Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Alexander von Appen"'
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
The Nup82–Nup159–Nsp1 complex, which plays a key role in mRNA export, is recruited late during the process of nuclear pore complex (NPC) assembly. Here the authors combine crosslinking mass spectrometry, biochemical reconstitution and molecular m
Externí odkaz:
https://doaj.org/article/78609ff12d0b48928339246d519bd94b
Autor:
Alma L. Burlingame, Adam Frost, Alexander von Appen, Michael J. Trnka, Katharine S. Ullman, Sarah M. Pick, Isabel E. Johnson, Dollie LaJoie
Publikováno v:
Nature
Nature, vol 582, iss 7810
Nature, vol 582, iss 7810
During cell division, remodelling of the nuclear envelope enables chromosome segregation by the mitotic spindle1. The reformation of sealed nuclei requires ESCRTs (endosomal sorting complexes required for transport) and LEM2, a transmembrane ESCRT ad
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Nature Communications
Nature Communications
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs), which are formed from multiple copies of ~30 different nucleoporins (Nups) and inserted into the double nuclear membrane. Many of these Nups are organized into subcomplexes, of
Publikováno v:
Chemical Science. 8:559-566
We present new fluorophore-conjugates for dual-color photoactivation and super-resolution imaging inside live mammalian cells. These custom-designed, photo-caged Q-rhodamines and fluoresceins are cell-permeable, bright and localize specifically to in
Autor:
Amparo Andres-Pons, Khanh Huy Bui, Alexander von Appen, Benjamin Vollmer, Joseph S. Glavy, Panagiotis L. Kastritis, Wim J. H. Hagen, Amanda L. DiGuilio, Marie-Therese Mackmull, Lenore Sparks, Wolfram Antonin, Jan Kosinski, Martin Beck, Katarzyna Buczak, Shyamal Mosalaganti, Edward A. Lemke, Niccolò Banterle, Peer Bork, Alessandro Ori, Luca Parca
Publikováno v:
Nature
Nuclear pore complexes are fundamental components of all eukaryotic cells that mediate nucleocytoplasmic exchange. Determining their 110-megadalton structure imposes a formidable challenge and requires in situ structural biology approaches. Of approx
Autor:
Linda S. Nikolova, Adam Frost, Opal S. Chen, Mark S. Ladinsky, Wesley I. Sundquist, Katharine S. Ullman, Michael J. Redd, Dollie LaJoie, Mingyu Gu, Pamela J. Bjorkman, Alexander von Appen
Publikováno v:
Gu, M; LaJoie, D; Chen, OS; Von Appen, A; Ladinsky, MS; Redd, MJ; et al.(2017). LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission yeast and human cells. Proceedings of the National Academy of Sciences of the United States of America, 114(11), E2166-E2175. doi: 10.1073/pnas.1613916114. UCSF: Retrieved from: http://www.escholarship.org/uc/item/98b9155s
Proceedings of the National Academy of Sciences of the United States of America, vol 114, iss 11
Proceedings of the National Academy of Sciences of the United States of America, vol 114, iss 11
ESCRT-III proteins have been implicated in sealing the nuclear envelope in mammals, spindle pole body dynamics in fission yeast, and surveillance of defective nuclear pore complexes in budding yeast. Here, we report that Lem2p (LEM2), a member of the
Autor:
Khanh Huy Bui, Joseph S. Glavy, Amanda L. DiGuilio, Thomas Bock, Alessandro Ori, Wim J. H. Hagen, Lenore Sparks, Martin Beck, Marie-Therese Mackmull, Alexander von Appen, Amparo Andres-Pons
Publikováno v:
Cell
SummaryThe nuclear pore complex (NPC) is a fundamental component of all eukaryotic cells that facilitates nucleocytoplasmic exchange of macromolecules. It is assembled from multiple copies of about 30 nucleoporins. Due to its size and complex composi
Autor:
Ed Hurt, Shyamal Mosalaganti, Wim J. H. Hagen, Martin Beck, John A. G. Briggs, Amanda L. DiGuilio, Khanh Huy Bui, Roman Teimer, Joseph S. Glavy, Jan Kosinski, Alexander von Appen, William Wan
Publikováno v:
Science
Blueprint for a macromolecular machine Nuclear pore complexes (NPCs) consist of around 1000 protein subunits, are embedded in the membrane that surrounds the nucleus, and regulate transport between the nucleus and the cytoplasm. Although the overall
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fab23a0fc9b26bf72ae26c3304371af1
https://europepmc.org/articles/PMC8926079/
https://europepmc.org/articles/PMC8926079/
Autor:
Martin Beck, Dirk Flemming, Philipp Stelter, Alexander von Appen, Jessica Fischer, Elisar Barbar, Panagiotis L. Kastritis, Norbert Mücke, Monika Gaik, Khanh Huy Bui, Alessandro Ori, Ed Hurt, Jochen Baßler
Publikováno v:
The Journal of Cell Biology
Journal of Cell Biology
Journal of Cell Biology
The yeast Nup82 complex forms an unusual asymmetric structure with a dimeric array of subunits that mediate its anchorage to the NPC scaffold and its concomitant interaction with the soluble nucleocytoplasmic transport machinery.
Nuclear pore co
Nuclear pore co
Autor:
Jan Kosinski, Christoph W. Müller, Alessandro Ori, Alexander von Appen, Kai Karius, Martin Beck
Publikováno v:
Journal of Structural Biology
Structural characterization of large multi-subunit protein complexes often requires integrating various experimental techniques. Cross-linking mass spectrometry (XL-MS) identifies proximal protein residues and thus is increasingly used to map protein