Protocol full text hidden due to copyright restrictions
Open the protocol to access the free full text link
>
Anatomy
>
Cell Component
>
Microtubules
Microtubules
Microtubules are cytoskeletal structures found in the cytoplasm of eukaryotic cells.
They are composed of tubulin dimers and play crucial roles in cell division, intracellular transport, and maintaining cell shape.
Microtubules are highly dynamic, undergoing constant assembly and disassembly, which is regulated by various cellular processes.
Studying microtubule structure, function, and regulation is crucial for understanding fundamental cellular mechanisms and developing therapies for microtubule-related diseases, such as cancer and neurodegenerative disorders.
Reserchers can optimize their microtubule studies by utilizing the power of PubCompare.ai, an AI-driven platform that helps locate the best protocols from literature, preprints, and patents, while comparing them to identify the most accurate and reproducible methods.
This tool can take your microtubule research to new heights and facilitate breakthroughs in this important field of cell biology.
They are composed of tubulin dimers and play crucial roles in cell division, intracellular transport, and maintaining cell shape.
Microtubules are highly dynamic, undergoing constant assembly and disassembly, which is regulated by various cellular processes.
Studying microtubule structure, function, and regulation is crucial for understanding fundamental cellular mechanisms and developing therapies for microtubule-related diseases, such as cancer and neurodegenerative disorders.
Reserchers can optimize their microtubule studies by utilizing the power of PubCompare.ai, an AI-driven platform that helps locate the best protocols from literature, preprints, and patents, while comparing them to identify the most accurate and reproducible methods.
This tool can take your microtubule research to new heights and facilitate breakthroughs in this important field of cell biology.
Most cited protocols related to «Microtubules»
5'-deoxy-5'-phosphonomethyladenosine phosphate
Axoneme
Chlamydomonas reinhardtii
Cone-Beam Computed Tomography
DNA Replication
Epistropheus
Hypersensitivity
Maritally Unattached
Mental Orientation
Microtubule-Associated Proteins
Microtubules
NADH Dehydrogenase Complex 1
Optimism
Plant Embryos
Radius
Seizures
Tomography
Yarrowia lipolytica
Actins
Adult
Animals, Transgenic
Bacteria
Biological Assay
Cloning Vectors
Dissection
DNA, Complementary
Drosophila
Electron Microscopy
Embryo
F-Actin
fascin
Fluorescence
G-Actin
Growth Cones
Hydroxybenzoates
Microscopy
Microtubules
Mixed Function Oxygenases
Mutation
Polymerization
Protein Isoforms
Proteins
Pupa
Pyrenes
Reconstructive Surgical Procedures
Sn protein, Drosophila
Transmission Electron Microscopy
Tubulin
While annotation alone is sufficient for certain types of cellular tomogram interpretation, subtomogram extraction and averaging remains a primary purpose for detailed annotation. To extract discrete objects like ribosomes or other macromolecules, we begin by identifying all connected voxels annotated as being the same feature. For each connected region, the maxima position in the annotation is used as the particle location. For continuous features like microtubules, we randomly seed points on the annotation output and use these points as box coordinates for particle extraction. In both cases, EMAN2 2D classification20 (link) is performed on a Z-axis projection of the particles in order to help identify and remove bad particles, in a similar fashion to single particle analysis. 3D alignment and averaging are performed using EMAN2 single particle tomography utilities2 (link).
Cells
Epistropheus
Microtubules
Ribosomes
Single Molecule Analysis
Tomography
The PHF and SF maps from the PT and FL data sets have complementary regions for model building. The β-helix motif at the tips of the C-shaped protofilaments is better ordered in the PHFs than in SFs, whereas the amino- and carboxy-terminal ends of the protofilament cores are best ordered in the SF map from the FL data set. Moreover, density for the cross-β structures near the termini of the PHFs is better defined in the PT reconstruction than in the FL reconstruction. Combined, the different maps allow for unambiguous main-chain tracing of the atomic models (Figure 2 ; Extended Data Figures 4 and 6 ). Initial model building started by fitting the L-type β-helix from the magic-angle spinning NMR-derived structure of filaments of the prion-forming domain HET-s218-289 (PDB-entry 2RNM) in the tip of the protofilaments of the PT PHF reconstruction. The sequence of only one of the four microtubule-binding repeats of Tau had a sequence that was compatible with the observed density in both PHFs and SFs (Extended Data Figure 4 ). Using the β-helix region as a starting point, we then built the remainder of the amino- and carboxy-terminal regions by manually adding amino acids and targeted real-space refinement in COOT54 (link).
Fourier-space refinement of the complete atomic model against the PHF and SF maps was performed in REFMAC55 (link). A stack of three consecutive monomers from each of the protofilaments was refined in order to preserve nearest-neighbour interactions for the middle chain. Local symmetry restraints were imposed in REFMAC to keep all β-strand rungs identical. Since most of the structure adopts a β-strand conformation, hydrogen-bond restraints were imposed to preserve a parallel, in-register hydrogen-bonding pattern in earlier stages of the model building process. In addition, ϕ/ψ angle restraints were imposed for the polyglycine II region, 333GGG335, and the three-residue β-arc, 347KDR349. The dihedral angles for polyglycine II were taken from Crick’s proposed fold27 (link) (ϕ = −80, ψ =150) and those for the three-residue β-arc from the crystal structure of PDB-entry 1QRE56 (link). Side-chain clashes were detected using MOLPROBITY57 (link) and corrected by iterative cycles of real-space refinement in COOT and Fourier-space refinement in REFMAC. Refinements of atomic models were performed for the FL and PT PHFs and for the FL SF. The refined model from the FL SF was rigid-body fitted into the PT SF map. For each refined structure, separate model refinements were performed against a single half-map, and the resulting model was compared to the other half-map to confirm the absence of overfitting. The final models were stable in refinements without additional restraints. Statistics for the final models are shown inExtended Data Table 1 .
Fourier-space refinement of the complete atomic model against the PHF and SF maps was performed in REFMAC55 (link). A stack of three consecutive monomers from each of the protofilaments was refined in order to preserve nearest-neighbour interactions for the middle chain. Local symmetry restraints were imposed in REFMAC to keep all β-strand rungs identical. Since most of the structure adopts a β-strand conformation, hydrogen-bond restraints were imposed to preserve a parallel, in-register hydrogen-bonding pattern in earlier stages of the model building process. In addition, ϕ/ψ angle restraints were imposed for the polyglycine II region, 333GGG335, and the three-residue β-arc, 347KDR349. The dihedral angles for polyglycine II were taken from Crick’s proposed fold27 (link) (ϕ = −80, ψ =150) and those for the three-residue β-arc from the crystal structure of PDB-entry 1QRE56 (link). Side-chain clashes were detected using MOLPROBITY57 (link) and corrected by iterative cycles of real-space refinement in COOT and Fourier-space refinement in REFMAC. Refinements of atomic models were performed for the FL and PT PHFs and for the FL SF. The refined model from the FL SF was rigid-body fitted into the PT SF map. For each refined structure, separate model refinements were performed against a single half-map, and the resulting model was compared to the other half-map to confirm the absence of overfitting. The final models were stable in refinements without additional restraints. Statistics for the final models are shown in
Amino Acids
Cytoskeletal Filaments
Helix (Snails)
Human Body
Hydrogen Bonds
Microtubule-Associated Proteins
Microtubules
Muscle Rigidity
polyglycine
Prions
Reconstructive Surgical Procedures
Repetitive Region
Protocol full text hidden due to copyright restrictions
Open the protocol to access the free full text link
Fluorescence
Microscopy
Microtubules
Proteins
Most recents protocols related to «Microtubules»
Cy5-labeled GDP-MT (10% labeled) was grown from Alexa Fluor 488–labeled GMPCPP-MT (2% labeled) in the same way as the microtubule expansion assay (see the Microtubule expansion assay section). After 30-min incubation to hydrolyze GTP completely, the chamber was washed with washout buffer (BRB80, 25% glycerol, and 2× blocking solution) with or without 4 μM D2 and incubated for 5 min. Subsequently, glycerol-free imaging buffer (BRB80, 1× blocking solution, 0.1% methylcellulose, 5 mM protocatechuic acid, 5 mM TSY, and 50 nM protocatechuate-3,4-dioxygenase) with or without 4 μM D2 was flowed into the chamber, and the image acquisition was started immediately. For experiments without D2, images were taken at 0.5-s intervals; for those with D2, images were taken at 5-s intervals. Signals from the mCherry channel were also taken for the experiments in Fig S4 .
Instead of building kymographs, we measured the decrease in Cy5 total intensity to quantify the depolymerization rate. Areas that microtubules occupied during depolymerization were manually drawn using maximum projection as the reference. The total Cy5 intensity in the area was measured for every frame, and the values were converted into length using the ratio of the microtubule length to total Cy5 intensity of the first frame. The depolymerization rate was determined by a linear regression of data points that corresponded to microtubule lengths longer than 0.5 μm using the scikit-learn package (v1.0.1; Pedregosa et al, 2011 (link)). This workflow was applied to all microtubules independently.
Instead of building kymographs, we measured the decrease in Cy5 total intensity to quantify the depolymerization rate. Areas that microtubules occupied during depolymerization were manually drawn using maximum projection as the reference. The total Cy5 intensity in the area was measured for every frame, and the values were converted into length using the ratio of the microtubule length to total Cy5 intensity of the first frame. The depolymerization rate was determined by a linear regression of data points that corresponded to microtubule lengths longer than 0.5 μm using the scikit-learn package (v1.0.1; Pedregosa et al, 2011 (link)). This workflow was applied to all microtubules independently.
5'-guanylylmethylenebisphosphonate
alexa fluor 488
Biological Assay
Buffers
Dioxygenases
Glycerin
Kymography
Methylcellulose
Microtubules
protocatechuic acid
Reading Frames
D2-mCherry in imaging buffer (BRB80, 25% glycerol 1× blocking solution, 0.1% methylcellulose, 5 mM protocatechuic acid (Pacific Bioscience), 5 mM TSY (Pacific Bioscience), and 50 nM protocatechuate-3,4-dioxygenase (Pacific Bioscience)) was applied to the microtubule-immobilized glass chamber (see the Preparation for binding assay section). After 5 min of incubation, image acquisition was conducted for all registered positions. To increase the signal-to-noise ratio, five frames were taken for every position and channel.
For assays in the presence of taxol, D2-mCherry in imaging buffer was supplemented with 20 μM taxol, and images were acquired the same way. Taxol depletion was conducted by exchanging the solution with a sample of same D2 concentration without taxol. Images were taken after 5-min incubation.
Because the binding activity of D2 was lost quickly after being thawed (<1 h), we prepared new samples every 30 min.
For assays in the presence of taxol, D2-mCherry in imaging buffer was supplemented with 20 μM taxol, and images were acquired the same way. Taxol depletion was conducted by exchanging the solution with a sample of same D2 concentration without taxol. Images were taken after 5-min incubation.
Because the binding activity of D2 was lost quickly after being thawed (<1 h), we prepared new samples every 30 min.
Biological Assay
Buffers
Dioxygenases
Glycerin
Methylcellulose
Microtubules
protocatechuic acid
Reading Frames
Taxol
During this experiment, 1 μM D2-mCherry in imaging buffer was used for the D2-mCherry samples, and variable concentrations of KIF5C in BRB30 with 25% glycerol were used for the KIF5C pretreatment. A microtubule-immobilized glass chamber (see the Preparation for binding assay section) was first incubated with D2-mCherry for 5 min. As a no pretreatment control, microtubule-bound D2 was dissociated by 1-min incubation in high-salt buffer (7.5× PEM, 25% glycerol) followed by washout with BRB80 containing 25% glycerol. Again, D2-mCherry was applied, and the chamber was incubated for 5 min before the image acquisition.
For 0.1, 0.5, and 2.0 μM KIF5C pretreatment, the incubation/dissociation cycle described below was repeated in the same chamber after the previous image acquisition of D2-bound microtubules. First, D2 was dissociated and washed out by 1-min incubation in high-salt buffer and 30-s incubation in BRB80 containing 25% glycerol. Microtubules were subsequently expanded by the addition of KIF5C and incubated for 1 min. Next, KIF5C was dissociated and washed out by a 1-min incubation in high-salt buffer and 30-s incubation in BRB80 containing 25% glycerol. Finally, D2 was applied and incubated for 5 min before the image acquisition.
For the compaction experiment, pretreatment with 2.0 μM KIF5C was repeated as above except the buffer used for the KIF5C dissociation was ADP buffer (BRB80, 25% glycerol, and 1 mM ADP) and not a high-salt buffer.
Note that because this assay takes ∼1 h for each run, new D2 samples were prepared between 0 and 0.1 μM pretreatments in addition to the 0.5 and 2.0 μM pretreatments.
For 0.1, 0.5, and 2.0 μM KIF5C pretreatment, the incubation/dissociation cycle described below was repeated in the same chamber after the previous image acquisition of D2-bound microtubules. First, D2 was dissociated and washed out by 1-min incubation in high-salt buffer and 30-s incubation in BRB80 containing 25% glycerol. Microtubules were subsequently expanded by the addition of KIF5C and incubated for 1 min. Next, KIF5C was dissociated and washed out by a 1-min incubation in high-salt buffer and 30-s incubation in BRB80 containing 25% glycerol. Finally, D2 was applied and incubated for 5 min before the image acquisition.
For the compaction experiment, pretreatment with 2.0 μM KIF5C was repeated as above except the buffer used for the KIF5C dissociation was ADP buffer (BRB80, 25% glycerol, and 1 mM ADP) and not a high-salt buffer.
Note that because this assay takes ∼1 h for each run, new D2 samples were prepared between 0 and 0.1 μM pretreatments in addition to the 0.5 and 2.0 μM pretreatments.
Afterimage
Biological Assay
Buffers
Glycerin
Microtubules
Sodium Chloride
Microtubule immobilization was carried out similar to the binding assay (see the Binding assay section) but slightly modified to fit the expansion assay. After GMPCPP-MT was added, 28 μM Cy5-labeled tubulin (10% labeled) was used for a 15-min polymerization period to lengthen and brighten the microtubules. Subsequently, 8 μM Alexa Fluor 488–labeled tubulin (2% labeled) with 1 mM GMPCPP was loaded into the chamber and polymerized for 20 min. Polymerization was terminated by washing free tubulin out with washout buffer. Images were acquired before and after 4 μM D2-mCherry in imaging buffer was added to the chamber followed by the dissociation of D2 by 1-min incubation in high-salt buffer and washout by imaging buffer for 30 s.
To calculate expansion, a background correction was performed in the same way as the data analysis for the binding assay (see the Data analysis of binding assays section). Microtubule lengths were measured using napari-filaments as follows (Fig S5 ): first, the Cy5 channel and Alexa Fluor 488 channel of the image were added with 1:1 weight to create a total intensity image. This image was used for 2D spline fitting as mentioned in the data analysis of the binding assay (see the Data analysis of binding assays section). Next, the spline curves were clipped at the Cy5-labeled microtubule edges by fitting to the error function:
The parameters of the error function indicate that intensity increases from to , where the inflection point of the intensity change is . Cy5-labeled microtubule lengths were obtained by fragmenting the spline curve into 1,024 pieces and summing the lengths of all fragments.
To calculate expansion, a background correction was performed in the same way as the data analysis for the binding assay (see the Data analysis of binding assays section). Microtubule lengths were measured using napari-filaments as follows (
The parameters of the error function indicate that intensity increases from to , where the inflection point of the intensity change is . Cy5-labeled microtubule lengths were obtained by fragmenting the spline curve into 1,024 pieces and summing the lengths of all fragments.
5'-guanylylmethylenebisphosphonate
alexa fluor 488
Biological Assay
Buffers
Cytoskeletal Filaments
Immobilization
Microtubules
Polymerization
Sodium Chloride
Tubulin
A PEG-biotin–coated glass chamber was made by silane coupling and a succinimidyl ester reaction. Cover glasses (C022221S; Matsunami Glass) were first subjected to sonication in 1 N KOH and plasma treatment. Glass surfaces were coated with an amino group by sandwiching N-2-(aminoethyl)-3-aminopropyl-triethoxysilane (KBE-603; Shin-Etsu Chemical) and incubation for 20 min at room temperature. These glasses were washed with deionized water 20 times and then incubated with 200 mg/ml of 0.5% biotinylated NHS-PEG (ME-050-TS and BI-050-TS; NOF) for 90 min at room temperature. Coated glasses were stuck to each other with 30-μm double-sided tape (5603; Nitto-Denko) to make an ∼2-mm wide flowing chamber. The glasses were sealed in a food saver in vacuo and stored at −80°C until use.
GMPCPP-bound tubulin labeled with Alexa Fluor 488 (2% labeled) and biotin (5% labeled) was incubated at 27°C for 1 h to promote nucleation, followed by 1 h of polymerization at 37°C. Polymerized microtubule samples were purified by centrifugation at 20,000g, 35°C for 25 min.
The glass chamber was treated as follows: first, 1 mg/ml NeutrAvidin was loaded into the chamber and incubated for 2 min to let it bind to biotin molecules covalently connected to the glass surface. The glass surface was subsequently deactivated by adding and incubating with 10× blocking solution (1 mg/ml casein and 1% pluronic F127) for 2 min. After washing them out with BRB80 containing 25% glycerol, GMPCPP-MT seeds were loaded into the chamber and incubated for 2 min to immobilize microtubules on the glass surface. Unbound microtubules were washed out with BRB80 containing 10x blocking solution and 1 mM GTP. To polymerize GDP-MT from the seeds, 28 μM Cy5-labeled tubulin (labeling rate 2%) in polymerization buffer (BRB80, 2× blocking solution, 1 mM GTP) was applied to the chamber, polymerized for 5 min, and terminated by washing free tubulin out with washout buffer (BRB80, 25% glycerol, and 2× blocking solution). To completely hydrolyze GTP, the chamber was incubated for more than 30 min before any subsequent experiments.
GMPCPP-bound tubulin labeled with Alexa Fluor 488 (2% labeled) and biotin (5% labeled) was incubated at 27°C for 1 h to promote nucleation, followed by 1 h of polymerization at 37°C. Polymerized microtubule samples were purified by centrifugation at 20,000g, 35°C for 25 min.
The glass chamber was treated as follows: first, 1 mg/ml NeutrAvidin was loaded into the chamber and incubated for 2 min to let it bind to biotin molecules covalently connected to the glass surface. The glass surface was subsequently deactivated by adding and incubating with 10× blocking solution (1 mg/ml casein and 1% pluronic F127) for 2 min. After washing them out with BRB80 containing 25% glycerol, GMPCPP-MT seeds were loaded into the chamber and incubated for 2 min to immobilize microtubules on the glass surface. Unbound microtubules were washed out with BRB80 containing 10x blocking solution and 1 mM GTP. To polymerize GDP-MT from the seeds, 28 μM Cy5-labeled tubulin (labeling rate 2%) in polymerization buffer (BRB80, 2× blocking solution, 1 mM GTP) was applied to the chamber, polymerized for 5 min, and terminated by washing free tubulin out with washout buffer (BRB80, 25% glycerol, and 2× blocking solution). To completely hydrolyze GTP, the chamber was incubated for more than 30 min before any subsequent experiments.
3-(triethoxysilyl)propylamine
5'-guanylylmethylenebisphosphonate
alexa fluor 488
Biotin
Buffers
Caseins
Centrifugation
Esters
Eyeglasses
Food
Glycerin
Immobilization
Microtubules
neutravidin
Plant Embryos
Plasma
Pluronic F-127
Silanes
Tubulin
Top products related to «Microtubules»
Sourced in United States, Germany, United Kingdom, Japan, Sao Tome and Principe, Canada, China, Switzerland, France, Poland, Macao, Australia
Nocodazole is a synthetic compound that acts as a microtubule-destabilizing agent. It functions by binding to and disrupting the polymerization of microtubules, which are essential components of the cytoskeleton in eukaryotic cells. This property makes Nocodazole a valuable tool in cell biology research for studying cell division, cell motility, and other cellular processes that rely on the dynamics of the microtubule network.
Sourced in United States, Germany, United Kingdom, France, China, Macao, Japan, Sao Tome and Principe, Canada, Poland, Spain, Israel, Australia, Switzerland, Italy
Paclitaxel is a pharmaceutical compound used in the production of various cancer treatment medications. It functions as a microtubule-stabilizing agent, which plays a crucial role in the development and regulation of cells. Paclitaxel is a key ingredient in the manufacture of certain anti-cancer drugs.
Sourced in United States, Germany, Macao, United Kingdom, China, Italy, Canada, Sao Tome and Principe
Cytochalasin D is a laboratory reagent that inhibits actin polymerization. It is commonly used in cell biology research to disrupt the cytoskeleton and study its role in cellular processes.
Sourced in United States, Germany, Japan, United Kingdom, China, Italy, Sao Tome and Principe, France, Macao, Canada, Switzerland, Spain, Australia, Denmark, India, Poland, Israel, Belgium, Sweden, Ireland, Netherlands, Panama, Brazil, Portugal, Czechia, Puerto Rico, Austria, Hong Kong, Singapore
DAPI is a fluorescent dye that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used as a nuclear counterstain in fluorescence microscopy to visualize and locate cell nuclei.
Sourced in United States, Germany, Canada, United Kingdom, China
Taxol is a laboratory product manufactured by Merck Group. It is a complex organic compound used in various research and analysis applications. The core function of Taxol is to facilitate the stabilization of microtubules, which are essential structural components within cells.
Sourced in United States, United Kingdom, Germany, Canada, Japan, Sweden, Austria, Morocco, Switzerland, Australia, Belgium, Italy, Netherlands, China, France, Denmark, Norway, Hungary, Malaysia, Israel, Finland, Spain
MATLAB is a high-performance programming language and numerical computing environment used for scientific and engineering calculations, data analysis, and visualization. It provides a comprehensive set of tools for solving complex mathematical and computational problems.
Sourced in United States, United Kingdom, Germany, Japan, France, Italy, Canada, China, Spain, Switzerland, Denmark, Australia, Hungary, Belgium, Ireland, Israel, Netherlands, Moldova, Republic of, India, Austria, Czechia, Poland
Alexa Fluor 488 is a fluorescent dye used in various biotechnological applications. It has an excitation maximum at 495 nm and an emission maximum at 519 nm, producing a green fluorescent signal. Alexa Fluor 488 is known for its brightness, photostability, and pH-insensitivity, making it a popular choice for labeling biomolecules in biological research.
Sourced in United States, Germany, United Kingdom, China, Italy, Sao Tome and Principe, France, Macao, India, Canada, Switzerland, Japan, Australia, Spain, Poland, Belgium, Brazil, Czechia, Portugal, Austria, Denmark, Israel, Sweden, Ireland, Hungary, Mexico, Netherlands, Singapore, Indonesia, Slovakia, Cameroon, Norway, Thailand, Chile, Finland, Malaysia, Latvia, New Zealand, Hong Kong, Pakistan, Uruguay, Bangladesh
DMSO is a versatile organic solvent commonly used in laboratory settings. It has a high boiling point, low viscosity, and the ability to dissolve a wide range of polar and non-polar compounds. DMSO's core function is as a solvent, allowing for the effective dissolution and handling of various chemical substances during research and experimentation.
Sourced in United States, Germany, France, Canada, India, Japan, United Kingdom, Italy, Spain, Macao
Colchicine is a chemical compound used in various laboratory and research applications. It is a naturally occurring alkaloid derived from the autumn crocus plant. Colchicine is primarily used as a research tool to study cell division and microtubule dynamics.
Sourced in United States, Germany, United Kingdom, Italy, China, Japan, France, Canada, Sao Tome and Principe, Switzerland, Macao, Poland, Spain, Australia, India, Belgium, Israel, Sweden, Ireland, Denmark, Brazil, Portugal, Panama, Netherlands, Hungary, Czechia, Austria, Norway, Slovakia, Singapore, Argentina, Mexico, Senegal
Triton X-100 is a non-ionic surfactant commonly used in various laboratory applications. It functions as a detergent and solubilizing agent, facilitating the solubilization and extraction of proteins and other biomolecules from biological samples.
More about "Microtubules"
Microtubules are essential cytoskeletal structures found within the cytoplasm of eukaryotic cells.
These dynamic filaments, composed of tubulin dimers, play crucial roles in diverse cellular processes, including cell division, intracellular transport, and the maintenance of cell shape.
Studying the structure, function, and regulation of microtubules is vital for understanding fundamental mechanisms in cell biology and developing therapies for microtubule-related diseases, such as cancer and neurodegenerative disorders.
Researchers can optimize their microtubule studies by utilizing the power of PubCompare.ai, an AI-driven platform that helps locate the best protocols from literature, preprints, and patents, while comparing them to identify the most accurate and reproducible methods.
This tool can take your microtubule research to new heights and facilitate breakthroughs in this important field.
Microtubules are highly dynamic structures, undergoing constant assembly and disassembly, which is regulated by various cellular processes.
Modulators of microtubule dynamics, such as Nocodazole, Paclitaxel, Cytochalasin D, and Colchicine, are widely used in microtubule research to investigate their effects on cellular processes.
Fluorescent dyes, such as DAPI and Alexa Fluor 488, are commonly employed to visualize and study microtubule structures, often in combination with techniques like immunofluorescence and live-cell imaging.
The use of MATLAB, a powerful computational software, can aid in the analysis and quantification of microtubule dynamics and organization.
By leveraging the insights and resources provided by PubCompare.ai, researchers can optimize their microtubule studies, leading to a better understanding of this crucial cellular component and paving the way for advancements in the fields of cell biology and therapeutics.
These dynamic filaments, composed of tubulin dimers, play crucial roles in diverse cellular processes, including cell division, intracellular transport, and the maintenance of cell shape.
Studying the structure, function, and regulation of microtubules is vital for understanding fundamental mechanisms in cell biology and developing therapies for microtubule-related diseases, such as cancer and neurodegenerative disorders.
Researchers can optimize their microtubule studies by utilizing the power of PubCompare.ai, an AI-driven platform that helps locate the best protocols from literature, preprints, and patents, while comparing them to identify the most accurate and reproducible methods.
This tool can take your microtubule research to new heights and facilitate breakthroughs in this important field.
Microtubules are highly dynamic structures, undergoing constant assembly and disassembly, which is regulated by various cellular processes.
Modulators of microtubule dynamics, such as Nocodazole, Paclitaxel, Cytochalasin D, and Colchicine, are widely used in microtubule research to investigate their effects on cellular processes.
Fluorescent dyes, such as DAPI and Alexa Fluor 488, are commonly employed to visualize and study microtubule structures, often in combination with techniques like immunofluorescence and live-cell imaging.
The use of MATLAB, a powerful computational software, can aid in the analysis and quantification of microtubule dynamics and organization.
By leveraging the insights and resources provided by PubCompare.ai, researchers can optimize their microtubule studies, leading to a better understanding of this crucial cellular component and paving the way for advancements in the fields of cell biology and therapeutics.