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Villin

Villin is a actin-binding protein found in the microvilli of intestinal epithelial cells.
It plays a key role in the organization and dynamics of the actin cytoskeleton, contributing to the maintenance of the intestinal absorptive surface.
Villin has been implicated in various cellular processes, including cell motitliy, vesicle trafficking, and signal transduction.
Researchers studying villin may leverage PubCompare.ai's AI-powered platform to quickly identify the most effective research protocols from the literature, preprints, and patents, streamlining their investigations and achieving better results.

Most cited protocols related to «Villin»

1
Detailed Molecular Dynamics Simulation Setup
Cited 70 times
Details of the MD simulation setup for each of the systems studied in this work can be found in SI Appendix, Table S16. All systems were simulated using the following force fields: a99SB*-ILDN (11 (link), 12 (link)) with TIP3P (13 ), C22* (14 (link)) with TIP3P-CHARMM (34 (link)), C36m (6 (link)), a03ws (containing modified TIP4P/2005 interactions) (8 (link)), a99SB and TIP4P-Ew (32 (link)) with the Head-Gordon vdW (9 (link)) and dihedral (33 (link)) modifications (termed a99SB-UCB), a99SB-ILDN (12 (link)) with TIP4P-D (7 (link)), and a99SB-disp. (The parameters for the a99SB-disp force field are listed in SI Appendix.) Systems were initially equilibrated at 300 K and 1 bar for 1 ns using the Desmond software (44 ). Production runs at 300 K were performed in the NPT ensemble (45 –47 (link, no link found)) with Anton specialized hardware (48 ) using a 2.5-fs time step and a 1:2 RESPA scheme (49 ). Bonds involving hydrogen atoms were restrained to their equilibrium lengths using the M-SHAKE algorithm (50 ). Nonbonded interactions were truncated at 12 Å, and the Gaussian split Ewald method (51 (link)) with a 32 × 32 × 32 mesh was used for the electrostatic interactions. All simulations were run at 300 K, with the exception of (AAQAA)3, CLN025, and the fast-folding proteins Trp-cage, villin, and GTT, which used simulated tempering (52 ) to improve sampling. In simulated tempering simulations of (AAQAA)3 and CLN025, 20 rungs were spaced geometrically spanning 278–390 K. In simulated tempering simulations of Trp-cage, villin, and GTT, 60 rungs were spaced geometrically spanning 278–400 K.
Robustelli P., Piana S, & Shaw D.E. (2018). Developing a molecular dynamics force field for both folded and disordered protein states. Proceedings of the National Academy of Sciences of the United States of America, 115(21), E4758-E4766.
Publication 2018
Electrostatics Folding, Protein Head Hydrogen Tremor villin YYDPETGTWY
2
Molecular Dynamics Simulations of Proteins and Peptides
Cited 37 times

Common methods. All production molecular dynamics simulations were performed on Anton [2] . Simulations were performed in the TIP3P water model ([32] ; for Amber and OPLS-AA force fields) or the CHARMM modified TIP3P water model ([18] (link), [32] ; for CHARMM force fields).
Simulations and analysis of the native state of ubiquitin and GB3. Production simulations of ubiquitin and GB3 were performed in the NVT ensemble. We used a 9.5-Å cutoff for the Lennard-Jones and short-range electrostatic interactions; long-range electrostatic interactions were treated with the Gaussian split Ewald method [33] (link). The starting structures for the simulations were the high-resolution NMR structures of ubiquitin ([34] ; PDB entry 1D3Z) and GB3 ([35] (link); PDB entry 1P7E). The structures were solvated in a cubic box with side lengths 58 Å, and were first minimized, heated to 300 K during 0.4 ns, and finally equilibrated in the NPT ensemble for 0.8 ns. The frame with the volume closest to the average during this NPT simulation was used as starting point for the production simulations in the NVT ensemble, thus ensuring that the average pressure in the simulations is close to the reference standard pressure. For both ubiquitin and GB3 we also performed simulations in the NPT ensemble (using ff99SB*-ILDN) and found that the calculated NMR observables are within error the same as those in the corresponding simulations in the NVT ensemble.
We calculated backbone scalar couplings using published Karplus relationships for HNHA, HNCO and HNCB [36] (link), and HACO [37] (link) couplings and compared to experimental data measured for ubiquitin ([38] ; HNHA, HNCO, HNCB and HACO) and GB3 ([36] (link); HNHA, HNCO and HNCB). We calculated backbone residual dipolar couplings and the associated Q scores as previously described [39] (link) and compared to experimental values in ubiquitin [34] and GB3 [35] (link). Order parameters were calculated from the values of the internal autocorrelation functions at lag times close to the experimentally determined rotational correlation times.
Simulated tempering simulations and analysis of AAQAA and CLN025 peptides. The temperature-dependent conformational properties of the (AAQAA)3[24] and CLN025 [25] (link) peptides were obtained using simulated tempering simulations [40] in the NPT ensemble. In contrast to the simulations of folded proteins or of protein folding, we found it necessary to perform these simulations in the NPT ensemble to avoid changing the average pressure as the temperature varied. We used a 9.5-Å cutoff for the Lennard-Jones and short-range electrostatic interactions; long-range electrostatic interactions were treated with the Gaussian split Ewald method [33] (link).
The helical fraction of the AAQAA-peptide was calculated as the fraction of helical residues [13] (link), [15] (link) at each temperature in the simulated tempering simulations and compared to the experimental values [24] . The fraction of the CLN025 that was folded was determined by applying a dual-cutoff approach [15] (link), [41] to separate the simulations into folded and unfolded states. In this analysis, a folding event was recorded if the Cα-RMSD to the experimental NMR structure dropped below 1.0 Å and an unfolding event was recorded once the same RMSD went above 4.0 Å.
Folding simulations of villin and WW domain. Simulations of fast-folding variants of villin [29] (link) and the WW domain [30] (link) were performed in the NVT ensemble using a Nose-Hoover thermostat and a force-shifted cutoff [42] (link) of 10.0 Å (villin) or 10.5 Å (WW domain) for the Lennard-Jones and electrostatic interactions. The starting structures for the simulations were heat-unfolded states of the two proteins in a cubic box of water with side length 52 Å. The simulations were performed near the experimental melting temperatures (at 360 K for villin and 370 K for the WW domain). For the WW domain, we recorded a folding event when the Cα-RMSDs (to PDB entry 2F21) calculated over four stretches of amino acids all were below the cutoff value: 2–33 (2.0 Å), 8–22 (1.1 Å), 12–18 (0.6 Å), 19–30 (0.9 Å). An unfolding event was recorded when the same set of RMSDs went above 7.0 Å, 5.8 Å, 1.8 Å and 3.8 Å, respectively. For villin, we recorded a folding event when the Cα-RMSDs (to PDB entry 2F4K) calculated over three stretches of amino acids were all below the cutoff value: 3–31 (1.2 Å), 3–18 (0.9 Å), 14–31 (0.9 Å). An unfolding event was recorded when the same set of RMSDs simultaneously went above 5.0 Å, 4.6 Å, and 2.5 Å, respectively.
Assigning a force field score. For each of the three sets of tests we manually assigned to each force field a number in the range 0–2, with 0 referring to a reasonable agreement, 1 to some agreement and 2 to severe discrepancies with respect to the experimental data. The assigned scores for each of these tests (folded proteins/peptides/folding) were 0/1/0 (ff99SB-ILDN), 0/0/0 (ff99SB*-ILDN), 1/2/1 (ff03), 1/1/0 (ff03*), 2/1/1 (OPLS-AA), 2/1/2 (CHARMM22), 0/2/1 (CHARMM27) and 0/0/0 (CHARMM22*). Each force field was then assigned an overall score (between 0 and 6) that was the sum of the values for each of the three tests. When evaluating the results of the simulations of the AAQAA and CLN025 peptides, we focused mostly on the temperature range around 280–320 K, where most biomolecular simulations are performed. Since simulations of the AAQAA peptide were used in the re-parameterization of the three helix coil–balanced force fields, one could argue that these results should not be included in the evaluation. The nature of the results presented in Figure 3, however, would not change even if the AAQAA tests were excluded. Finally, we stress that the assigned scores rely in part on subjective choices and that different sets of scores could be derived from the data presented in Figures 1 and 2 and Table 1.
Lindorff-Larsen K., Maragakis P., Piana S., Eastwood M.P., Dror R.O, & Shaw D.E. (2012). Systematic Validation of Protein Force Fields against Experimental Data. PLoS ONE, 7(2), e32131.
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Publication 2012
3
Microarray Analysis of AMP Genes
Cited 29 times
A glossary of terms used in the analysis is provided in Appendix S1.
The Affymetrix raw data (.cel files) were analyzed using Bioconductor tools [29] (link) in R (version 2.7.2, http://www.r-project.org/). The robust multichip average method [30] (link) was performed on the Affymetrix raw data (.cel files) to obtain a log2 expression value for each probe set. Probe set annotations were obtained through the Affymetrix NetAffx website (http://www.affymetrix.com/analysis/index.affx) or the UCSC Genome Browser website (http://genome.ucsc.edu/) or the NCBI website (http://www.ncbi.nlm.nih.gov/). For comparative analysis, linear models for microarray data (LIMMA) [31] (link) was performed for all the probe sets (54675 probe sets) present on the microarray to identify probe sets that are different between the groups, based on moderated t-statistics. To correct for multiple testing, the false discovery rate (FDR) was estimated from p-values derived from the moderated t-statistics using the method of Benjamini and Hochberg [32] . Probe sets with a>2-fold change (FC) and a FDR<0.05 were considered biologically significant. In this study, we focused on the microarray data of AMP genes. We selected the results from all performed comparative analyses for the probe sets encoding AMP genes, interleukin 8 (IL8) gene (probe set 202859_x_at) and villin 1 (VIL1) gene (probe set 205506_at) (Table S2).
Arijs I., De Hertogh G., Lemaire K., Quintens R., Van Lommel L., Van Steen K., Leemans P., Cleynen I., Van Assche G., Vermeire S., Geboes K., Schuit F, & Rutgeerts P. (2009). Mucosal Gene Expression of Antimicrobial Peptides in Inflammatory Bowel Disease Before and After First Infliximab Treatment. PLoS ONE, 4(11), e7984.
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Publication 2009
Genes Genome Interleukin-8 Microarray Analysis villin
4
Gαi1/Gαi3 Regulation of Glioma and Brain Metastatic Cancer
Cited 27 times
Ethics. Protocols of this study were approved by the Ethics Committee of Soochow University.
Reagents. From Gibco (Shanghai, China) cell culture reagents were obtained. The antibodies were described early 26 (link). NLGN3, pertussis toxin (PTX), LY294002 and PD98059 were purchased from Sigma-Aldrich (St. Louis, Mo). All primers, sequences and viral constructs were provided by Shanghai Genechem Co. (Shanghai, China), unless otherwise mentioned.
Cell lines. U251MG glioma cell line was obtained from the Cell Bank of Shanghai Biological Institution (Shanghai, China), cultivated as described. The cell line has previously been tested and authenticated by the Cell Bank of Shanghai Biological Institution. Wild-type (WT), Gαi1 and Gαi3 double knockout (DKO), Gαi1, Gαi2 or Gαi3 single knockout (SKO) mouse embryonic fibroblasts (MEFs), as well as WT and Gab1 KO MEFs, were cultivated as previously described 25 (link), 27 (link)-30 (link). Cells were starved in 0.5% FBS medium overnight plus 30 min warm PBS for signaling analyses.
Human glioma tissues. According to principles of the Declaration of Helsinki, this study was approved by the Ethics Committee of Soochow University. Human tissues, including the glioma tissues and surrounding normal brain tissues, were described previously 26 (link). Tissues were obtained from The First, Second, Third Affiliated and Children Hospitals of Soochow University. All participates provided written-informed consent.
Primary culture of human cancer cells. The source and culturing of primary human glioma cells were previously described 26 (link). From a lung cancer patient with brain metastases (female, 50 years old, brain metastatic lung papillary adenocarcinoma, CK7+, CK20—, Villin—, TTF-1+, CDX2—, PAX8—, CD10—, CAIX—, PR—, EMA+, GFAP—), surgical removed brain metastatic cancer tissues were washed, minced into small pieces, and digested with Collagenase I and DNase (Sigma-Aldrich). Single-cell suspensions were then pelleted and washed. Fibroblasts, blood vessel cells, immune cells and other non-cancerous cells were abandoned. Purified brain-metastatic human lung cancer cells (bmLCs) were ex vivo cultured in the described medium 31 (link). The study protocols were reviewed and approved by the Ethics Committee of Soochow University, and conformed to the guidelines of Helsinki declaration. The informed consent was obtained from all subjects before their participation.
Quantitative real-time reverse transcriptase polymerase chain reaction (qPCR). As described, qPCR was carried out by an ABI 7600 Prism equipment through utilizing a SYBR Green PCR kit. Gαi3 and NLGN3 mRNA levels were quantified by a ΔΔCt protocol 32 (link), using GAPDH as the internal control 26 (link). Primers are listed in Table 1.
Western blotting and co-immunoprecipitation. Protocols for Western blotting and co-immunoprecipitation (co-IP), as well as data quantification, have been extensively described previously 25 (link), 28 (link). For all Western blotting assays, each lane was loaded with exact same amount of quantified protein lysates (30-40 μg in each treatment). Same set of lysate samples were run in parallel (“sister”) gels to test different proteins when necessary. Expression of indicated proteins was quantified via ImageJ software, with results normalized to the equal loadings.
Endosome fractions. Cells with the applied treatments were harvested and re-suspended in the hypotonic swelling buffer 33 (link), and lysed with 30 strokes in a Dounce homogenizer using a tight pestle, and swelling was stopped by the addition of two fold homogenization buffer 33 (link). Lysates were centrifuged to obtain the post-nuclear supernatants, and centrifuged 33 (link). The resulting supernatants were centrifuged, and the pellet solubilized in the homogenization buffer 33 (link). Insoluble particles were removed by short centrifugation and the supernatant loaded onto a 5-20% continuous OptiprepTM (Sigma-Aldrich), poured using homogenization buffer. The gradient was further centrifuged at 60,000 g for 24h, with total 10 endosomal fractions collected, and proteins precipitated with 12% TCA for 1h. Fractions were centrifuged at 12,000 g for 1h. The protein pellets, combining all ten endosomal fractions, were dissolved in SDS-sample buffer for analysis by Western blotting.
Gαi1/3 shRNA. Glioma cells or bmLCs were seeded into six-well plates at 50-60% confluence, treated with Gαi1 shRNA lentiviral particles (sc-105382-V) (Santa Cruz, CA) and Gαi3 shRNA lentiviral particles 29 (link). After 24h, cells were further cultured in puromycin (1.0 μg/mL)-containing complete medium for 12-14 days. Gαi1/3 knockdown (over 95% efficiency) in stable cells was confirmed by Western blotting. shRNA-mediated knockdown of Gαi1 and Gαi3 in MEFs was reported previously 27 (link)-29 (link). Gab1 shRNA lentiviral particles, for both human and mouse, were also obtained from Santa Cruz Biotech.
CRISPR/Cas9 knockout of Gαi1 and Gαi3. The lentiviral CRISPR/Cas-9 Gαi1 KO construct and the lentiviral CRISPR/Cas-9 Gαi3 KO construct were provided by Shanghai Genechem (Shanghai, China), transfected into MEFs, and selected with puromycin. Gαi1/3 knockout was confirmed by Western blotting. Control cells were treated with the empty vector with nonsense sgRNA (Santa Cruz Biotech). The sgRNA sequences used for Gαi1 and Gαi3 KO are listed in Table 1.
Gαi1/3 overexpression. The recombinant adenovirus containing full-length Gαi1 (“Ad-Gαi1”, human or mouse) and Gαi3 (“Ad-Gαi3”, human or mouse) were described earlier 29 (link). Virus was filtered, enriched and added to cultured MEFs, glioma cells or bmLCs. Stable cells were established following selection by puromycin, and Gαi1/3 overexpression confirmed by Western blotting.
Glioma cell functional assays. Cell growth, proliferation, CCK-8 viability and EdU staining assays 26 (link), 34 (link), 35 (link) and cell migration by the “Transwell” assays 29 (link), 36 (link), 37 (link), were carried out using previously described protocols.
The orthotopic primary-derived xenograft assay. For intracranial tumor implantation, primary human glioma cells or bmLCs (5 × 105 cells of each mouse in 200 µL of Matrigel gel/10% FBS medium, with different genetic treatments) were implanted using the previously described coordinates 26 (link), 38 (link). Magnetic resonance imaging (MRI) was carried out to visualize tumor xenografts. On the day when the first mouse in any group exhibited symptoms (severe fever, vomiting, or greater than 15% body weight loss), all groups were sacrificed and tumors isolated through surgery. Tumor volumes were measured by the formula: π/6 × larger diameter × (smaller diameter)2. Immunohistochemistry (IHC) was performed using the previously described procedures 26 (link). All animal procedures were approved by Soochow University Ethics Review Board.
Statistical analysis. The in vitro experiments were replicated three times or more, and data expressed as means ± standard deviation (SD). To examine statistical differences among different groups one-way ANOVA was carried out with multiple comparisons performed by post hoc Bonferroni test (SPSS 18.0). P values < 0.05 were considered statistically significant. A two-tailed unpaired t test (Excel 2007) was applied to examine significance between two treatment groups.
Wang Y., Liu Y.Y., Chen M.B., Cheng K.W., Qi L.N., Zhang Z.Q., Peng Y., Li K.R., Liu F., Chen G, & Cao C. (2021). Neuronal-driven glioma growth requires Gαi1 and Gαi3. Theranostics, 11(17), 8535-8549.
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Publication 2021
5
GPU-accelerated CpHMD Simulations of Protein Protonation
Cited 22 times
The Compute Unified Device Architecture (CUDA) code of the GB molecular dynamics method in the pmemd.cuda program33 (link) of Amber (version 2018)34 was modified. The energies, forces, and other numbers computed with the code matched those given by our CPU implementation, subject to the precision differences between the GPU and CPU code. As in the CPU implementation, the code is currently limited to using the GB-Neck2 model36 (link) for both conformational and titration dynamics. Although the method does not impose a limit on the total number of titration sites, the maximal number of titratable sites is currently set to an arbitrary number 1000 (Asp/Glu has 2 titratable groups due to double-site titration), which however can be changed in the future.
We performed single-pH simulations on 11 proteins: the 36-residue villin headpiece subdomain (HP36, pdbid 1VII), 45-residue binding domain of 2-oxoglutarate dehydrogenase multi-enzyme complex (BBL, pdbid 1W4H), 56-residue N-terminal domain of ribosomal protein L9 (NTL9, pdbid 1CQU), 56-residue turkey ovomucoid third domain (OMTKY, pdbid 1OMU), 105-residue reduced form of human thioredoxin (pdbid 1ERT), 129-residue hen egg-white lysozyme (HEWL, pdbid 2LZT), 143-residue hyperstable Δ+PHS variant of staphylococcal nuclease (SNase, pdbid 3BDC), 124-residue ribonuclease A (RNase A, pdbid 7RSA), 155-residue E. coli ribonuclease H (RNase HI, pdbid 2RN2), 185-residue oxidized form of Bacillus circulans xylanase (xylanase, pdbid 1BCX), and 389-residue unbound β-secretase 1 catalytic domain (BACE1, pdbid 1SGZ). These proteins have been previously used to validate our CPU implementation of the same continuous CpHMD method.35 (link)The initial structures for the simulations were taken from our previous paper.35 (link) We started from the PDB coordinates by adding acetylated N terminus and amidated C terminus caps, building any disulfide bonds, and adding hydrogens with the CHARMM program (version c42a1).37 (link) The protonation states of the titratable residues were set so that Asp/Glu were deprotonated and His/Lys/Arg/Cys/Tyr were protonated. The structures then underwent 50 steps of steepest descent minimization in GBSW implicit solvent38 (link) with a harmonic force constant of 50 kcal/mol/Å2 applied to each heavy atom. Next, dummy atoms were added to the Asp/Glu residues, and the structure was minimized for 10 steps of steepest descent and 10 steps of Newton-Raphson minimization. These final structures were then converted to the structure files with the Leap utility in Amber.34 All simulations used the Amber ff14SB force field39 (link) and the GB-Neck2 implicit-solvent model.36 (link) All bonds containing hydrogens were constrained with the SHAKE algorithm,40 the salt concentration was set to 0.15 M, and a 2 fs timestep was used. For the 2 proteins without His residues (HP36 and NTL9), 14 single-pH simulations were run with pH 1–7.5 in 0.5 unit increments, and for the other proteins 18 simulations were run with pH 1–9.5 in 0.5 unit increments. Each simulation lasted 2 ns except for BACE1 simulations which were extended to 10 ns each. The CpHMD settings and options were the same as in our previous replica-exchange simulations,35 (link) except that the latter also employed a pH replica-exchange protocol, in which exchanges between adjacent pH replicas were attempted every 250 MD steps (exchange attempt frequency of 2 ps−1). In the current work, we performed additional replica-exchange simulations for SNase and RNase H with exchanges attempted every 500 and 1000 MD steps which correspond to the exchange attempt frequencies of 1 ps−1 and 0.5 ps−1, respectively. Larger pH ranges were used in the replica-exchange simulations. For the 2 proteins without His, 16 replicas were used with pH 0–7.5 in increments of 0.5 units, and for the other proteins 20 replicas with pH ranging from 0–9.5 in increments of 0.5 units were used.
To calculate pKa’s, the probability of deprotonation (unprotonated fraction) was fit to the generalized Henderson-Hasselbalch (HH) equation, as in our previous work.35 (link) For simplicity, the word generalized will be omitted in later discussions. The statistical errors in the pKa’s were estimated from the covariances of the fit parameters. For the macroscopic pKa of histidine, the total unprotonated fraction was used in the fitting. For the pKa’s of HID and HIE, the fractions of the respective tautomers were used (see more explanation in the footnote of Table 1).
Harris R.C, & Shen J. (2019). GPU-Accelerated Implementation of Continuous Constant pH Molecular Dynamics in Amber: pKa Predictions with Single-pH Simulations. Journal of chemical information and modeling, 59(11), 4821-4832.
Publication 2019

Most recents protocols related to «Villin»

1
Conditional Eif3h Knockout in Colitis-Associated Colorectal Cancer
Male Eif3hflox/wt mice on the C57BL/6 background were generated by the CRISPR/Cas9 method (GemPharmatech Co., Ltd., China). Eif3hflox/wt mice were intercrossed with Villin-CreERT mice to obtain Eif3hflox/wt, Villin-CreERT mice, as Eif3hflox/flox, Villin-CreERT mice were not viable. To induce heterozygous conditional Eif3h knockout, the female Eif3hflox/wt, Villin-CreERT mice were intraperitoneally injected with 50 mg/kg tamoxifen at an age of 4–5 weeks for five consecutive days. Three days after the last injection of tamoxifen, Eif3hflox/wt mice and Eif3hflox/wt, Villin-CreERT mice were injected once with AOM (10 mg/kg, intraperitoneally). 5 days later, mice were given 2% dextran sulfate sodium (DSS) (MP Biomedicals) in drinking water for 7 days followed by 2 weeks of regular drinking water. DSS treatments were repeated for two additional cycles, and mini-endoscopy was used to monitored tumor development. The mice were sacrificed on day 84 after the AOM injection.
Jin H., Huang X., Pan Q., Ma N., Xie X., Wei Y., Yu F., Wen W., Zhang B., Zhang P., Chen X., Wang J., Liu R.Y., Lin J., Meng X, & Lee M.H. (2024). The EIF3H-HAX1 axis increases RAF-MEK-ERK signaling activity to promote colorectal cancer progression. Nature Communications, 15, 2551.
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Publication 2024
2
Transgenic Murine Model for Autoimmune Studies
Mice were bred and housed in the Freimann Life Sciences Center at the University of Notre Dame (protocol#23-03-7746). No anesthesia or analgesia was performed. Euthanasia was performed by carbon dioxide asphyxiation with secondary cervical dislocation. All protocols were performed at the University of Notre Dame Freimann Life Science Center approved by Institutional Animal Care and Use Committees. All mice were bred and maintained on the C57BL/6 background. The villin-TNFAIP3 strain was generated previously using BAC-recombineering of the villin locus and characterized as described [9 (link)]. RAG1-/- and Rorc-/- mice (C57Bl/6) were purchased from Jackson Laboratories and interbred to villin-TNFAIP3 mice to generate villin-TNFAIP3 × RAG1-/- (TRAG) mice, Rorc-/- x TRAG mice, or RAG1-/- littermate controls.
Torres-Huerta A., Ruley-Haase K., Reed T., Boger-May A., Rubadeux D., Mayer L., Rajashekara A.M., Hiller M., Frech M., Roncagli C., Pedersen C., Camacho M.C., Hollmer L., English L., Kane G, & Boone D.L. (2024). Retinoid orphan receptor gamma t (rorγt) promotes inflammatory eosinophilia but is dispensable for innate immune-mediated colitis. PLOS ONE, 19(3), e0300892.
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Publication 2024
3
Sirolimus Attenuates GVHD in Villin-Cre+ Atg5-/- Mice
Villin-Cre+Atg5–/– (B6 Villin-KO), Villin-Cre–Atg5fl/fl littermate control (B6 WT), and C57BL/6 mice were used as BMT recipients, as described above. After BMT on day 0, recipients started daily intraperitoneal injections of either diluent control (CMC) or sirolimus (2rapamycin; Cayman Chemical) at a dose of 4.5 mg/kg/mouse for 14 days, after which dosing shifted to 3 d/wk for the remainder of the study. GVHD scoring was recorded weekly (50 (link)).
Oravecz-Wilson K., Lauder E., Taylor A., Maneix L., Van Nostrand J.L., Sun Y., Li L., Zhao D., Liu C, & Reddy P. (2024). Autophagy differentially regulates tissue tolerance of distinct target organs in graft-versus-host disease models. The Journal of Clinical Investigation, 134(5), e167369.
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Publication 2024
4
Villin-Cre and Lsd1 Knockout Mice
Villin-Cre (Jackson Laboratories, Strain #: 021504, RRID:IMSR_JAX:021504), Villin-CreERT227 (link) (kind gift from Dr. Robine), and Lsd1f/f 69 (link) (kind gift from Stuart Orkin) mice were housed in CoMed. Villin-Cre Lsd1f/f (cKO) mice were housed under specific-pathogen-free (SPF) conditions, and Villin-CreERT2 Lsd1f/f (icKO) mice were maintained in the minimal disease unit at CoMed. Mice were housed with controlled temperature between 21 and 22 degrees Celsius and relative humidity between 45 and 60%. The animals are housed in a 12-h dark/12-h light cycle, with 1 h of dusk/dawn. All mice used were between 8–14 weeks of age. By conventionally bred or conventionally raised animals, we refer to mice (of all genotypes) housed in these conditions and not treated with antibiotics.
Díez-Sánchez A., Lindholm H.T., Vornewald P.M., Ostrop J., Yao R., Single A.B., Marstad A., Parmar N., Shaw T.N., Martín-Alonso M, & Oudhoff M.J. (2024). LSD1 drives intestinal epithelial maturation and controls small intestinal immune cell composition independent of microbiota in a murine model. Nature Communications, 15, 3412.
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Publication 2024
5
Genetically Engineered Colon Cancer Mouse Model
To generate the genetically engineered CRC mouse model, the Villin-CreERT2 mice were crossed with LSL-KrasG12D/+ mice and Apcflox/+ mice to obtain Villin-CreERT2Apcflox/+ (KrasWT) or Villin-CreERT2KrasG12D/+Apcflox/+ (KrasMUT) mice. Each group consisted of five mice. When mice were at the age of 8 weeks, 1 mg/mL 4-hydroxytamoxifen (4-OHT) was introduced into the adult colon via enema. All mice were sacrificed 10 weeks later, and the colonic tumors were for IHC analysis and flow cytometry.
Zhou C., Li W., Liang Z., Wu X., Cheng S., Peng J., Zeng K., Li W., Lan P., Yang X., Xiong L., Zeng Z., Zheng X., Huang L., Fan W., Liu Z., Xing Y., Kang L, & Liu H. (2024). Mutant KRAS-activated circATXN7 fosters tumor immunoescape by sensitizing tumor-specific T cells to activation-induced cell death. Nature Communications, 15, 499.
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Publication 2024

Top products related to «Villin»

1
Tamoxifen by Merck Group
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Tamoxifen is a drug used in the treatment of certain types of cancer, primarily breast cancer. It is a selective estrogen receptor modulator (SERM) that can act as both an agonist and antagonist of the estrogen receptor. Tamoxifen is used to treat and prevent breast cancer in both men and women.
2
Villin cre mice by Jackson ImmunoResearch
Sourced in United States, Montenegro
Villin-Cre mice are a genetically engineered strain of mice that express the Cre recombinase enzyme under the control of the villin promoter. Villin is a protein found in the intestinal epithelial cells of mice. The Cre recombinase enzyme can be used to induce site-specific genetic modifications in the intestinal cells of these mice.
3
Villin cre by Jackson ImmunoResearch
Sourced in United States
Villin-Cre is a lab equipment product that serves as a genetic tool for research purposes. It is used to enable cell-specific gene expression or deletion in the intestinal epithelium of mice.
4
Anti villin by Santa Cruz Biotechnology
Sourced in United States
Anti-villin is a laboratory reagent used in scientific research. It is a specific antibody that recognizes and binds to the villin protein, which is a key component of the cytoskeleton in certain cell types. Anti-villin can be used in various experimental techniques, such as Western blotting, immunohistochemistry, and immunocytochemistry, to detect and analyze the presence and distribution of villin in biological samples.
5
Lgr5 egfp ires creert2 by Jackson ImmunoResearch
Sourced in United States, Montenegro
The Lgr5-EGFP-IRES-CreERT2 is a genetically modified mouse strain that expresses the enhanced green fluorescent protein (EGFP) and a tamoxifen-inducible Cre recombinase (CreERT2) under the control of the Lgr5 gene promoter. Lgr5 is a marker for adult stem cells in several tissues. This mouse model allows for the identification and tracking of Lgr5-expressing cells.
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C57bl 6 by Jackson ImmunoResearch
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C57BL/6 is a widely used inbred mouse strain. It is a robust, readily available laboratory mouse model.
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Dextran sulfate sodium (dss) by MP Biomedicals
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The DSS is a laboratory instrument designed for the separation and analysis of molecules and particles in complex samples. It utilizes a specialized technique called differential sedimentation to achieve precise separation and characterization of the components within a sample. The core function of the DSS is to provide accurate and reliable data on the size, distribution, and concentration of the analytes present, without interpretation or extrapolation on its intended use.
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Villin by Santa Cruz Biotechnology
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Villin is a cytoskeletal protein found in the microvilli of epithelial cells. It is responsible for the organization and maintenance of the actin cytoskeleton within these specialized membrane protrusions.
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Anti β actin by Merck Group
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Anti-β-actin is a laboratory reagent used to detect and quantify the presence of the β-actin protein, which is a widely expressed cytoskeletal protein found in eukaryotic cells. It is commonly used as a control or reference protein in various biochemical and cell biology techniques, such as Western blotting and immunocytochemistry.
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Rneasy mini kit by Qiagen
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The RNeasy Mini Kit is a laboratory equipment designed for the purification of total RNA from a variety of sample types, including animal cells, tissues, and other biological materials. The kit utilizes a silica-based membrane technology to selectively bind and isolate RNA molecules, allowing for efficient extraction and recovery of high-quality RNA.

More about "Villin"

Villin, an actin-binding protein, plays a crucial role in the organization and dynamics of the intestinal epithelial cell cytoskeleton.
This versatile protein is found in the microvilli of intestinal epithelial cells, contributing to the maintenance of the absorptive surface.
Villin has been implicated in various cellular processes, including cell motility, vesicle trafficking, and signal transduction.
Researchers studying villin may leverage PubCompare.ai's AI-powered platform to quickly identify the most effective research protocols from the literature, preprints, and patents, streamlining their investigations and achieving better results.
The platform's advanced AI comparisons can help researchers locate the best protocols, identify the most effective methods and products, and gain data-driven insights to optimize their villin studies.
Villin-Cre mice, a genetic model, have been used extensively in research to investigate the role of villin in intestinal development and function.
Anti-villin antibodies are also commonly used to detect and quantify villin expression in various experimental settings.
Additionally, the Lgr5-EGFP-IRES-CreERT2 mouse model, which labels intestinal stem cells, has been utilized to study the relationship between villin and intestinal stem cell biology.
Tamoxifen, a selective estrogen receptor modulator, has been used in conjunction with Villin-Cre mice to induce the expression of Cre recombinase and study the specific roles of villin in the intestine.
The RNeasy Mini Kit, a widely-used RNA extraction method, can be employed to isolate high-quality RNA from intestinal samples for villin gene expression analysis.
In villin-related research, the C57BL/6 mouse strain is often used as a common genetic background.
The dextran sulfate sodium (DSS) model of colitis has also been leveraged to investigate the impact of villin on intestinal inflammation and tissue repair.
By incorporating these related terms, abbreviations, and key subtopics, researchers can enhance their understanding of villin and its role in intestinal biology, ultimately streamlining their investigations and achieving better results with the help of PubCompare.ai's AI-powered platform.