Ideal for Protein Extraction
Ideal preparation for aggresome extraction, activity assays, chromatin IP, cytokine assays, ELISA, HPLC, immunoassays, immunoblotting, Western blots, Southern blots, immunoprecipitation, SDS-PAGE, SDS-VAGE, protein fractionation, mass spectrometry and protein purification. Do you spend lots of time and effort homogenizing protein samples? The Bullet Blender® is a multi-sample homogenizer that delivers high quality and superior yields. No other homogenizer comes close to delivering the Bullet Blender’s winning combination of top-quality performance and budget-friendly affordability.
The Bullet Blender®
Save Time, Effort and Get Superior Results
- Consistent and High Yield Results
Run up to 24 samples at the same time under microprocessor-controlled conditions, ensuring experimental reproducibility and high yield. Process samples from 10mg or less up to 3.5g. - No Cross Contamination
No part of the Bullet Blender® ever touches the protein samples – the sample tubes are kept closed during homogenization. There are no probes to clean between samples. - Samples Stay Cool
Homogenizing causes only a few degrees of heating. Our Gold models keep samples at 4°C. - Easy and Convenient to Use
Just place beads and buffer along with your protein sample in standard tubes, load tubes directly in the Bullet Blender, select time and speed, and press start. - Risk Free Purchase
The Bullet Blender® comes with a 2 year warranty, with a 3 year warranty on the motor. The simple, reliable design enables the Bullet Blenders to sell for a fraction of the price of ultrasonic or other agitation based instruments, yet provides an easier, quicker technique.
Bullet Blender settings for Protein Extraction
Proteins can be extracted from almost any sample using the Bullet Blender. Explore our Protocols page to find a protocol appropriate for your sample.
Selected publications for Protein Extraction
See all of our Bullet Blender publications!
Santos, A. C. C., Gatto, M., Mota, G. A. F., Borim, P. A., Silva, R. C. F., Meirelles, A. L. B., Souza, L. M., Ojopi, E. P. B., Rodrigues, E. A., Pagan, L. U., Marreiros, A. P. S., Brandao, G., Zornoff, L. A. M., Maranhão, R. C., Okoshi, K., & Okoshi, M. P. (2026). Effects of Early Treatment with Lipid Core Nanoparticles-Associated Methotrexate on Cardiac Remodeling and Soleus Muscle Inflammasomes in Infarcted Rats. International Journal of Molecular Sciences, 27(9), 4140. https://doi.org/10.3390/ijms27094140
Hobby, E. L., Weber, A. J., Liu, E., Hurst, C., Greathouse, K. M., Gaiteri, C., Seyfried, N. T., & Herskowitz, J. H. (2026). A Multi-Network Approach Identifies Proteins Related to Dendritic Spines in Alzheimer’s Disease. Eneuro, 13(4), ENEURO.0468-25.2026. https://doi.org/10.1523/ENEURO.0468-25.2026
Fliflet, A. M., Tan, Y., Barnes, T. M., Vijayan, A. N., Choi, S. J., Deutz, M. T., Zupancic, Z., Spradlin, R. A., Miller, B. F., Burd, N. A., Sweedler, J. V., & Boppart, M. D. (2026). Human plasma extracellular vesicles as an exercise mimetic to preserve skeletal muscle plasticity during disuse. Npj Microgravity, 12(1), 48. https://doi.org/10.1038/s41526-026-00582-4
He, Y., Miggiels, P., Harms, A., Rijksen, Y., Brandt, R. M. C., Vermeij, W. P., Wouters, B., & Hankemeier, T. (2025). A fully automated, high-throughput electro-extraction and analysis workflow for acylcarnitines in human plasma and mouse muscle tissues. Analytica Chimica Acta, 1364, 344224. https://doi.org/10.1016/j.aca.2025.344224
Zizmare, L., Hofmann, U., Jarboui, M. A., Klose, F., Fraschka, S., Matthes, J., Krüger, M., Schaeffeler, E., Schwab, M., Ueffing, M., Pichler, B. J., Boldt, K., Casadei, N., & Trautwein, C. (2025). Cryogenic mouse tissue homogenization as an alternative to fresh-frozen biopsy use for genomics, transcriptomics, proteomics and metabolomics. Scientific Reports, 15(1), 20254. https://doi.org/10.1038/s41598-025-06438-3
Frostadottir, D., Welinder, C., Perez, R., & Dahlin, L. B. (2025). Refinement of Protein Extraction Protocols for Human Peripheral Nerve Tissue. ACS Omega, 10(5), 5111–5118. https://doi.org/10.1021/acsomega.4c11373
Tong, W.-, & Rouault, T. (2024). In-Gel Activity Assay of Mammalian Mitochondrial and Cytosolic Aconitases, Surrogate Markers of Compartment-Specific Oxidative Stress and Iron Status. BIO-PROTOCOL, 14(1360). https://doi.org/10.21769/BioProtoc.5126
McCabe, M., Saviola, A., & Hansen, K. (2024). Compartment-Resolved Proteomics with Deep Extracellular Matrix Coverage. BIO-PROTOCOL, 14(1360). https://doi.org/10.21769/BioProtoc.5123
Arıkan, M., Demir, T. K., Yıldız, Z., Nalbantoğlu, Ö. U., Korkmaz, N. D., Yılmaz, N. H., Şen, A., Özcan, M., Muth, T., Hanoğlu, L., & Yıldırım, S. (2023). Metaproteogenomic analysis of saliva samples from Parkinson’s disease patients with cognitive impairment. Npj Biofilms and Microbiomes, 9(1), 86. https://doi.org/10.1038/s41522-023-00452-x
Hamzelou, S., Belobrajdic, D., Juhász, A., Brook, H., Bose, U., Colgrave, M. L., & Broadbent, J. A. (2023). Nutrition, allergenicity and physicochemical qualities of food-grade protein extracts from Nannochloropsis oculata. Food Chemistry, 424, 136459. https://doi.org/10.1016/j.foodchem.2023.136459
Zaman, M., Fu, Y., Chen, P.-C., Sun, H., Yang, S., Wu, Z., Wang, Z., Poudel, S., Serrano, G. E., Beach, T. G., Li, L., Wang, X., & Peng, J. (2023). Dissecting Detergent-Insoluble Proteome in Alzheimer’s Disease by TMTc-Corrected Quantitative Mass Spectrometry. Molecular & Cellular Proteomics, 22(8), 100608. https://doi.org/10.1016/j.mcpro.2023.100608
Blackwood, S. J., Horwath, O., Moberg, M., Pontén, M., Apró, W., Ekblom, M. M., Larsen, F. J., & Katz, A. (2023). Insulin resistance after a 3-day fast is associated with an increased capacity of skeletal muscle to oxidize lipids. American Journal of Physiology-Endocrinology and Metabolism, 324(5), E390–E401. https://doi.org/10.1152/ajpendo.00317.2022
Beltrà, M., Pöllänen, N., Fornelli, C., Tonttila, K., Hsu, M. Y., Zampieri, S., Moletta, L., Corrà, S., Porporato, P. E., Kivelä, R., Viscomi, C., Sandri, M., Hulmi, J. J., Sartori, R., Pirinen, E., & Penna, F. (2023). NAD+ repletion with niacin counteracts cancer cachexia. Nature Communications, 14(1), 1849. https://doi.org/10.1038/s41467-023-37595-6
Chou, T.-J., Lu, C.-W., Lin, L.-Y., Hsu, Y.-J., Huang, C.-C., & Huang, K.-C. (2023). Proteomic Analysis of Skeletal Muscle and White Adipose Tissue after Aerobic Exercise Training in High Fat Diet Induced Obese Mice. International Journal of Molecular Sciences, 24(6), 5743. https://doi.org/10.3390/ijms24065743
Finicle, B. T., Eckenstein, K. H., Revenko, A. S., Anderson, B. A., Wan, W. B., McCracken, A. N., Gil, D., Fruman, D. A., Hanessian, S., Seth, P. P., & Edinger, A. L. (2023). Simultaneous inhibition of endocytic recycling and lysosomal fusion sensitizes cells and tissues to oligonucleotide therapeutics. Nucleic Acids Research, 51(4), 1583–1599. https://doi.org/10.1093/nar/gkad023
Macedo, G. C., Kreifeldt, M., Goulding, S. P., Okhuarobo, A., Sidhu, H., & Contet, C. (2023). Chronic MAP4343 reverses escalated alcohol drinking in a mouse model of alcohol use disorder. Neuropsychopharmacology. https://doi.org/10.1038/s41386-023-01529-z
Qian, L., Rawashdeh, O., Kasas, L., Milne, M. R., Garner, N., Sankorrakul, K., Marks, N., Dean, M. W., Kim, P. R., Sharma, A., Bellingham, M. C., & Coulson, E. J. (2022). Cholinergic basal forebrain degeneration due to sleep-disordered breathing exacerbates pathology in a mouse model of Alzheimer’s disease. Nature Communications, 13(1), 6543. https://doi.org/10.1038/s41467-022-33624-y
Lee, R. G., Balasubramaniam, S., Stentenbach, M., Kralj, T., McCubbin, T., Padman, B., Smith, J., Riley, L. G., Priyadarshi, A., Peng, L., Nuske, M. R., Webster, R., Peacock, K., Roberts, P., Stark, Z., Lemire, G., Ito, Y. A., Care4Rare Canada Consortium, Boycott, K. M., … Filipovska, A. (2022). Deleterious variants in CRLS1 lead to cardiolipin deficiency and cause an autosomal recessive multi-system mitochondrial disease. Human Molecular Genetics, 31(21), 3597–3612. https://doi.org/10.1093/hmg/ddac040
Killinger, B. J., Whidbey, C., Sadler, N. C., DeLeon, A. J., Munoz, N., Kim, Y.-M., & Wright, A. T. (2022). Activity-based protein profiling identifies alternating activation of enzymes involved in the bifidobacterium shunt pathway or mucin degradation in the gut microbiome response to soluble dietary fiber. Npj Biofilms and Microbiomes, 8(1), 60. https://doi.org/10.1038/s41522-022-00313-z
Rayaprolu, S., Bitarafan, S., Santiago, J. V., Betarbet, R., Sunna, S., Cheng, L., Xiao, H., Nelson, R. S., Kumar, P., Bagchi, P., Duong, D. M., Goettemoeller, A. M., Oláh, V. J., Rowan, M., Levey, A. I., Wood, L. B., Seyfried, N. T., & Rangaraju, S. (2022). Cell type-specific biotin labeling in vivo resolves regional neuronal and astrocyte proteomic differences in mouse brain. Nature Communications, 13(1), 2927. https://doi.org/10.1038/s41467-022-30623-x
Zhang, H., Dammer, E. B., Duong, D. M., Danelia, D., Seyfried, N. T., & Yu, D. S. (2022). Quantitative proteomic analysis of the lysine acetylome reveals diverse SIRT2 substrates. Scientific Reports, 12(1), 3822. https://doi.org/10.1038/s41598-022-06793-5
Leggett, A., Li, D.-W., Sindeldecker, D., Staats, A., Rigel, N., Bruschweiler-Li, L., Brüschweiler, R., & Stoodley, P. (2022). Cadaverine Is a Switch in the Lysine Degradation Pathway in Pseudomonas aeruginosa Biofilm Identified by Untargeted Metabolomics. Frontiers in Cellular and Infection Microbiology, 12, 833269. https://doi.org/10.3389/fcimb.2022.833269
Kralj, T., Nuske, M., Hofferek, V., Sani, M.-A., Lee, T.-H., Separovic, F., Aguilar, M.-I., & Reid, G. E. (2022). Multi-Omic Analysis to Characterize Metabolic Adaptation of the E. coli Lipidome in Response to Environmental Stress. Metabolites, 12(2), 171. https://doi.org/10.3390/metabo12020171
Geddes-McAlister, J. (Ed.). (2022). Proteomics in systems biology: methods and protocols. Humana Press.
Chepyala, S. R., Liu, X., Yang, K., Wu, Z., Breuer, A. M., Cho, J.-H., Li, Y., Mancieri, A., Jiao, Y., Zhang, H., & Peng, J. (2021). JUMPt: Comprehensive Protein Turnover Modeling of In Vivo Pulse SILAC Data by Ordinary Differential Equations. Analytical Chemistry, 93(40), 13495–13504. https://doi.org/10.1021/acs.analchem.1c02309
Roichman, A., Elhanati, S., Aon, M. A., Abramovich, I., Di Francesco, A., Shahar, Y., Avivi, M. Y., Shurgi, M., Rubinstein, A., Wiesner, Y., Shuchami, A., Petrover, Z., Lebenthal-Loinger, I., Yaron, O., Lyashkov, A., Ubaida-Mohien, C., Kanfi, Y., Lerrer, B., Fernández-Marcos, P. J., … Cohen, H. Y. (2021). Restoration of energy homeostasis by SIRT6 extends healthy lifespan. Nature Communications, 12(1), 3208. https://doi.org/10.1038/s41467-021-23545-7
Zhou, B., Thao, T. T. N., Hoffmann, D., Taddeo, A., Ebert, N., Labroussaa, F., Pohlmann, A., King, J., Steiner, S., Kelly, J. N., Portmann, J., Halwe, N. J., Ulrich, L., Trüeb, B. S., Fan, X., Hoffmann, B., Wang, L., Thomann, L., Lin, X., … Beer, M. (2021). SARS-CoV-2 spike D614G change enhances replication and transmission. Nature, 592(7852), 122–127. https://doi.org/10.1038/s41586-021-03361-1
McCabe, M. C., Schmitt, L. R., Hill, R. C., Dzieciatkowska, M., Maslanka, M., Daamen, W. F., Van Kuppevelt, T. H., Hof, D. J., & Hansen, K. C. (2021). Evaluation and Refinement of Sample Preparation Methods for Extracellular Matrix Proteome Coverage. Molecular & Cellular Proteomics, 20, 100079. https://doi.org/10.1016/j.mcpro.2021.100079
French, C. E., Sales, M. A., Rochell, S. J., Rodriguez, A., & Erf, G. F. (2020). Local and systemic inflammatory responses to lipopolysaccharide in broilers: new insights using a two-window approach. Poultry Science, 99(12), 6593–6605. https://doi.org/10.1016/j.psj.2020.09.078
Gallart-Palau, X., Guo, X., Serra, A., & Sze, S. K. (2020). Alzheimer’s disease progression characterized by alterations in the molecular profiles and biogenesis of brain extracellular vesicles. Alzheimer’s Research & Therapy, 12(1), 54. https://doi.org/10.1186/s13195-020-00623-4
Nguyen, H. M., Yadav, N. S., Barak, S., Lima, F. P., Sapir, Y., & Winters, G. (2020). Responses of Invasive and Native Populations of the Seagrass Halophila stipulacea to Simulated Climate Change. Frontiers in Marine Science, 6, 812. https://doi.org/10.3389/fmars.2019.00812
Traber, K. E., Dimbo, E. L., Symer, E. M., Korkmaz, F. T., Jones, M. R., Mizgerd, J. P., & Quinton, L. J. (2019). Roles of interleukin-11 during acute bacterial pneumonia. PLOS ONE, 14(8), e0221029. https://doi.org/10.1371/journal.pone.0221029
Wingo, A. P., Dammer, E. B., Breen, M. S., Logsdon, B. A., Duong, D. M., Troncosco, J. C., Thambisetty, M., Beach, T. G., Serrano, G. E., Reiman, E. M., Caselli, R. J., Lah, J. J., Seyfried, N. T., Levey, A. I., & Wingo, T. S. (2019). Large-scale proteomic analysis of human brain identifies proteins associated with cognitive trajectory in advanced age. Nature Communications, 10(1), 1619. https://doi.org/10.1038/s41467-019-09613-z
Sarasamma, S., Audira, G., Juniardi, S., Sampurna, B., Lai, Y.-H., Hao, E., Chen, J.-R., & Hsiao, C.-D. (2018). Evaluation of the Effects of Carbon 60 Nanoparticle Exposure to Adult Zebrafish: A Behavioral and Biochemical Approach to Elucidate the Mechanism of Toxicity. International Journal of Molecular Sciences, 19(12), 3853. https://doi.org/10.3390/ijms19123853
Mahinrad, S., Bulk, M., van der Velpen, I., Mahfouz, A., van Roon-Mom, W., Fedarko, N., Yasar, S., Sabayan, B., van Heemst, D., & van der Weerd, L. (2018). Natriuretic Peptides in Post-mortem Brain Tissue and Cerebrospinal Fluid of Non-demented Humans and Alzheimer’s Disease Patients. Frontiers in Neuroscience, 12, 864. https://doi.org/10.3389/fnins.2018.00864
Pinacho, R., Vila, E., Prades, R., Tarragó, T., Castro, E., Ferrer, I., & Ramos, B. (2016). The glial phosphorylase of glycogen isoform is reduced in the dorsolateral prefrontal cortex in chronic schizophrenia. Schizophrenia Research. https://doi.org/10.1016/j.schres.2016.04.024
Dong, Z., Ba, H., Zhang, W., Coates, D., & Li, C. (2016). iTRAQ-Based Quantitative Proteomic Analysis of the Potentiated and Dormant Antler Stem Cells. International Journal of Molecular Sciences, 17(11), 1778. https://doi.org/10.3390/ijms17111778
Kim, J. M., Park, S. K., Guo, T. J., Kang, J. Y., Ha, J. S., Lee, D. S., Lee, U., & Heo, H. J. (2016). Anti-amnesic effect of Dendropanax morbifera via JNK signaling pathway on cognitive dysfunction in high-fat diet-induced diabetic mice. Behavioural Brain Research, 312, 39–54. https://doi.org/10.1016/j.bbr.2016.06.013
Hubbard, J. A., Szu, J. I., Yonan, J. M., & Binder, D. K. (2016). Regulation of astrocyte glutamate transporter-1 (GLT1) and aquaporin-4 (AQP4) expression in a model of epilepsy. Experimental Neurology. https://doi.org/10.1016/j.expneurol.2016.05.003
Xiao, L., Cao, W., Liu, G., Fang, T., Wu, X., Jia, G., Chen, X., Zhao, H., Wang, J., Wu, C., & Cai, J. (2016). Arginine, N-carbamylglutamate, and glutamine exert protective effects against oxidative stress in rat intestine. Animal Nutrition. https://doi.org/10.1016/j.aninu.2016.04.005
Murray, H. C., Low, V. F., Swanson, M. E. V., Dieriks, B. V., Turner, C., Faull, R. L. M., & Curtis, M. A. (2016). Distribution of PSA-NCAM in normal, Alzheimer’s and Parkinson’s disease human brain. Neuroscience, 330, 359–375. https://doi.org/10.1016/j.neuroscience.2016.06.003
Krutzke, L., Prill, J. M., Engler, T., Schmidt, C. Q., Xu, Z., Byrnes, A. P., Simmet, T., & Kreppel, F. (2016). Substitution of blood coagulation factor X-binding to Ad5 by position-specific PEGylation: Preventing vector clearance and preserving infectivity. Journal of Controlled Release, 235, 379–392. https://doi.org/10.1016/j.jconrel.2016.06.022
Jensen, A. R., Manning, M. M., Khaneki, S., Drucker, N. A., & Markel, T. A. (2016). Harvest tissue source does not alter the protective power of stromal cell therapy after intestinal ischemia and reperfusion injury. Journal of Surgical Research. https://doi.org/10.1016/j.jss.2016.05.006
Rocha, B. S., Lundberg, J. O., Radi, R., & Laranjinha, J. (2016). Role of nitrite, urate and pepsin in the gastroprotective effects of saliva. Redox Biology, 8, 407–414. https://doi.org/10.1016/j.redox.2016.04.002
Alqaisi, K. M., Lamare, M. D., Grattan, D. R., Damsteegt, E. L., Schneider, W. J., & Lokman, P. M. (2016). A comparative study of vitellogenesis in Echinodermata: Lessons from the sea star. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 198, 72–86. https://doi.org/10.1016/j.cbpa.2016.04.013
Ohana, D., Dalebout, H., Marissen, R. J., Wulff, T., Bergquist, J., Deelder, A. M., & Palmblad, M. (2016). Identification of meat products by shotgun spectral matching. Food Chemistry, 203, 28–34. https://doi.org/10.1016/j.foodchem.2016.01.138
Zhou, L., Zheng, Y., Li, Z., Bao, L., Dou, Y., Tang, Y., Zhang, J., Zhou, J., Liu, Y., Jia, Y., & Li, X. (2016). Compound K Attenuates the Development of Atherosclerosis in ApoE−/− Mice via LXRα Activation. International Journal of Molecular Sciences, 17(7), 1054. https://doi.org/10.3390/ijms17071054
Shreeram, S., Ramesh, S., Puthan, J. K., Balakrishnan, G., Subramanian, R., Reddy, M. T., & Pereira, S. L. (2016). Age associated decline in the conversion of leucine to β-Hydroxy-β-Methylbutyrate in rats. Experimental Gerontology, 80, 6–11. https://doi.org/10.1016/j.exger.2016.03.021
Bonney, E. A., Krebs, K., Saade, G., Kechichian, T., Trivedi, J., Huaizhi, Y., & Menon, R. (2016). Differential senescence in feto-maternal tissues during mouse pregnancy. Placenta, 43, 26–34. https://doi.org/10.1016/j.placenta.2016.04.018
Gunderson, M. P., Pickett, M. A., Martin, J. T., Hulse, E. J., Smith, S. S., Smith, L. A., Campbell, R. M., Lowers, R. H., Boggs, A. S. P., & Guillette Jr., L. J. (2016). Variations in hepatic biomarkers in American alligators (Alligator mississippiensis) from three sites in Florida, USA. Chemosphere, 155, 180–187. https://doi.org/10.1016/j.chemosphere.2016.04.018
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
David, C. N., Frias, E. S., Szu, J. I., Vieira, P. A., Hubbard, J. A., Lovelace, J., Michael, M., Worth, D., McGovern, K. E., Ethell, I. M., Stanley, B. G., Korzus, E., Fiacco, T. A., Binder, D. K., & Wilson, E. H. (2016). GLT-1-Dependent Disruption of CNS Glutamate Homeostasis and Neuronal Function by the Protozoan Parasite Toxoplasma gondii. PLOS Pathog, 12(6), e1005643. https://doi.org/10.1371/journal.ppat.1005643
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
Zheng, Y., Xie, J., Huang, X., Dong, J., Park, M. S., & Chan, W. K. (2016). Binding studies using Pichia pastoris expressed human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins. Protein Expression and Purification, 122, 72–81. https://doi.org/10.1016/j.pep.2016.02.011
Chatzopoulou, A., Heijmans, J. P. M., Burgerhout, E., Oskam, N., Spaink, H. P., Meijer, A. H., & Schaaf, M. J. M. (2016). Glucocorticoid-induced attenuation of the inflammatory response in zebrafish. Endocrinology, en20152050. https://doi.org/10.1210/en.2015-2050
Vadnie, C. A., Ayers-Ringler, J., Oliveros, A., Abulseoud, O. A., Choi, S., Hitschfeld, M. J., & Choi, D.-S. (2016). Antipsychotic-like effects of a neurotensin receptor type 1 agonist. Behavioural Brain Research, 305, 8–17. https://doi.org/10.1016/j.bbr.2016.02.019
Molina, A. J. A., Bharadwaj, M. S., Van Horn, C., Nicklas, B. J., Lyles, M. F., Eggebeen, J., Haykowsky, M. J., Brubaker, P. H., & Kitzman, D. W. (2016). Skeletal Muscle Mitochondrial Content, Oxidative Capacity, and Mfn2 Expression Are Reduced in Older Patients With Heart Failure and Preserved Ejection Fraction and Are Related to Exercise Intolerance. JACC: Heart Failure. https://doi.org/10.1016/j.jchf.2016.03.011
Hoover, C. E., Davenport, K. A., Henderson, D. M., Pulscher, L. A., Mathiason, C. K., Zabel, M. D., & Hoover, E. A. (2016). Detection and Quantification of CWD Prions in Fixed Paraffin Embedded Tissues by Real-Time Quaking-Induced Conversion. Scientific Reports, 6. https://doi.org/10.1038/srep25098
Wang, Y., & Pfeiffer, J. K. (2016). Emergence of a Large-Plaque Variant in Mice Infected with Coxsackievirus B3. mBio, 7(2), e00119-16. https://doi.org/10.1128/mBio.00119-16
Coughlan, M. T., Nguyen, T.-V., Penfold, S. A., Higgins, G. C., Thallas-Bonke, V., Tan, S. M., Bergen, N. J. V., Sourris, K. C., Harcourt, B. E., Thorburn, D. R., Trounce, I. A., Cooper, M. E., & Forbes, J. M. (2016). Mapping time-course mitochondrial adaptations in the kidney in experimental diabetes. Clinical Science, 130(9), 711–720. https://doi.org/10.1042/CS20150838
Johns, M., Esmaeili Mohsen Abadi, S., Malik, N., Lee, J., Neumann, W. L., Rausaria, S., Imani-Nejad, M., McPherson, T., Schober, J., & Kwon, G. (2016). Oral administration of SR-110, a peroxynitrite decomposing catalyst, enhances glucose homeostasis, insulin signaling, and islet architecture in B6D2F1 mice fed a high fat diet. Archives of Biochemistry and Biophysics, 596, 126–137. https://doi.org/10.1016/j.abb.2016.03.002
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
Ayers-Ringler, J. R., Oliveros, A., Qiu, Y., Lindberg, D. M., Hinton, D. J., Moore, R. M., Dasari, S., & Choi, D.-S. (2016). Label-Free Proteomic Analysis of Protein Changes in the Striatum during Chronic Ethanol Use and Early Withdrawal. Frontiers in Behavioral Neuroscience, 10. https://doi.org/10.3389/fnbeh.2016.00046
Bennike, T. B., Kastaniegaard, K., Padurariu, S., Gaihede, M., Birkelund, S., Andersen, V., & Stensballe, A. (2016). Comparing the proteome of snap frozen, RNAlater preserved, and formalin-fixed paraffin-embedded human tissue samples. EuPA Open Proteomics, 10, 9–18. https://doi.org/10.1016/j.euprot.2015.10.001
Zhang, F., Hartnett, S., Sample, A., Schnack, S., & Li, Y. (2016). High fat diet induced alterations of atrial electrical activities in mice. American Journal of Cardiovascular Disease, 6(1), 1–9. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4788723/
Rosner, J. Y., Gupta, M., McGill, M., Xue, X., Chatterjee, P. K., Yoshida-Hay, M., Robeson, W., & Metz, C. N. (2016). Magnesium deficiency during pregnancy in mice impairs placental size and function. Placenta, 39, 87–93. https://doi.org/10.1016/j.placenta.2016.01.009
Bosch, M., Fajardo, A., Alcalá-Vida, R., Fernández-Vidal, A., Tebar, F., Enrich, C., Cardellach, F., Pérez-Navarro, E., & Pol, A. (2016). Hepatic Primary and Secondary Cholesterol Deposition and Damage in Niemann-Pick Disease. The American Journal of Pathology, 186(3), 517–523. https://doi.org/10.1016/j.ajpath.2015.12.002
Bennike, T. B., Kastaniegaard, K., Padurariu, S., Gaihede, M., Birkelund, S., Andersen, V., & Stensballe, A. (2016). Proteome stability analysis of snap frozen, RNAlater preserved, and formalin-fixed paraffin-embedded human colon mucosal biopsies. Data in Brief, 6, 942–947. https://doi.org/10.1016/j.dib.2016.01.061
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