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Items: 1 to 20 of 25

1.
Efficient In Silico Identification of a Common Insertion in the MAK Gene which Causes Retinitis Pigmentosa
Kinga M. Bujakowska, Joseph White, Emily Place, Mark Consugar, Jason Comander
PLoS One. 2015; 10(11): e0142614. Published online 2015 Nov 11. doi: 10.1371/journal.pone.0142614
PMCID:
PMC4641726
AbstractArticlePDF–1.0M
2.
Autosomal Recessive Retinitis Pigmentosa Caused by Mutations in the MAK Gene
Edwin M. Stone, Xunda Luo, Elise Héon, Byron L. Lam, Richard G. Weleber, Jennifer A. Halder, Louisa M. Affatigato, Jacqueline B. Goldberg, Alexander Sumaroka, Sharon B. Schwartz, Artur V. Cideciyan, Samuel G. Jacobson
Invest Ophthalmol Vis Sci. 2011 Dec; 52(13): 9665–9673. Published online 2011 Dec 24. doi: 10.1167/iovs.11-8527
PMCID:
PMC3341124
AbstractArticlePDF–3.1M
3.
Exome Sequencing and cis-Regulatory Mapping Identify Mutations in MAK, a Gene Encoding a Regulator of Ciliary Length, as a Cause of Retinitis Pigmentosa
Rıza Köksal Özgül, Anna M. Siemiatkowska, Didem Yücel, Connie A. Myers, Rob W.J. Collin, Marijke N. Zonneveld, Avigail Beryozkin, Eyal Banin, Carel B. Hoyng, L. Ingeborgh van den Born, The European Retinal Disease Consortium, Ron Bose, Wei Shen, Dror Sharon, Frans P.M. Cremers, B. Jeroen Klevering, Anneke I. den Hollander, Joseph C. Corbo
Am J Hum Genet. 2011 Aug 12; 89(2): 253–264. doi: 10.1016/j.ajhg.2011.07.005
PMCID:
PMC3155188
AbstractArticlePDF–1.2M
4.
Testis-specific mak protein kinase is expressed specifically in the meiotic phase in spermatogenesis and is associated with a 210-kilodalton cellular phosphoprotein.
A Jinno, K Tanaka, H Matsushime, T Haneji, M Shibuya
Mol Cell Biol. 1993 Jul; 13(7): 4146–4156. doi: 10.1128/mcb.13.7.4146
PMCID:
PMC359964
SummaryPage BrowsePDF–2.8M
5.
Exome sequencing and analysis of induced pluripotent stem cells identify the cilia-related gene male germ cell-associated kinase (MAK) as a cause of retinitis pigmentosa
Budd A. Tucker, Todd E. Scheetz, Robert F. Mullins, Adam P. DeLuca, Jeremy M. Hoffmann, Rebecca M. Johnston, Samuel G. Jacobson, Val C. Sheffield, Edwin M. Stone
Proc Natl Acad Sci U S A. 2011 Aug 23; 108(34): E569–E576. Published online 2011 Aug 8. doi: 10.1073/pnas.1108918108
PMCID:
PMC3161526
AbstractArticlePDF–1.3M
6.
CCRK depletion inhibits glioblastoma cell proliferation in a cilium-dependent manner
Ying Yang, Niina Roine, Tomi P Mäkelä
EMBO Rep. 2013 Aug; 14(8): 741–747. Published online 2013 Jun 7. doi: 10.1038/embor.2013.80
PMCID:
PMC3736126
AbstractArticlePDF–739K
7.
A novel mammalian protein kinase gene (mak) is highly expressed in testicular germ cells at and after meiosis.
H Matsushime, A Jinno, N Takagi, M Shibuya
Mol Cell Biol. 1990 May; 10(5): 2261–2268. doi: 10.1128/mcb.10.5.2261
PMCID:
PMC360573
SummaryPage BrowsePDF–1.8M
8.
Male germ cell-associated kinase is overexpressed in prostate cancer cells and causes mitotic defects via deregulation of APC/C-CDH1
Ling-Yu Wang, Hsing-Jien Kung
Oncogene. Author manuscript; available in PMC 2013 Feb 7.
Published in final edited form as: Oncogene. 2012 Jun 14; 31(24): 2907–2918. Published online 2011 Oct 10. doi: 10.1038/onc.2011.464
PMCID:
PMC3566783
AbstractArticlePDF–5.3M
9.
Distinct Expression Patterns of ICK/MAK/MOK Protein Kinases in the Intestine Implicate Functional Diversity
Tufeng Chen, Di Wu, Christopher A. Moskaluk, Zheng Fu
PLoS One. 2013; 8(11): e79359. Published online 2013 Nov 7. doi: 10.1371/journal.pone.0079359
PMCID:
PMC3820702
AbstractArticlePDF–2.0M
10.
Identification of Yin-Yang Regulators and a Phosphorylation Consensus for Male Germ Cell-Associated Kinase (MAK)-Related Kinase
Zheng Fu, Katherine A. Larson, Raghu K. Chitta, Sirlester A. Parker, Benjamin E. Turk, Matthew W. Lawrence, Philipp Kaldis, Konstantin Galaktionov, Steven M. Cohn, Jeffrey Shabanowitz, Donald F. Hunt, Thomas W. Sturgill
Mol Cell Biol. 2006 Nov; 26(22): 8639–8654. Published online 2006 Sep 5. doi: 10.1128/MCB.00816-06
PMCID:
PMC1636783
AbstractArticlePDF–1.2M
11.
Negative regulation of ciliary length by ciliary male germ cell-associated kinase (Mak) is required for retinal photoreceptor survival
Yoshihiro Omori, Taro Chaya, Kimiko Katoh, Naoko Kajimura, Shigeru Sato, Koichiro Muraoka, Shinji Ueno, Toshiyuki Koyasu, Mineo Kondo, Takahisa Furukawa
Proc Natl Acad Sci U S A. 2010 Dec 28; 107(52): 22671–22676. Published online 2010 Dec 8. doi: 10.1073/pnas.1009437108
PMCID:
PMC3012466
AbstractArticlePDF–1.3M
12.
A role for mitochondrial translation in promotion of viability in K-Ras mutant cells
Timothy D. Martin, Danielle R. Cook, Mei Yuk Choi, Mamie Z. Li, Kevin M. Haigis, Stephen J. Elledge
Cell Rep. Author manuscript; available in PMC 2017 Aug 11.
Published in final edited form as: Cell Rep. 2017 Jul 11; 20(2): 427–438. doi: 10.1016/j.celrep.2017.06.061
PMCID:
PMC5553568
AbstractArticlePDF–1.8M
13.
Gsk3β and Tomm20 are substrates of the SCFFbxo7/PARK15 ubiquitin ligase associated with Parkinson's disease
Felipe Roberti Teixeira, Suzanne J. Randle, Shachi P. Patel, Tycho E.T. Mevissen, Grasilda Zenkeviciute, Tie Koide, David Komander, Heike Laman
Biochem J. 2016 Oct 15; 473(20): 3563–3580. Prepublished online 2016 Aug 8. Published online 2016 Oct 11. doi: 10.1042/BCJ20160387
PMCID:
PMC5260939
AbstractArticlePDF–1.1M
14.
The HIV-1 Tat protein recruits a ubiquitin ligase to reorganize the 7SK snRNP for transcriptional activation
Tyler B Faust, Yang Li, Curtis W Bacon, Gwendolyn M Jang, Amit Weiss, Bhargavi Jayaraman, Billy W Newton, Nevan J Krogan, Iván D'Orso, Alan D Frankel
eLife. 2018; 7: e31879. Published online 2018 May 30. doi: 10.7554/eLife.31879
PMCID:
PMC5999396
AbstractArticlePDF–3.6M
15.
Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions
Yutaka Suzuki, Riu Yamashita, Matsuyuki Shirota, Yuta Sakakibara, Joe Chiba, Junko Mizushima-Sugano, Kenta Nakai, Sumio Sugano
Genome Res. 2004 Sep; 14(9): 1711–1718. doi: 10.1101/gr.2435604
PMCID:
PMC515316
AbstractArticlePDF–181K
16.
An organelle-specific protein landscape identifies novel diseases and molecular mechanisms
Karsten Boldt, Jeroen van Reeuwijk, Qianhao Lu, Konstantinos Koutroumpas, Thanh-Minh T. Nguyen, Yves Texier, Sylvia E. C. van Beersum, Nicola Horn, Jason R. Willer, Dorus A. Mans, Gerard Dougherty, Ideke J. C. Lamers, Karlien L. M. Coene, Heleen H. Arts, Matthew J. Betts, Tina Beyer, Emine Bolat, Christian Johannes Gloeckner, Khatera Haidari, Lisette Hetterschijt, Daniela Iaconis, Dagan Jenkins, Franziska Klose, Barbara Knapp, Brooke Latour, Stef J. F. Letteboer, Carlo L. Marcelis, Dragana Mitic, Manuela Morleo, Machteld M. Oud, Moniek Riemersma, Susan Rix, Paulien A. Terhal, Grischa Toedt, Teunis J. P. van Dam, Erik de Vrieze, Yasmin Wissinger, Ka Man Wu, Gordana Apic, Philip L. Beales, Oliver E. Blacque, Toby J. Gibson, Martijn A. Huynen, Nicholas Katsanis, Hannie Kremer, Heymut Omran, Erwin van Wijk, Uwe Wolfrum, François Kepes, Erica E. Davis, Brunella Franco, Rachel H. Giles, Marius Ueffing, Robert B. Russell, Ronald Roepman, UK10K Rare Diseases Group
Nat Commun. 2016; 7: 11491. Published online 2016 May 13. doi: 10.1038/ncomms11491
PMCID:
PMC4869170
AbstractArticlePDF–2.0M
17.
Interactions of Pathological Hallmark Proteins: TUBULIN POLYMERIZATION PROMOTING PROTEIN/p25, β-AMYLOID, AND α-SYNUCLEIN
Judit Oláh, Orsolya Vincze, Dezső Virók, Dóra Simon, Zsolt Bozsó, Natália Tőkési, István Horváth, Emma Hlavanda, János Kovács, Anna Magyar, Mária Szűcs, Ferenc Orosz, Botond Penke, Judit Ovádi
J Biol Chem. 2011 Sep 30; 286(39): 34088–34100. Published online 2011 Aug 8. doi: 10.1074/jbc.M111.243907
PMCID:
PMC3190826
AbstractArticlePDF–5.7M
18.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases
Marija Buljan, Rodolfo Ciuffa, Audrey van Drogen, Anton Vichalkovski, Martin Mehnert, George Rosenberger, Sohyon Lee, Markku Varjosalo, Lucia Espona Pernas, Vincent Spegg, Berend Snijder, Ruedi Aebersold, Matthias Gstaiger
Mol Cell. 2020 Aug 6; 79(3): 504–520.e9. doi: 10.1016/j.molcel.2020.07.001
PMCID:
PMC7427327
AbstractArticle
19.
Toward an understanding of the protein interaction network of the human liver
Jian Wang, Keke Huo, Lixin Ma, Liujun Tang, Dong Li, Xiaobi Huang, Yanzhi Yuan, Chunhua Li, Wei Wang, Wei Guan, Hui Chen, Chaozhi Jin, Junchen Wei, Wanqiao Zhang, Yongsheng Yang, Qiongming Liu, Ying Zhou, Cuili Zhang, Zhihao Wu, Wangxiang Xu, Ying Zhang, Tao Liu, Donghui Yu, Yaping Zhang, Liang Chen, Dewu Zhu, Xing Zhong, Lixin Kang, Xiang Gan, Xiaolan Yu, Qi Ma, Jing Yan, Li Zhou, Zhongyang Liu, Yunping Zhu, Tao Zhou, Fuchu He, Xiaoming Yang
Mol Syst Biol. 2011; 7: 536. Published online 2011 Oct 11. doi: 10.1038/msb.2011.67
Correction in:
Mol Syst Biol. 2017 Dec; 13(12): 965.
PMCID:
PMC3261708
AbstractArticlePDF–2.0M
20.
Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes
Kouichi Kimura, Ai Wakamatsu, Yutaka Suzuki, Toshio Ota, Tetsuo Nishikawa, Riu Yamashita, Jun-ichi Yamamoto, Mitsuo Sekine, Katsuki Tsuritani, Hiroyuki Wakaguri, Shizuko Ishii, Tomoyasu Sugiyama, Kaoru Saito, Yuko Isono, Ryotaro Irie, Norihiro Kushida, Takahiro Yoneyama, Rie Otsuka, Katsuhiro Kanda, Takahide Yokoi, Hiroshi Kondo, Masako Wagatsuma, Katsuji Murakawa, Shinichi Ishida, Tadashi Ishibashi, Asako Takahashi-Fujii, Tomoo Tanase, Keiichi Nagai, Hisashi Kikuchi, Kenta Nakai, Takao Isogai, Sumio Sugano
Genome Res. 2006 Jan; 16(1): 55–65. doi: 10.1101/gr.4039406
PMCID:
PMC1356129
AbstractArticlePDF–438K

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