Bullet Blender Publications: Cultured Cells

Publications that use the Bullet Blender® to process cultured cells, including bacteria and tissue culture.

Rasool, A., Ahmed, M. S., & Li, C. (2016). Overproduction of squalene synergistically downregulates ethanol production in Saccharomyces cerevisiae. Chemical Engineering Science, 152, 370–380. https://doi.org/10.1016/j.ces.2016.06.014
Orgil, O., Mor, H., Matityahu, A., & Onn, I. (2016). Identification of a region in the coiled-coil domain of Smc3 that is essential for cohesin activity. Nucleic Acids Research, gkw539. https://doi.org/10.1093/nar/gkw539
Shwartz, M., Matityahu, A., & Onn, I. (2016). Identification of Functional Domains in the Cohesin Loader Subunit Scc4 by a Random Insertion/Dominant Negative Screen. G3: Genes|Genomes|Genetics, g3.116.031674. https://doi.org/10.1534/g3.116.031674
Mashock, M. J. (2016). Examining mechanism of toxicity of copper oxide nanoparticles to Saccharomyces cerevisiae and Caenorhabditis elegans. Marquette University.
Thapa, H. R., Naik, M. T., Okada, S., Takada, K., Molnár, I., Xu, Y., & Devarenne, T. P. (2016). A squalene synthase-like enzyme initiates production of tetraterpenoid hydrocarbons in Botryococcus braunii Race L. Nature Communications, 7, 11198. https://doi.org/10.1038/ncomms11198
Otwell, A. E., Callister, S. J., Zink, E. M., Smith, R. D., & Richardson, R. E. (2016). Comparative Proteomic Analysis of Desulfotomaculum reducens MI-1: Insights into the Metabolic Versatility of a Gram-Positive Sulfate- and Metal-Reducing Bacterium. Frontiers in Microbiology, 7. https://doi.org/10.3389/fmicb.2016.00191
Pomraning, K. R., Kim, Y.-M., Nicora, C. D., Chu, R. K., Bredeweg, E. L., Purvine, S. O., Hu, D., Metz, T. O., & Baker, S. E. (2016). Multi-omics analysis reveals regulators of the response to nitrogen limitation in Yarrowia lipolytica. BMC Genomics, 17, 138. https://doi.org/10.1186/s12864-016-2471-2
Park, S. J., Lee, H. W., Kim, H.-R., Kang, C., & Kim, H. M. (2016). A carboxylesterase-selective ratiometric fluorescent two-photon probe and its application to hepatocytes and liver tissues. Chem. Sci., 7(6), 3703–3709. https://doi.org/10.1039/C5SC05001D
Glatz, A., Pilbat, A.-M., Németh, G. L., Vince-Kontár, K., Jósvay, K., Hunya, Á., Udvardy, A., Gombos, I., Péter, M., Balogh, G., Horváth, I., Vígh, L., & Török, Z. (2015). Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe. Cell Stress and Chaperones. https://doi.org/10.1007/s12192-015-0662-4
Lee, D., Ahn, C., An, B.-S., & Jeung, E.-B. (2015). Induction of the Estrogenic Marker Calbindn-D9k by Octamethylcyclotetrasiloxane. International Journal of Environmental Research and Public Health, 12(11), 14610–14625. https://doi.org/10.3390/ijerph121114610
Avbelj, M., Zupan, J., Kranjc, L., & Raspor, P. (2015). Quorum-Sensing Kinetics in Saccharomyces cerevisiae : A Symphony of ARO Genes and Aromatic Alcohols. Journal of Agricultural and Food Chemistry, 63(38), 8544–8550. https://doi.org/10.1021/acs.jafc.5b03400
Upadhyay, A., Fontes, F. L., Gonzalez-Juarrero, M., McNeil, M. R., Crans, D. C., Jackson, M., & Crick, D. C. (2015). Partial Saturation of Menaquinone in Mycobacterium tuberculosis : Function and Essentiality of a Novel Reductase, MenJ. ACS Central Science, 1(6), 292–302. https://doi.org/10.1021/acscentsci.5b00212
Giengkam, S., Blakes, A., Utsahajit, P., Chaemchuen, S., Atwal, S., Blacksell, S. D., Paris, D. H., Day, N. P. J., & Salje, J. (2015). Improved Quantification, Propagation, Purification and Storage of the Obligate Intracellular Human Pathogen Orientia tsutsugamushi. PLOS Neglected Tropical Diseases, 9(8), e0004009. https://doi.org/10.1371/journal.pntd.0004009
Orgil, O., Matityahu, A., Eng, T., Guacci, V., Koshland, D., & Onn, I. (2015). A Conserved Domain in the Scc3 Subunit of Cohesin Mediates the Interaction with Both Mcd1 and the Cohesin Loader Complex. PLOS Genetics, 11(3), e1005036. https://doi.org/10.1371/journal.pgen.1005036
Merkley, E. D., Wrighton, K. C., Castelle, C. J., Anderson, B. J., Wilkins, M. J., Shah, V., Arbour, T., Brown, J. N., Singer, S. W., Smith, R. D., & Lipton, M. S. (2015). Changes in Protein Expression Across Laboratory and Field Experiments in Geobacter bemidjiensis. Journal of Proteome Research, 14(3), 1361–1375. https://doi.org/10.1021/pr500983v
Sahu, R. (2015). Expression of the platelet-activating factor receptor enhances benzyl isothiocyanate-induced apoptosis in murine and human melanoma cells. Molecular Medicine Reports. https://doi.org/10.3892/mmr.2015.3371
de la Torre, A., Metivier, A., Chu, F., Laurens, L. M. L., Beck, D. A. C., Pienkos, P. T., Lidstrom, M. E., & Kalyuzhnaya, M. G. (2015). Genome-scale metabolic reconstructions and theoretical investigation of methane conversion in Methylomicrobium buryatense strain 5G(B1). Microbial Cell Factories, 14(1). https://doi.org/10.1186/s12934-015-0377-3
Sanchez-Ingunza, R., Guard, J., Morales, C. A., & Icard, A. H. (2015). Reduction of Salmonella Enteritidis in the Spleens of Hens by Bacterins That Vary in Fimbrial Protein SefD. Foodborne Pathogens and Disease, 12(10), 836–843. https://doi.org/10.1089/fpd.2015.1971
Lydic, T. A., Townsend, S., Adda, C. G., Collins, C., Mathivanan, S., & Reid, G. E. (2015). Rapid and comprehensive ‘shotgun’ lipidome profiling of colorectal cancer cell derived exosomes. Methods, 87, 83–95. https://doi.org/10.1016/j.ymeth.2015.04.014
Lemon, D. D., Harrison, B. C., Horn, T. R., Stratton, M. S., Ferguson, B. S., Wempe, M. F., & McKinsey, T. A. (2015). Promiscuous actions of small molecule inhibitors of the protein kinase D-class IIa HDAC axis in striated muscle. FEBS Letters, 589(10), 1080–1088. https://doi.org/10.1016/j.febslet.2015.03.017
Zhang, Z., He, L., Hu, S., Wang, Y., Lai, Q., Yang, P., Yu, Q., Zhang, S., Xiong, F., Simsekyilmaz, S., Ning, Q., Li, J., Zhang, D., Zhang, H., Xiang, X., Zhou, Z., Sun, H., & Wang, C.-Y. (2015). AAL exacerbates pro-inflammatory response in macrophages by regulating Mincle/Syk/Card9 signaling along with the Nlrp3 inflammasome assembly. American Journal of Translational Research, 7(10), 1812–1825.
Orellana, R., Hixson, K. K., Murphy, S., Mester, T., Sharma, M. L., Lipton, M. S., & Lovley, D. R. (2014). Proteome of Geobacter sulfurreducens in the presence of U(VI). Microbiology, 160(Pt_12), 2607–2617. https://doi.org/10.1099/mic.0.081398-0
Shemesh, A., Wang, Y., Yang, Y., Yang, G.-S., Johnson, D. E., Backer, J. M., Pessin, J. E., & Zong, H. (2014). Suppression of mTORC1 activation in acid- -glucosidase-deficient cells and mice is ameliorated by leucine supplementation. AJP: Regulatory, Integrative and Comparative Physiology, 307(10), R1251–R1259. https://doi.org/10.1152/ajpregu.00212.2014
Offer, S. M., Fossum, C. C., Wegner, N. J., Stuflesser, A. J., Butterfield, G. L., & Diasio, R. B. (2014). Comparative functional analysis of DPYD variants of potential clinical relevance to dihydropyrimidine dehydrogenase activity. Cancer Research, 74(9), 2545–2554. https://doi.org/10.1158/0008-5472.CAN-13-2482
Caruso, V., Hägglund, M. G., Badiali, L., Bagchi, S., Roshanbin, S., Ahmad, T., Schiöth, H. B., & Fredriksson, R. (2014). The G protein-coupled receptor GPR162 is widely distributed in the CNS and highly expressed in the hypothalamus and in hedonic feeding areas. Gene, 553(1), 1–6. https://doi.org/10.1016/j.gene.2014.09.042
Henrich, M., Huber, K., Rydzewski, L., Kirsten, S., Spengler, B., Römpp, A., & Reinacher, M. (2014). Identification of T cell receptor signaling pathway proteins in a feline large granular lymphoma cell line by liquid chromatography tandem mass spectrometry. Veterinary Immunology and Immunopathology, 161(1–2), 116–121. https://doi.org/10.1016/j.vetimm.2014.06.004
Bartnikowski, M., Klein, T. J., Melchels, F. P. W., & Woodruff, M. A. (2014). Effects of scaffold architecture on mechanical characteristics and osteoblast response to static and perfusion bioreactor cultures: Scaffold Architecture Static Perfusion Bioreactor. Biotechnology and Bioengineering, 111(7), 1440–1451. https://doi.org/10.1002/bit.25200
Kurtzman, C. P., & Robnett, C. J. (2014). Three new anascosporic genera of the Saccharomycotina: Danielozyma gen. nov., Deakozyma gen. nov. and Middelhovenomyces gen. nov. Antonie van Leeuwenhoek, 105(5), 933–942. https://doi.org/10.1007/s10482-014-0149-9
Menon, R., Boldogh, I., Urrabaz-Garza, R., Polettini, J., Syed, T. A., Saade, G. R., Papaconstantinou, J., & Taylor, R. N. (2013). Senescence of Primary Amniotic Cells via Oxidative DNA Damage. PLoS ONE, 8(12), e83416. https://doi.org/10.1371/journal.pone.0083416
Ullah, A., Kemp, G., Lee, B., Alves, C., Young, H., Sykes, B. D., & Fliegel, L. (2013). Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2. Journal of Biological Chemistry, 288(34), 24609–24624. https://doi.org/10.1074/jbc.M113.483065
Townsend, K. L., An, D., Lynes, M. D., Huang, T. L., Zhang, H., Goodyear, L. J., & Tseng, Y.-H. (2013). Increased Mitochondrial Activity in BMP7-Treated Brown Adipocytes, Due to Increased CPT1- and CD36-Mediated Fatty Acid Uptake. Antioxidants & Redox Signaling, 19(3), 243–257. https://doi.org/10.1089/ars.2012.4536
Tong, K., Zhang, Y., Liu, G., Ye, Z., & Chu, P. K. (2013). Treatment of heavy oil wastewater by a conventional activated sludge process coupled with an immobilized biological filter. International Biodeterioration & Biodegradation, 84, 65–71. https://doi.org/10.1016/j.ibiod.2013.06.002
Nicora, C. D., Anderson, B. J., Callister, S. J., Norbeck, A. D., Purvine, S. O., Jansson, J. K., Mason, O. U., David, M. M., Jurelevicius, D., Smith, R. D., & Lipton, M. S. (2013). Amino acid treatment enhances protein recovery from sediment and soils for metaproteomic studies. PROTEOMICS, n/a-n/a. https://doi.org/10.1002/pmic.201300003
Kurtzman, C. P., & Robnett, C. J. (2013). Alloascoidea hylecoeti gen. nov., comb. nov., Alloascoidea africana comb. nov., Ascoidea tarda sp. nov., and Nadsonia starkeyi-henricii comb. nov., new members of the Saccharomycotina ( Ascomycota ). FEMS Yeast Research, 13(5), 423–432. https://doi.org/10.1111/1567-1364.12044
Thoene, J., Goss, T., Witcher, M., Mullet, J., N’Kuli, F., Van Der Smissen, P., Courtoy, P., & Hahn, S. H. (2013). In vitro correction of disorders of lysosomal transport by microvesicles derived from baculovirus-infected Spodoptera cells. Molecular Genetics and Metabolism, 109(1), 77–85. https://doi.org/10.1016/j.ymgme.2013.01.014
Liu, G., Ye, Z., Tong, K., & Zhang, Y. (2013). Biotreatment of heavy oil wastewater by combined upflow anaerobic sludge blanket and immobilized biological aerated filter in a pilot-scale test. Biochemical Engineering Journal, 72, 48–53. https://doi.org/10.1016/j.bej.2012.12.017
Sarachana, T., & Hu, V. W. (2013). Genome-wide identification of transcriptional targets of RORA reveals direct regulation of multiple genes associated with autism spectrum disorder. Molecular Autism, 4(1), 14. https://doi.org/10.1186/2040-2392-4-14
Wiedner, S. D., Burnum, K. E., Pederson, L. M., Anderson, L. N., Fortuin, S., Chauvigne-Hines, L. M., Shukla, A. K., Ansong, C., Panisko, E. A., Smith, R. D., & Wright, A. T. (2012). Multiplexed Activity-based Protein Profiling of the Human Pathogen Aspergillus fumigatus Reveals Large Functional Changes upon Exposure to Human Serum. Journal of Biological Chemistry, 287(40), 33447–33459. https://doi.org/10.1074/jbc.M112.394106
Badrane, H., Nguyen, M. H., Blankenship, J. R., Cheng, S., Hao, B., Mitchell, A. P., & Clancy, C. J. (2012). Rapid Redistribution of Phosphatidylinositol-(4,5)-Bisphosphate and Septins during the Candida albicans Response to Caspofungin. Antimicrobial Agents and Chemotherapy, 56(9), 4614–4624. https://doi.org/10.1128/AAC.00112-12
Diaz-Campos, D. V. (2012). Molecular Epidemiology and Genetic Analysis of Staphylococcus species in Companion Animal Medicine. Auburn University.
Koles, K., Nunnari, J., Korkut, C., Barria, R., Brewer, C., Li, Y., Leszyk, J., Zhang, B., & Budnik, V. (2012). Mechanism of Evenness Interrupted (Evi)-Exosome Release at Synaptic Boutons. Journal of Biological Chemistry, 287(20), 16820–16834. https://doi.org/10.1074/jbc.M112.342667
Petrie, J. R., Vanhercke, T., Shrestha, P., El Tahchy, A., White, A., Zhou, X.-R., Liu, Q., Mansour, M. P., Nichols, P. D., & Singh, S. P. (2012). Recruiting a New Substrate for Triacylglycerol Synthesis in Plants: The Monoacylglycerol Acyltransferase Pathway. PLoS ONE, 7(4), e35214. https://doi.org/10.1371/journal.pone.0035214
Kochneva-Pervukhova, N. V., Alexandrov, A. I., & Ter-Avanesyan, M. D. (2012). Amyloid-Mediated Sequestration of Essential Proteins Contributes to Mutant Huntingtin Toxicity in Yeast. PLoS ONE, 7(1), e29832. https://doi.org/10.1371/journal.pone.0029832
Fanning, S., Xu, W., Beaurepaire, C., Suhan, J. P., Nantel, A., & Mitchell, A. P. (2012). Functional control of the Candida albicans cell wall by catalytic protein kinase A subunit Tpk1: Tpk1 control of C. albicans cell wall function. Molecular Microbiology, 86(2), 284–302. https://doi.org/10.1111/j.1365-2958.2012.08193.x
Thomas, S. N., Waters, K. M., Morgan, W. F., Yang, A. J., & Baulch, J. E. (2012). Quantitative proteomic analysis of mitochondrial proteins reveals prosurvival mechanisms in the perpetuation of radiation-induced genomic instability. Free Radical Biology and Medicine, 53(3), 618–628. https://doi.org/10.1016/j.freeradbiomed.2012.03.025
Kim, J. E., Eom, H.-J., Kim, Y., Ahn, J. E., Kim, J. H., & Han, N. S. (2012). Enhancing acid tolerance of Leuconostoc mesenteroides with glutathione. Biotechnology Letters, 34(4), 683–687. https://doi.org/10.1007/s10529-011-0815-1
Hou, X. (2012). Anaerobic xylose fermentation by Spathaspora passalidarum. Applied Microbiology and Biotechnology, 94(1), 205–214. https://doi.org/10.1007/s00253-011-3694-4
Hou, X., & Yao, S. (2012). Improved inhibitor tolerance in xylose-fermenting yeast Spathaspora passalidarum by mutagenesis and protoplast fusion. Applied Microbiology and Biotechnology, 93(6), 2591–2601. https://doi.org/10.1007/s00253-011-3693-5
Zinkeviciene, A., Girkontaite, I., & Citavicius, D. (2012). Specific immunoglobulin E antibodies to saprophytic yeasts in sera of atopic patients allergic to house dust mites. Journal of Investigational Allergology & Clinical Immunology, 22(6), 412–418.
Ganguly, S., Bishop, A. C., Xu, W., Ghosh, S., Nickerson, K. W., Lanni, F., Patton-Vogt, J., & Mitchell, A. P. (2011). Zap1 Control of Cell-Cell Signaling in Candida albicans Biofilms. Eukaryotic Cell, 10(11), 1448–1454. https://doi.org/10.1128/EC.05196-11

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