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Items: 1 to 20 of 22

1.
Genetic determinants of micronucleus formation in vivo
D. J. Adams, B. Barlas, R. E. McIntyre, I. Salguero, L. van der Weyden, A. Barros, J. R. Vicente, N. Karimpour, A. Haider, M. Ranzani, G. Turner, N. A. Thompson, V. Harle, R. Olvera-León, C. D. Robles-Espinoza, A. O. Speak, N. Geisler, W. J. Weninger, S. H. Geyer, J. Hewinson, N. A. Karp, The Sanger Mouse Genetics Project, B. Fu, F. Yang, Z. Kozik, J. Choudhary, L. Yu, M. S. van Ruiten, B. D. Rowland, C. J. Lelliott, M. del Castillo Velasco-Herrera, R. Verstraten, L. Bruckner, A. G. Henssen, M. A. Rooimans, J. de Lange, T. J. Mohun, M. J. Arends, K. A. Kentistou, P. A. Coelho, Y. Zhao, H. Zecchini, J. R. B. Perry, S. P. Jackson, G. Balmus
Nature. 2024; 627(8002): 130–136. Published online 2024 Feb 14. doi: 10.1038/s41586-023-07009-0
PMCID:
PMC10917660
AbstractArticlePDF–4.8M
2.
Calcium-binding protein 7 expressed in muscle negatively regulates age-related degeneration of neuromuscular junctions in mice
Takahiro Eguchi, Tohru Tezuka, Yuji Watanabe, Akane Inoue-Yamauchi, Hiroshi Sagara, Manabu Ozawa, Yuji Yamanashi
iScience. 2024 Feb 16; 27(2): 108997. Published online 2024 Jan 26. doi: 10.1016/j.isci.2024.108997
PMCID:
PMC10847746
AbstractArticlePDF–5.7M
3.
Peroxisome proliferator-activated receptor γ coactivator 1α regulates downstream of tyrosine kinase-7 (Dok-7) expression important for neuromuscular junction formation
Takumi Sugimoto, Chihiro Sakamaki, Tokushi Kimura, Takahiro Eguchi, Shinji Miura, Yasutomi Kamei
Sci Rep. 2024; 14: 1780. Published online 2024 Jan 20. doi: 10.1038/s41598-024-52198-x
PMCID:
PMC10799880
AbstractArticlePDF–1.6M
4.
Mechanism of disease and therapeutic rescue of Dok7 congenital myasthenia
Julien Oury, Wei Zhang, Nadia Leloup, Akiko Koide, Alexis D. Corrado, Gayatri Ketavarapu, Takamitsu Hattori, Shohei Koide, Steven J. Burden
Nature. 2021; 595(7867): 404–408. Published online 2021 Jun 23. doi: 10.1038/s41586-021-03672-3
PMCID:
PMC8277574
AbstractArticlePDF–6.6M
5.
AAV9-DOK7 Gene Therapy Reduces Disease Severity in Smn2B/− SMA Model Mice
Kevin A. Kaifer, Eric Villalón, Caley E. Smith, Madeline E. Simon, Jose Marquez, Abigail E. Hopkins, Toni I. Morcos, Christian L. Lorson
Biochem Biophys Res Commun. Author manuscript; available in PMC 2021 Sep 10.
Published in final edited form as: Biochem Biophys Res Commun. 2020 Sep 10; 530(1): 107–114. Published online 2020 Jul 30. doi: 10.1016/j.bbrc.2020.07.031
PMCID:
PMC7453709
AbstractArticlePDF–1.4M
6.
Effect of salbutamol on neuromuscular junction function and structure in a mouse model of DOK7 congenital myasthenia
Richard G Webster, An E Vanhaesebrouck, Susan E Maxwell, Judith A Cossins, Weiwei Liu, Ryo Ueta, Yuji Yamanashi, David M W Beeson
Hum Mol Genet. 2020 Aug 11; 29(14): 2325–2336. Published online 2020 Jun 16. doi: 10.1093/hmg/ddaa116
PMCID:
PMC7424765
AbstractArticlePDF–1.6M
7.
Damage-Induced Neuronal Endopeptidase Is Critical for Presynaptic Formation of Neuromuscular Junctions
Kenichi Nagata, Sumiko Kiryu-Seo, Mitsuyo Maeda, Kayo Yoshida, Takashi Morita, Hiroshi Kiyama
J Neurosci. 2010 May 19; 30(20): 6954–6962. doi: 10.1523/JNEUROSCI.4521-09.2010
PMCID:
PMC6632665
AbstractArticlePDF–2.1M
8.
Mechanisms and Consequences of Dopamine Depletion-Induced Attenuation of the Spinophilin/Neurofilament Medium Interaction
Andrew C. Hiday, Michael C. Edler, Asma B. Salek, Cameron W. Morris, Morrent Thang, Tyler J. Rentz, Kristie L. Rose, Lisa M. Jones, Anthony J. Baucum, II
Neural Plast. 2017; 2017: 4153076. Published online 2017 May 28. doi: 10.1155/2017/4153076
PMCID:
PMC5467389
AbstractArticlePDF–3.2M
9.
Protein Kinase CK2 Interacts at the Neuromuscular Synapse with Rapsyn, Rac1, 14-3-3γ, and Dok-7 Proteins and Phosphorylates the Latter Two
Dustin Herrmann, Marion Straubinger, Said Hashemolhosseini
J Biol Chem. 2015 Sep 11; 290(37): 22370–22384. Published online 2015 Jul 21. doi: 10.1074/jbc.M115.647610
PMCID:
PMC4566213
AbstractArticlePDF–3.8M
10.
The International Mouse Phenotyping Consortium Web Portal, a unified point of access for knockout mice and related phenotyping data
Gautier Koscielny, Gagarine Yaikhom, Vivek Iyer, Terrence F. Meehan, Hugh Morgan, Julian Atienza-Herrero, Andrew Blake, Chao-Kung Chen, Richard Easty, Armida Di Fenza, Tanja Fiegel, Mark Grifiths, Alan Horne, Natasha A. Karp, Natalja Kurbatova, Jeremy C. Mason, Peter Matthews, Darren J. Oakley, Asfand Qazi, Jack Regnart, Ahmad Retha, Luis A. Santos, Duncan J. Sneddon, Jonathan Warren, Henrik Westerberg, Robert J. Wilson, David G. Melvin, Damian Smedley, Steve D. M. Brown, Paul Flicek, William C. Skarnes, Ann-Marie Mallon, Helen Parkinson
Nucleic Acids Res. 2014 Jan 1; 42(Database issue): D802–D809. Published online 2013 Nov 3. doi: 10.1093/nar/gkt977
PMCID:
PMC3964955
AbstractArticlePDF–5.7M
11.
Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium
Pascale Gaudet, Michael S. Livstone, Suzanna E. Lewis, Paul D. Thomas
Brief Bioinform. 2011 Sep; 12(5): 449–462. Published online 2011 Aug 27. doi: 10.1093/bib/bbr042
PMCID:
PMC3178059
AbstractArticlePDF–1.0M
12.
A High-Resolution Anatomical Atlas of the Transcriptome in the Mouse Embryo
Graciana Diez-Roux, Sandro Banfi, Marc Sultan, Lars Geffers, Santosh Anand, David Rozado, Alon Magen, Elena Canidio, Massimiliano Pagani, Ivana Peluso, Nathalie Lin-Marq, Muriel Koch, Marchesa Bilio, Immacolata Cantiello, Roberta Verde, Cristian De Masi, Salvatore A. Bianchi, Juliette Cicchini, Elodie Perroud, Shprese Mehmeti, Emilie Dagand, Sabine Schrinner, Asja Nürnberger, Katja Schmidt, Katja Metz, Christina Zwingmann, Norbert Brieske, Cindy Springer, Ana Martinez Hernandez, Sarah Herzog, Frauke Grabbe, Cornelia Sieverding, Barbara Fischer, Kathrin Schrader, Maren Brockmeyer, Sarah Dettmer, Christin Helbig, Violaine Alunni, Marie-Annick Battaini, Carole Mura, Charlotte N. Henrichsen, Raquel Garcia-Lopez, Diego Echevarria, Eduardo Puelles, Elena Garcia-Calero, Stefan Kruse, Markus Uhr, Christine Kauck, Guangjie Feng, Nestor Milyaev, Chuang Kee Ong, Lalit Kumar, MeiSze Lam, Colin A. Semple, Attila Gyenesei, Stefan Mundlos, Uwe Radelof, Hans Lehrach, Paolo Sarmientos, Alexandre Reymond, Duncan R. Davidson, Pascal Dollé, Stylianos E. Antonarakis, Marie-Laure Yaspo, Salvador Martinez, Richard A. Baldock, Gregor Eichele, Andrea Ballabio
PLoS Biol. 2011 Jan; 9(1): e1000582. Published online 2011 Jan 18. doi: 10.1371/journal.pbio.1000582
PMCID:
PMC3022534
AbstractArticlePDF–3.8M
13.
Dok-7 regulates neuromuscular synapse formation by recruiting Crk and Crk-L
Peter T. Hallock, Chong-Feng Xu, Tae-Ju Park, Thomas A. Neubert, Tom Curran, Steven J. Burden
Genes Dev. 2010 Nov 1; 24(21): 2451–2461. doi: 10.1101/gad.1977710
PMCID:
PMC2964755
AbstractArticlePDF–1.0M
14.
Lrp4 is a Receptor for Agrin and Forms a Complex with MuSK
N. Kim, A.L. Stiegler, T.O. Cameron, P.T. Hallock, A.M. Gomez, J.H. Huang, S.R. Hubbard, M.L. Dustin, S.J. Burden
Cell. Author manuscript; available in PMC 2010 Sep 6.
Published in final edited form as: Cell. 2008 Oct 17; 135(2): 334–342. Published online 2008 Oct 9. doi: 10.1016/j.cell.2008.10.002
PMCID:
PMC2933840
AbstractArticlePDF–3.9M
15.
The Cytoplasmic Adapter-Protein Dok7 Activates the Receptor Tyrosine Kinase MuSK via Dimerization
Elisa Bergamin, Peter T. Hallock, Steven J. Burden, Stevan R. Hubbard
Mol Cell. Author manuscript; available in PMC 2011 Jul 9.
Published in final edited form as: Mol Cell. 2010 Jul 9; 39(1): 100–109. doi: 10.1016/j.molcel.2010.06.007
PMCID:
PMC2917201
AbstractArticlePDF–3.4M
16.
Mutations in MUSK causing congenital myasthenic syndrome impair MuSK–Dok-7 interaction
Ricardo A. Maselli, Juan Arredondo, Órla Cagney, Jarae J. Ng, Jennifer A. Anderson, Colette Williams, Bae J. Gerke, Betty Soliven, Robert L. Wollmann
Hum Mol Genet. 2010 Jun 15; 19(12): 2370–2379. Published online 2010 Apr 6. doi: 10.1093/hmg/ddq110
PMCID:
PMC2876883
AbstractArticlePDF–277K
17.
LRP4 serves as a co-receptor of agrin
Bin Zhang, Shiwen Luo, Qiang Wang, Tatsuo Suzuki, Wen C. Xiong, Lin Mei
Neuron. Author manuscript; available in PMC 2009 Oct 23.
Published in final edited form as: Neuron. 2008 Oct 23; 60(2): 285–297. doi: 10.1016/j.neuron.2008.10.006
PMCID:
PMC2743173
AbstractArticlePDF–1.8M
18.
The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)
Genome Res. 2004 Oct; 14(10b): 2121–2127. doi: 10.1101/gr.2596504
Correction in:
Genome Res. 2006 Jun; 16(6): 804.
PMCID:
PMC528928
AbstractArticlePDF–140K
19.
RIKEN Integrated Sequence Analysis (RISA) System—384-Format Sequencing Pipeline with 384 Multicapillary Sequencer
Kazuhiro Shibata, Masayoshi Itoh, Katsunori Aizawa, Sumiharu Nagaoka, Nobuya Sasaki, Piero Carninci, Hideaki Konno, Junichi Akiyama, Katsuo Nishi, Tokuji Kitsunai, Hideo Tashiro, Mari Itoh, Noriko Sumi, Yoshiyuki Ishii, Shin Nakamura, Makoto Hazama, Tsutomu Nishine, Akira Harada, Rintaro Yamamoto, Hiroyuki Matsumoto, Sumito Sakaguchi, Takashi Ikegami, Katsuya Kashiwagi, Syuji Fujiwake, Kouji Inoue, Yoshiyuki Togawa, Masaki Izawa, Eiji Ohara, Masanori Watahiki, Yuko Yoneda, Tomokazu Ishikawa, Kaori Ozawa, Takumi Tanaka, Shuji Matsuura, Jun Kawai, Yasushi Okazaki, Masami Muramatsu, Yorinao Inoue, Akira Kira, Yoshihide Hayashizaki
Genome Res. 2000 Nov; 10(11): 1757–1771. doi: 10.1101/gr.152600
PMCID:
PMC310992
AbstractArticlePDF–3.4M
20.
Normalization and Subtraction of Cap-Trapper-Selected cDNAs to Prepare Full-Length cDNA Libraries for Rapid Discovery of New Genes
Piero Carninci, Yuko Shibata, Norihito Hayatsu, Yuichi Sugahara, Kazuhiro Shibata, Masayoshi Itoh, Hideaki Konno, Yasushi Okazaki, Masami Muramatsu, Yoshihide Hayashizaki
Genome Res. 2000 Oct; 10(10): 1617–1630. doi: 10.1101/gr.145100
PMCID:
PMC310980
AbstractArticlePDF–1.4M

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