Cargando…

Modulation of Kinesin’s Load-Bearing Capacity by Force Geometry and the Microtubule Track

Mostrar otras versiones (1)

Detalles Bibliográficos
Autores principales:	Pyrpassopoulos, Serapion, Shuman, Henry, Ostap, E. Michael
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	The Biophysical Society 2022
Materias:	Correction
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9748335/ https://www.ncbi.nlm.nih.gov/pubmed/36455557 http://dx.doi.org/10.1016/j.bpj.2022.11.2939

Ejemplares similares

Modulation of Kinesin’s Load-Bearing Capacity by Force Geometry and the Microtubule Track
por: Pyrpassopoulos, Serapion, et al.
Publicado: (2020)

Adhesion force and attachment lifetime of the KIF16B-PX domain interaction with lipid membranes
por: Pyrpassopoulos, Serapion, et al.
Publicado: (2017)

Force Generation by Membrane-Associated Myosin-I
por: Pyrpassopoulos, Serapion, et al.
Publicado: (2016)

Endocytic myosin-1 is a force-insensitive, power-generating motor
por: Pedersen, Ross TA, et al.
Publicado: (2023)

KIF1A is kinetically tuned to be a superengaging motor under hindering loads
por: Pyrpassopoulos, Serapion, et al.
Publicado: (2023)

Endocytic myosin-1 is a force-insensitive, power-generating motor
por: Pedersen, Ross T.A., et al.
Publicado: (2023)

Microtubule dynamics influence the retrograde biased motility of kinesin-4 motor teams in neuronal dendrites
por: Masucci, Erin M., et al.
Publicado: (2022)

Anchoring geometry is a significant factor in determining the direction of kinesin-14 motility on microtubules
por: Yamagishi, Masahiko, et al.
Publicado: (2022)

Structure of Microtubule-Trapped Human Kinesin-5 and Its Mechanism of Inhibition Revealed Using Cryoelectron Microscopy
por: Peña, Alejandro, et al.
Publicado: (2021)

Author Correction: Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
por: Benoit, Matthieu P. M. H., et al.
Publicado: (2018)

Kinesin-binding protein remodels the kinesin motor to prevent microtubule binding
por: Solon, April L., et al.
Publicado: (2021)

Force- and kinesin-8-dependent effects in the spatial regulation of fission yeast microtubule dynamics
por: Tischer, Christian, et al.
Publicado: (2009)

Expression Levels of a Kinesin-13 Microtubule Depolymerase Modulates the Effectiveness of Anti-Microtubule Agents
por: Schimizzi, Gregory V., et al.
Publicado: (2010)

Microtubule organization by the antagonistic mitotic motors kinesin-5 and kinesin-14
por: Hentrich, Christian, et al.
Publicado: (2010)

Rapid Movements of Vimentin on Microtubule Tracks: Kinesin-dependent Assembly of Intermediate Filament Networks
por: Prahlad, Veena, et al.
Publicado: (1998)

Single Molecule Imaging Reveals Differences in Microtubule Track Selection Between Kinesin Motors
por: Cai, Dawen, et al.
Publicado: (2009)

Activation of mitotic kinesin by microtubule bundling
por: Tomishige, Michio
Publicado: (2008)

Kinesin follows the microtubule's protofilament axis
Publicado: (1993)

Electrostatically Biased Binding of Kinesin to Microtubules
por: Grant, Barry J., et al.
Publicado: (2011)

Kinesin-5 is a microtubule polymerase
por: Chen, Yalei, et al.
Publicado: (2015)

High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation
por: Shang, Zhiguo, et al.
Publicado: (2014)

Conserved mechanisms of microtubule-stimulated ADP release, ATP binding, and force generation in transport kinesins
por: Atherton, Joseph, et al.
Publicado: (2014)

Diffusive tail anchorage determines velocity and force produced by kinesin-14 between crosslinked microtubules
por: Lüdecke, Annemarie, et al.
Publicado: (2018)

Inhibition of kinesin-driven microtubule motility by monoclonal antibodies to kinesin heavy chains
Publicado: (1988)

Author Correction: Formation of helical membrane tubes around microtubules by single-headed kinesin KIF1A
por: Oriola, David, et al.
Publicado: (2019)

Modulation of substrate adhesion dynamics via microtubule targeting requires kinesin-1
por: Krylyshkina, Olga, et al.
Publicado: (2002)

Microtubule-associated septin complexes modulate kinesin and dynein motility with differential specificities
por: Suber, Yani, et al.
Publicado: (2023)

Kinesin-13s form rings around microtubules
por: Tan, Dongyan, et al.
Publicado: (2006)

Kinesin expands and stabilises the GDP-microtubule lattice
por: Peet, Daniel R., et al.
Publicado: (2018)

Parts list for a microtubule depolymerising kinesin
por: Friel, Claire T., et al.
Publicado: (2018)

An allosteric propofol-binding site in kinesin disrupts kinesin-mediated processive movement on microtubules
por: Woll, Kellie A., et al.
Publicado: (2018)

Different motilities of microtubules driven by kinesin-1 and kinesin-14 motors patterned on nanopillars
por: Kaneko, Taikopaul, et al.
Publicado: (2020)

Kinesin-14 motors participate in a force balance at microtubule plus-ends to regulate dynamic instability
por: Ogren, Allison, et al.
Publicado: (2022)

Correction: Involvement of C-terminal truncation mutation of kinesin-5 in resistance to kinesin-5 inhibitor
por: Saeki, Eri, et al.
Publicado: (2019)

A microtubule polymerase cooperates with the kinesin-6 motor and a microtubule cross-linker to promote bipolar spindle assembly in the absence of kinesin-5 and kinesin-14 in fission yeast
por: Yukawa, Masashi, et al.
Publicado: (2017)

Changes in microtubule overlap length regulate kinesin-14-driven microtubule sliding
por: Braun, Marcus, et al.
Publicado: (2017)

The motor domain of the kinesin Kip2 promotes microtubule polymerization at microtubule tips
por: Chen, Xiuzhen, et al.
Publicado: (2023)

Kinesin-5, a mitotic microtubule-associated motor protein, modulates neuronal migration
por: Falnikar, Aditi, et al.
Publicado: (2011)

A kinesin-13 mutant catalytically depolymerizes microtubules in ADP
por: Wagenbach, Michael, et al.
Publicado: (2008)

How Essential Kinesin-5 Becomes Non-Essential in Fission Yeast: Force Balance and Microtubule Dynamics Matter
por: Yukawa, Masashi, et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_bp0aqmft4k9md821rkfdl9or1n