Zobrazeno 1 - 10
of 120
pro vyhledávání: '"Tom H. Stevens"'
Autor:
Eric J. R. Jansen, Sharita Timal, Margret Ryan, Angel Ashikov, Monique van Scherpenzeel, Laurie A. Graham, Hanna Mandel, Alexander Hoischen, Theodore C. Iancu, Kimiyo Raymond, Gerry Steenbergen, Christian Gilissen, Karin Huijben, Nick H. M. van Bakel, Yusuke Maeda, Richard J. Rodenburg, Maciej Adamowicz, Ellen Crushell, Hans Koenen, Darius Adams, Julia Vodopiutz, Susanne Greber-Platzer, Thomas Müller, Gregor Dueckers, Eva Morava, Jolanta Sykut-Cegielska, Gerard J. M. Martens, Ron A. Wevers, Tim Niehues, Martijn A. Huynen, Joris A. Veltman, Tom H. Stevens, Dirk J. Lefeber
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Here, Dirk Lefeber and colleagues identify functional mutations in ATP6AP1 encoding Ac45. The authors show that Ac45 is the functional ortholog of yeast V-ATPase assembly factor Voa1 and provide evidence for tissue-specific Ac45 processing, associate
Externí odkaz:
https://doaj.org/article/afaab16f854a454bb591193eef588aa6
Autor:
Elzbieta Czarnowska, Magda Cannata Serio, Pavel Pichurin, Sharita Timal, Jos C. Jansen, Hannu Kalimo, Adriaan G. Holleboom, Can Ficicioglu, Margret Ryan, Johan W. Jonker, Richard J. Rodenburg, Linda Hasadsri, Angel Ashikov, Christian Gilissen, Miao He, W. Alfredo Ríos-Ocampo, Matias Simons, Lars E. Larsen, Dirk Lefeber, Berge A. Minassian, Alessandra Rugierri, Joris A. Veltman, Tom H. Stevens, Gwenn Le Meur, Eva Morava, Piotr Socha, Kimiyo Raymond, Laurie A. Graham
Publikováno v:
Hepatology (Baltimore, Md.)
Hepatology (Baltimore, Md.), 72(6), 1968-1986. John Wiley and Sons Ltd
Hepatology, 72, 6, pp. 1968-1986
Hepatology, 72(6), 1968-1986. Wiley
Hepatology, 72, 1968-1986
Hepatology
Hepatology (Baltimore, Md.), 72(6), 1968-1986. John Wiley and Sons Ltd
Hepatology, 72, 6, pp. 1968-1986
Hepatology, 72(6), 1968-1986. Wiley
Hepatology, 72, 1968-1986
Hepatology
Background and Aims Vacuolar H+-ATP complex (V-ATPase) is a multisubunit protein complex required for acidification of intracellular compartments. At least five different factors are known to be essential for its assembly in the endoplasmic reticulum
Autor:
Trina A. Schroer, Frances M. Brodsky, Robert G. Parton, Sandra L. Schmid, Michael S. Marks, Mark Marsh, Sharon A. Tooze, Gerrit van Meer, Gillian M. Griffiths, Tom H. Stevens
Publikováno v:
Traffic (Copenhagen, Denmark)REFERENCES. 21(12)
Publikováno v:
Traffic. 18:93-95
Autor:
Tom H. Stevens, Tobias Hermle, Laurie A. Graham, Virginie Hauser, Matias Simons, Maria Clara Guida, Margret Ryan
Publikováno v:
Molecular Biology of the Cell
ATP6AP2 (also known as the [pro]renin receptor) is a type I transmembrane protein that can be cleaved into two fragments in the Golgi apparatus. While in Drosophila ATP6AP2 functions in the planar cell polarity (PCP) pathway, recent human genetic stu
Autor:
Martijn A. Huynen, Laurie A. Graham, Margret Ryan, Ellen Crushell, Kimiyo Raymond, G Dueckers, Jolanta Sykut-Cegielska, Nick H.M. van Bakel, Karin Huijben, Eric J. R. Jansen, Theodore C. Iancu, Dirk Lefeber, Joris A. Veltman, Darius Adams, Hans J. P. M. Koenen, Julia Vodopiutz, Thomas Müller, Eva Morava, Yusuke Maeda, Susanne Greber-Platzer, Gerard J.M. Martens, Tom H. Stevens, Gerry Steenbergen, Tim Niehues, Maciej Adamowicz, Christian Gilissen, Angel Ashikov, Alexander Hoischen, Monique van Scherpenzeel, Ron A. Wevers, Hanna Mandel, Sharita Timal, Richard J. Rodenburg
Publikováno v:
Nature Communications
Nature Communications, 7
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Nature Communications, 7:11600. Nature Publishing Group
Nature Communications, 7
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Nature Communications, 7:11600. Nature Publishing Group
The V-ATPase is the main regulator of intra-organellar acidification. Assembly of this complex has extensively been studied in yeast, while limited knowledge exists for man. We identified 11 male patients with hemizygous missense mutations in ATP6AP1
Autor:
Hae J. Park, Gregory C. Finnigan, Glen E. Cronan, Tom H. Stevens, Shuba Srinivasan, Florante A. Quiocho
Publikováno v:
Journal of Biological Chemistry. 287:19487-19500
Subunit a of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase) is responsible for both proton translocation and subcellular localization of this highly conserved molecular machine. Inclusion of the Vph1p isoform causes th
Publikováno v:
Nature. 481:360-364
Increased complexity in an essential molecular machine evolved through simple, high-probability genetic mechanisms. In a real-life variation on the 'Jurassic Park' theme, ancestral proteins have been resurrected from synthetic DNA using sequences inf
Publikováno v:
Molecular Biology of the Cell
The vacuolar ATPase complex in yeast contains two isoforms of subunit a that dictate the subcellular localization of the V-ATPase enzyme. The most recent common ancestor of subunit a (Anc.a) is reconstructed, and its function and localization in mode
Autor:
Emily M. Coonrod, Tom H. Stevens
Publikováno v:
Molecular Biology of the Cell
In 1992, Raymond et al. published a compilation of the 41 yeast vacuolar protein sorting (vps) mutant groups and described a large class of mutants (class E vps mutants) that accumulated an exaggerated prevacuolar endosome-like compartment. Further a