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6. Assessment of Manned-Unmanned Team Performance: Comprehensive After-Action Review Technology Development

Author

Brewer, Ralph W., II, Walker, Anthony J., Pursel, E. Ray, Cerame, Eduardo J., Baker, Anthony L., Schaefer, Kristin E., Kacprzyk, Janusz, Series Editor, Pal, Nikhil R., Advisory Editor, Bello Perez, Rafael, Advisory Editor, Corchado, Emilio S., Advisory Editor, Hagras, Hani, Advisory Editor, Kóczy, László T., Advisory Editor, Kreinovich, Vladik, Advisory Editor, Lin, Chin-Teng, Advisory Editor, Lu, Jie, Advisory Editor, Melin, Patricia, Advisory Editor, Nedjah, Nadia, Advisory Editor, Nguyen, Ngoc Thanh, Advisory Editor, Wang, Jun, Advisory Editor, and Chen, Jessie, editor

Published
2020
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26. Correction: Corrigendum: Whole genome analysis of a schistosomiasis-transmitting freshwater snail

Author

Adema, Coen M., Hillier, LaDeana W., Jones, Catherine S., Loker, Eric S., Knight, Matty, Minx, Patrick, Oliveira, Guilherme, Raghavan, Nithya, Shedlock, Andrew, do Amaral, Laurence Rodrigues, Arican-Goktas, Halime D., Assis, Juliana G., Baba, Elio Hideo, Baron, Olga L., Bayne, Christopher J., Bickham-Wright, Utibe, Biggar, Kyle K., Blouin, Michael, Bonning, Bryony C., Botka, Chris, Bridger, Joanna M., Buckley, Katherine M., Buddenborg, Sarah K., Lima Caldeira, Roberta, Carleton, Julia, Carvalho, Omar S., Castillo, Maria G., Chalmers, Iain W., Christensens, Mikkel, Clifton, Sandra, Cosseau, Celine, Coustau, Christine, Cripps, Richard M., Cuesta-Astroz, Yesid, Cummins, Scott F., Di Stefano, Leon, Dinguirard, Nathalie, Duval, David, Emrich, Scott, Feschotte, Cédric, Feyereisen, Rene, FitzGerald, Peter, Fronick, Catrina, Fulton, Lucinda, Galinier, Richard, Gava, Sandra G., Geusz, Michael, Geyer, Kathrin K., Giraldo-Calderón, Gloria I., de Souza Gomes, Matheus, Gordy, Michelle A., Gourbal, Benjamin, Grunau, Christoph, Hanington, Patrick C., Hoffmann, Karl F., Hughes, Daniel, Humphries, Judith, Jackson, Daniel J., Jannotti-Passos, Liana K., de Jesus Jeremias, Wander, Jobling, Susan, Kamel, Bishoy, Kapusta, Aurélie, Kaur, Satwant, Koene, Joris M., Kohn, Andrea B., Lawson, Dan, Lawton, Scott P., Liang, Di, Limpanont, Yanin, Liu, Sijun, Lockyer, Anne E., Lovato, Ty Anna L., Ludolf, Fernanda, Magrini, Vince, McManus, Donald P., Medina, Monica, Misra, Milind, Mitta, Guillaume, Mkoji, Gerald M., Montague, Michael J., Montelongo, Cesar, Moroz, Leonid L., Munoz-Torres, Monica C., Niazi, Umar, Noble, Leslie R., Oliveira, Francislon S., Pais, Fabiano S., Papenfuss, Anthony T., Peace, Rob, Pena, Janeth J., Pila, Emmanuel A., Quelais, Titouan, Raney, Brian J., Rast, Jonathan P., Rollinson, David, Rosse, Izinara C., Rotgans, Bronwyn, Routledge, Edwin J., Ryan, Kathryn M., Scholte, Larissa L. S., Storey, Kenneth B., Swain, Martin, Tennessen, Jacob A., Tomlinson, Chad, Trujillo, Damian L., Volpi, Emanuela V., Walker, Anthony J., Wang, Tianfang, Wannaporn, Ittiprasert, Warren, Wesley C., Wu, Xiao-Jun, Yoshino, Timothy P., Yusuf, Mohammed, Zhang, Si-Ming, Zhao, Min, and Wilson, Richard K.

Published
2017
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29. Additional file 6 of Molecular insights into the heat shock proteins of the human parasitic blood fluke Schistosoma mansoni

Author

Aguoru, Nancy A., Kirk, Ruth S., and Walker, Anthony J.

Abstract

Additional file 6: Figure S2. Comparative pairwise alignments of human HSP amino acid sequences against corresponding Schistosoma mansoni sequences (identifiers are provided in the figure), with homologous phosphorylation sites highlighted (in red). Phosphorylation sites from human HSPs were obtained from PhosphoSitePlus ( https://www.phosphosite.org/homeAction.action ) and were matched to S. mansoni sites obtained from the S. mansoni phosphoprotein dataset (Additional file 4: Figure S1).

Published
2022
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30. Additional file 8 of Molecular insights into the heat shock proteins of the human parasitic blood fluke Schistosoma mansoni

Author

Aguoru, Nancy A., Kirk, Ruth S., and Walker, Anthony J.

Abstract

Additional file 8: Figure S4. Negative controls for the different life stages under study showing no/minimal background staining in the absence of anti-HSP antibodies. Samples were processed for immunofluorescence using Alexa Fluor 488 mouse (first slide) or rabbit (second slide) secondary antibodies and rhodamine phalloidin (in red) but without the addition of a primary antibody. Samples were mounted on slides and imaged using a Zeiss LSM 800 laser scanning confocal microscope. Representative micrographs are single z-sections through the parasites. Scale bars = 25 µm (for cercariae and somules) and 50 µm (for adult worms).

Published
2022
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31. Additional file 4 of Molecular insights into the heat shock proteins of the human parasitic blood fluke Schistosoma mansoni

Author

Aguoru, Nancy A., Kirk, Ruth S., and Walker, Anthony J.

Abstract

Additional file 4: Figure S1. Phosphorylation sites within Schistosoma mansoni HSPs. Data on the phosphorylation sites of S. mansoni HSPs were mined from the S. mansoni phosphoproteome published by Hirst et al. [54]. Thirteen HSPs are shown, the remaining four can be viewed in Fig. 6. Domains within each HSP were identified using the conserved protein domain tool within InterPro and NCBI. Identification of putative upstream kinases, phosphatases and binding motifs were obtained using HPRD motif finder and PHOSIDA. Kinases are in black and are denoted by a plus or a cross symbol, phosphatases are in red and are denoted by a minus symbol, binding motifs are in blue and are denoted by an asterisk.

Published
2022
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32. Additional file 7 of Molecular insights into the heat shock proteins of the human parasitic blood fluke Schistosoma mansoni

Author

Aguoru, Nancy A., Kirk, Ruth S., and Walker, Anthony J.

Abstract

Additional file 7: Figure S3. Comparative pairwise alignments of human HSP amino acid sequences [HSP 10 (CAG28616), HSP 40 (NP_006136.1), HSP 60 (NP_002147), HSP 70 (NP_005336.3) and HSP 90 (NP_001258898.1)] against a corresponding Schistosoma mansoni HSP sequence {HSP 10 (Smp_097380), HSP 40 (Smp_104730), HSP 60 (Smp_008545), HSP 70 [Smp_106930 (Smp_302170)] and HSP 90 (Smp_072330)}. Highlighted areas are antibody recognition sites in the human protein. Where the antibody is raised to the whole protein sequence (such as anti-HSP 40 antibody and anti-HSP 70 antibodies), no regions are highlighted. Asterisks indicate positions that have a single, fully conserved residue; colons represent conservation between groups with strongly similar properties; periods indicate conservation between groups of weakly similar properties

Published
2022
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41. FGF signalling facilitates cervical cancer progression.

Author

Mahmood, Hiba‐Tun‐Noor Afshan, Tomas Bort, Elena, Walker, Anthony J., Grose, Richard P., and Chioni, Athina‐Myrto

Subjects
CELL culture, CERVICAL cancer, FIBROBLAST growth factor receptors, CANCER invasiveness
Abstract

Cervical cancer is one of the most frequently diagnosed cancers in women worldwide. While cervical cancer is caused by human papillomavirus (HPV), not all females infected with HPV develop the disease, suggesting that other factors might facilitate its progression. Growing evidence supports the involvement of the fibroblast growth factor receptor (FGFR) axis in several cancers, including gynecological. However, for cervical cancer, the molecular mechanisms that underpin the disease remain poorly understood, including the role of FGFR signaling. The aim of this study was to investigate FGF(R) signaling in cervical cancer through bioinformatic analysis of cell line and patient data and through detailed expression profiling, manipulation of the FGFR axis, and downstream phenotypic analysis in cell lines (HeLa, SiHa, and CaSki). Expression (protein and mRNA) analysis demonstrated that FGFR1b/c, FGFR2b/c, FGFR4, FGF2, FGF4, and FGF7 were expressed in all three lines. Interestingly, FGFR1 and 2 localized to the nucleus, supporting that nuclear FGFRs could act as transcription factors. Importantly, 2D and 3D cell cultures demonstrated that FGFR activation can facilitate cell functions correlated with invasive disease. Collectively, this study supports an association between FGFR signaling and cervical cancer progression, laying the foundations for the development of therapeutic approaches targeting FGFR in this disease. [ABSTRACT FROM AUTHOR]

Published
2022
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