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Links from Nucleotide

Items: 7

1.
Widespread expansion of protein interaction capabilities by alternative splicing
Xinping Yang, Jasmin Coulombe-Huntington, Shuli Kang, Gloria M. Sheynkman, Tong Hao, Aaron Richardson, Song Sun, Fan Yang, Yun A. Shen, Ryan R. Murray, Kerstin Spirohn, Bridget E. Begg, Miquel Duran-Frigola, Andrew MacWilliams, Samuel J. Pevzner, Quan Zhong, Shelly A. Wanamaker, Stanley Tam, Lila Ghamsari, Nidhi Sahni, Song Yi, Maria D. Rodriguez, Dawit Balcha, Guihong Tan, Michael Costanzo, Brenda Andrews, Charles Boone, Xianghong J. Zhou, Kourosh Salehi-Ashtiani, Benoit Charloteaux, Alyce A. Chen, Michael A. Calderwood, Patrick Aloy, Frederick P. Roth, David E. Hill, Lilia M. Iakoucheva, Yu Xia, Marc Vidal
Cell. Author manuscript; available in PMC 2017 Feb 11.
Published in final edited form as: Cell. 2016 Feb 11; 164(4): 805–817. doi: 10.1016/j.cell.2016.01.029
PMCID:
PMC4882190
AbstractArticlePDF–1.9M
2.
Widespread Macromolecular Interaction Perturbations in Human Genetic Disorders
Nidhi Sahni, Song Yi, Mikko Taipale, Juan I. Fuxman Bass, Jasmin Coulombe-Huntington, Fan Yang, Jian Peng, Jochen Weile, Georgios I. Karras, Yang Wang, István A. Kovács, Atanas Kamburov, Irina Krykbaeva, Mandy H. Lam, George Tucker, Vikram Khurana, Amitabh Sharma, Yang-Yu Liu, Nozomu Yachie, Quan Zhong, Yun Shen, Alexandre Palagi, Adriana San-Miguel, Changyu Fan, Dawit Balcha, Amelie Dricot, Daniel M. Jordan, Jennifer M. Walsh, Akash A. Shah, Xinping Yang, Ani Stoyanova, Alex Leighton, Michael A. Calderwood, Yves Jacob, Michael E. Cusick, Kourosh Salehi-Ashtiani, Luke J. Whitesell, Shamil Sunyaev, Bonnie Berger, Albert-László Barabási, Benoit Charloteaux, David E. Hill, Tong Hao, Frederick P. Roth, Yu Xia, Albertha J.M. Walhout, Susan Lindquist, Marc Vidal
Cell. Author manuscript; available in PMC 2016 Apr 23.
Published in final edited form as: Cell. 2015 Apr 23; 161(3): 647–660. doi: 10.1016/j.cell.2015.04.013
PMCID:
PMC4441215
AbstractArticlePDF–1.2M
3.
Congenital disorder of glycosylation due to DPM1 mutations presenting with dystroglycanopathy-type congenital muscular dystrophy
Amy C. Yang, Bobby G. Ng, Steven A. Moore, Jeffrey Rush, Charles J. Waechter, Kimiyo M. Raymond, Tobias Willer, Kevin P. Campbell, Hudson H. Freeze, Lakshmi Mehta
Mol Genet Metab. Author manuscript; available in PMC 2014 Nov 1.
Published in final edited form as: Mol Genet Metab. 2013 Nov; 110(3): 345–351. Published online 2013 Jun 28. doi: 10.1016/j.ymgme.2013.06.016
PMCID:
PMC3800268
AbstractArticlePDF–919K
4.
DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate.
Y Maeda, S Tomita, R Watanabe, K Ohishi, T Kinoshita
EMBO J. 1998 Sep 1; 17(17): 4920–4929. doi: 10.1093/emboj/17.17.4920
PMCID:
PMC1170821
SummaryPDF–527K
5.
Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie
Timo Imbach, Barbara Schenk, Els Schollen, Patricie Burda, Andreas Stutz, Stephanie Grünewald, Nicola M. Bailie, Mary D. King, Jaak Jaeken, Gert Matthijs, Eric G. Berger, Markus Aebi, Thierry Hennet
J Clin Invest. 2000 Jan 15; 105(2): 233–239. doi: 10.1172/JCI8691
PMCID:
PMC377434
AbstractArticlePDF–274K
6.
Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)
Soohyun Kim, Vibeke Westphal, Geetha Srikrishna, Darshini P. Mehta, Sandra Peterson, James Filiano, Pamela S. Karnes, Marc C. Patterson, Hudson H. Freeze
J Clin Invest. 2000 Jan 15; 105(2): 191–198. doi: 10.1172/JCI7302
PMCID:
PMC377427
AbstractArticlePDF–255K
7.
Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe
Paul A. Colussi, Christopher H. Taron, Jamey C. Mack, Peter Orlean
Proc Natl Acad Sci U S A. 1997 Jul 22; 94(15): 7873–7878. doi: 10.1073/pnas.94.15.7873
PMCID:
PMC21522
AbstractArticlePDF–413K

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