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ndc80 (Dr. Bill Wasserman's take on microtuble shortening and "Chromosomal Mechanics" in anaphase
Another of Bill's pioneer 3d animations.
published: 13 Oct 2024
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Detecting Sumoylation & Ubiquitination (Ndc10 & Ndc80) (Purification Technique)
Watch the Full Video at https://www.jove.com/v/52482/protein-purification-technique-that-allows-detection-sumoylation?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022.
Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80 - a 2 minute Preview of the Experimental Protocol
Kentaro Ohkuni, Yoshimitsu Takahashi, Munira A. Basrai
National Cancer Institute, National Institute of Health, Genetics Branch, Center for Cancer Research;
This manuscript describes the detection of sumoylation and ubiquitination of kinetochore proteins, Ndc10 and Ndc80, in the budding yeast Saccharomyces cerevisiae.
Visit https://www.jove.com?utm_source=youtube&utm_medium=social_global&utm_campaign=rese...
published: 26 May 2022
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Kinetochore | Structure and Function
It is a disc-shaped protein structure associated with duplicated chromatids in eukaryotic cells where the spindle fibers attach during cell division to pull sister chromatids apart. The kinetochore assembles on the centromere and links the chromosome to microtubule polymers from the mitotic spindle during mitosis and meiosis. Its proteins also help to hold the sister chromatids together and play a role in chromosome editing.
Kinetochores start, control, and supervise the striking movements of chromosomes during cell division. During mitosis, which occurs after chromosomes are duplicated in S phase, two sister chromatids are held together by a centromere. Each chromatid has its own kinetochore, which face in opposite directions and attach to opposite poles of the mitotic spindle apparatu...
published: 12 Apr 2021
-
Mechanisms for chromosome movement
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At mitotic metaphase, the fully-formed spindle is composed of many microtubules that extend from the poles.
Some of these, the kinetochore microtubules, are attached to the kinetochores of each chromosome.
Kinetochores are located at the centromeres.
At anaphase, sister chromatids separate and are pulled to opposite poles of the cell.
During this chromosomal movement, the kinetochore microtubules become progressively shorter.
The shortening occurs because the kinetodiore disassembles the microtubule into tubulin protein subunits as...
published: 06 Jan 2022
-
Molecular Biophysics of Mitosis: Single molecule of NDC80 diffuses on microtubule
Molecular Biophysics of Mitosis: Single unphosphorylated NDC80-GFP complexes bind and diffuse along the taxol-stabilized microtubules
Reference:
Zaytsev, A.V., Mick, J.E., Maslennikov, E., Nikashin, B., DeLuca, J.G., Grishchuk, E.L. (2015) Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Mol. Biol. Cell., 26(10):1829-44.
published: 08 Jan 2016
-
Molecular Biophysics of Mitosis: Molecular dynamics simulation of NDC80 with unphosphorylated “tail”
Two NDC80 complexes (blue and yellow) were positioned on a microtubule patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilament is shown in these videos for clarity. Tubulin C-terminal extensions are in red; the initial conformation of the Hec1 tail (in dark blue) is extended.
Reference:
Zaytsev, A.V., Mick, J.E., Maslennikov, E., Nikashin, B., DeLuca, J.G., Grishchuk, E.L. (2015) Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Mol. Biol. Cell., 26(10):1829-44.
published: 08 Jan 2016
-
Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity
Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Anatoly V. Zaytsev et al (2015), Molecular Biology of the Cell http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E14-11-1539
Microtubule attachment to kinetochores is vitally important for cell division, but how these interactions are controlled by phosphorylation is not well known. We used quantitative approaches in vitro combined with molecular dynamics simulations to examine phosphoregulation of the NDC80 complex, a core kinetochore component. We show that the outputs from multiple phosphorylation events on the unstructured tail of its Hec1 subunit are additively integrated to elicit gradual tuning of NDC80-microtubule binding both in vitro and in silico. Conformational plasticity of the Hec1 ...
published: 25 Mar 2015
-
MD simulation of the NDC80-MT interface with unphosphorylated Hec1 tail
MD simulation of the NDC80-MT interface with unphosphorylated Hec1 tail.Two NDC80 complexes (blue and yellow) were positioned on a MT patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilament is shown in these videos for clarity. Tubulin C-terminal extensions are in red; the initial conformation of the Hec1 tail (in dark blue) is extended.
published: 13 Oct 2015
-
Gene Music using Protein Sequence of NDC80 "NDC80 KINETOCHORE COMPLEX COMPONENT"
Shop NDC80 - https://www.redbubble.com/people/genemusic/works/51706688-ndc80?asc=u
Subscribe - https://www.youtube.com/c/GeneMusicStudio?sub_confirmation=1
Gene Music Studio - A channel to taste (visually & musically) gene information (particularly protein sequences)
Gene Music using Protein Sequence of NDC80 'NDC80 KINETOCHORE COMPLEX COMPONENT'
published: 10 Dec 2016
-
Molecular Biophysics of Mitosis: Microtubule binding to the molecular lawn of Ndc80 at kinetochore.
Stochastic model of kinetochore-microtubule interface composed of the molecular lawn with phosphorylation-controlled microtubule binding by the Ndc80 complexes.
Reference:
Zaytsev, A.V., Sundin, L.J.R., DeLuca, K.F., Grishchuk, E.L. and J.D. DeLuca (2014) Accurate phosphoregulation of kinetochore-microtubule affinity requires unconstrained molecular interactions. J. Cell Biol., 206(1):45-59.
published: 31 Jan 2015
2:01
Detecting Sumoylation & Ubiquitination (Ndc10 & Ndc80) (Purification Technique)
Watch the Full Video at https://www.jove.com/v/52482/protein-purification-technique-that-allows-detection-sumoylation?utm_source=youtube&utm_medium=social_globa...
Watch the Full Video at https://www.jove.com/v/52482/protein-purification-technique-that-allows-detection-sumoylation?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022.
Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80 - a 2 minute Preview of the Experimental Protocol
Kentaro Ohkuni, Yoshimitsu Takahashi, Munira A. Basrai
National Cancer Institute, National Institute of Health, Genetics Branch, Center for Cancer Research;
This manuscript describes the detection of sumoylation and ubiquitination of kinetochore proteins, Ndc10 and Ndc80, in the budding yeast Saccharomyces cerevisiae.
Visit https://www.jove.com?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022 to explore our entire library of 14,000+ videos of laboratory methods and science concepts.
JoVE is the world-leading producer and provider of science videos with the mission to improve scientific research and education. Millions of scientists, educators, and students at 1500+ institutions worldwide, including schools like Harvard, MIT and Stanford benefit from using JoVE's extensive library of 14,000+ videos in their research,education and teaching.
Subscribe to our channel: https://www.youtube.com/c/JoVEJournalofVisualizedExperiments
https://wn.com/Detecting_Sumoylation_Ubiquitination_(Ndc10_Ndc80)_(Purification_Technique)
Watch the Full Video at https://www.jove.com/v/52482/protein-purification-technique-that-allows-detection-sumoylation?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022.
Protein Purification Technique that Allows Detection of Sumoylation and Ubiquitination of Budding Yeast Kinetochore Proteins Ndc10 and Ndc80 - a 2 minute Preview of the Experimental Protocol
Kentaro Ohkuni, Yoshimitsu Takahashi, Munira A. Basrai
National Cancer Institute, National Institute of Health, Genetics Branch, Center for Cancer Research;
This manuscript describes the detection of sumoylation and ubiquitination of kinetochore proteins, Ndc10 and Ndc80, in the budding yeast Saccharomyces cerevisiae.
Visit https://www.jove.com?utm_source=youtube&utm_medium=social_global&utm_campaign=reseach-videos-2022 to explore our entire library of 14,000+ videos of laboratory methods and science concepts.
JoVE is the world-leading producer and provider of science videos with the mission to improve scientific research and education. Millions of scientists, educators, and students at 1500+ institutions worldwide, including schools like Harvard, MIT and Stanford benefit from using JoVE's extensive library of 14,000+ videos in their research,education and teaching.
Subscribe to our channel: https://www.youtube.com/c/JoVEJournalofVisualizedExperiments
- published: 26 May 2022
- views: 116
4:07
Kinetochore | Structure and Function
It is a disc-shaped protein structure associated with duplicated chromatids in eukaryotic cells where the spindle fibers attach during cell division to pull sis...
It is a disc-shaped protein structure associated with duplicated chromatids in eukaryotic cells where the spindle fibers attach during cell division to pull sister chromatids apart. The kinetochore assembles on the centromere and links the chromosome to microtubule polymers from the mitotic spindle during mitosis and meiosis. Its proteins also help to hold the sister chromatids together and play a role in chromosome editing.
Kinetochores start, control, and supervise the striking movements of chromosomes during cell division. During mitosis, which occurs after chromosomes are duplicated in S phase, two sister chromatids are held together by a centromere. Each chromatid has its own kinetochore, which face in opposite directions and attach to opposite poles of the mitotic spindle apparatus. Following the transition from metaphase to anaphase, the sister chromatids separate from each other, and the individual kinetochores on each chromatid drive their movement to the spindle poles that will define the two new daughter cells. The kinetochore is therefore essential for the chromosome segregation that is classically associated with mitosis and meiosis.
The kinetochore contains two regions:
an inner kinetochore, which is tightly associated with the centromere DNA and assembled in a specialized form of chromatin that persists throughout the cell cycle;
an outer kinetochore, which interacts with microtubules; the outer kinetochore is a very dynamic structure with many identical components, which are assembled and functional only during cell division.
Even the simplest kinetochores consist of more than 19 different proteins. Many of these proteins are conserved between eukaryotic species, including a specialized histone H3 variant (called CENP-A or CenH3) which helps the kinetochore associate with DNA. Other proteins in the kinetochore adhere it to the microtubules (MTs) of the mitotic spindle. There are also motor proteins, including both dynein and kinesin, which generate forces that move chromosomes during mitosis. Other proteins, such as Mad2, monitor the microtubule attachment as well as the tension between sister kinetochores and activate the spindle checkpoint to arrest the cell cycle when either of these is absent. The actual set of genes essential for kinetochore function varies from one species to another.
https://wn.com/Kinetochore_|_Structure_And_Function
It is a disc-shaped protein structure associated with duplicated chromatids in eukaryotic cells where the spindle fibers attach during cell division to pull sister chromatids apart. The kinetochore assembles on the centromere and links the chromosome to microtubule polymers from the mitotic spindle during mitosis and meiosis. Its proteins also help to hold the sister chromatids together and play a role in chromosome editing.
Kinetochores start, control, and supervise the striking movements of chromosomes during cell division. During mitosis, which occurs after chromosomes are duplicated in S phase, two sister chromatids are held together by a centromere. Each chromatid has its own kinetochore, which face in opposite directions and attach to opposite poles of the mitotic spindle apparatus. Following the transition from metaphase to anaphase, the sister chromatids separate from each other, and the individual kinetochores on each chromatid drive their movement to the spindle poles that will define the two new daughter cells. The kinetochore is therefore essential for the chromosome segregation that is classically associated with mitosis and meiosis.
The kinetochore contains two regions:
an inner kinetochore, which is tightly associated with the centromere DNA and assembled in a specialized form of chromatin that persists throughout the cell cycle;
an outer kinetochore, which interacts with microtubules; the outer kinetochore is a very dynamic structure with many identical components, which are assembled and functional only during cell division.
Even the simplest kinetochores consist of more than 19 different proteins. Many of these proteins are conserved between eukaryotic species, including a specialized histone H3 variant (called CENP-A or CenH3) which helps the kinetochore associate with DNA. Other proteins in the kinetochore adhere it to the microtubules (MTs) of the mitotic spindle. There are also motor proteins, including both dynein and kinesin, which generate forces that move chromosomes during mitosis. Other proteins, such as Mad2, monitor the microtubule attachment as well as the tension between sister kinetochores and activate the spindle checkpoint to arrest the cell cycle when either of these is absent. The actual set of genes essential for kinetochore function varies from one species to another.
- published: 12 Apr 2021
- views: 25473
1:44
Mechanisms for chromosome movement
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At mitotic metaphase, the fully-formed spindle is composed of many microtubules that extend from the poles.
Some of these, the kinetochore microtubules, are attached to the kinetochores of each chromosome.
Kinetochores are located at the centromeres.
At anaphase, sister chromatids separate and are pulled to opposite poles of the cell.
During this chromosomal movement, the kinetochore microtubules become progressively shorter.
The shortening occurs because the kinetodiore disassembles the microtubule into tubulin protein subunits as it passes.
A motor protein actively "walks" the kinetochore along the microtubule.
The tubulin subunits are reused for later microtubule assembly.
The following experiment shows that the kinetodiore microtubules are shortened by disassembly rather than by contraction or movement toward the pole.
Researchers used a microscopic beam of ultraviolet light to "bleach" a section of the microtubules.
As the chromosomes moved toward the pole, the bleached segment did not move, indicating that the microtubules themselves do not move.
More recent experiments suggest that kinetochore microtubules may also be disassembled at the poles, contributing to their shortening.
In contrast to the kinetochore microtubules, nonkinetochore microtubules of the spindle (those not attached to chromosomes) do move, causing the spindle to lengthen and pushing the poles apart.
The lengthening of the spindle contributes to the movement of chromosomes away from each other.
In the zone where microtubules from different poles overlap, they are pushed apart by motor proteins "walking" between adjacent microtubules.
https://wn.com/Mechanisms_For_Chromosome_Movement
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At mitotic metaphase, the fully-formed spindle is composed of many microtubules that extend from the poles.
Some of these, the kinetochore microtubules, are attached to the kinetochores of each chromosome.
Kinetochores are located at the centromeres.
At anaphase, sister chromatids separate and are pulled to opposite poles of the cell.
During this chromosomal movement, the kinetochore microtubules become progressively shorter.
The shortening occurs because the kinetodiore disassembles the microtubule into tubulin protein subunits as it passes.
A motor protein actively "walks" the kinetochore along the microtubule.
The tubulin subunits are reused for later microtubule assembly.
The following experiment shows that the kinetodiore microtubules are shortened by disassembly rather than by contraction or movement toward the pole.
Researchers used a microscopic beam of ultraviolet light to "bleach" a section of the microtubules.
As the chromosomes moved toward the pole, the bleached segment did not move, indicating that the microtubules themselves do not move.
More recent experiments suggest that kinetochore microtubules may also be disassembled at the poles, contributing to their shortening.
In contrast to the kinetochore microtubules, nonkinetochore microtubules of the spindle (those not attached to chromosomes) do move, causing the spindle to lengthen and pushing the poles apart.
The lengthening of the spindle contributes to the movement of chromosomes away from each other.
In the zone where microtubules from different poles overlap, they are pushed apart by motor proteins "walking" between adjacent microtubules.
- published: 06 Jan 2022
- views: 26626
0:46
Molecular Biophysics of Mitosis: Single molecule of NDC80 diffuses on microtubule
Molecular Biophysics of Mitosis: Single unphosphorylated NDC80-GFP complexes bind and diffuse along the taxol-stabilized microtubules
Reference:
Zaytsev, A.V.,...
Molecular Biophysics of Mitosis: Single unphosphorylated NDC80-GFP complexes bind and diffuse along the taxol-stabilized microtubules
Reference:
Zaytsev, A.V., Mick, J.E., Maslennikov, E., Nikashin, B., DeLuca, J.G., Grishchuk, E.L. (2015) Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Mol. Biol. Cell., 26(10):1829-44.
https://wn.com/Molecular_Biophysics_Of_Mitosis_Single_Molecule_Of_Ndc80_Diffuses_On_Microtubule
Molecular Biophysics of Mitosis: Single unphosphorylated NDC80-GFP complexes bind and diffuse along the taxol-stabilized microtubules
Reference:
Zaytsev, A.V., Mick, J.E., Maslennikov, E., Nikashin, B., DeLuca, J.G., Grishchuk, E.L. (2015) Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Mol. Biol. Cell., 26(10):1829-44.
- published: 08 Jan 2016
- views: 147
0:14
Molecular Biophysics of Mitosis: Molecular dynamics simulation of NDC80 with unphosphorylated “tail”
Two NDC80 complexes (blue and yellow) were positioned on a microtubule patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilame...
Two NDC80 complexes (blue and yellow) were positioned on a microtubule patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilament is shown in these videos for clarity. Tubulin C-terminal extensions are in red; the initial conformation of the Hec1 tail (in dark blue) is extended.
Reference:
Zaytsev, A.V., Mick, J.E., Maslennikov, E., Nikashin, B., DeLuca, J.G., Grishchuk, E.L. (2015) Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Mol. Biol. Cell., 26(10):1829-44.
https://wn.com/Molecular_Biophysics_Of_Mitosis_Molecular_Dynamics_Simulation_Of_Ndc80_With_Unphosphorylated_“Tail”
Two NDC80 complexes (blue and yellow) were positioned on a microtubule patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilament is shown in these videos for clarity. Tubulin C-terminal extensions are in red; the initial conformation of the Hec1 tail (in dark blue) is extended.
Reference:
Zaytsev, A.V., Mick, J.E., Maslennikov, E., Nikashin, B., DeLuca, J.G., Grishchuk, E.L. (2015) Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Mol. Biol. Cell., 26(10):1829-44.
- published: 08 Jan 2016
- views: 195
1:19
Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity
Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Anatoly V. Zaytsev et al (2015), Molecular Biology of the Cell ...
Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Anatoly V. Zaytsev et al (2015), Molecular Biology of the Cell http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E14-11-1539
Microtubule attachment to kinetochores is vitally important for cell division, but how these interactions are controlled by phosphorylation is not well known. We used quantitative approaches in vitro combined with molecular dynamics simulations to examine phosphoregulation of the NDC80 complex, a core kinetochore component. We show that the outputs from multiple phosphorylation events on the unstructured tail of its Hec1 subunit are additively integrated to elicit gradual tuning of NDC80-microtubule binding both in vitro and in silico. Conformational plasticity of the Hec1 tail enables it to serve as a phosphorylation-controlled rheostat, providing a new paradigm for regulating the affinity of microtubule binders. We also show that cooperativity of NDC80 interactions is weak and it is unaffected by NDC80 phosphorylation. This in vitro finding strongly supports our model that independent molecular binding events to microtubules by NDC80 complexes, rather than their structured oligomers, regulate the dynamics and stability of kinetochore-microtubule attachments in dividing cells.
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https://wn.com/Multisite_Phosphorylation_Of_The_Ndc80_Complex_Gradually_Tunes_Its_Microtubule_Binding_Affinity
Multisite phosphorylation of the NDC80 complex gradually tunes its microtubule-binding affinity. Anatoly V. Zaytsev et al (2015), Molecular Biology of the Cell http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E14-11-1539
Microtubule attachment to kinetochores is vitally important for cell division, but how these interactions are controlled by phosphorylation is not well known. We used quantitative approaches in vitro combined with molecular dynamics simulations to examine phosphoregulation of the NDC80 complex, a core kinetochore component. We show that the outputs from multiple phosphorylation events on the unstructured tail of its Hec1 subunit are additively integrated to elicit gradual tuning of NDC80-microtubule binding both in vitro and in silico. Conformational plasticity of the Hec1 tail enables it to serve as a phosphorylation-controlled rheostat, providing a new paradigm for regulating the affinity of microtubule binders. We also show that cooperativity of NDC80 interactions is weak and it is unaffected by NDC80 phosphorylation. This in vitro finding strongly supports our model that independent molecular binding events to microtubules by NDC80 complexes, rather than their structured oligomers, regulate the dynamics and stability of kinetochore-microtubule attachments in dividing cells.
Good channel: https://www.youtube.com/Dlium
Subscribe, like and comment.
Good website: https://www.dlium.com
Bookmark, subscribe and comment.
- published: 25 Mar 2015
- views: 236
0:14
MD simulation of the NDC80-MT interface with unphosphorylated Hec1 tail
MD simulation of the NDC80-MT interface with unphosphorylated Hec1 tail.Two NDC80 complexes (blue and yellow) were positioned on a MT patch containing 9 tubulin...
MD simulation of the NDC80-MT interface with unphosphorylated Hec1 tail.Two NDC80 complexes (blue and yellow) were positioned on a MT patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilament is shown in these videos for clarity. Tubulin C-terminal extensions are in red; the initial conformation of the Hec1 tail (in dark blue) is extended.
https://wn.com/Md_Simulation_Of_The_Ndc80_Mt_Interface_With_Unphosphorylated_Hec1_Tail
MD simulation of the NDC80-MT interface with unphosphorylated Hec1 tail.Two NDC80 complexes (blue and yellow) were positioned on a MT patch containing 9 tubulin monomers, organized in 3 protofilaments but only 1 protofilament is shown in these videos for clarity. Tubulin C-terminal extensions are in red; the initial conformation of the Hec1 tail (in dark blue) is extended.
- published: 13 Oct 2015
- views: 40
1:22
Gene Music using Protein Sequence of NDC80 "NDC80 KINETOCHORE COMPLEX COMPONENT"
Shop NDC80 - https://www.redbubble.com/people/genemusic/works/51706688-ndc80?asc=u
Subscribe - https://www.youtube.com/c/GeneMusicStudio?sub_confirmation=1
Gene...
Shop NDC80 - https://www.redbubble.com/people/genemusic/works/51706688-ndc80?asc=u
Subscribe - https://www.youtube.com/c/GeneMusicStudio?sub_confirmation=1
Gene Music Studio - A channel to taste (visually & musically) gene information (particularly protein sequences)
Gene Music using Protein Sequence of NDC80 'NDC80 KINETOCHORE COMPLEX COMPONENT'
https://wn.com/Gene_Music_Using_Protein_Sequence_Of_Ndc80_Ndc80_Kinetochore_Complex_Component
Shop NDC80 - https://www.redbubble.com/people/genemusic/works/51706688-ndc80?asc=u
Subscribe - https://www.youtube.com/c/GeneMusicStudio?sub_confirmation=1
Gene Music Studio - A channel to taste (visually & musically) gene information (particularly protein sequences)
Gene Music using Protein Sequence of NDC80 'NDC80 KINETOCHORE COMPLEX COMPONENT'
- published: 10 Dec 2016
- views: 33
0:45
Molecular Biophysics of Mitosis: Microtubule binding to the molecular lawn of Ndc80 at kinetochore.
Stochastic model of kinetochore-microtubule interface composed of the molecular lawn with phosphorylation-controlled microtubule binding by the Ndc80 complexes....
Stochastic model of kinetochore-microtubule interface composed of the molecular lawn with phosphorylation-controlled microtubule binding by the Ndc80 complexes.
Reference:
Zaytsev, A.V., Sundin, L.J.R., DeLuca, K.F., Grishchuk, E.L. and J.D. DeLuca (2014) Accurate phosphoregulation of kinetochore-microtubule affinity requires unconstrained molecular interactions. J. Cell Biol., 206(1):45-59.
https://wn.com/Molecular_Biophysics_Of_Mitosis_Microtubule_Binding_To_The_Molecular_Lawn_Of_Ndc80_At_Kinetochore.
Stochastic model of kinetochore-microtubule interface composed of the molecular lawn with phosphorylation-controlled microtubule binding by the Ndc80 complexes.
Reference:
Zaytsev, A.V., Sundin, L.J.R., DeLuca, K.F., Grishchuk, E.L. and J.D. DeLuca (2014) Accurate phosphoregulation of kinetochore-microtubule affinity requires unconstrained molecular interactions. J. Cell Biol., 206(1):45-59.
- published: 31 Jan 2015
- views: 328