Structural Basis of Assembly Chaperone- Mediated snRNP Formation-Reference-Cited by-同舟云学术

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Structural Basis of Assembly Chaperone- Mediated snRNP Formation

Published:2013-02 Issue:4 Volume:49 Page:692-703
ISSN:1097-2765
Container-title:Molecular Cell
language:en
Short-container-title:Molecular Cell

Author:

Grimm Clemens,Chari Ashwin,Pelz Jann-Patrick,Kuper Jochen,Kisker Caroline,Diederichs Kay,Stark Holger,Schindelin Hermann,Fischer Utz

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology

Reference33 articles.

1. The cell as a collection of protein machines: preparing the next generation of molecular biologists;Alberts;Cell,1998

2. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B’ and the Sm-like protein LSm4, and their interaction with the SMN protein;Brahms;RNA,2001

3. Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy;Bühler;Hum. Mol. Genet.,1999

4. Cellular strategies for the assembly of molecular machines;Chari;Trends Biochem. Sci.,2010

5. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs;Chari;Cell,2008

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1. A unique mechanism of snRNP core assembly;2024-07-10

2. Disordered-to-ordered transitions in assembly factors allow the complex II catalytic subunit to switch binding partners;Nature Communications;2024-01-11

3. Mechanism of assembly of snRNP cores assisted by ICln and the SMN complex in fission yeast;iScience;2023-09

4. Evaluation of <i>in vitro</i> functional activity of ANB4 drug for the treatment of spinal muscular atrophy;Genes & Cells;2023-08-23

5. In vitro methylation of the U7 snRNP subunits Lsm11 and SmE by the PRMT5/MEP50/pICln methylosome;RNA;2023-08-10

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