Výsledky vyhledávání - "Erin M. Romes"

The Crystal Structure of the Ubiquitin-like Domain of Ribosome Assembly Factor Ytm1 and Characterization of Its Interaction with the AAA-ATPase Midasin

Autor: Erin M. Romes, Robin E. Stanley, Mack Sobhany

Publikováno v: Journal of Biological Chemistry. 291:882-893

The synthesis of eukaryotic ribosomes is a complex, energetically demanding process requiring the aid of numerous non-ribosomal factors, such as the PeBoW complex. The mammalian PeBoW complex, composed of Pes1, Bop1, and WDR12, is essential for the p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b5e7f4813ab6645be70ddb7cb60431b
https://doi.org/10.1074/jbc.m115.693259

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Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2

Autor: Mack Sobhany, Robin E. Stanley, Monica C. Pillon, Erin M. Romes, Yu-Hua Lo

Publikováno v: Structure (London, England : 1993). 25(5)

Ribosome assembly is a complex process that requires hundreds of essential assembly factors, including Rix7 (NVL2 in mammals) and Nsa1 (WDR74 in mammals). Rix7 is a type II double ring, AAA-ATPase, which is closely related to the well-known Cdc48/p97

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::051301d74904606fd1e17f7f895c1f39
https://pubmed.ncbi.nlm.nih.gov/28416111

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The Mechanism of Dynein Light Chain LC8-mediated Oligomerization of the Ana2 Centriole Duplication Factor

Autor: Erin M. Romes, Lauren K. Slevin, Kevin C. Slep, Mary G. Dandulakis

Publikováno v: Journal of Biological Chemistry. 289:20727-20739

Centrioles play a key role in nucleating polarized microtubule networks. In actively dividing cells, centrioles establish the bipolar mitotic spindle and are essential for genomic stability. Drosophila anastral spindle-2 (Ana2) is a conserved centrio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d711b0c62a840d5711faa4f9acaed64
https://doi.org/10.1074/jbc.m114.576041

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The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization

Autor: Kevin C. Slep, Matthew P. Nicholas, Lu Rao, Erin M. Romes, Sibylle Brenner, Arne Gennerich, Ashutosh Tripathy

Publikováno v: Molecular Biology of the Cell

Studying the role of accessory chains in dynein single-molecule motility shows that the dynein light chain (LC) and intermediate chain (IC) promote motor dimerization, increase velocity, and potentiate processivity. The crystal structure of the yeast

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6d084d9dbe22e28fa608e3d14552ee9
https://pubmed.ncbi.nlm.nih.gov/23761070

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Structure of a Yeast Dyn2-Nup159 Complex and Molecular Basis for Dynein Light Chain-Nuclear Pore Interaction

Autor: Kevin C. Slep, Ashutosh Tripathy, Erin M. Romes

The nuclear pore complex gates nucleocytoplasmic transport through a massive, eight-fold symmetric channel capped by a nucleoplasmic basket and structurally unique, cytoplasmic fibrils whose tentacles bind and regulate asymmetric traffic. The conserv

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