Human–Mouse Chimeras with Normal Expressionand Function Reveal That Major Domain Swapping Is Tolerated by P-Glycoprotein(ABCB1)
Human–Mouse Chimeras with Normal Expressionand Function Reveal That Major Domain Swapping Is Tolerated by P-Glycoprotein(ABCB1)
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01064/20160210/images/medium/bi-2015-01064e_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01064
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/zhYScDUkhL8
More...
nmrlearner
Journal club
0
02-11-2016 10:03 AM
[NMR paper] (19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
(19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
(19) F NMR Spectroscopy as a Probe of Cytoplasmic Viscosity and Weak Protein Interactions in Living Cells.
Chemistry. 2013 Aug 6;
Authors: Ye Y, Liu X, Zhang Z, Wu Q, Jiang B, Jiang L, Zhang X, Liu M, Pielak GJ, Li C
Abstract
Protein mobility in living cells is vital for cell function. Both cytosolic viscosity and weak protein-protein interactions affect mobility, but examining viscosity and weak interaction effects is challenging....
nmrlearner
Journal club
0
08-08-2013 03:46 PM
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
nmrlearner
Journal club
0
06-08-2011 11:30 AM
[NMR paper] NMR structure of the 3' stem-loop from human U4 snRNA.
NMR structure of the 3' stem-loop from human U4 snRNA.
Related Articles NMR structure of the 3' stem-loop from human U4 snRNA.
Nucleic Acids Res. 2002 Oct 15;30(20):4371-9
Authors: Comolli LR, Ulyanov NB, Soto AM, Marky LA, James TL, Gmeiner WH
The NMR structure of the 3' stem-loop (3'SL) from human U4 snRNA was determined to gain insight into the structural basis for conservation of this stem-loop sequence from vertebrates. 3'SL sequences from human, rat, mouse and chicken U4 snRNA each consist of a 7 bp stem capped by a UACG tetraloop. No...
nmrlearner
Journal club
0
11-24-2010 08:58 PM
[NMR paper] Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta
Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.
Related Articles Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies.
Biochemistry. 1999 Nov 16;38(46):15116-28
Authors: Buchko GW, Daughdrill GW, de Lorimier R, Rao B K, Isern NG, Lingbeck JM, Taylor JS, Wold MS, Gochin M, Spicer LD, Lowry DF, Kennedy MA
Human XPA is an essential component in the...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] NMR solution structure of a cytoplasmic surface loop of the human red cell anion tran
NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Related Articles NMR solution structure of a cytoplasmic surface loop of the human red cell anion transporter, band 3.
Biochemistry. 1998 Aug 18;37(33):11670-8
Authors: Askin D, Bloomberg GB, Chambers EJ, Tanner MJ
The membrane domain of the human red cell anion transport protein, band 3, is too large to be studied by solution nuclear magnetic resonance spectroscopy (NMR), and its amphiphilic nature requires the use of detergents for...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a syn
Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).
Related Articles Human nucleotide excision repair protein XPA: 1H NMR and CD solution studies of a synthetic peptide fragment corresponding to the zinc-binding domain (101-141).
J Biomol Struct Dyn. 1997 Jun;14(6):677-90
Authors: Buchko GW, Kennedy MA
A peptide corresponding to residues 101-141 of the human nucleotide excision repair protein XPA was synthesized with an isoleucine...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for
NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Related Articles NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21.
Biochemistry. 1990 Apr 10;29(14):3509-14
Authors: Redfield AG, Papastavros MZ
The structure of the phosphoryl binding region of human N-ras p21 was probed by using heteronuclear proton-observed NMR methods. Normal protein and a Gly-12----Asp-12 mutant protein were prepared...
Drugs Modulate Interactions between the First Nucleotide-BindingDomain and the Fourth Cytoplasmic Loop of Human P-Glycoprotein
Linear Mode
