TransIT-HeLaMONSTER citations

Product usage

Cell type	Nucleic acid
HeLa	Plasmid DNA

Allison, R., Lumb, J.H., Fassier, C., Connell, J.W., Ten Martin, D., Seaman, M.N.J., Hazan, J. and Reid, E. (2013). An ESCRT–spastin interaction promotes fission of recycling tubules from the endosome. Journal of Cell Biology, [online] 202(3), pp.527–543. Available at: https://rupress.org/jcb/article/202/3/527/37402/ [Accessed 3 Mar. 2020].

Anderson, K., Nordquist, K.A., Gao, X., Hicks, K.C., Zhai, B., Gygi, S.P. and Patel, T.B. (2011). Regulation of Cellular Levels of Sprouty2 Protein by Prolyl Hydroxylase Domain and von Hippel-Lindau Proteins. Journal of Biological Chemistry, [online] 286(49), pp.42027–42036. Available at: https://www.jbc.org/content/286/49/42027.full [Accessed 3 Mar. 2020].

Arking, D.E., Krebsova, A., Macek, M., Macek, M., Arking, A., Mian, I.S., Fried, L., Hamosh, A., Dey, S., McIntosh, I. and Dietz, H.C. (2002). Association of human aging with a functional variant of klotho. Proceedings of the National Academy of Sciences of the United States of America, [online] 99(2), pp.856–861. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC117395/ [Accessed 3 Mar. 2020].

Duncan, L.M., Nathan, J.A. and Lehner, P.J. (2010). Stabilisation of an E3 ligase-E2-Ubiquitin complex increases cell surface MHC Class I expression. Journal of immunology (Baltimore, Md. : 1950), [online] 184(12), pp.6978–6985. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3551299/ [Accessed 25 Mar. 2020].

Xu, S. and Powers, M.A. (2010). Nup98-homeodomain fusions interact with endogenous Nup98 during interphase and localize to kinetochores and chromosome arms during mitosis. Molecular Biology of the Cell, [online] 21(9), pp.1585–1596. Available at: https://www.ncbi.nlm.nih.gov/pubmed/20237156 [Accessed 25 Mar. 2020].

Hearn, A., York, I.A. and Rock, K.L. (2009). The Specificity of Trimming of MHC Class I-Presented Peptides in the Endoplasmic Reticulum. The Journal of Immunology, [online] 183(9), pp.5526–5536. Available at: https://www.jimmunol.org/content/183/9/5526 [Accessed 3 Mar. 2020].

Cowell, C.F., Döppler, H., Yan, I.K., Hausser, A., Umezawa, Y. and Storz, P. (2009). Mitochondrial diacylglycerol initiates protein-kinase-D1-mediated ROS signaling. Journal of Cell Science, [online] 122(7), pp.919–928. Available at: https://jcs.biologists.org/content/122/7/919 [Accessed 3 Mar. 2020].

Heier, C.R. and DiDonato, C.J. (2009). Translational readthrough by the aminoglycoside geneticin (G418) modulates SMN stability in vitro and improves motor function in SMA mice in vivo. Human Molecular Genetics, [online] 18(7), pp.1310–1322. Available at: https://www.ncbi.nlm.nih.gov/pubmed/19150990 [Accessed 25 Mar. 2020].

Ashiru, O., Bennett, N.J., Boyle, L.H., Thomas, M., Trowsdale, J. and Wills, M.R. (2009). NKG2D Ligand MICA Is Retained in the cis-Golgi Apparatus by Human Cytomegalovirus Protein UL142. Journal of Virology, [online] 83(23), pp.12345–12354. Available at: https://jvi.asm.org/content/83/23/12345 [Accessed 3 Mar. 2020].

Storz, P., Döppler, H., Copland, J.A., Simpson, K.J. and Toker, A. (2009). FOXO3a Promotes Tumor Cell Invasion through the Induction of Matrix Metalloproteinases. Molecular and Cellular Biology, [online] 29(18), pp.4906–4917. Available at: https://mcb.asm.org/content/29/18/4906 [Accessed 3 Mar. 2020].

Castilla-Llorente, V., Spraggon, L., Miwako Okamura, Saif Naseeruddin, Adamow, M., Qamar, S. and Jidong Liu (2012). Mammalian GW220/TNGW1 is essential for the formation of GW/P bodies containing miRISC. [online] undefined. Available at: https://www.semanticscholar.org/paper/Mammalian-GW220%2FTNGW1-is-essential-for-the-of-GW%2FP-Castilla-Llorente-Spraggon/d008b6ad750ee47ed43fc8773e1dbf264675ee0a [Accessed 3 Mar. 2020].

Clement, S.I., Scheckel, C., Stoecklin, G. and Lykke-Andersen, J. (2011). Phosphorylation of Tristetraprolin by MK2 Impairs AU-rich Element mRNA Decay by Preventing Deadenylase Recruitment. [online] Molecular and cellular biology. Available at: https://pubmed.ncbi.nlm.nih.gov/21078877-phosphorylation-of-tristetraprolin-by-mk2-impairs-au-rich-element-mrna-decay-by-preventing-deadenylase-recruitment/ [Accessed 3 Mar. 2020].

Crevenna, A.H., Blank, B., Maiser, A., Emin, D., Prescher, J., Beck, G., Kienzle, C., Bartnik, K., Habermann, B., Pakdel, M., Leonhardt, H., Lamb, D.C. and von Blume, J. (2016). Secretory cargo sorting by Ca2+-dependent Cab45 oligomerization at the trans-Golgi network. Journal of Cell Biology, [online] 213(3), pp.305–314. Available at: https://rupress.org/jcb/article/213/3/305/38671/Secretory-cargo-sorting-by-Ca2-dependent-Cab45 [Accessed 3 Mar. 2020].

Dachsel, J.C., Ngok, S.P., Lewis-Tuffin, L.J., Kourtidis, A., Geyer, R., Johnston, L., Feathers, R. and Anastasiadis, P.Z. (2013). The Rho Guanine Nucleotide Exchange Factor Syx Regulates the Balance of Dia and ROCK Activities To Promote Polarized-Cancer-Cell Migration. Molecular and Cellular Biology, [online] 33(24), pp.4909–4918. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3889543/ [Accessed 3 Mar. 2020].

Damgaard, C.K. and JLykke-Andersen, L.-A. (2011). Translational Coregulation of 5’TOP mRNAs by TIA-1 and TIAR. [online] Genes & development. Available at: https://pubmed.ncbi.nlm.nih.gov/21979918-translational-coregulation-of-5top-mrnas-by-tia-1-and-tiar/ [Accessed 3 Mar. 2020].

Davies, A.K., Itzhak, D.N., Edgar, J.R., Archuleta, T.L., Hirst, J., Jackson, L.P., Robinson, M.S. and Borner, G.H.H. (2018). AP-4 vesicles contribute to spatial control of autophagy via RUSC-dependent peripheral delivery of ATG9A. Nature Communications, [online] 9(1), pp.1–21. Available at: https://www.nature.com/articles/s41467-018-06172-7 [Accessed 6 Mar. 2020].

Döppler, H., Storz, P., Li, J., Comb, M.J. and Toker, A. (2005). A Phosphorylation State-specific Antibody Recognizes Hsp27, a Novel Substrate of Protein Kinase D. Journal of Biological Chemistry, [online] 280(15), pp.15013–15019. Available at: https://www.jbc.org/content/280/15/15013.short?trendmd-shared=0 [Accessed 3 Mar. 2020].

Döppler, H.R., Bastea, L.I., Lewis-Tuffin, L.J., Anastasiadis, P.Z. and Storz, P. (2013). Protein Kinase D1-mediated Phosphorylations Regulate Vasodilator-stimulated Phosphoprotein (VASP) Localization and Cell Migration. Journal of Biological Chemistry, [online] 288(34), pp.24382–24393. Available at: https://www.jbc.org/content/288/34/24382.abstract [Accessed 3 Mar. 2020].

Fink, S. i., Jayewickreme, T.R., Molony, R.D., Iwawaki, T., Landis, C.S., Lindenbach, B.D. and Iwasaki, A. (2017). IRE1α Promotes Viral Infection by Conferring Resistance to Apoptosis. [online] Science signaling. Available at: https://pubmed.ncbi.nlm.nih.gov/28588082-ire1-promotes-viral-infection-by-conferring-resistance-to-apoptosis/ [Accessed 6 Mar. 2020].

Franks, T.M. and Lykke-Andersen, J. (2007). TTP and BRF proteins nucleate processing body formation to silence mRNAs with AU-rich elements. Genes & Development, [online] 21(6), pp.719–735. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1820945/ [Accessed 3 Mar. 2020].

Gao, X., Chaturvedi, D. and Patel, T.B. (2012). Localization and retention of p90 ribosomal S6 kinase 1 in the nucleus: implications for its function. Molecular Biology of the Cell, 23(3), pp.503–515. Available at: https://pubmed.ncbi.nlm.nih.gov/22130794-localization-and-retention-of-p90-ribosomal-s6-kinase-1-in-the-nucleus-implications-for-its-function/ [Accessed 3 Mar. 2020].

Gao, X. and Patel, T.B. (2009). Regulation of Protein Kinase A Activity by p90 Ribosomal S6 Kinase 1. [online] The Journal of biological chemistry. Available at: https://pubmed.ncbi.nlm.nih.gov/19808666-regulation-of-protein-kinase-a-activity-by-p90-ribosomal-s6-kinase-1/ [Accessed 3 Mar. 2020].

Grimsey, N., Han, G.-S., O’Hara, L., Rochford, J.J., Carman, G.M. and Siniossoglou, S. (2008). Temporal and Spatial Regulation of the Phosphatidate Phosphatases Lipin 1 and 2. Journal of Biological Chemistry, [online] 283(43), pp.29166–29174. Available at: https://www.jbc.org/content/283/43/29166 [Accessed 3 Mar. 2020].

Gu, H. and Schoenberg, D.R. (2003). U2AF modulates poly(A) length control by the poly(A)-limiting element. Nucleic Acids Research, [online] 31(21), pp.6264–6271. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC275465/ [Accessed 3 Mar. 2020].

Hirose, T., Shu, M.-D. and Steitz, J.A. (2004). Splicing of U12-type introns deposits an exon junction complex competent to induce nonsense-mediated mRNA decay. Proceedings of the National Academy of Sciences, [online] 101(52), pp.17976–17981. Available at: https://www.pnas.org/content/101/52/17976 [Accessed 3 Mar. 2020].

Huang, J., Li, X., Maguire, C.A., Hilf, R., Bambara, R.A. and Muyan, M. (2005). Binding of Estrogen Receptor Beta to Estrogen Response Element in Situ Is Independent of Estradiol and Impaired by Its Amino Terminus. [online] Molecular endocrinology (Baltimore, Md.). Available at: https://pubmed.ncbi.nlm.nih.gov/15976006-binding-of-estrogen-receptor-beta-to-estrogen-response-element-in-situ-is-independent-of-estradiol-and-impaired-by-its-amino-terminus/ [Accessed 3 Mar. 2020].

Jakobi, R., McCarthy, C.C., Koeppel, M.A. and Stringer, D.K. (2003). Caspase-activated PAK-2 Is Regulated by Subcellular Targeting and Proteasomal Degradation. [online] The Journal of biological chemistry. Available at: https://pubmed.ncbi.nlm.nih.gov/12853446-caspase-activated-pak-2-is-regulated-by-subcellular-targeting-and-proteasomal-degradation/ [Accessed 3 Mar. 2020].

Lahousse, S.A., Beall, S.A. and Johnson, K.J. (2006). Mono-(2-ethylhexyl) Phthalate Rapidly Increases celsr2 Protein Phosphorylation in HeLa Cells via Protein Kinase C and Casein Kinase 1. [online] Toxicological sciences : an official journal of the Society of Toxicology. Available at: https://pubmed.ncbi.nlm.nih.gov/16484285-mono-2-ethylhexyl-phthalate-rapidly-increases-celsr2-protein-phosphorylation-in-hela-cells-via-protein-kinase-c-and-casein-kinase-1/ [Accessed 3 Mar. 2020].

Lubben, N.B., Sahlender, D.A., Motley, A.M., Lehner, P.J., Benaroch, P. and Robinson, M.S. (2007). HIV-1 Nef-induced Down-Regulation of MHC Class I Requires AP-1 and Clathrin but Not PACS-1 and Is Impeded by AP-2. Molecular Biology of the Cell, 18(9), pp.3351–3365. Available at: https://pubmed.ncbi.nlm.nih.gov/17581864-hiv-1-nef-induced-down-regulation-of-mhc-class-i-requires-ap-1-and-clathrin-but-not-pacs-1-and-is-impeded-by-ap-2/ Accessed 3 Mar. 2020].

Lykke-Andersen, J. and Wagner, E. (2005). Recruitment and Activation of mRNA Decay Enzymes by Two ARE-mediated Decay Activation Domains in the Proteins TTP and BRF-1. [online] Genes & development. Available at: https://pubmed.ncbi.nlm.nih.gov/15687258-recruitment-and-activation-of-mrna-decay-enzymes-by-two-are-mediated-decay-activation-domains-in-the-proteins-ttp-and-brf-1/ [Accessed 3 Mar. 2020].

Lytle, J.R., Yario, T.A. and Steitz, J.A. (2007). Target mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR. Proceedings of the National Academy of Sciences, [online] 104(23), pp.9667–9672. Available at: https://www.pnas.org/content/104/23/9667 [Accessed 3 Mar. 2020].

Markosyan, R.M., Cohen, F.S. and Melikyan, G.B. (2003). HIV-1 Envelope Proteins Complete Their Folding into Six-helix Bundles Immediately after Fusion Pore Formation. Molecular Biology of the Cell, [online] 14(3), pp.926–938. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC151570/ [Accessed 3 Mar. 2020].

Martinez, I., Cazalla, D., Almstead, L.L., Steitz, J.A. and DiMaio, D. (2011). miR-29 and miR-30 regulate B-Myb expression during cellular senescence. Proceedings of the National Academy of Sciences, [online] 108(2), pp.522–527. Available at: https://www.pnas.org/content/108/2/522 [Accessed 3 Mar. 2020].

Mirkin, N., Fonseca, D., Mohammed, S., Cevher, M.A., Manley, J.L. and Kleiman, F.E. (2008). The 3′ processing factor CstF functions in the DNA repair response. Nucleic Acids Research, [online] 36(6), pp.1792–1804. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2330234/ [Accessed 3 Mar. 2020].

Park, N., Katikaneni, P., Skern, T. and Gustin, K.E. (2008). Differential Targeting of Nuclear Pore Complex Proteins in Poliovirus-Infected Cells. Journal of Virology, [online] 82(4), pp.1647–1655. Available at: https://jvi.asm.org/content/82/4/1647 [Accessed 3 Mar. 2020].

Pawlicki, J.M. and Steitz, J.A. (2008). Primary microRNA transcript retention at sites of transcription leads to enhanced microRNA production. Journal of Cell Biology, [online] 182(1), pp.61–76. Available at: https://rupress.org/jcb/article/182/1/61/45333/Primary-microRNA-transcript-retention-at-sites-of [Accessed 3 Mar. 2020].

Sengupta, S., den Boon, J.A., Chen, I.-H., Newton, M.A., Stanhope, S.A., Cheng, Y.-J., Chen, C.-J., Hildesheim, A., Sugden, B. and Ahlquist, P. (2008). MicroRNA 29c is down-regulated in nasopharyngeal carcinomas, up-regulating mRNAs encoding extracellular matrix proteins. Proceedings of the National Academy of Sciences of the United States of America, [online] 105(15), pp.5874–5878. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2311339/ [Accessed 3 Mar. 2020].

Shimi, T., Pfleghaar, K., Kojima, S., Pack, C.G., Solovei, I., Goldman, A.E., Adam, S.A., Shumaker, D.K., Kinjo, M., Cremer, T. and Goldman, R.D. (2008). The A- And B-type Nuclear Lamin Networks: Microdomains Involved in Chromatin Organization and Transcription. [online] Genes & development. Available at: https://pubmed.ncbi.nlm.nih.gov/19141474-the-a-and-b-type-nuclear-lamin-networks-microdomains-involved-in-chromatin-organization-and-transcription/ [Accessed 3 Mar. 2020].

St Gelais, C., de Silva, S., Amie, S.M., Coleman, C.M., Hoy, H., Hollenbaugh, J.A., Kim, B. and Wu, L. (2012). SAMHD1 restricts HIV-1 infection in dendritic cells (DCs) by dNTP depletion, but its expression in DCs and primary CD4+ T-lymphocytes cannot be upregulated by interferons. Retrovirology, 9(1), p.105. Available at: https://retrovirology.biomedcentral.com/articles/10.1186/1742-4690-9-105 [Accessed 3 Mar. 2020].

Storz, P., Döppler, H. and Toker, A. (2004). Activation Loop Phosphorylation Controls Protein Kinase D-Dependent Activation of Nuclear Factor κB. Molecular Pharmacology, 66(4), pp.870–879. Available at: https://pubmed.ncbi.nlm.nih.gov/15226414-activation-loop-phosphorylation-controls-protein-kinase-d-dependent-activation-of-nuclear-factor-kappab/[Accessed 3 Mar. 2020].

Storz, P., Doppler, H. and Toker, A. (2004). Protein Kinase C Selectively Regulates Protein Kinase D-Dependent Activation of NF- B in Oxidative Stress Signaling. Molecular and Cellular Biology, 24(7), pp.2614–2626. Available at: https://pubmed.ncbi.nlm.nih.gov/15024053-protein-kinase-cdelta-selectively-regulates-protein-kinase-d-dependent-activation-of-nf-kappab-in-oxidative-stress-signaling/ [Accessed 3 Mar. 2020].

Storz, P., Döppler, H. and Toker, A. (2005). Protein Kinase D Mediates Mitochondrion-To-Nucleus Signaling and Detoxification From Mitochondrial Reactive Oxygen Species. [online] Molecular and cellular biology. Available at: https://pubmed.ncbi.nlm.nih.gov/16166634-protein-kinase-d-mediates-mitochondrion-to-nucleus-signaling-and-detoxification-from-mitochondrial-reactive-oxygen-species/ [Accessed 3 Mar. 2020].

Thomas, J.A., Bosche, W.J., Shatzer, T.L., Johnson, D.G. and Gorelick, R.J. (2008). Mutations in Human Immunodeficiency Virus Type 1 Nucleocapsid Protein Zinc Fingers Cause Premature Reverse Transcription. [online] Journal of virology. Available at: https://pubmed.ncbi.nlm.nih.gov/18667500-mutations-in-human-immunodeficiency-virus-type-1-nucleocapsid-protein-zinc-fingers-cause-premature-reverse-transcription/ [Accessed 3 Mar. 2020].

Towne, C.F., York, I.A., Neijssen, J., Karow, M.I., Murphy, A.J., Valenzuela, D.M., Yancopoulos, G.D., Neefjes, J.J. and Rock, K.L. (2005). Leucine Aminopeptidase Is Not Essential for Trimming Peptides in the Cytosol or Generating Epitopes for MHC Class I Antigen Presentation. [online] Journal of immunology (Baltimore, Md. : 1950). Available at: https://pubmed.ncbi.nlm.nih.gov/16272315-leucine-aminopeptidase-is-not-essential-for-trimming-peptides-in-the-cytosol-or-generating-epitopes-for-mhc-class-i-antigen-presentation/ [Accessed 3 Mar. 2020].

Wagner, E., Clement, S.I. and Lykke-Andersen, J. (2007). An Unconventional Human Ccr4-Caf1 Deadenylase Complex in Nuclear Cajal Bodies. [online] Molecular and cellular biology. Available at: https://pubmed.ncbi.nlm.nih.gov/17178830-an-unconventional-human-ccr4-caf1-deadenylase-complex-in-nuclear-cajal-bodies/ [Accessed 3 Mar. 2020].

Watkins, J.L., Lewandowski, K.T., Meek, S.E.M., Storz, P., Toker, A. and Piwnica-Worms, H. (2008). Phosphorylation of the Par-1 polarity kinase by protein kinase D regulates 14-3-3 binding and membrane association. Proceedings of the National Academy of Sciences, [online] 105(47), pp.18378–18383. Available at: https://www.pnas.org/content/105/47/18378 [Accessed 3 Mar. 2020].

Xu, S. and Powers, M.A. (2010). Nup98-homeodomain Fusions Interact With Endogenous Nup98 During Interphase and Localize to Kinetochores and Chromosome Arms During Mitosis. [online] Molecular biology of the cell. Available at: https://pubmed.ncbi.nlm.nih.gov/20237156-nup98-homeodomain-fusions-interact-with-endogenous-nup98-during-interphase-and-localize-to-kinetochores-and-chromosome-arms-during-mitosis/ [Accessed 3 Mar. 2020].

York, I.A., Bhutani, N., Zendzian, S., Goldberg, A.L. and Rock, K.L. (2006). Tripeptidyl Peptidase II Is the Major Peptidase Needed to Trim Long Antigenic Precursors, but Is Not Required for Most MHC Class I Antigen Presentation. The Journal of Immunology, [online] 177(3), pp.1434–1443. Available at: https://www.jimmunol.org/content/177/3/1434 [Accessed 3 Mar. 2020].

Zhang, J., Clatterbuck, R.E., Rigamonti, D., Chang, D.D. and Dietz, H.C. (2001). Interaction Between krit1 and icap1alpha Infers Perturbation of Integrin beta1-mediated Angiogenesis in the Pathogenesis of Cerebral Cavernous Malformation. [online] Human molecular genetics. Available at: https://pubmed.ncbi.nlm.nih.gov/11741838-interaction-between-krit1-and-icap1alpha-infers-perturbation-of-integrin-beta1-mediated-angiogenesis-in-the-pathogenesis-of-cerebral-cavernous-malformation/ [Accessed 3 Mar. 2020].

Zolov, S.N. and Lupashin, V.V. (2005). Cog3p Depletion Blocks Vesicle-Mediated Golgi Retrograde Trafficking in HeLa Cells. [online] The Journal of cell biology. Available at: https://pubmed.ncbi.nlm.nih.gov/15728195-cog3p-depletion-blocks-vesicle-mediated-golgi-retrograde-trafficking-in-hela-cells/ [Accessed 3 Mar. 2020].

Boyle, L.H., Hermann, C., Boname, J.M., Porter, K.M., Patel, P.A., Burr, M.L., Duncan, L.M., Harbour, M.E., Rhodes, D.A., Skjødt, K., Lehner, P.J. and Trowsdale, J. (2013). Tapasin-related protein TAPBPR is an additional component of the MHC class I presentation pathway. Proceedings of the National Academy of Sciences, [online] 110(9), pp.3465–3470. Available at: https://www.pnas.org/content/110/9/3465 [Accessed 3 Mar. 2020].

Ngok, S.P., Geyer, R., Kourtidis, A., Storz, P. and Anastasiadis, P.Z. (2013b). Phosphorylation-mediated 14-3-3 Protein Binding Regulates the Function of the Rho-specific Guanine Nucleotide Exchange Factor (RhoGEF) Syx. Journal of Biological Chemistry, [online] 288(9), pp.6640–6650. Available at: https://www.jbc.org/content/288/9/6640.full [Accessed 3 Mar. 2020].

Ngok, S.P., Geyer, R., Kourtidis, A., Mitin, N., Feathers, R., Der, C. and Anastasiadis, P.Z. (2013a). TEM4 is a junctional Rho GEF required for cell–cell adhesion, monolayer integrity and barrier function. Journal of Cell Science, [online] 126(15), pp.3271–3277. Available at: https://jcs.biologists.org/content/126/15/3271 [Accessed 3 Mar. 2020].

Borner, G.H.H., Antrobus, R., Hirst, J., Bhumbra, G.S., Kozik, P., Jackson, L.P., Sahlender, D.A. and Robinson, M.S. (2012). Multivariate proteomic profiling identifies novel accessory proteins of coated vesicles. The Journal of Cell Biology, [online] 197(1), pp.141–160. Available at: https://www.ncbi.nlm.nih.gov/pubmed/22472443 [Accessed 25 Mar. 2020].

von Blume, J., Alleaume, A.-M., Kienzle, C., Carreras-Sureda, A., Valverde, M. and Malhotra, V. (2012). Cab45 is required for Ca(2+)-dependent secretory cargo sorting at the trans-Golgi network. The Journal of Cell Biology, [online] 199(7), pp.1057–1066. Available at: https://www.ncbi.nlm.nih.gov/pubmed/23266954 [Accessed 25 Mar. 2020].

Ngok, S.P., Geyer, R., Liu, M., Kourtidis, A., Agrawal, S., Wu, C., Seerapu, H.R., Lewis-Tuffin, L.J., Moodie, K.L., Huveldt, D., Marx, R., Baraban, J.M., Storz, P., Horowitz, A. and Anastasiadis, P.Z. (2012). VEGF and Angiopoietin-1 exert opposing effects on cell junctions by regulating the Rho GEF Syx. The Journal of Cell Biology, [online] 199(7), pp.1103–1115. Available at: https://www.ncbi.nlm.nih.gov/pubmed/23253477 [Accessed 25 Mar. 2020].

Castilla-Llorente, V., Spraggon, L., Okamura, M., Naseeruddin, S., Adamow, M., Qamar, S. and Liu, J. (2012). Mammalian GW220/TNGW1 is essential for the formation of GW/P bodies containing miRISC. The Journal of Cell Biology, [online] 198(4), pp.529–544. Available at: https://www.ncbi.nlm.nih.gov/pubmed/22891262 [Accessed 25 Mar. 2020].

Damgaard, C.K. and Lykke-Andersen, J. (2011). Translational coregulation of 5’TOP mRNAs by TIA-1 and TIAR. Genes & Development, [online] 25(19), pp.2057–2068. Available at: https://www.ncbi.nlm.nih.gov/pubmed/21979918 [Accessed 25 Mar. 2020].

Hendrix, J., Gijsbers, R., De Rijck, J., Voet, A., Hotta, J., McNeely, M., Hofkens, J., Debyser, Z. and Engelborghs, Y. (2011). The transcriptional co-activator LEDGF/p75 displays a dynamic scan-and-lock mechanism for chromatin tethering. Nucleic Acids Research, [online] 39(4), pp.1310–1325. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3045605/ [Accessed 3 Mar. 2020].

Hearn, A., York, I.A., Bishop, C. and Rock, K.L. (2010). Characterizing the Specificity and Cooperation of Aminopeptidases in the Cytosol and Endoplasmic Reticulum during MHC Class I Antigen Presentation. The Journal of Immunology. [online] Available at: https://www.jimmunol.org/content/early/2010/03/29/jimmunol.0903125 [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid	Application
HeLa Tet-Off	Plasmid DNA	Gene/protein expression
Flp-In T-REx 293	Plasmid DNA	Reporter assays

Erickson, S., Corpuz, E.O., Maloy, J.P., Fillman, C., Webb, K., Bennett, E.J. and Lykke-Andersen, J. (2015). Competition Between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity. [online] Molecular and cellular biology. Available at: https://pubmed.ncbi.nlm.nih.gov/25870104-competition-between-decapping-complex-formation-and-ubiquitin-mediated-proteasomal-degradation-controls-human-dcp2-decapping-activity/ [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid	Application
HeLa Tet-Off	Plasmid DNA	Gene/protein expression

Arribas-Layton, M., Dennis, J., Bennett, E.J., Damgaard, C.K. and Lykke-Andersen, J. (2016). The C-Terminal RGG Domain of Human Lsm4 Promotes Processing Body Formation Stimulated by Arginine Dimethylation. Molecular and Cellular Biology, [online] 36(17), pp.2226–2235. Available at: https://mcb.asm.org/content/36/17/2226.abstract.

Toma, K.G., Rebbapragada, I., Durand, S. and Lykke-Andersen, J. (2015). Identification of Elements in Human Long 3’ UTRs That Inhibit Nonsense-Mediated Decay. [online] RNA (New York, N.Y.). Available at: https://pubmed.ncbi.nlm.nih.gov/25805855-identification-of-elements-in-human-long-3-utrs-that-inhibit-nonsense-mediated-decay/ [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid	Application
HeLa	Plasmid DNA	Gene/protein expression

von Blume, J., Alleaume, A., Kienzle, C., Carreras-Sureda, A., Valverde, M. and Malhotra, V. (2012). Cab45 Is Required for Ca(2+)-dependent Secretory Cargo Sorting at the trans-Golgi Network. [online] The Journal of cell biology. Available at: https://pubmed.ncbi.nlm.nih.gov/23266954-cab45-is-required-for-ca2-dependent-secretory-cargo-sorting-at-the-trans-golgi-network/ [Accessed 3 Mar. 2020].

van den Boomen, D.J., Timms, R.T., Grice, G., Stagg, H., Skødt, K., Dougan, G., Nathan, J.A. and Lehner, P.J. (2014). TMEM129 Is a Derlin-1 Associated ERAD E3 Ligase Essential for Virus-Induced Degradation of MHC-I. [online] Proceedings of the National Academy of Sciences of the United States of America. Available at: https://pubmed.ncbi.nlm.nih.gov/25030448-tmem129-is-a-derlin-1-associated-erad-e3-ligase-essential-for-virus-induced-degradation-of-mhc-i/ [Accessed 3 Mar. 2020].

Durrington, H.J., Upton, P.D., Hoer, S., Boname, J., Dunmore, B.J., Yang, J., Crilley, T.K., Butler, L.M., Blackbourn, D.J., Nash, G.B., Lehner, P.J. and Morrell, N.W. (2010). Identification of a Lysosomal Pathway Regulating Degradation of the Bone Morphogenetic Protein Receptor Type II. [online] The Journal of biological chemistry. Available at: https://pubmed.ncbi.nlm.nih.gov/20870717-identification-of-a-lysosomal-pathway-regulating-degradation-of-the-bone-morphogenetic-protein-receptor-type-ii/ [Accessed 3 Mar. 2020].

Eiseler, T., Wille, C., Koehler, C., Illing, A. and Seufferlein, T. (2016). Protein Kinase D2 Assembles a Multiprotein Complex at the Trans-Golgi Network to Regulate Matrix Metalloproteinase Secretion. Journal of Biological Chemistry, [online] 291(1), pp.462–477. Available at: https://www.jbc.org/content/291/1/462 [Accessed 3 Mar. 2020].

Heier, C.R. and DiDonato, C.J. (2009). Translational Readthrough by the Aminoglycoside Geneticin (G418) Modulates SMN Stability in Vitro and Improves Motor Function in SMA Mice in Vivo. [online] Human molecular genetics. Available at: https://pubmed.ncbi.nlm.nih.gov/19150990-translational-readthrough-by-the-aminoglycoside-geneticin-g418-modulates-smn-stability-in-vitro-and-improves-motor-function-in-sma-mice-in-vivo/ [Accessed 3 Mar. 2020].

Hicks, K.C. and Patel, T.B. (2016). Sprouty2 Protein Regulates Hypoxia-inducible Factor-α (HIFα) Protein Levels and Transcription of HIFα-responsive Genes. Journal of Biological Chemistry, [online] 291(32), pp.16787–16801. Available at: https://www.jbc.org/content/291/32/16787.full [Accessed 3 Mar. 2020].

Kirui, J., Bucci, M.D., Poole, D.S. and Mehle, A. (2014). Conserved Features of the PB2 627 Domain Impact Influenza Virus Polymerase Function and Replication. [online] Journal of virology. Available at: https://pubmed.ncbi.nlm.nih.gov/24623411-conserved-features-of-the-pb2-627-domain-impact-influenza-virus-polymerase-function-and-replication/ [Accessed 3 Mar. 2020].

Koestler, B.J., Seregin, S.S., Rastall, D.P.W., Aldhamen, Y.A., Godbehere, S., Amalfitano, A. and Waters, C.M. (2014). Stimulation of Innate Immunity by In Vivo Cyclic di-GMP Synthesis Using Adenovirus. Clinical and Vaccine Immunology, [online] 21(11), pp.1550–1559. Available at: https://cvi.asm.org/content/21/11/1550 [Accessed 3 Mar. 2020].

Ngok, S.P., Geyer, R., Liu, M., Kourtidis, A., Agrawal, S., Wu, C., Seerapu, H.R., Lewis-Tuffin, L.J., Moodie, K.I., DHuveldt, H., Marx, R., Baraban, J.M., Storz, P., Horowitz, A. and Anastasiadis, P.Z. (2012). VEGF and Angiopoietin-1 Exert Opposing Effects on Cell Junctions by Regulating the Rho GEF Syx. [online] The Journal of cell biology. Available at: https://pubmed.ncbi.nlm.nih.gov/23253477-vegf-and-angiopoietin-1-exert-opposing-effects-on-cell-junctions-by-regulating-the-rho-gef-syx/ [Accessed 3 Mar. 2020].

Nogueira, C., Erlmann, P., Villeneuve, J., Santos, A.J., Martínez-Alonso, E., Martínez-Menárguez, J.A. and Malhotra, V. (2014). SLY1 and Syntaxin 18 Specify a Distinct Pathway for Procollagen VII Export From the Endoplasmic Reticulum. [online] eLife. Available at: https://pubmed.ncbi.nlm.nih.gov/24842878-sly1-and-syntaxin-18-specify-a-distinct-pathway-for-procollagen-vii-export-from-the-endoplasmic-reticulum/ [Accessed 3 Mar. 2020].

Wille, C., Köhler, C., Armacki, M., Jamali, A., Gössele, U., Pfizenmaier, K., Seufferlein, T. and Eiseler, T. (2014). Protein kinase D2 induces invasion of pancreatic cancer cells by regulating matrix metalloproteinases. Molecular Biology of the Cell, [online] 25(3), pp.324–336. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3907273/ [Accessed 3 Mar. 2020].

‌

Product usage

Cell type	Nucleic acid	Application
HeLa	Plasmid DNA	Transient transfection

Borner, G.H., Antrobus, R., Hirst, J., Bhumbra, G., Kozik, P., Jackson, L., Sahlender, D. and Robinson, M.S. (2012). Multivariate Proteomic Profiling Identifies Novel Accessory Proteins of Coated Vesicles. [online] The Journal of cell biology. Available at: https://pubmed.ncbi.nlm.nih.gov/22472443-multivariate-proteomic-profiling-identifies-novel-accessory-proteins-of-coated-vesicles/ [Accessed 3 Mar. 2020].

Braun, A.C., Hendrick, J., Eisler, S.A., Schmid, S., Hausser, A. and Olayioye, M.A. (2015). The Rho-specific GAP protein DLC3 coordinates endocytic membrane trafficking. [online] undefined. Available at: https://www.semanticscholar.org/paper/The-Rho-specific-GAP-protein-DLC3-coordinates-Braun-Hendrick/f2a295dbc9616fa56c0187ada5f29200f303719f [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid
MDA-MB-231	Plasmid DNA

Dulyaninova, N.G., House, R.P., Betapudi, V. and Bresnick, A.R. (2007). Myosin-IIA Heavy-Chain Phosphorylation Regulates the Motility of MDA-MB-231 Carcinoma Cells. Molecular Biology of the Cell, 18(8), pp.3144–3155. Available at: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1949358/ [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid	Application
HeLa	Plasmid DNA	Co-transfection

Sivanesan, D., Beauchamp, C., Quinou, C., Lee, J., Lesage, S., Chemtob, S., Rioux, J.D. and Michnick, S. (2016). IL23R variants protective against inflammatory bowel diseases (IBD) display loss of function due to impaired protein stability and intracellular trafficking. Journal of Biological Chemistry, [online] p.jbc.M116.715870. Available at: https://www.jbc.org/content/early/2016/02/17/jbc.M116.715870.abstract [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid	Application
HeLa	Plasmid DNA	Gene/protein expression
HeLa	Plasmid DNA and siRNA	Gene/protein expression

Sui, H., Zhou, M., Chen, Q., Lane, H.C. and Imamichi, T. (2014). siRNA Enhances DNA-mediated Interferon lambda-1 Response Through Crosstalk Between RIG-I and IFI16 Signalling Pathway. [online] Nucleic acids research. Available at: https://pubmed.ncbi.nlm.nih.gov/24049081-sirna-enhances-dna-mediated-interferon-lambda-1-response-through-crosstalk-between-rig-i-and-ifi16-signalling-pathway/ [Accessed 3 Mar. 2020].

Product usage

Cell type	Nucleic acid
HeLa Tet-Off	Plasmid DNA

Clement, S.L., Scheckel, C., Stoecklin, G. and Lykke-Andersen, J. (2011). Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Molecular and Cellular Biology, [online] 31(2), pp.256–266. Available at: https://www.ncbi.nlm.nih.gov/pubmed/21078877 [Accessed 25 Mar. 2020].

Product usage

Cell type	Nucleic acid
HeLa	Plasmid DNA
BC-3
Sultan

Durrington, H.J., Upton, P.D., Hoer, S., Boname, J., Dunmore, B.J., Yang, J., Crilley, T.K., Butler, L.M., Blackbourn, D.J., Nash, G.B., Lehner, P.J. and Morrell, N.W. (2010). Identification of a lysosomal pathway regulating degradation of the bone morphogenetic protein receptor type II. The Journal of Biological Chemistry, [online] 285(48), pp.37641–37649. Available at: https://www.ncbi.nlm.nih.gov/pubmed/20870717 [Accessed 25 Mar. 2020].