Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

[Simulation of Mutant P32T Homo- and Heterodimers of Human Inosine Triphosphate Pyrophosphatase hITPA].

Biofizika - 1 Jan 2000

Dushanov E B, Kholmurodov Kh T, Koltovaya N A

Abstract excerpt

The structure of three forms of a dimeric enzyme, human inosine triphosphate pyrophosphatase, is considered to identify the enzyme conformation changes causing the inactivation effect of a P32T mutation. Analysis of a nanosecond molecular dynamics is performed; the mean square deviations of the atoms between the wild-type and mutant homodimers, and also the heterodimer are calculated. A 3 ns modeling shows a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acids
Share to Molecular Dynamics Simulation
Share to Protein Multimerization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Structure, Secondary

Share to Protein Structure, Tertiary

Share to Pyrophosphatases

Share to Static Electricity

Share to Thermodynamics

Source

Identifiers

PMID: 26394463

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

[Simulation of Mutant P32T Homo- and Heterodimers of Human Inosine Triphosphate Pyrophosphatase hITPA].PMID 26394463Read ↗

Structural dynamics of inosine triphosphate pyrophosphatase (ITPA) protein and two clinically relevant mutants: molecular dynamics simulations.Semantic proximity Read ↗

The human ITPA polymorphic variant P32T is destabilized by the unpacking of the hydrophobic core.Semantic proximity Read ↗

Conformational Dynamics of Mitochondrial Inorganic Pyrophosphatase hPPA2 and Its Changes Caused by Pathogenic MutationsSemantic proximity Read ↗

Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T.Semantic proximity Read ↗

[COMPUTATIONAL MODELING OF MOLECULAR DYNAMICS OF G41R MUTANT FORM OF HUMAN TYROSYL-tRNA SYNTHETASE, ASSOSIATED WITH CHARCOT-MARIE-TOOTH NEUROPATHY].Semantic proximity Read ↗

Investigating effect of mutation on structure and function of G6PD enzyme: a comparative molecular dynamics simulation study.Semantic proximity Read ↗

Analysis of the Structure-Function-Dynamics Relationships of GALT Enzyme and of Its Pathogenic Mutant p.Q188R: A Molecular Dynamics Simulation Study in Different Experimental Conditions.Semantic proximity Read ↗

Insights on the structural perturbations in human MTHFR Ala222Val mutant by protein modeling and molecular dynamics.Semantic proximity Read ↗

[Simulation of kinase CDK2-cyclin A by the molecular dynamics method: effect of Gly16-->Ser16 and Arg274-->Gln274 substitutions on conformation of a kinase subunit].Semantic proximity Read ↗

Molecular dynamics study of the recognition of ATP by nucleic acid aptamers.Semantic proximity Read ↗

Understanding the non-catalytic behavior of human butyrylcholinesterase silent variants: Comparison of wild-type enzyme, catalytically active Ala328Cys mutant, and silent Ala328Asp variant.Semantic proximity Read ↗

Use of long term molecular dynamics simulation in predicting cancer associated SNPs.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.