Related ArticlesDifferentiation of the P-gp and MRP1 multidrug resistance systems by mobile lipid 1H-NMR spectroscopy and phosphatidylserine externalization.
Anticancer Res. 2001 Nov-Dec;21(6A):3915-9
Authors: Mannechez A, Collet B, Payen L, Lecureur V, Fardel O, Le Moyec L, de Certaines JD, Leray G
We have previously demonstrated that proton NMR spectra of fatty acid chains in erythroleukemia K562 wild-type cells and their MDR1 counterparts show variations related to the phenotype over-expressing the P-glycoprotein (P-gp). Human lung cancer cells whose multidrug resistance (MDR) counterparts over-express the multidrug resistance-associated protein MRP1 have not yet been studied by NMR. Both P-gp and MRP1 belong to the same ATP-binding cassette transporter superfamily. A comparison of NMR spectra from both these multidrug-resistance phenotypes showed that the results previously obtained on the MDR1 family are not valid for MRP1. Furthermore, flow cytofluorimetry studies with external phosphatidylserine labelling showed that P-gp and MRP1 overexpressions have strong but differentiated effects on cell lipid pools.
NMR spectroscopy of 14-3-3? reveals a flexible C-terminal extension. Differentiation of the chaperone and phosphoserine binding activities of 14-3-3?
NMR spectroscopy of 14-3-3? reveals a flexible C-terminal extension. Differentiation of the chaperone and phosphoserine binding activities of 14-3-3?
NMR spectroscopy of 14-3-3? reveals a flexible C-terminal extension. Differentiation of the chaperone and phosphoserine binding activities of 14-3-3?
Biochem J. 2011 May 10;
Authors: Williams DM, Ecroyd H, Goodwin KL, Dai H, Fu H, Woodcock JM, Zhang L, Carver JA
Intracellular 14-3-3 proteins bind to many proteins, via a specific phosphoserine motif, regulating diverse cellular tasks including cell...
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05-12-2011 03:40 PM
A NMR-based metabolomic approach for differentiation of hagfish dental and somatic skeletal muscles.
A NMR-based metabolomic approach for differentiation of hagfish dental and somatic skeletal muscles.
A NMR-based metabolomic approach for differentiation of hagfish dental and somatic skeletal muscles.
Fish Physiol Biochem. 2011 Feb 15;
Authors: Chiu KH, Ding S, Chen YW, Lee CH, Mok HK
The hagfish dental muscle is a large and specialized element of the feeding apparatus that helps ingest food. This muscle has enzymatic activities and contractile properties different from the hagfish somatic skeletal muscle. To verify the functional relevance of...
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02-18-2011 08:07 PM
(1)H-NMR-based metabolomic study on resistance to diet-induced obesity in AHNAK knock
(1)H-NMR-based metabolomic study on resistance to diet-induced obesity in AHNAK knock-out mice.
(1)H-NMR-based metabolomic study on resistance to diet-induced obesity in AHNAK knock-out mice.
Biochem Biophys Res Commun. 2010 Nov 18;
Authors: Kim IY, Jung J, Jang M, Ahn YG, Shin JH, Choi JW, Sohn MR, Shin SM, Kang DG, Lee HS, Bae YS, Ryu DH, Seong JK, Hwang GS
AHNAK is a giant protein of approximately 700 kD identified in human neuroblastomas and skin epithelial cells. Recently, we found that AHNAK knock-out (AHNAK(-/-)) mice have a strong...
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11-26-2010 05:32 PM
[NMR paper] Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cel
Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
Related Articles Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
Cancer Cell Int. 2005 Feb 9;5(1):2
Authors: Mannechez A, Reungpatthanaphong P, de Certaines JD, Leray G, Le Moyec L
BACKGROUND: Most cancer cells are characterized by mobile lipids visible on proton NMR (1H-NMR), these being comprised mainly of methyl and methylene signals from lipid acyl chains....
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11-24-2010 11:14 PM
[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...
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[NMR paper] Functionally significant mobile regions of Escherichia coli SecA ATPase identified by
Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR.
Related Articles Functionally significant mobile regions of Escherichia coli SecA ATPase identified by NMR.
J Biol Chem. 2002 Dec 27;277(52):50985-90
Authors: Chou YT, Swain JF, Gierasch LM
SecA, a 204-kDa homodimeric protein, is a major component of the cellular machinery that mediates the translocation of proteins across the Escherichia coli plasma membrane. SecA promotes translocation by nucleotide-modulated insertion and deinsertion into the...
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11-24-2010 08:58 PM
[NMR paper] Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid
Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Related Articles Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy.
Biochemistry. 1990 Apr 24;29(16):3828-34
Authors: Van Gorkom LC, Horváth LI, Hemminga MA, Sternberg B, Watts A
The major coat protein of M13 bacteriophage has been incorporated into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine, deuterated in the trimethyl segments of...
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08-21-2010 10:48 PM
[NMR paper] The mobile loop region of the NAD(H) binding component (dI) of proton-translocating n
The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
Biochim Biophys Acta. 1999...
Differentiation of the P-gp and MRP1 multidrug resistance systems by mobile lipid 1H-
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