scholarly article | Q13442814 |
P819 | ADS bibcode | 2014PLoSO...991916O |
P356 | DOI | 10.1371/JOURNAL.PONE.0091916 |
P932 | PMC publication ID | 3954865 |
P698 | PubMed publication ID | 24632881 |
P5875 | ResearchGate publication ID | 260841273 |
P50 | author | Alan Mark | Q21684355 |
Megan L O'Mara | Q40290874 | ||
P2860 | cites work | Substrate versus inhibitor dynamics of P-glycoprotein. | Q50996579 |
Definition and testing of the GROMOS force-field versions 54A7 and 54B7 | Q56225271 | ||
GROMACS 3.0: a package for molecular simulation and trajectory analysis | Q57082068 | ||
An Automated Force Field Topology Builder (ATB) and Repository: Version 1.0 | Q57204661 | ||
Molecular dynamics with coupling to an external bath | Q57569060 | ||
Drug-stimulated ATPase Activity of Human P-glycoprotein Requires Movement between Transmembrane Segments 6 and 12 | Q57976942 | ||
Inhibition of Oxidative Cross-linking between Engineered Cysteine Residues at Positions 332 in Predicted Transmembrane Segments (TM) 6 and 975 in Predicted TM12 of Human P-glycoprotein by Drug Substrates | Q57976949 | ||
Folding-unfolding thermodynamics of a beta-heptapeptide from equilibrium simulations | Q74452346 | ||
Conformational changes induced by ATP-hydrolysis in an ABC transporter: a molecular dynamics study of the Sav1866 exporter | Q83846383 | ||
On the Validation of Molecular Dynamics Simulations of Saturated and cis-Monounsaturated Phosphatidylcholine Lipid Bilayers: A Comparison with Experiment | Q86822781 | ||
H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB | Q24529132 | ||
Modeling large regions in proteins: applications to loops, termini, and folding | Q24598781 | ||
ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer | Q24602726 | ||
ABC transporters: the power to change | Q24634548 | ||
Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding | Q24657908 | ||
Flexibility in the ABC transporter MsbA: Alternating access with a twist | Q24676413 | ||
Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily | Q27625340 | ||
A Tweezers-like Motion of the ATP-Binding Cassette Dimer in an ABC Transport Cycle | Q27642284 | ||
Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP | Q27643828 | ||
Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans | Q27673547 | ||
Kinetics of the Association/Dissociation Cycle of an ATP-binding Cassette Nucleotide-binding Domain | Q27676117 | ||
Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation | Q27678196 | ||
Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states | Q27678363 | ||
Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain | Q27679289 | ||
Refined structures of mouse P-glycoprotein | Q27680445 | ||
VMD: visual molecular dynamics | Q27860554 | ||
ModLoop: automated modeling of loops in protein structures | Q28190686 | ||
Environment and exposure to solvent of protein atoms. Lysozyme and insulin | Q28245387 | ||
Significance of root-mean-square deviation in comparing three-dimensional structures of globular proteins | Q28258813 | ||
Structure of a bacterial multidrug ABC transporter | Q29617308 | ||
Subunit interactions in ABC transporters: towards a functional architecture | Q30175332 | ||
Insights on P-Glycoprotein's Efflux Mechanism Obtained by Molecular Dynamics Simulations. | Q30381678 | ||
Characterization of an asymmetric occluded state of P-glycoprotein with two bound nucleotides: implications for catalysis | Q33748171 | ||
The catalytic cycle of P-glycoprotein | Q34370183 | ||
Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter | Q34377172 | ||
Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs | Q35863914 | ||
Structure of a multidrug transporter | Q36083039 | ||
The translocation mechanism of P-glycoprotein. | Q36354417 | ||
Recent progress in understanding the mechanism of P-glycoprotein-mediated drug efflux. | Q36386127 | ||
Human multidrug resistance ABCB and ABCG transporters: participation in a chemoimmunity defense system | Q36610461 | ||
Computational studies of membrane proteins: models and predictions for biological understanding | Q37952425 | ||
Mechanism of the ABC transporter ATPase domains: catalytic models and the biochemical and biophysical record | Q38058157 | ||
Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by arginine mutagenesis | Q39828462 | ||
Nucleotide binding, ATP hydrolysis, and mutation of the catalytic carboxylates of human P-glycoprotein cause distinct conformational changes in the transmembrane segments | Q40106045 | ||
The Effect of Environment on the Structure of a Membrane Protein: P-Glycoprotein under Physiological Conditions | Q40290755 | ||
Transmembrane segment 1 of human P-glycoprotein contributes to the drug-binding pocket | Q40313463 | ||
ATP hydrolysis promotes interactions between the extracellular ends of transmembrane segments 1 and 11 of human multidrug resistance P-glycoprotein. | Q40393600 | ||
Processing mutations located throughout the human multidrug resistance P-glycoprotein disrupt interactions between the nucleotide binding domains. | Q40537131 | ||
The packing of the transmembrane segments of human multidrug resistance P-glycoprotein is revealed by disulfide cross-linking analysis. | Q40899411 | ||
Proteolytic Cleavage of the Linker Region of the Human P-glycoprotein Modulates Its ATPase Function | Q42051257 | ||
Functional role of the linker region in purified human P-glycoprotein. | Q42454700 | ||
The ATPase and ATP-binding functions of P-glycoprotein--modulation by interaction with defined phospholipids | Q42461420 | ||
Both ATP sites of human P-glycoprotein are essential but not symmetric | Q42479018 | ||
Activation of the human P-glycoprotein ATPase by trypsin | Q42485272 | ||
Reconstitution of drug-stimulated ATPase activity following co-expression of each half of human P-glycoprotein as separate polypeptides | Q42800768 | ||
Human P-glycoprotein is active when the two halves are clamped together in the closed conformation | Q43098331 | ||
Determining the dimensions of the drug-binding domain of human P-glycoprotein using thiol cross-linking compounds as molecular rulers | Q43717027 | ||
P-glycoprotein retains function when reconstituted into a sphingolipid- and cholesterol-rich environment | Q44982216 | ||
P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
P6216 | copyright status | copyrighted | Q50423863 |
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | e91916 | |
P577 | publication date | 2014-03-14 | |
P1433 | published in | PLOS One | Q564954 |
P1476 | title | Structural characterization of two metastable ATP-bound states of P-glycoprotein | |
P478 | volume | 9 |
Q57050158 | Allosteric Role of Substrate Occupancy Toward the Alignment of P-glycoprotein Nucleotide Binding Domains |
Q51404012 | Allosteric effects of ATP binding on the nucleotide-binding domain of a heterodimeric ATP-binding cassette transporter. |
Q53461492 | Dissecting the Forces that Dominate Dimerization of the Nucleotide Binding Domains of ABCB1. |
Q30636997 | Equilibrated atomic models of outward-facing P-glycoprotein and effect of ATP binding on structural dynamics |
Q48269107 | Insights Into the Molecular Mechanism of Triptan Transport by P-glycoprotein. |
Q61450544 | Lipid-Dependent Alternating Access Mechanism of a Bacterial Multidrug ABC Exporter |
Q26777721 | Providing a molecular mechanism for P-glycoprotein; why would I bother? |
Q42576636 | Release of Entropic Spring Reveals Conformational Coupling Mechanism in the ABC Transporter BtuCD-F. |
Q28545890 | The Nucleotide-Free State of the Multidrug Resistance ABC Transporter LmrA: Sulfhydryl Cross-Linking Supports a Constant Contact, Head-to-Tail Configuration of the Nucleotide-Binding Domains |
Q48165185 | The reliability of molecular dynamics simulations of the multidrug transporter P-glycoprotein in a membrane environment. |
Search more.