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 08-21-2010, 11:16 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,779
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 Study on the erythrocytes from myotonic dystrophy with multi-nuclear NMR.

Study on the erythrocytes from myotonic dystrophy with multi-nuclear NMR.

Related Articles Study on the erythrocytes from myotonic dystrophy with multi-nuclear NMR.

Muscle Nerve. 1991 Jan;14(1):57-63

Authors: Kuwabara T, Yuasa T, Ohno T, Yamamuro M, Miyatake T

We have studied the water permeability through membranes, the function of the Na pump, and glucose metabolism of erythrocytes of patients with myotonic muscular dystrophy (MyD) using 1H--, 23Na, and 13C-NMR techniques. A significant decrease in water permeability was recognized in the MyD erythrocyte membrane, and impaired Na pumping was suspected to be correlated with the former biochemical abnormalities in band III protein of MyD erythrocyte membrane. Significant acceleration of glycolysis in the erythrocyte for the first 160 minutes was also recognized in MyD; however, the production of lactate showed no difference between MyD and controls. The increased glucose uptake in MyD may be compensatory to the diminished pumping mechanism, but further information, such as inorganic phosphate permeability and the activity of the rate-limiting enzyme of erythrocyte glycolysis, is needed.

PMID: 1992297 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Role of aminotransferases in glutamate metabolism of human erythrocytes
Role of aminotransferases in glutamate metabolism of human erythrocytes Abstract Human erythrocytes require a continual supply of glutamate to support glutathione synthesis, but are unable to transport this amino acid across their cell membrane. Consequently, erythrocytes rely on de novo glutamate biosynthesis from α-ketoglutarate and glutamine to maintain intracellular levels of glutamate. Erythrocytic glutamate biosynthesis is catalyzed by three enzymes, alanine aminotransferase (ALT), aspartate aminotransferase (AST), and glutamine aminohydrolase (GA). Although the presence of these...
nmrlearner Journal club 0 03-09-2011 04:19 AM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1 http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101896j/aop/images/medium/bi-2010-01896j_0004.gif Biochemistry DOI: 10.1021/bi101896j http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/OhiVTgV2ZTI More...
nmrlearner Journal club 0 01-14-2011 01:59 AM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1. NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1. Biochemistry. 2011 Jan 4; Authors: Parkesh R, Disney MD, Fountain M The NMR structure of an RNA with a copy of the 5'CUG/3'GUC motif found in the triplet repeating disorder myotonic dystrophy type 1 (DM1) is disclosed. The lowest energy conformation of the UU pair is a single...
nmrlearner Journal club 0 01-06-2011 11:21 AM
[NMR paper] Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.
Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study. Related Articles Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study. Anal Bioanal Chem. 2004 Aug;379(7-8):1045-9 Authors: Nissler L, Gebhardt R, Berger S Flavonoids are well known to inhibit the function of the multi-drug-resistance (mdr) transporter by interacting with their ATP binding domains. The precise orientation of these molecules inside the ATP binding pocket is still unclear. We applied the saturation transfer...
nmrlearner Journal club 0 11-24-2010 09:51 PM
[NMR paper] Fast multi-dimensional NMR of proteins.
Fast multi-dimensional NMR of proteins. Related Articles Fast multi-dimensional NMR of proteins. J Biomol NMR. 2003 Apr;25(4):349-54 Authors: Kupce E, Freeman R Three-dimensional HNCO and HNCA subspectra from a small protein (agitoxin, 4 kDa, enriched in carbon-13 and nitrogen-15), have been obtained by direct frequency-domain excitation of selected carbon and nitrogen sites. This new technique applies an array of several simultaneous soft radiofrequency spin-inversion pulses, encoded (on or off) according to nested Hadamard matrices, and the...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] 7Li NMR relaxation study of Li+ binding in human erythrocytes.
7Li NMR relaxation study of Li+ binding in human erythrocytes. Related Articles 7Li NMR relaxation study of Li+ binding in human erythrocytes. Biochemistry. 1993 Dec 14;32(49):13490-8 Authors: Rong Q, Espanol M, Mota de Freitas D, Geraldes CF We used 7Li NMR spin-lattice (T1) and spin-spin (T2) relaxation time measurements to investigate the binding of Li+ in human red blood cell (RBC) suspensions. In RBCs containing 1.4 mM Li+, the intracellular 7Li NMR T2 relaxation value (0.30 +/- 0.03 s) was much smaller than the corresponding T1 value...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Hypophosphite transport in human erythrocytes studied by overdetermined one-dimension
Hypophosphite transport in human erythrocytes studied by overdetermined one-dimensional NMR exchange analysis. Related Articles Hypophosphite transport in human erythrocytes studied by overdetermined one-dimensional NMR exchange analysis. NMR Biomed. 1990 Apr;3(2):59-63 Authors: Price WS, Kuchel PW The membrane transport kinetics of the disubstituted phosphorus oxyacid, hypophosphite, were studied in human red cells under equilibrium exchange conditions. Hypophosphite is an analogue of both the bicarbonate and phosphate ions and is known to be...
nmrlearner Journal club 0 08-21-2010 10:48 PM
[Stan NMR blog] An inequality for multi-exponential decays
An inequality for multi-exponential decays A simple and universal inequality which should find applications to relaxation phenomena. More...
nmrlearner News from NMR blogs 0 08-21-2010 05:42 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 06:17 PM.


Map