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Cytoskeleton

The cytoskeleton is a complex, dynamic network of interlinking filaments and tubules that provide structural support and organization within eukaryotic cells.
It is composed of three main components: microfilaments, intermediate filaments, and microtubules.
The cytoskeleton plays a crucial role in cellular processes such as cell division, intracellular transport, cell motility, and signal transduction.
Proper cytoskeletal function is essential for cellular homeostasis and organismal development.
Disruptions in the cytoskeleton have been implicated in a variety of diseases, including cancer, neurodegenerative disorders, and autoimmune conditions.
Reserach into the cytoskeleton and its components is vital for understanding fundamental cell biology and developing targeted therapeutic interventios. [Optmize your cytoakeleton research with PubCompare.ai, the AI-driven platform that enhances reproducibility and accuracy.]

Most cited protocols related to «Cytoskeleton»

1
Quantifying Axonal Cytoskeleton Density
The evaluation of cytoskeleton density was performed on 10 images of correctly-myelinated axons for each experimental point among three different experiments. Furthermore, we chose those axons that showed at least one region of myelin concentric layers stacking in the myelin sheaths to check the orthogonal sectioning. After an automatic adjustment of brightness and contrast, axons were isolated from the surrounding myelin sheath and the axonal area evaluated. Cytoplasmic organelles were deleted from the micrograph and, following an automatic thresholding of the images the generation of bit-maps, the number of identified particle was counted and normalized for axonal area.
Cappello V., Marchetti L., Parlanti P., Landi S., Tonazzini I., Cecchini M., Piazza V, & Gemmi M. (2016). Ultrastructural Characterization of the Lower Motor System in a Mouse Model of Krabbe Disease. Scientific Reports, 6, 1.
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Publication 2016
Axon Cytoplasm Cytoskeleton Microtubule-Associated Proteins Myelin Sheath Organelles
2
Super-resolution Imaging of Fixed Cells
BS-C-1 cells (ATCC) were fixed, immunostained with rabbit anti-Tom20 (Santa Cruz Biotech) and/or mouse anti-β-tubulin (TUB2.1, Cytoskeleton) (See Supplementary Methods online for the detailed immunostaining procedure). The stained cells were imaged in PBS with the addition of 100 mM mercaptoethylamine at pH 8.5, 5% glucose (w/v) and oxygen scavenging enzymes (0.5 mg/mL glucose oxidase (Sigma-Aldrich), and 40 μg/mL catalase (Roche Applied Science)), unless otherwise mentioned. This above imaging buffer has a refractive index of 1.34. Media with higher refractive index (1.45) based on 80% (v/v) glycerol and 5% (w/v) glucose, or 60% (w/w) sucrose solution and 5% (w/w) glucose, were used in some experiments, both with the same amount of mercaptoethylamine and oxygen scavenging enzymes as described above. The slight mismatch between the medium refractive index and coverglass is needed for focus locking during imaging. Although a high concentration of mercaptoethylamine and oxygen scavenging system were used here for fixed cell imaging, the cyanine dyes also switch in buffers with lower concentrations of thiol and oxygen scavenger system compatible with live cell imaging12 (link).
Data acquisition was performed on a fluorescence microscope as described in the Supplementary Methods online. Specifically for 3D imaging, a cylindrical lens with a focal length of 1 m was inserted into the imaging optical path for 3D localization8 (link). To stabilize the microscope focusing during data acquisition, the reflected excitation laser from the coverglass-medium interface was directed to a quadrant photodiode. The position read out of the quadrant photodiode, which was sensitive to the distance between the coverglass and the objective focal plane, was used to provide feedback to a piezo objective positioner (Nano-F100, MadCity Labs), allowing compensation for the focus drift. The residual drift, < 40 nm (Supplementary Fig. 7 online), was corrected during data analysis. For whole cell imaging in an aqueous medium, the objective positioner was stepped in 300 nm intervals, which corresponds to a focal plane displacement of 216 nm after correcting for the refractive index mismatch at the glass-medium interface. Molecules within 270 nm below the focal plane were accepted for image reconstruction. Whole cell images were obtained from 9 partially overlapped z-slices. For imaging in media with a refractive index of 1.45, the positioner was stepped in 650 nm intervals, corresponding to an actual focal plane displacement of 580 nm. Molecules within 360 nm above and below the focal plane are accepted and whole cell images were obtained from 4 partially overlapped z-slices.
For single color imaging, the A405-Cy5 labeled sample was continuously illuminated with a 657 nm imaging laser (~30 mW). A low intensity 405 nm laser was used to activate the probes, with intensity adjusted such that only an optically resolved subset of the probes were activated at any given time. In certain cases, the 405 nm laser can be omitted because the 657 nm laser can also activate Cy5, albeit at a low rate. Emission from the fluorophores were recorded by the camera at a frame rate of 20 Hz. 3D localization of individual molecules was performed as described previously8 (link) and described in the Supplementary Methods online. Multicolor imaging was performed by illuminating the sample repetitively with each frame of an activation laser followed by 3 frames of the 657 nm imaging laser. An alternating sequence of two activation lasers was used for two-color imaging. The 405 nm, 460 nm and 532 nm lasers were used to activated A405-Cy5, A488-Cy5, and A555-Cy5, respectively. Subtraction of crosstalk between different color channels were performed during data analysis as described in the Supplementary Methods online.
Huang B., Jones S.A., Brandenburg B, & Zhuang X. (2008). Whole cell 3D STORM reveals interactions between cellular structures with nanometer-scale resolution. Nature methods, 5(12), 1047-1052.
Publication 2008
A-A-1 antibiotic Buffers Catalase Cells Cross Reactions Cysteamine Cytoskeleton Dyes Enzymes Gas Scavengers Glucose Glycerin Lens, Crystalline Microscopy Microscopy, Fluorescence Mus Oxidase, Glucose Oxygen Rabbits Reading Frames Sucrose Sulfhydryl Compounds Tubulin
3
Complementing Homology-Ontology Annotations with Subcellular Localization Predictions
To complement incomplete annotations in the background database, a homology-ontology annotation retrieved by BLAST should be accompanied by an accurate subcellular localization prediction for each homologous sequence. CELLO has been shown to be helpful for the prediction of subcellular localizations of the proteins found in a proteomic data. [28] (link) Using multiple, integrated machine-learned classifiers, CELLO predicts which of four subcellular localizations in archaea and in Gram-positive bacteria, five subcellular localizations in Gram-negative bacteria, and twelve subcellular localizations in eukaryotes that the targeted protein might be found in, with the four archaeal and Gram-positive bacterial localizations being the extracellular space, the cell wall, the cytoplasmic membrane, and the cytoplasm; the five Gram-positive bacterial localizations being the extracellular space, the outer membrane, the periplasmic and cytoplasmic (inner) membranes, and the cytoplasm; and the 12 eukaryotic localizations being chloroplasts, the cytoplasm, the cytoskeleton, the endoplasmic reticulum, the extracellular/secretory space, the Golgi, lysosomes, mitochondria, the nucleus, peroxisomes, the plasma membrane, and vacuoles. Due to subcellular data increased exponentially over the years, CELLO has been trained on latest models and denoted as update version wrapping in CELLO2GO. And the resultant datasets used for prediction and evaluation is from PSORTb3.0 [23] (link).
Yu C.S., Cheng C.W., Su W.C., Chang K.C., Huang S.W., Hwang J.K, & Lu C.H. (2014). CELLO2GO: A Web Server for Protein subCELlular LOcalization Prediction with Functional Gene Ontology Annotation. PLoS ONE, 9(6), e99368.
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Publication 2014
Archaea Cell Nucleus Cell Wall Chloroplasts Cytoplasm Cytoskeleton Endoplasmic Reticulum Eukaryota Eukaryotic Cells Extracellular Space Golgi Apparatus Gram-Positive Bacteria Gram Negative Bacteria Homologous Sequences Lysosomes Mitochondria Periplasm Peroxisome Plasma Membrane Proteins secretion Tissue, Membrane Vacuole
4
Optimizing Hi-C Library Complexity

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Publication 2012
cDNA Library Cell Lines Centrifugation Chromatin Culture Media Cytoplasm Cytoskeleton Formaldehyde Freezing Genome Glycine Hypersensitivity Ligation Mammals Serum Staphylococcal Protein A Tissues
5
Microtubule Visualization in HeLa Cells
HeLa cells were fixed with 4% paraformaldehyde for 10 min, washed 3 times for 5 minutes with PBS, and permeabilized with 0.1% Triton-X for 15 min. Microtubules in fixed HeLa were stained with primary antibodies (Sheep Anti-Tubulin, Cytoskeleton ATN02) in blocking buffer 1× PBS with 0.1% Triton X-100 and 2% normal donkey serum (PBT) at a concentration of 10 μg/mL for 1–4 hours and then washed in PBS three times for 5 minutes each. Specimens were then incubated with secondary antibodies (Donkey Anti-Sheep Alexa 488, Life Technologies, 10 μg/mL) in PBT for 1–4 hours and then washed in PBS three times for 5 minutes. 50 μm brain tissue slices were prepared and stained with primary and secondary antibodies (Rabbit Anti-Tom20, Santa Cruz Biotech sc-11415 and Goat Anti-Rabbit Alexa 568 (Life Technologies)) as described below. Super-resolution structured illumination microscope imaging was performed on a Deltavision OMX Blaze (GE healthcare) SIM microscope with 100× 1.40 NA (Olympus) oil objective. Stained cells were imaged with SlowFade Gold (Invitrogen) antifade reagent for suppression of photobleaching and refractive index matching for pre-expansion imaging.
Tillberg P.W., Chen F., Piatkevich K.D., Zhao Y., Yu C.C., English B.P., Gao L., Martorell A., Suk H.J., Yoshida F., DeGennaro E.M., Roossien D.H., Gong G., Seneviratne U., Tannenbaum S.R., Desimone R., Cai D, & Boyden E.S. (2016). Protein-retention expansion microscopy of cells and tissues labeled using standard fluorescent proteins and antibodies. Nature biotechnology, 34(9), 987-992.
Publication 2016
alexa 568 Antibodies Brain Buffers Cardiac Arrest Cells Cytoskeleton Domestic Sheep Equus asinus Goat Gold HeLa Cells Light Microscopy Microscopy Microtubules paraform Rabbits Serum Tissues Triton X-100 Tubulin

Most recents protocols related to «Cytoskeleton»

1
Pathways Regulating Cell Adhesion and Motility
Not available on PMC !

Example 3

The phenotype did not depend specifically on the RasC/TORC2 or PI3K pathways. Rather, signals from multiple pathways impinging on the cytoskeleton can be integrated to generate the phenotype. RAM (Regulator of Adhesion and Motility) mutants were isolated in a screen for regulators of cell morphology and migration. Mutant cells were more spread and adhered more strongly than wild-type cells. Most of the mutants also displayed strong defects in cell motility and chemotaxis. When constitutively active RasCQ62L was expressed in the RAM mutants, these cells also formed extremely spread cells like those seen in the pten− cell background (FIG. 5). In another example, Rap1 is a small GTPase that controls cell adhesion in a variety of cell types. When constitutively active Rap1AG12V was expressed in pten− or RAM cells, a similar phenotype was observed.

US11878045B2. Inducing cell death by hyperactivation of motility networks (2024-01-23). The Johns Hopkins University [US]. Inventors: Peter Devreotes [US], Huaqing Cai [US], Marc Edwards [US], Jun Liu [US], Thomas Lampert [US], Yu Long [US].
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Patent 2024
Cell Adhesion Cells Chemotaxis Complex 2, TOR Cytoskeleton Monomeric GTP-Binding Proteins Motility, Cell Phenotype Phosphatidylinositol 3-Kinases PTEN protein, human Signal Pathways Vision
2
Ezrin-Actin Cytoskeleton Reconstitution
Ezrin
T567D was bound to the SLBs at a concentration of 1 μm overnight at 4 °C. Excess protein was removed by a 10-fold
buffer exchange with ezrin buffer and F-actin buffer (50 mM KCl, 20
mM Tris, 2 mM MgCl2, 0.1 mM NaN3, pH 7.4). For
F-actin pre-polymerization, ATTO 594-NHS ester (ATTO-TEC, Siegen,
Germany) labeled nonmuscle G-actin and unlabeled monomers (Cytoskeleton,
Denver, CO, USA) were solved in a 1:10 ratio and a final concentration
of 0.44 mg/mL in G-buffer (5 mM Tris, 0.2 mM CaCl2, 0.1
mM NaN3, pH 8.0). Actin oligomers were depolymerized by
the addition of dithiothreitol (DTT, 0.5 mM) and adenosine 5′-triphosphate
(ATP, 0.2 mM) for 1 h on ice. Remaining actin aggregates were centrifuged
(17,000 × g, 20 min, 4 °C) and polymerization
was induced by the addition of 10% of the total volume of polymerization
solution (500 mM KCl, 20 mm MgCl2, 20 mM ATP,
50 mM guanidine carbonate, pH 7.4). After a polymerization time of
20 min at 20 °C, the F-actin solution was mixed with unlabeled
phalloidin in a 1.5% (n/n) ratio
and incubated for another 20 min. Minimal actin networks were formed
at 20 °C by incubating the ezrin T567D-decorated SLBs with polymerized
F-actin at a concentration of 4.6 μM for at least 2 h. Unbound
filaments were washed off by a 10-fold buffer exchange with F-actin
buffer.
Liebe N.L., Mey I., Vuong L., Shikho F., Geil B., Janshoff A, & Steinem C. (2023). Bioinspired Membrane Interfaces: Controlling Actomyosin Architecture and Contractility. ACS Applied Materials & Interfaces, 15(9), 11586-11598.
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Publication 2023
Actins Adenosine Triphosphate Buffers Carbonates Cytoskeleton Dithiothreitol Esters F-Actin G-Actin Guanidine Magnesium Chloride Polymerization Proteins Sodium Azide Tromethamine VIL2 protein, human
3
Osteoclast Rho GTPase Activation
Osteoclasts were starved for 4 h in 2% FBS containing α-MEM, and then stimulated with 20 ng/ml M-CSF and 30 ng/ml RANKL for 15 min and lysed. Cell lysates were harvested, and Rho GTPase activity analyzed using RhoA/Rac1 G-LISA Activation Assay kits (BK135; Cytoskeleton) according to the manufacturer’s instructions.
Zhu L., Tang Y., Li X.Y., Kerk S.A., Lyssiotis C.A., Sun X., Wang Z., Cho J.S., Ma J, & Weiss S.J. (2023). Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption. The Journal of Cell Biology, 222(4), e202206121.
Publication 2023
Biological Assay Cells Cytoskeleton Macrophage Colony-Stimulating Factor Osteoclasts RHOA protein, human rho GTP-Binding Proteins TNFSF11 protein, human
4
Preparation and Application of Double-Cycled Microtubule Seeds
Double-cycled MT seeds were prepared by combining TRITC-labeled (49%), biotinylated (18%), and unlabeled tubulin (33%; Cytoskeleton) reconstituted in MRB80 (80 mM K-Pipes, 1 mM EGTA, 4 mM MgCl2; pH 6.80 with KOH) to a final concentration of 20 µM with 1 mM GMPCPP (Jena Bioscience) on ice. The mixture was incubated at 35°C for 30 min to allow MTs to polymerize. Seeds were pelleted by centrifugation in an airfuge (Beckman coulter) at 20 psi for 5 min, resuspended in MRB80, and depolymerized on ice for 25 min. The tubulin was then repolymerized upon the addition of fresh GMPCPP by incubating at 35°C for 30 min. These seeds were pelleted by centrifugation in an airfuge at 20 psi for 5 min, resuspended and diluted sixfold in MRB80 supplemented with 10% [vol/vol] glycerol, aliquoted, flash-frozen in liquid nitrogen, and stored at −80°C until use.
To prepare the chambers, a clean glass coverslip was plasma-treated and fixed to a clean glass slide using strips of double-sided tape to create two parallel chambers of ∼10 µl. The surface was blocked and functionalized by incubating with a mix of 95% PLL-g-PEG and 5% PLL-g-PEG-biotin (0.1 mg/ml in 10 mM Hepes, pH 7.40; SuSoS) for 10 min. After washing with MRB80 supplemented with 40% [vol/vol] glycerol (MRB80-gly40), NeutrAvidin was introduced and incubated for 10 min. After washing, 50-fold diluted GMPCPP seeds were introduced and incubated for 5 min before washing once more and then incubating with Κ-casein for >3 min.
All reaction mixtures (MT mix, expansion mix, rigor mix, washout mix) were prepared at double the volume for the paired compacted/expanded lattice samples and split into two equal parts prior to the addition of DMSO (compacted control) or 20 µM Taxol (expanded). Reagents were added to MRB80-gly40 such that the effective glycerol concentration in the MT mix was 20% and in the other mixes was ∼27%. All mixes contained 0.1% [wt/vol] methylcellulose, 0.5 mg/ml K-casein, 50 mM glucose, 0.2 mg/ml catalase, 0.5 mg/ml glucose oxidase, and 10 mM DTT. The MT mix additionally contained 1 mM GTP, 10.8 µM porcine tubulin (Cytoskeleton), and 0.6 µM TRITC-labeled porcine tubulin (Cytoskeleton). The expansion mix additionally contained 50 mM KCl and 20 µM Taxol (or the equivalent dilution of DMSO). The rigor mix additionally contained 50 mM KCl, 20 µM Taxol (or the equivalent dilution of DMSO), 2 mM ATP, and 15.2 pM StableMARK. The washout mixture additionally contained 50 mM KCl, 20 µM Taxol (or the equivalent dilution of DMSO), and 2 mM ATP. After preparation, these mixtures were spun in an airfuge at 20 psi for 5 min, transferred to clean tubes, and kept on ice until use.
Samples were then moved to the TIRF microscope equipped with a stage-top incubator to maintain them at a constant temperature of 30°C. MTs were grown by flowing in two chamber volumes (ChV) of the MT mix and letting it incubate for 15 min. Subsequently, the chambers were flushed with five ChV MRB80-gly40. Next, the lattices were (mock) expanded by adding two ChV expansion mix (or DMSO equivalent) and incubating for 10 min. Next, two ChV rigor mix was added and incubated for 90 s. Finally, four ChV washout mix was added before imaging. For imaging, the following sequence was used: 2 × Taxol, 4 × DMSO, 4 × Taxol, 4 × DMSO, and either 2 × Taxol or 4 × Taxol and 2 × DMSO (8 or 10 images/condition/assay), and images were taken at similar heights within the channels.
Jansen K.I., Iwanski M.K., Burute M, & Kapitein L.C. (2023). A live-cell marker to visualize the dynamics of stable microtubules throughout the cell cycle. The Journal of Cell Biology, 222(5), e202106105.
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Publication 2023
5'-guanylylmethylenebisphosphonate Biological Assay Biotin Caseins Catalase Centrifugation Cytoskeleton Egtazic Acid Freezing Glucose Glycerin HEPES K-Casein Magnesium Chloride Methylcellulose Microscopy Muscle Rigidity neutravidin Nitrogen Oxidase, Glucose Pigs piperazine-N,N'-bis(2-ethanesulfonic acid) Plant Embryos Plasma polylysine-graft-(poly(ethylene glycol)) Sulfoxide, Dimethyl Taxol Technique, Dilution tetramethylrhodamine isothiocyanate Tubulin
5
Fibroblast Morphology Analysis under Temperature and COPA3 Treatment
The fibroblasts morphology was measured at different temperatures after COPA3 treatment. A total of 1×106 cells were seeded in each well of a 6-well plate. After attaining 50% confluence, the cells were subjected to different temperatures (38 and 43°C) and COPA3 peptide (5 μg/mL) treatment. After 48 h of incubation, the media was removed and the cells were fixed using 100% methanol for 20 min. The cells were then aspirated with distilled water and Coomassie brilliant blue was added for 30 min. Next, the cells were washed three times with distilled water and dipped in xylene for 15 min to differentiate the cytoskeleton from the background. Finally, the images were observed using an inverter microscope (Olympus).
Siddiqui S.H., Khan M., Park J., Lee J., Choe H., Shim K, & Kang D. (2023). COPA3 peptide supplementation alleviates the heat stress of chicken fibroblasts. Frontiers in Veterinary Science, 10, 985040.
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Publication 2023
brilliant blue G Cells Cytoskeleton Fibroblasts Methanol Microscopy Peptides Xylene

Top products related to «Cytoskeleton»

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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.
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Rhodamine phalloidin by Cytoskeleton
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Rhodamine phalloidin is a fluorescent probe that binds specifically to F-actin, the filamentous form of the actin protein. It is a useful tool for visualizing the actin cytoskeleton in cells.
4
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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.
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Alexa Fluor 488 phalloidin is a fluorescent dye that selectively binds to F-actin, a component of the cytoskeleton. It is used in microscopy and flow cytometry applications to visualize and study the distribution and organization of actin filaments within cells.
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Rhodamine phalloidin is a fluorescent dye used for staining and visualizing actin filaments in cells. It binds specifically to actin and can be used to label the cytoskeleton in fixed cells for microscopy analysis.
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4 6 diamidino 2 phenylindole (dapi) by Beyotime
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DAPI is a fluorescent dye used in molecular biology and microscopy to stain and visualize DNA. It selectively binds to the minor groove of double-stranded DNA, emitting a blue fluorescence when excited by ultraviolet light. DAPI is commonly used for nuclear staining and counterstaining in various applications such as fluorescence microscopy and flow cytometry.
10
Paraformaldehyde (pfa) by Merck Group
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Paraformaldehyde is a white, crystalline solid compound that is a polymer of formaldehyde. It is commonly used as a fixative in histology and microscopy applications to preserve biological samples.

More about "Cytoskeleton"

The cytoskelton is a complex, dynamic network of filaments and tubules that provide structural support and organization within eukaryotic cells.
This intricate cellular scaffolding is composed of three main components: microfilaments, intermediate filaments, and microtubules.
The cytoskeleton plays a crucial role in a variety of essential cellular processes, such as cell division, intracellular transport, cell motility, and signal transduction.
Proper cytoskeletal function is vital for cellular homeostasis and organismal development.
Disruptions to the cytoskeleton have been implicated in a range of diseases, including cancer, neurodegenerative disorders, and autoimmune conditions.
Researchers studying the cytoskeleton and its components are working to advance our fundamental understanding of cell biology and develop targeted therapeutic interventions.
Techniqes like DAPI staining, Rhodamine phalloidin labeling, and Triton X-100 permeabilization are commonly used to visualize and analyze the cytoskeleton.
Optimizing your cytoskeleton research with AI-driven platforms like PubCompare.ai can enhance reproducibility and accuracy.
These tools help researchers easily locate relevant protocols from literature, pre-prints, and patents, while leveraging AI-comparisons to identify the best methods and products for their experiments.
Improving the efficiency and reliability of cytoskeletal studies is crucial for driving progress in this vital field of cell biology.
Whether your focus is on micro-filaments, intermediate filaments, or microtubules, PubCompare.ai can help take your cytoskeleton research to the next level.