Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Megan Mayerle"'
Publikováno v:
Circulation Research. 124:1420-1424
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dcfcfa490bfe114b537ab56a55ba3927
https://doi.org/10.1161/circresaha.119.310761
https://doi.org/10.1161/circresaha.119.310761
Autor:
J. Matthew Ragle, Christine Guthrie, Megan Mayerle, Sol Katzman, Samira Yitiz, Lucero E Rogel, Alan M. Zahler, Cameron M. Soulette, Andrea Ramirez
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 6
Pre-mRNA splicing must occur with extremely high fidelity. Spliceosomes assemble onto pre-mRNA guided by specific sequences (5′ splice site, 3′ splice site, and branchpoint). When splice sites are mutated, as in many hereditary diseases, the spli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2cc6d448e5a659eab1812458c5b3c60
https://doi.org/10.1073/pnas.1819020116
https://doi.org/10.1073/pnas.1819020116
Publikováno v:
RNA. :rna.079448.122
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6bc747c8ba3d64096e93be0bd9d3425
https://doi.org/10.1261/rna.079448.122
https://doi.org/10.1261/rna.079448.122
Autor:
Megan Mayerle, Christine Guthrie
Publikováno v:
Methods. 125:3-9
The spliceosome is not a single macromolecular machine. Rather it is a collection of dynamic heterogeneous subcomplexes that rapidly interconvert throughout the course of a typical splicing cycle. Because of this, for many years the only high resolut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5c984a78f926db1059e65a5e50f2554
https://doi.org/10.1016/j.ymeth.2017.01.006
https://doi.org/10.1016/j.ymeth.2017.01.006
Autor:
Megan Mayerle, Christine Guthrie
Publikováno v:
RNA. 22:793-809
Pre-mRNA splicing must occur with high fidelity and efficiency for proper gene expression. The spliceosome uses DExD/H box helicases to promote on-pathway interactions while simultaneously minimizing errors. Prp8 and Snu114, an EF2-like GTPase, regul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::babe5756580aca537c7e00c1fadce8ea
https://doi.org/10.1261/rna.055459.115
https://doi.org/10.1261/rna.055459.115
Autor:
Christine Guthrie, Megan Mayerle
Many spliceosomal DExD/H box helicases act as fidelity factors during pre-mRNA splicing, promoting on-pathway interactions while simultaneously minimizing errors. Mutations linked to Retinitis Pigmentosa (RP), a form of heritable blindness, map to ke
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90837cfdd95b00518052e3feb4b0525d
https://doi.org/10.1101/354514
https://doi.org/10.1101/354514
Autor:
Melissa S. Jurica, Alma L. Burlingame, Andrew J. MacRae, Robert J. Chalkley, Megan Mayerle, Christine Guthrie, Eva Hrabeta-Robinson
Publikováno v:
RNA (New York, N.Y.), vol 24, iss 6
Prp8 is an essential protein that regulates spliceosome assembly and conformation during pre-mRNA splicing. Recent cryo-EM structures of the spliceosome model Prp8 as a scaffold for the spliceosome's catalytic U snRNA components. Using a new amino ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc95d561e214c4438bda2b737555dff5
https://pubmed.ncbi.nlm.nih.gov/29487104
https://pubmed.ncbi.nlm.nih.gov/29487104
Autor:
Zaida Luthey-Schulten, Kaushik Ragunathan, Taekjip Ha, Megan Mayerle, Hajin Kim, Ke Chen, Sanjaya C. Abeysirigunawarden, Sarah A. Woodson
Publikováno v:
Nature. 506:334-338
The assembly of 30S ribosomes requires the precise addition of 20 proteins to the 16S ribosomal RNA. How early binding proteins change the ribosomal RNA structure so that later proteins may join the complex is poorly understood. Here we use single-mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::727a00a3b42ac87e5c3db12f64e392c8
https://doi.org/10.1038/nature13039
https://doi.org/10.1038/nature13039
Autor:
Sarah A. Woodson, Megan Mayerle
Publikováno v:
RNA. 19:574-585
Assembly of bacterial 30S ribosomal subunits requires structural rearrangements to both its 16S rRNA and ribosomal protein components. Ribosomal protein S4 nucleates 30S assembly and associates rapidly with the 5′ domain of the 16S rRNA. In vitro,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::634e60f943a9192414416b1d2e732044
https://doi.org/10.1261/rna.037028.112
https://doi.org/10.1261/rna.037028.112
Publikováno v:
Biophysical Journal. 114:253a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a7141f6ef312ad740219f749c179c1f
https://doi.org/10.1016/j.bpj.2017.11.1405
https://doi.org/10.1016/j.bpj.2017.11.1405