The HIV-1 Rev Activation Domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
- U. Fischer, J. Huber, W. Boelens, Lain W Mattajt, R. Lührmann
- Biology, ChemistryCell
- 11 August 1995
The Spinal Muscular Atrophy Disease Gene Product, SMN, and Its Associated Protein SIP1 Are in a Complex with Spliceosomal snRNP Proteins
- Qing Liu, U. Fischer, Fan Wang, G. Dreyfuss
- BiologyCell
- 19 September 1997
Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN complex and the role of a new component, Lsm11, in histone RNA processing.
- R. Pillai, M. Grimmler, D. Schümperli
- BiologyGenes & Development
- 15 September 2003
The U7-specific Lsm11 protein not only specifies the assembly of the U7 Sm core but also fulfills an important role in U7 snRNP-mediated histone mRNA processing.
The SMN–SIP1 Complex Has an Essential Role in Spliceosomal snRNP Biogenesis
- U. Fischer, Qing Liu, G. Dreyfuss
- BiologyCell
- 19 September 1997
A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs
- G. Meister, D. Bühler, R. Pillai, F. Lottspeich, U. Fischer
- BiologyNature Cell Biology
- 1 November 2001
It is shown that assembly of U1 snRNP depends on ATP, the first direct evidence that a complex containing SMN and Gemin2 mediates the active assembly of spliceosomal U snRNPs.
Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
- G. Meister, Christian Eggert, D. Bühler, H. Brahms, C. Kambach, U. Fischer
- Biology, ChemistryCurrent Biology
- 11 December 2001
HIV‐1 infection of non‐dividing cells: evidence that the amino‐terminal basic region of the viral matrix protein is important for Gag processing but not for post‐entry nuclear import
- R. Fouchier, B. Meyer, J. Simon, U. Fischer, M. Malim
- BiologyEMBO Journal
- 1 August 1997
It is found that disruption of this region (26KK→TT) reduces the rate at which the viral Gag polyprotein (p55Gag) is post‐translationally processed by the viral protease.
SMN Tudor domain structure and its interaction with the Sm proteins
- Philipp Selenko, R. Sprangers, G. Stier, D. Bühler, U. Fischer, M. Sattler
- Biology, ChemistryNature Structural Biology
- 2001
The three-dimensional structure of the Tudor domain of human SMN is determined and it is shown that a conserved negatively charged surface that is shown to interact with the C-terminal Arg and Gly-rich tails of Sm proteins.
Interaction of the Human Immunodeficiency Virus Type 1 Vpr Protein with the Nuclear Pore Complex
- R. Fouchier, B. Meyer, M. Malim
- BiologyJournal of Virology
- 1 July 1998
These findings not only demonstrate that Vpr harbors a bona fide NLS but also raise the possibility that one (or more) of Vpr’s functions may take place at the NPC.
Reduced U snRNP assembly causes motor axon degeneration in an animal model for spinal muscular atrophy.
- C. Winkler, Christian Eggert, U. Fischer
- BiologyGenes & Development
- 1 October 2005
Gen silencing is used to assess the effect of SMN protein deficiency on U snRNP metabolism in living cells and organisms and suggests that motoneuron degeneration in SMA patients is a direct consequence of impaired production of U snRNPs.
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