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

Theoretical Investigations of the Role of Mutations in Dynamics of Kinesin Motor Proteins.

The journal of physical chemistry. B - 3 May 2018

Misiura Mikita, Wang Qian, Cheung Margaret S, Kolomeisky Anatoly B

Abstract excerpt

Motor proteins are active enzymatic molecules that are critically important for a variety of biological phenomena. It is known that some neurodegenerative diseases are caused by specific mutations in motor proteins that lead to their malfunctioning. Hereditary spastic paraplegia is one of such diseases, and it is associated with the mutations in the neuronal conventional kinesin gene, producing the decreased...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Binding Sites
Share to Kinesins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Molecular Dynamics Simulation

Share to Mutation

Share to Protein Conformation

Source

Identifiers

PMID: 29630822
DOI: 10.1021/acs.jpcb.8b00830

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Theoretical Investigations of the Role of Mutations in Dynamics of Kinesin Motor Proteins.PMID 29630822Read ↗

Road-blocker HSP disease mutation disrupts pre-organization for ATP hydrolysis in kinesin through a second sphere control.Semantic proximity Read ↗

Interaction between motor domains can explain the complex dynamics of heterodimeric kinesins.Semantic proximity Read ↗

Kinetic effects of kinesin switch I and switch II mutations.Semantic proximity Read ↗

Model for kinetics of wild-type and mutant kinesins.Semantic proximity Read ↗

A highly conserved 310 helix within the kinesin motor domain is critical for kinesin function and human health.Semantic proximity Read ↗

Identifying and elucidating the roles of Y198N and Y204F mutations in the PAH enzyme through molecular dynamic simulations.Semantic proximity Read ↗

Allostery Wiring Map for Kinesin Energy Transduction and Its Evolution.Semantic proximity Read ↗

Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.Semantic proximity Read ↗

Structural Dynamics and Catalytic Mechanism of ATP13A2 (PARK9) from SimulationsSemantic proximity Read ↗

A Highly Conserved 3 <sub>10</sub> -Helix Within the Kinesin Motor Domain is Critical for Kinesin Function and Human HealthSemantic proximity Read ↗

The structural switch of nucleotide-free kinesin.Semantic proximity Read ↗

Intracellular force comparison of pathogenic KIF1A, KIF5, and dynein by fluctuation analysisSemantic proximity Read ↗

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