NMR-based metabonomic investigation of heat stress in myotubes reveals a time-depende
NMR-based metabonomic investigation of heat stress in myotubes reveals a time-dependent change in the metabolites.
Related Articles NMR-based metabonomic investigation of heat stress in myotubes reveals a time-dependent change in the metabolites.
J Agric Food Chem. 2010 May 26;58(10):6376-86
Authors: Straadt IK, Young JF, Bross P, Gregersen N, Oksbjerg N, Theil PK, Bertram HC
NMR-based metabonomics was applied to elucidate the time-dependent stress responses in mouse myotubes after heat exposure of either 42 or 45 degrees C for 1 h. Principal...
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[NMR paper] Yeast heat shock transcription factor N-terminal activation domains are unstructured
Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy.
Protein Sci. 1996 Feb;5(2):262-9...
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[NMR paper] NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
Related Articles NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
Biochemistry. 1995 Jul 11;34(27):8631-41
Authors: Zhang J, Peng X, Jonas A, Jonas J
The reversible cold, heat, and pressure unfolding of RNase A and RNase A--inhibitor complex were studied by 1D and 2D 1H NMR spectroscopy. The reversible pressure denaturation experiments in the pressure range from 1 bar to 5 kbar were carried out at pH 2.0 and 10 degrees C. The cold denaturation was...
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[NMR paper] 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation
13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
Related Articles 13C-NMR studies of membrane lipid-protein interactions upon protein heat denaturation.
J Biochem Biophys Methods. 1991 Oct-Nov;23(3):259-61
Authors: YashRoy RC
Spinach chloroplast membranes were studied by natural abundance carbon-13 nuclear magnetic resonance (13C-NMR) spectroscopy in their normal state and after heat denaturation of membrane proteins. The membrane proteins were denatured by raising the temperature of the sample to 67...