Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Anna L. Mallam"'
Autor:
Anna L. Mallam, Wisath Sae-Lee, Jeffrey M. Schaub, Fan Tu, Anna Battenhouse, Yu Jin Jang, Jonghwan Kim, John B. Wallingford, Ilya J. Finkelstein, Edward M. Marcotte, Kevin Drew
Publikováno v:
Cell Reports, Vol 29, Iss 5, Pp 1351-1368.e5 (2019)
Summary: RNA-binding proteins (RBPs) play essential roles in biology and are frequently associated with human disease. Although recent studies have systematically identified individual RNA-binding proteins, their higher-order assembly into ribonucleo
Externí odkaz:
https://doaj.org/article/e8a21dcd8f5c43018b9c8767abe0acbb
Publikováno v:
Cell Reports, Vol 24, Iss 1, Pp 259-268.e3 (2018)
Summary: Multi-protein complexes are necessary for nearly all cellular processes, and understanding their structure is required for elucidating their function. Current high-resolution strategies in structural biology are effective but lag behind othe
Externí odkaz:
https://doaj.org/article/a43ae9534dac4cd4bc68c8d8cf79bb5d
Autor:
Claire D McWhite, Wisath Sae-Lee, Yaning Yuan, Anna L Mallam, Nicolas A Gort-Freitas, Silvia Ramundo, Masayuki Onishi, Edward M Marcotte
Publikováno v:
Molecular Systems Biology, Vol 20, Iss 8, Pp 933-951 (2024)
Abstract The variability of proteins at the sequence level creates an enormous potential for proteome complexity. Exploring the depths and limits of this complexity is an ongoing goal in biology. Here, we systematically survey human and plant high-th
Externí odkaz:
https://doaj.org/article/6953cb1a1b2148c5b640f8b922f7ea45
Autor:
Claire D. McWhite, Wisath Sae-Lee, Yaning Yuan, Anna L. Mallam, Nicolas A. Gort-Freitas, Silvia Ramundo, Masayuki Onishi, Edward M. Marcotte
Variability of proteins at the sequence level creates an enormous potential for proteome complexity. Exploring the depths and limits of this complexity is an ongoing goal in biology. Here, we systematically survey human and plant high-throughput bott
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f7c797c898fadd70a3303859b7610b9e
https://doi.org/10.1101/2022.09.21.508930
https://doi.org/10.1101/2022.09.21.508930
Publikováno v:
PLoS Biology, Vol 12, Iss 12, p e1002028 (2014)
The Neurospora crassa mitochondrial tyrosyl-tRNA synthetase (mtTyrRS; CYT-18 protein) evolved a new function as a group I intron splicing factor by acquiring the ability to bind group I intron RNAs and stabilize their catalytically active RNA structu
Externí odkaz:
https://doaj.org/article/ab0c0e9e13c94bb29202a42b4157ae4b
Publikováno v:
eLife, Vol 3 (2014)
How different helicase families with a conserved catalytic ‘helicase core’ evolved to function on varied RNA and DNA substrates by diverse mechanisms remains unclear. In this study, we used Mss116, a yeast DEAD-box protein that utilizes ATP to lo
Externí odkaz:
https://doaj.org/article/d44ba9bd88d343c38994244d1e27d1a5
Autor:
Anna L. Mallam, Edward M. Marcotte
Publikováno v:
Cell Systems. 4:483-494
Recent mass spectrometry maps of the human interactome independently support the existence of a large multiprotein complex, dubbed "Commander." Broadly conserved across animals and ubiquitously expressed in nearly every human cell type examined thus
Autor:
Anna L. Mallam, David W. Taylor, Andrew P. Horton, Yi Zhou, Edward M. Marcotte, Eric J. Verbeke
Publikováno v:
J Struct Biol
Single particle analysis for structure determination in cryo-electron microscopy is traditionally applied to samples purified to near homogeneity as current reconstruction algorithms are not designed to handle heterogeneous mixtures of structures fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4375da88f6223d2372b3d26418f656ad
https://doi.org/10.1101/611566
https://doi.org/10.1101/611566
Publikováno v:
Cell reports
Cell Reports, Vol 24, Iss 1, Pp 259-268.e3 (2018)
Cell Reports, Vol 24, Iss 1, Pp 259-268.e3 (2018)
SUMMARY Multi-protein complexes are necessary for nearly all cellular processes, and understanding their structure is required for elucidating their function. Current high-resolution strategies in structural biology are effective but lag behind other
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3491e31b2564cb9f4c7e4d4694e639c8
https://doi.org/10.1101/247254
https://doi.org/10.1101/247254
Autor:
Kevin Drew, Edward M. Marcotte, Anna L. Mallam, Jeffrey M. Schaub, John B. Wallingford, Yu Jin Jang, Ilya J. Finkelstein, Wisath Sae-Lee, Jonghwan Kim, Anna Battenhouse, Fan Tu
Publikováno v:
Cell Reports, Vol 29, Iss 5, Pp 1351-1368.e5 (2019)
Cell reports
Cell reports
SUMMARY RNA-binding proteins (RBPs) play essential roles in biology and are frequently associated with human disease. Although recent studies have systematically identified individual RNA-binding proteins, their higher-order assembly into ribonucleop