Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Sharita Timal"'
Autor:
Marisa W. Friederich, Sharita Timal, Christopher A. Powell, Cristina Dallabona, Alina Kurolap, Sara Palacios-Zambrano, Drago Bratkovic, Terry G. J. Derks, David Bick, Katelijne Bouman, Kathryn C. Chatfield, Nadine Damouny-Naoum, Megan K. Dishop, Tzipora C. Falik-Zaccai, Fuad Fares, Ayalla Fedida, Ileana Ferrero, Renata C. Gallagher, Rafael Garesse, Micol Gilberti, Cristina González, Katherine Gowan, Clair Habib, Rebecca K. Halligan, Limor Kalfon, Kaz Knight, Dirk Lefeber, Laura Mamblona, Hanna Mandel, Adi Mory, John Ottoson, Tamar Paperna, Ger J. M. Pruijn, Pedro F. Rebelo-Guiomar, Ann Saada, Bruno Sainz, Hayley Salvemini, Mirthe H. Schoots, Jan A. Smeitink, Maciej J. Szukszto, Hendrik J. ter Horst, Frans van den Brandt, Francjan J. van Spronsen, Joris A. Veltman, Eric Wartchow, Liesbeth T. Wintjes, Yaniv Zohar, Miguel A. Fernández-Moreno, Hagit N. Baris, Claudia Donnini, Michal Minczuk, Richard J. Rodenburg, Johan L. K. Van Hove
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Abstract Mitochondrial protein synthesis requires charging mt-tRNAs with their cognate amino acids by mitochondrial aminoacyl-tRNA synthetases, with the exception of glutaminyl mt-tRNA (mt-tRNAGln). mt-tRNAGln is indirectly charged by a transamidatio
Externí odkaz:
https://doaj.org/article/5e2c03b6081043e5add48aba3812d059
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db692db53432f9043d5a54c01ef20dcb
https://hdl.handle.net/2066/230139
https://hdl.handle.net/2066/230139
Autor:
Angel, Ashikov, Nurulamin, Abu Bakar, Xiao-Yan, Wen, Marco, Niemeijer, Glentino, Rodrigues Pinto Osorio, Koroboshka, Brand-Arzamendi, Linda, Hasadsri, Hana, Hansikova, Kimiyo, Raymond, Dorothée, Vicogne, Nina, Ondruskova, Marleen E H, Simon, Rolph, Pfundt, Sharita, Timal, Roel, Beumers, Christophe, Biot, Roel, Smeets, Marjan, Kersten, Karin, Huijben, Peter T A, Linders, Geert, van den Bogaart, Sacha A F T, van Hijum, Richard, Rodenburg, Lambertus P, van den Heuvel, Francjan, van Spronsen, Tomas, Honzik, Francois, Foulquier, Monique, van Scherpenzeel, Dirk J, Lefeber, Wamelink, Mirjam, Brunner, Han, Mundy, Helen, Michelakakis, Helen, van Hasselt, Peter, van de Kamp, Jiddeke, Martinelli, Diego, Morkrid, Lars, Brocke Holmefjord, Katja, Hertecant, Jozef, Alfadhel, Majid, Carpenter, Kevin, Te Water Naude, Johann
Publikováno v:
CDG group 2018, ' Integrating glycomics and genomics uncovers SLC10A7 as essential factor for bone mineralization by regulating post-Golgi protein transport and glycosylation ', Human Molecular Genetics, vol. 27, no. 17, pp. 3029-3045 . https://doi.org/10.1093/hmg/ddy213
Human Molecular Genetics, 27(17), 3029-3045. Oxford University Press
Human Molecular Genetics, 27, 3029-3045
Human Molecular Genetics
Human Molecular Genetics, Oxford University Press (OUP), 2018, 27 (17), pp.3029-3045. ⟨10.1093/hmg/ddy213⟩
Human Molecular Genetics, 27(17), 3029. Oxford University Press
Human Molecular Genetics, 27, 17, pp. 3029-3045
Human Molecular Genetics, 2018, 27 (17), pp.3029-3045. ⟨10.1093/hmg/ddy213⟩
Human Molecular Genetics, 27(17), 3029-3045. Oxford University Press
Human Molecular Genetics, 27, 3029-3045
Human Molecular Genetics
Human Molecular Genetics, Oxford University Press (OUP), 2018, 27 (17), pp.3029-3045. ⟨10.1093/hmg/ddy213⟩
Human Molecular Genetics, 27(17), 3029. Oxford University Press
Human Molecular Genetics, 27, 17, pp. 3029-3045
Human Molecular Genetics, 2018, 27 (17), pp.3029-3045. ⟨10.1093/hmg/ddy213⟩
Genomics methodologies have significantly improved elucidation of Mendelian disorders. The combination with high-throughput functional-omics technologies potentiates the identification and confirmation of causative genetic variants, especially in sin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e709730c784b1fbb4d2aab2a8939fd5a
https://research.rug.nl/en/publications/f2f95986-9727-4cad-968f-2627eb4a6a0e
https://research.rug.nl/en/publications/f2f95986-9727-4cad-968f-2627eb4a6a0e
Autor:
Hanka Venselaar, Jan A.M. Smeitink, Ulrich Brandt, Joris A. Veltman, Ger J. M. Pruijn, Francjan von Spronsen, Hermine E. Veenstra-Knol, Vesna Stojanović, Carla Onnekink, Robert Kopajtich, Saskia B. Wortmann, Terry G J Derks, Liesbeth T. Wintjes, Sharita Timal, Wolfgang Sperl, Richard J. Rodenburg, Peter Freisinger, René G. Feichtinger, Mark A. Tarnopolsky, Johannes A. Mayr, Dirk Lefeber, Mareike Mühlmeister, Agnès Rötig, Holger Prokisch
Publikováno v:
Human Mutation, 38(12), 1786-1795. Wiley
Human Mutation, 38, 1786-1795
Hum. Mutat. 38, 1786-1795 (2017)
Human Mutation, 38, 12, pp. 1786-1795
Human Mutation, 38, 1786-1795
Hum. Mutat. 38, 1786-1795 (2017)
Human Mutation, 38, 12, pp. 1786-1795
Mitochondrial protein synthesis involves an intricate interplay between mitochondrial DNA encoded RNAs and nuclear DNA encoded proteins, such as ribosomal proteins and aminoacyl-tRNA synthases. Eukaryotic cells contain 17 mitochondria-specific aminoa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a5ed0782c7e89615ad98bd8a2bf998
https://doi.org/10.1002/humu.23340
https://doi.org/10.1002/humu.23340
Autor:
Marjolein A.W. van den Boogert, Joost P.H. Drenth, Gerry Steenbergen, Adriaan G. Holleboom, Marie-Cécile Nassogne, Dirk Lefeber, Gert Matthijs, Ulrike Schara, Luísa Diogo, Ron A. Wevers, Sharita Timal, Belén Pérez, Yoshinao Wada, Etienne Sokal, Jaak Jaeken, Peter Krawitz, Martijn A. Huynen, Monique van Scherpenzeel, Lambertus P. van den Heuvel, Patrick Gerner, Celia Medrano, Dorothée Vicogne, Sebahattin Cirak, Eva Morava, Joris A. Veltman, Alexander Hoischen, Daisy Rymen, Geert van den Bogaart, Janine Reunert, Andrea Arnoldy, Thorsten Marquardt, François Foulquier, O. Kaiser, Angel Ashikov, Stephan Rust, Dulce Quelhas, David Cheillan, Celia Pérez-Cerdá, Karin Huijben, Yusuke Maeda, Nathalie Guffon, Jody Salomon, Jos C. Jansen
Publikováno v:
Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid
Consejería de Sanidad de la Comunidad de Madrid
American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2016, 98 (2), pp.310-21. ⟨10.1016/j.ajhg.2015.12.010⟩
American Journal of Human Genetics, 98, 2, pp. 310-21
American Journal of Human Genetics, 98(2), 310-321. Cell Press
American journal of human genetics, 98(2), 310-321. Cell Press
American Journal of Human Genetics, 98, 310-21
Consejería de Sanidad de la Comunidad de Madrid
American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2016, 98 (2), pp.310-21. ⟨10.1016/j.ajhg.2015.12.010⟩
American Journal of Human Genetics, 98, 2, pp. 310-21
American Journal of Human Genetics, 98(2), 310-321. Cell Press
American journal of human genetics, 98(2), 310-321. Cell Press
American Journal of Human Genetics, 98, 310-21
Contains fulltext : 167630.pdf (Publisher’s version ) (Closed access) Disorders of Golgi homeostasis form an emerging group of genetic defects. The highly heterogeneous clinical spectrum is not explained by our current understanding of the underlyi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e4dce4a750b57ce8f0342620efa3f31b
https://cris.maastrichtuniversity.nl/en/publications/5e16210e-7d6c-4008-a101-fb305a6fbd08
https://cris.maastrichtuniversity.nl/en/publications/5e16210e-7d6c-4008-a101-fb305a6fbd08
Autor:
Hanna Mandel, Ger J. M. Pruijn, Sharita Timal, Clair Habib, Richard J. Rodenburg, Dirk Lefeber, Pedro Rebelo-Guiomar, Mirthe H. Schoots, Frans van den Brandt, Jan A.M. Smeitink, Alina Kurolap, Rebecca Halligan, Marisa W. Friederich, Kathryn C. Chatfield, Liesbeth T. Wintjes, Hagit N. Baris, Ileana Ferrero, Terry G J Derks, Bruno Sainz, Hendrik J. ter Horst, Maciej J. Szukszto, Miguel Ángel Fernández-Moreno, Limor Kalfon, Claudia Donnini, Michal Minczuk, Megan K. Dishop, Tamar Paperna, Francjan J. van Spronsen, Sara Palacios-Zambrano, Ann Saada, Fuad Fares, Micol Gilberti, Eric P. Wartchow, Yaniv Zohar, Tzipora C. Falik-Zaccai, Ayalla Fedida, Katherine Gowan, Rafael Garesse, Nadine Damouny-Naoum, Johan L.K. Van Hove, Cristina Dallabona, Christopher A. Powell, Adi Mory, Joris A. Veltman, Cristina González, Kaz M. Knight, David Bick, Renata C. Gallagher, Katelijne Bouman, John Ottoson, Hayley Salvemini, Drago Bratkovic, Laura Mamblona
Publikováno v:
Nature Communications, 9(1):4065. Nature Publishing Group
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, 9
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biblos-e Archivo. Repositorio Institucional de la UAM
Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid
Consejería de Sanidad de la Comunidad de Madrid
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, 9
Digital.CSIC. Repositorio Institucional del CSIC
instname
Biblos-e Archivo. Repositorio Institucional de la UAM
Repositorio Institucional de la Consejería de Sanidad de la Comunidad de Madrid
Consejería de Sanidad de la Comunidad de Madrid
Mitochondrial protein synthesis requires charging mt-tRNAs with their cognate amino acids by mitochondrial aminoacyl-tRNA synthetases, with the exception of glutaminyl mt-tRNA (mt-tRNAGln). mt-tRNAGln is indirectly charged by a transamidation reactio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e96e045c0b287003de5f67c13f22fb98
https://www.repository.cam.ac.uk/handle/1810/286571
https://www.repository.cam.ac.uk/handle/1810/286571
Autor:
Mariël A.M. van den Brand, Felix Distelmaier, Leo G.J. Nijtmans, Laura Sánchez-Caballero, Fabian Baertling, Sharita Timal, Richard J. Rodenburg, Lock Hock Ngu
Publikováno v:
Molecular Genetics and Metabolism, 120, 243-246
Molecular Genetics and Metabolism, 120, 3, pp. 243-246
Molecular Genetics and Metabolism, 120, 3, pp. 243-246
Contains fulltext : 170197.pdf (Publisher’s version ) (Closed access) NDUFAF3 is an assembly factor of mitochondrial respiratory chain complex I. Variants in NDUFAF3 have been identified as a cause of severe multisystem mitochondrial disease. In a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c34e7d1f08be953cfb2942376916ad82
https://doi.org/10.1016/j.ymgme.2016.12.005
https://doi.org/10.1016/j.ymgme.2016.12.005
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6307108e622174d83ba89c4b355a105
http://europepmc.org/articles/PMC4894975
http://europepmc.org/articles/PMC4894975
Autor:
Sharita Timal, Richard J. Rodenburg, Helen Michelakakis, Mersyni Mavrikou, Marina Moraitou, Karin Huijben, Angel Ashikov, Dirk Lefeber, Jos C. Jansen, Ron A. Wevers, Jody Salomon, Monique van Scherpenzeel, Giovanna Cenacchi, Marjolein A.W. van den Boogert, Martijn A. Huynen, Pier Luigi Calvo, Joris A. Veltman, Francesco Porta, François Foulquier, Adriaan G. Holleboom, Dorothée Vicogne, Alexander Hoischen, Eva Morava, Joost P.H. Drenth, Gerry Steenbergen, Geert van den Bogaart
Publikováno v:
American Journal of Human Genetics, 98, 322-30
American journal of human genetics, 98(2), 322-330. Cell Press
American Journal of Human Genetics, 98(2), 322-330. Cell Press
American Journal of Human Genetics, 98, 2, pp. 322-30
American journal of human genetics, 98(2), 322-330. Cell Press
American Journal of Human Genetics, 98(2), 322-330. Cell Press
American Journal of Human Genetics, 98, 2, pp. 322-30
none 26 si This work was financially supported by grants from the Institute of Genetic and Metabolic Disease (to D.J.L., R.J.R., and J.A.V.), the Dutch Organization for Scientific Research (ZONMW Medium Investment Grant 40-00506-98-9001 and VIDI Gran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f676b066f24cd6b03e358518662532bb
http://hdl.handle.net/2066/168169
http://hdl.handle.net/2066/168169