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

Mapping the Processivity Determinants of the Kinesin-3 Motor Domain.

Biophysical journal - 20 Oct 2015

Scarabelli Guido, Soppina Virupakshi, Yao Xin-Qiu, Atherton Joseph, Moores Carolyn A, Verhey Kristen J, Grant Barry J

Abstract excerpt

Kinesin superfamily members play important roles in many diverse cellular processes, including cell motility, cell division, intracellular transport, and regulation of the microtubule cytoskeleton. How the properties of the family-defining motor domain of distinct kinesins are tailored to their different cellular roles remains largely unknown. Here, we employed molecular-dynamics simulations coupled with...

Read the complete abstract on PubMed

Topics

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

Share to Kinesins
Share to Microtubules
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis

Share to Mutation

Share to Protein Interaction Domains and Motifs

Share to Tubulin

Source

Open in PubMed Open full text

Identifiers

PMID: 26488644
DOI: 10.1016/j.bpj.2015.08.027
PMCID: PMC4624112

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping the Processivity Determinants of the Kinesin-3 Motor Domain.PMID 26488644Read ↗

Pathogenic KIF1A R350 Variants Disrupt A Conserved Kinesin-Tubulin Salt BridgeSemantic 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 ↗

Pathogenic KIF1A R350 mutations disrupt a conserved and conformation-dependent kinesin-tubulin salt bridge.Semantic proximity Read ↗

Cryo-EM Unveils the Processivity Mechanism of Kinesin KIF1A and the Impact of its Pathogenic Variant P305LSemantic proximity Read ↗

Cryo-EM unveils kinesin KIF1A's processivity mechanism and the impact of its pathogenic variant P305L.Semantic proximity Read ↗

Intrinsically disordered domain of kinesin-3 Kif14 enables unique functional diversitySemantic proximity Read ↗

ATPase kinetic characterization and single molecule behavior of mutant human kinesin motors defective in microtubule-based motility.Semantic proximity Read ↗

Modular aspects of kinesin force generation machinery.Semantic proximity Read ↗

Pathogenic Mutations in the Kinesin-3 Motor KIF1A Diminish Force Generation and Movement Through Allosteric MechanismsSemantic proximity Read ↗

Cryo-EM Reveals the Mechanochemical Cycle of Reactive Full-length Human Dynein-1Semantic proximity Read ↗

Distinct Clinical Phenotypes in KIF1A-Associated Neurological Disorders Result from Different Amino Acid Substitutions at the Same Residue in KIF1ASemantic proximity Read ↗

The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner.Semantic proximity Read ↗

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