Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III - Wikidata - wikimedia - TriplyDB

Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III

Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III

http://www.wikidata.org/entity/Q27678433

about

Molecular simulations reveal that the long range fluctuations of human DPP III change upon ligand binding.Substrate complexes of human dipeptidyl peptidase III reveal the mechanism of enzyme inhibition.Bacterial protease uses distinct thermodynamic signatures for substrate recognition.The Development of Translational Biomarkers as a Tool for Improving the Understanding, Diagnosis and Treatment of Chronic Neuropathic Pain.Transcription factor C/EBP-β mediates downregulation of dipeptidyl-peptidase III expression by interleukin-6 in human glioblastoma cells.Phenylalanine 664 of dipeptidyl peptidase (DPP) 7 and Phenylalanine 671 of DPP11 mediate preference for P2-position hydrophobic residues of a substrate.An optics-based variable-temperature assay system for characterizing thermodynamics of biomolecular reactions on solid support.A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain.Crystal structure of dipeptidyl peptidase III from the human gut symbiont Bacteroides thetaiotaomicron.A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III.Dipeptidyl peptidase 3, a novel protease from Leishmania braziliensis.Protein conformational flexibility modulates kinetics and thermodynamics of drug binding.Dynamic properties of dipeptidyl peptidase III from Bacteroides thetaiotaomicron and the structural basis for its substrate specificity - a computational study.Trimethylphosphate and Dimethylphosphate Hydrolysis by Binuclear CdII , MnII , and ZnII -FeII Promiscuous Organophosphate-Degrading Enzyme: Reaction Mechanisms.Validation of flavonoids as potential dipeptidyl peptidase III inhibitors: Experimental and computational approach.The effect of 17β-estradiol on the expression of dipeptidyl peptidase III and heme oxygenase 1 in liver of CBA/H mice.The first dipeptidyl peptidase III from a thermophile: Structural basis for thermal stability and reduced activity.Concerted nitrogen inversion and hydrogen bonding to Glu451 are responsible for protein-controlled suppression of the reverse reaction in human DPP III.

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P2860

Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III

http://www.wikidata.org/entity/Q27678433

description

2012 nî lūn-bûn

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2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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PNAS.1118005109

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Proceedings of the National Academy of Sciences of the United States of America

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Entropy-driven binding of opio ...... human dipeptidyl peptidase III

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Aiping Dong

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Alexandra Binter

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Elena Dobrovetsky

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Gustavo A Bezerra

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Marija Abramic

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Roland Viertlmayr

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P2860

Initial characterization of the human central proteome

The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme

The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding

Induced-fit mechanism for prolyl endopeptidase.

Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase

A mutant T4 lysozyme displays five different crystal conformations

Protein secondary structure prediction based on position-specific scoring matrices

Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences

Dipeptidyl peptidase III from human erythrocytes

Enkephalinase inhibitors: potential agents for the management of pain

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6525-30

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scholarly article

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10.1073/PNAS.1118005109

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17

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109

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Sirano Dhe-Paganon

Peter Macheroux

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2012-04-24T00:00:00Z

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