BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
Quality Control Check
NMR spectrum prediction:
FANDAS
MestReS
V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
Gromacs
Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
Shifty
Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 02-03-2013, 10:19 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.

A Chemical-biological Study Reveals C9-type Iridoids as Novel Heat Shock Protein 90 (Hsp90) inhibitors.

Related Articles A 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]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
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
nmrlearner Journal club 0 09-08-2012 08:44 AM
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...
nmrlearner Journal club 0 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...
nmrlearner Journal club 0 11-24-2010 09:16 PM
[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...
nmrlearner Journal club 0 11-17-2010 11:06 PM
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...
nmrlearner Journal club 0 10-19-2010 04:51 PM
[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...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[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...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[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...
nmrlearner Journal club 0 08-21-2010 11:12 PM



Posting Rules
You may not post new threads
You may not post replies
You may not post attachments
You may not edit your posts

BB code is On
Smilies are On
[IMG] code is On
HTML code is On
Trackbacks are Off
Pingbacks are Off
Refbacks are Off



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 08:30 AM.


Map