Solution NMR Insights into Docking Interactions Involving Inactive ERK2.
Solution NMR Insights into Docking Interactions Involving Inactive ERK2.
Solution NMR Insights into Docking Interactions Involving Inactive ERK2.
Biochemistry. 2011 Mar 30;
Authors: Piserchio A, Warthaka M, Devkota AK, Kaoud TS, Lee S, Abramczyk O, Ren P, Dalby KN, Ghose R
The mitogen activated protein (MAP) kinase ERK2 contains recruitment sites that engage canonical and non-canonical motifs found in a variety of upstream kinases, regulating phosphatases and downstream targets. Interactions involving two of these sites, the D-recruitment site...
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[NMR paper] The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into
The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.
Related Articles The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.
J Mol Biol. 2004 Sep 17;342(3):813-32
Authors: Sauvé S, Tremblay L, Lavigne P
Basic region-helix1-loop-helix2-leucine zipper (b/H(1)LH(2)/LZ) transcription factors bind specific DNA sequence...
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11-24-2010 10:01 PM
[NMR paper] Insights into the interactions between a drug and a membrane protein target by fluori
Insights into the interactions between a drug and a membrane protein target by fluorine cross-polarization magic angle spinning NMR.
Related Articles Insights into the interactions between a drug and a membrane protein target by fluorine cross-polarization magic angle spinning NMR.
Magn Reson Chem. 2004 Feb;42(2):204-11
Authors: Boland MP, Middleton DA
The fluorinated anti-psychotic drug trifluoperazine (TFP) has been shown to be a K(+)-competitive inhibitor of gastric H(+)/K(+)-ATPase, a membrane-embedded therapeutic target for peptic ulcer...
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11-24-2010 09:25 PM
[NMR paper] New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Related Articles New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
Curr Opin Struct Biol. 2003 Oct;13(5):646-53
Authors: Kogelberg H, Solís D, Jiménez-Barbero J
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the...
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11-24-2010 09:16 PM
[NMR paper] NMR investigations of protein-carbohydrate interactions: insights into the topology o
NMR investigations of protein-carbohydrate interactions: insights into the topology of the bound conformation of a lactose isomer and beta-galactosyl xyloses to mistletoe lectin and galectin-1.
Related Articles NMR investigations of protein-carbohydrate interactions: insights into the topology of the bound conformation of a lactose isomer and beta-galactosyl xyloses to mistletoe lectin and galectin-1.
Biochim Biophys Acta. 2001 Dec 19;1568(3):225-36
Authors: Alonso-Plaza JM, Canales MA, Jiménez M, Roldán JL, García-Herrero A, Iturrino L, Asensio JL,...
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11-19-2010 08:44 PM
[NMR paper] Insights into the mechanism of heterodimerization from the 1H-NMR solution structure
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
Related Articles Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.
J Mol Biol. 1998 Aug 7;281(1):165-81
Authors: Lavigne P, Crump MP, Gagné SM, Hodges RS, Kay CM, Sykes BD
The oncoprotein c-Myc (a member of the helix-loop-helix-leucine zipper (b-HLH-LZ) family of transcription factors) must heterodimerize with the b-HLH-LZ Max...
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11-17-2010 11:15 PM
[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c
NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins.
Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209
Authors: Carver JA, Lindner RA
The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...