Results 71 to 80 of about 1,440,487 (305)
Improving eukaryotic genome annotation using single molecule mRNA sequencing
BMC Genomics, 2018 Background The advantages of Pacific Biosciences (PacBio) single-molecule real-time (SMRT) technology include long reads, low systematic bias, and high consensus read accuracy.Vincent Magrini, Xin Gao, Bruce A. Rosa, Sean McGrath, Xu Zhang, Kymberlie Hallsworth-Pepin, John Martin, John Hawdon, Richard K. Wilson, Makedonka Mitreva +9 moredoaj +1 more sourceInvestigating transcription factor dynamics in health and disease using FRAP
FEBS Letters, EarlyView.FRAP analysis of GFP‐tagged transcription factors reveals how molecular mobility and target engagement change in response to drug treatment. By combining live‐cell imaging, quantitative model fitting, and statistical analysis, this approach uncovers transcription factor dynamics linked to disease mechanisms, providing a powerful framework for ...Kannan Govindaraj, Carolina Vazquez Garzon, Jose Joaquin Velasco, Janine N. Post +3 morewiley +1 more sourceAn epithelial GPR35 isoform supports tumor‐associated transcriptional and metabolic phenotypes
FEBS Letters, EarlyView.GPR35 generates two functionally distinct isoforms with previously unresolved roles. GPR35‐short mediates immune‐cell chemotaxis, while GPR35‐long is enriched in colorectal cancer epithelium, where it supports increased metabolism, proliferation, and tumor‐associated transcriptional programs.Jørgen D. Rønneberg, Martine Hjeltnes, Josephine Krieger, Joshua E. Elias, Maria Stensland, Kristian Holm, Xiaojun Jiang, Chuki Khangsar, Tuula A. Nyman, Arthur Kaser, Johannes R. Hov, Tom H. Karlsen, Nicole C. Kaneider, Frode L. Jahnsen, Georg Schneditz +14 morewiley +1 more sourceData Mining of the Coffee Rust Genome [PDF]
, 2012 The genomes of nine isolates of _Hemileia vastatrix_, the causal agent of coffee leaf rust were sequenced by Illumina and 454. Quality control, cleaning and _de novo_ assemblies of data were performed.Silvia Restrepo, David Octavio Botero-Rozo, Alvaro Gaitan, Diego M. Riaño-Pachon, Marco Cristancho, William Giraldo +5 morecore +1 more sourceStructure‐forward targeting of claudins with synthetic binders
FEBS Letters, EarlyView.Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.Alex J. Vecchiowiley +1 more sourceDiscerning protein pools by selective staining with self‐labeling tags
FEBS Letters, EarlyView.Cell surface proteins have an intra‐ and extracellular pool. Combining genetic fusion to self‐labeling tags that can be addressed with small molecule fluorophores allows separating these pools. We highlight recent developments and techniques for state‐of‐the‐art interrogation of cell surface proteins in the complex tissue setting.Kati Fischermanns, Johannes Broichhagenwiley +1 more sourceThe H-Invitational Database (H-InvDB), a comprehensive annotation resource for human genes and transcripts [PDF]
, 2007 Here we report the new features and improvements in our latest release of the H-Invitational Database (H-InvDB; http://www.h-invitational.jp/), a comprehensive annotation resource for human genes and transcripts.Murakami, Katsuhiko, Shionyu, Masafumi, Nagata, Naoki, Tanaka, S., Kuryshev, Vladimir, Eveno, E., Mukai, Yuri, Imbeaud, S., Makalowski, W., Zhang, Q., Sakai, Katsunaga, Thomas, Michael A., Imanishi, T., Lee, Kyung-Bum, Tanaka, Masayuki, Thomas, M.A., Barrero, Roberto, Osanger, A., Tanaka, Susumu, Lenhard, B., Shiba, Rie, Sugano, S., Sakate, Ryuichi, Nakai, K., Wilming, L., Jia, Libin, Kawamura, Toshiyuki, Nishikawa, T., Thierry-Mieg, J., Kawahara, Yoshihiro, Harada, E., Kimura, K., Suzuki, Yutaka, Tanaka, Nobuhiko, Yasuda, T., Kawamura, T., Sanbonmatsu, Ryoko, Barrero, R.A., Yamaguchi, Kaori, Hide, Winston, Auffray, C., Horton, Paul, Niimura, Y., Shimoyama, Mary, Thomas, Michael, Tonellato, Peter, Hilton, P.B., Kikuno, Reiko, Kanno, Masako, Sugawara, Hideaki, Isogai, T., Sakai, Hiroaki, Whitfield, Eleanor, Nishikata, K., Matsuya, Aki, Halligan, B., Ohtsubo, Masafumi, Shiba, R., Fukuchi, S., Lee, K-B, Takabayashi, K., Sakate, R., Nurimoto, S., Kaneko, Yayoi, Nagasaki, H., Hayashizaki, Yoshihide, Lin, Yi-Chueh, Bellgard, M., Minoshima, Shinsei, Motono, C., Amid, Clara, Schupp, Ingo, Osato, N., Wagner, L., Isogai, Takao, Ohyanagi, H., Yura, Kei, Akiyama, Y., Jia, Ji, Yamaguchi, K., O’Donovan, C., Endo, T., O'Donovan, C., Matsuya, Akihiro, Yamamoto, N., Jin, L., Hirakawa, M., Chun, Hong-Woo, Makino, Takashi, Thierry-Mieg, D., Jia, L., Tada, Masahito, Twigger, Simon, Jin, Ji, Zhang, Qinghua, Nurimoto, Shin, Tamura, T., Bonaldo, M.D.F., Todokoro, Fusano, Nozaki, A., Ohara, Osamu, De Souza, Sandro J., Hayakawa, Yosuke, Nagata, N., Koyanagi, K.O., Gojobori, T., Kim, N-S, Yamasaki, Chisato, Shimoyama, M., Makalowska, I., Yoo, H-S, Lancet, D., Imbeaud, Sandrine, Takeda, Jun, Sanbonmatsu, R., Nakai, Kenta, Debily, Anne, Yura, K., Shionyu, M., Todokoro, F., Ikeo, K., Osanger, Andreas, Hanaoka, Hideki, Tanino, Motohiko, Eveno, Eric, Estreicher, Anne, Nozaki, Asami, Sugano, Sumio, O'Donovan, Claire, De Souza, S.J., Bonaldo, Maria de Fatima, Kikuno, R., Murakami, K., Mukai, Y., Lancet, Doron, Hayakawa, Y., Lin, Y., Ogura Noda, Akiko, Hashizume, A., Kim, Nam-Soon, Takeda, J., Thierry-Mieg, Jean, Koyanagi, Kanako O., Mashima, J., Hilton, Phillip, Nakao, M., Saitou, N., Ohtsubo, M., Niimura, Yoshihito, Takahashi, Aiko, Nishikawa, K., Suzuki, Yoshiyuki, Habara, Takuya, Kikugawa, S., Han, Michael, Kuryshev, V., Tamura, Takuro, Shimada, M., Ohyanagi, Hajime, Tanino, M., Tateno, Y., Yamaguchi-Kabata, Y., Sato, Y., Suzuki, Mami, Ikeo, Kazuho, Chiusano, Maria Luisa, Lenhard, Boris, Go, Mitiko, Taniya, Takayuki, Itoh, Takeshi, Takahashi, A., Hinz, Ursula, Kikugawa, Shingo, Hide, Hideaki, Tanaka, M., Matsuya, A., Amid, C., Hirakawa, Mika, Debily, M.A., Akiyama, Yutaka, Suzuki, Y., Hishiki, T., Nomura, N., Koyanagi, Kanako, Fujii, Y., Hinz, U., Sugawara, H., Saitou, Naruya, Zhang, J., Chakraborty, R., Debily, Marie Anne, Wagner, Lukas, Noda, Aki, Sakai, H., Schupp, I., Nishikata, Ken, Hanaoka, H., Miyazaki, S., Kaneko, Y., Kim, S., Habara, T., Tanaka, N., Hishiki, Teruyoshi, Minoshima, S., Satake, Ryuichi, Nakai, Ken, Lin, Y-C, Bellgard, Matthew, Yoo, H., Suwa, M., Nishikawa, Tetsuo, Chun, H., Nagasaki, H, Okido, T., Wiemann, S., Kawahara, Y., Hayashizaki, Y., Barrero, Roberto A., Nishikata, Kensaku, Miyazaki, Satoru, Soares, Marcelo Bento, Han, M., Chen, Z., Kikugawa, Shin, Whitfield, E., Debily, M., Hide, W., Takabayashi, Kazuhiko, Fukuchi, Satoshi, Motono, Chie, Yoo, Hyang-Sook, Tada, M., Fujii, Yasuyuki, Nomura, Nobuo, Estreicher, A., Auffray, Charles, Gough, Craig, Tonellato, P., Wilming, Laurens, Mashima, Jun, Wiemann, Stefan, Ohara, O., Graudens, E., Hanada, Kousuke, Hashizume, Aki, Go, M., Zhang, Ji, Gough, C., Noda, A.O., Yasuda, Tomohiro, Chen, Zhu, Graudens, Esther, Nakao, Mitsuteru, Imanishi, Tadashi, Harada, Erimi, Kimura, Kouichi, Suwa, Makiko, Nagasaki, Hideki, Hilton, Philip B., Yamaguchi-Kabata, Yumi, Chiusano, M.L., Kulikova, T., Yamamoto, Naoyuki, Chakraborty, Ranajit, Saichi, Naomi, Kim, Sangsoo, Kulikova, Tamara, Makalowska, Izabela, Thierry-Mieg, Danielle, Suzuki, M., Taniya, T., Sakai, K., Okido, Toshihisa, Halligan, Brian, Chun, H-W, Twigger, S., De Souza, Sandro, Takeda, Jun-ichi, Yamasaki, C., Makino, T., Tiffin, Nicola, Nishikawa, Ken, Gojobori, Takashi, Kanno, M., Shimada, Makoto, Makalowski, Wojciech, Horton, P., Hanada, K., Tiffin, N., Osato, Naoki, Sato, Yoshiharu, Tateno, Yoshio, Saichi, N., Takeda, J-I, Jin, Lihua, Endo, Toshinori, Bonaldo, M., Soares, M.B., Itoh, T., Lee, K., Kim, N., K Murakami, T Imanishi, T Gojobori, Hyang Sook Yoo, Nam-Soon Kim, Y Sato, E Harada, J Takeda, Y Fujii, S Kim, C Yamasaki +311 morecore +1 more sourcePeripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics
FEBS Letters, EarlyView.Proximity‐dependent labeling at the LAMTOR complex revealed the Rho GEF PLEKHG3 as a lysosome‐proximal protein directing the study toward the influence of lysosome positioning on actin dynamics and cell motility. We show that PLEKHG3 colocalizes with lysosomes at focal adhesion sites and observe that forced peripheral dispersion of lysosomes hinders ...Rainer Ettelt, Ana‐Maria Sandru, Georg Vucak, Sebastian Didusch, Biljana Riemelmoser, Karin Ehrenreiter, Markus Hartl, Lukas A. Huber, Manuela Baccarini +8 morewiley +1 more source