Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Daniel M. Passon"'
Autor:
Arjen J. Jakobi, Daniel M. Passon, Kèvin Knoops, Francesco Stellato, Mengning Liang, Thomas A. White, Thomas Seine, Marc Messerschmidt, Henry N. Chapman, Matthias Wilmanns
Publikováno v:
IUCrJ, Vol 3, Iss 2, Pp 88-95 (2016)
The possibility of using femtosecond pulses from an X-ray free-electron laser to collect diffraction data from protein crystals formed in their native cellular organelle has been explored. X-ray diffraction of submicrometre-sized alcohol oxidase crys
Externí odkaz:
https://doaj.org/article/0e8bb1c71e8b4e489bc877f3c0bf30f4
Autor:
Ralf Erdmann, Wolfgang Schliebs, Katharina Reglinski, Ye Lou, Krisztián Fodor, Janina Wolf, Matthias Wilmanns, Daniel M. Passon
Publikováno v:
Traffic. 16:85-98
Peroxisomes entirely rely on the import of their proteome across the peroxisomal membrane. Recognition efficiencies of peroxisomal proteins vary by more than 1000-fold, but the molecular rationale behind their subsequent differential import and sorti
Autor:
Marc Messerschmidt, Mengning Liang, Henry N. Chapman, Matthias Wilmanns, Thomas A. White, Francesco Stellato, Daniel M. Passon, Arjen J. Jakobi, Kèvin Knoops, Thomas Seine
Publikováno v:
IUCrJ, Vol 3, Iss 2, Pp 88-95 (2016)
IUCrJ 3(2), 88-95 (2016). doi:10.1107/S2052252515022927
IUCrJ, 3(2), 88-95
IUCrJ
IUCrJ 3(2), 88-95 (2016). doi:10.1107/S2052252515022927
IUCrJ, 3(2), 88-95
IUCrJ
The application of serial femtosecond crystallography to naturally occurring peroxisomal protein crystals within yeast cells is described. The concept of utilizing peroxisomes for the production of protein nanocrystals is outlined.
The possibili
The possibili
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f90f0b981db55dea5e6e8e56a3dc6be
http://hdl.handle.net/2108/266642
http://hdl.handle.net/2108/266642
Autor:
Charles S. Bond, Mihwa Lee, Aleksandra Filipovska, Daniel M. Passon, Archa H. Fox, Oliver Rackham, Will A. Stanley, Agata Sadowska
Publikováno v:
Proceedings of the National Academy of Sciences. 109:4846-4850
Proteins of the Drosophila behavior/human splicing (DBHS) family include mammalian SFPQ (PSF), NONO (p54nrb), PSPC1, and invertebrate NONA and Hrp65. DBHS proteins are predominately nuclear, and are involved in transcriptional and posttranscriptional
Publikováno v:
Acta Crystallographica Section D. Biological Crystallography, 67(Pt 11), 981-7. International Union of Crystallography
Lee, M, Passon, D M, Hennig, S, Fox, A H & Bond, C S 2011, ' Construct optimization for studying protein complexes : obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer ', Acta Crystallographica Section D. Biological Crystallography, vol. 67, no. Pt 11, pp. 981-7 . https://doi.org/10.1107/S0907444911039606
Lee, M, Passon, D M, Hennig, S, Fox, A H & Bond, C S 2011, ' Construct optimization for studying protein complexes : obtaining diffraction-quality crystals of the pseudosymmetric PSPC1-NONO heterodimer ', Acta Crystallographica Section D. Biological Crystallography, vol. 67, no. Pt 11, pp. 981-7 . https://doi.org/10.1107/S0907444911039606
The methodology of protein crystallography provides a number of potential bottlenecks. Here, an approach to successful structure solution of a difficult heterodimeric complex of two human proteins, paraspeckle component 1 (PSPC1) and non-POU domain-c
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:1231-1234
The paraspeckle component 1 (PSPC1) and non-POU-domain-containing octamer-binding protein (NONO) heterodimer is an essential structural component of paraspeckles, ribonucleoprotein bodies found in the interchromatin space of mammalian cell nuclei. PS
Autor:
Daniel M. Passon, Wolfgang Schliebs, Krisztián Fodor, Matthias Wilmanns, Harald W. Platta, Stefanie Hagen, Friedel Drepper, Sven Fischer, Michael Zenn, Bettina Warscheid, Wolfgang Girzalsky, Ralf Erdmann
The peroxisomal matrix protein import is facilitated by cycling import receptors that shuttle between the cytosol and the peroxisomal membrane. The import receptor Pex5p mediates the import of proteins harboring a peroxisomal targeting signal of type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39b0083d9dbdc9f5a45bc5dae17bf04f
https://europepmc.org/articles/PMC4646318/
https://europepmc.org/articles/PMC4646318/
Publikováno v:
Protein science : a publication of the Protein Society. 24(12)
Members of the Drosophila behavior/human splicing (DBHS) protein family have been characterized in the vertebrates Homo sapiens and Mus musculus, and the invertebrates Drosophila melanogaster and Chironomus tentans. Collectively, both vertebrate and
Autor:
Leonidas Emmanouilidis, Daniel M. Passon, Michael Sattler, Matthias Wilmanns, Mohanraj Gopalswamy
Publikováno v:
Biochim. Biophys. Acta-Mol. Cell Res. 1863, 804-813 (2016)
The peroxisomal proteins (peroxins) that mediate the import of peroxisomal matrix proteins have been identified. Recently, the purification of a functional peroxisomal translocon has been reported. However, the molecular details of the import pathway
Autor:
Gavin J. Knott, Agata Sadowska, Daniel M. Passon, Archa H. Fox, Maria R. Conte, Charles S. Bond, Mihwa Lee
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 70:C1655-C1655
The Drosophila behaviour/human splicing (DBHS) proteins are a family of obligatory dimeric proteins found in higher order mammals down to the simplest invertebrates. `Multifunctional protein family' essentially captures what is understood regarding D