Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Mack Sobhany"'
Autor:
Monica C. Pillon, Meredith N. Frazier, Lucas B. Dillard, Jason G. Williams, Seda Kocaman, Juno M. Krahn, Lalith Perera, Cassandra K. Hayne, Jacob Gordon, Zachary D. Stewart, Mack Sobhany, Leesa J. Deterding, Allen L. Hsu, Venkata P. Dandey, Mario J. Borgnia, Robin E. Stanley
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nsp15 is a uridine specific endoribonuclease present in all coronaviruses. Here, the authors determine the cryo-EM structures of SARS-CoV-2 Nsp15 in the apo and UTP-bound states, which together with biochemical experiments, mass spectrometry and mole
Externí odkaz:
https://doaj.org/article/3b3bd68422cc4508a02721056de1a082
Autor:
Soumyadip Sahu, Jacob Gordon, Chunfang Gu, Mack Sobhany, Dorothea Fiedler, Robin E. Stanley, Stephen B. Shears
Publikováno v:
Biomolecules, Vol 13, Iss 1, p 153 (2023)
Inositol pyrophosphates (PP-InsPs); are a functionally diverse family of eukaryotic molecules that deploy a highly-specialized array of phosphate groups as a combinatorial cell-signaling code. One reductive strategy to derive a molecular-level unders
Externí odkaz:
https://doaj.org/article/cdac5d5e38e7480aa0830c4af3bf7ffa
Autor:
Yu-Hua Lo, Mack Sobhany, Allen L. Hsu, Brittany L. Ford, Juno M. Krahn, Mario J. Borgnia, Robin E. Stanley
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
Rix7 is a type II AAA-ATPase that is required for the assembly of the large ribosomal subunit. Here the authors present the 4.5 Å cryo-EM structure of the Rix7 homohexamer with a polypeptide fragment bound in its central channel and provide insight
Externí odkaz:
https://doaj.org/article/532b14f2bbab448784ac75464a65da1f
Autor:
Robin E. Stanley, Mack Sobhany
Publikováno v:
J Vis Exp
Polysome fractionation by sucrose density gradient centrifugation is a powerful tool that can be used to create ribosome profiles, identify specific mRNAs being translated by ribosomes, and analyze polysome associated factors. While automated gradien
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45262176cb3badff4d6eafbe041306b3
https://doi.org/10.3791/62680-v
https://doi.org/10.3791/62680-v
Autor:
Monica C. Pillon, Mack Sobhany, Mario J. Borgnia, Juno M. Krahn, Allen L. Hsu, Jason Williams, Robin E. Stanley, Kevin H Goslen
Publikováno v:
Nature structural & molecular biology
Ribosome assembly is a complex process reliant on the coordination of trans-acting enzymes to produce functional ribosomal subunits and secure the translational capacity of cells. The endoribonuclease (RNase) Las1 and the poly-nucleotide kinase (PNK)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6693290b197680cc4a076bb56bf515f3
https://doi.org/10.1038/s41594-019-0289-8
https://doi.org/10.1038/s41594-019-0289-8
Autor:
Lucas B. Dillard, Cassandra K. Hayne, Meredith N Frazier, Lalith Perera, Robin E. Stanley, Allen L. Hsu, Leesa J. Deterding, Jason Williams, Zachary D. Stewart, Mario J. Borgnia, Jacob Gordon, Venkata P. Dandey, Monica C. Pillon, Mack Sobhany, Seda Kocaman, Juno M. Krahn
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
bioRxiv
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
bioRxiv
Nsp15, a uridine specific endoribonuclease conserved across coronaviruses, processes viral RNA to evade detection by host defense systems. Crystal structures of Nsp15 from different coronaviruses have shown a common hexameric assembly, yet how the en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fd88fa61a41e36bf913df39126d8bfb
Autor:
Monica C. Pillon, Meredith N. Frazier, Lucas B. Dillard, Jason G. Williams, Seda Kocaman, Juno M. Krahn, Lalith Perera, Cassandra K. Hayne, Jacob Gordon, Zachary D. Stewart, Mack Sobhany, Leesa J. Deterding, Allen L. Hsu, Venkata P. Dandey, Mario J. Borgnia, Robin E. Stanley
Publikováno v:
Nature Communications
Nsp15, a uridine specific endoribonuclease conserved across coronaviruses, processes viral RNA to evade detection by host defense systems. Crystal structures of Nsp15 from different coronaviruses have shown a common hexameric assembly, yet how the en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c681bcbdd8d24dd78f6f58a25417f339
https://pubmed.ncbi.nlm.nih.gov/33504779
https://pubmed.ncbi.nlm.nih.gov/33504779
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
https://doi.org/10.1074/jbc.m115.693259
Mitochondrial acetyl-CoA reversibly regulates locus-specific histone acetylation and gene expression
Autor:
Mack Sobhany, Gonzalo Riadi, Janine H. Santos, Oswaldo A. Lozoya, Douglas Ganini da Silva, Taylor C. Wolfgang, Tianyuan Wang, Navdeep S. Chandel, Dagoberto Grenet, Richard P. Woychik
Publikováno v:
Life Science Alliance
This study shows that genetic or pharmacological manipulation of the TCA cycle, when mitochondria are dysfunctional, can modulate histone acetylation and gene expression in the nucleus with physiological outcomes.
The impact of mitochondrial dys
The impact of mitochondrial dys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3771e28caf3af5e52e3d20941dd6d55f
https://pubmed.ncbi.nlm.nih.gov/30737248
https://pubmed.ncbi.nlm.nih.gov/30737248
Publikováno v:
RNA (New York, N.Y.). 24(5)
Grc3 is an essential well-conserved eukaryotic polynucleotide kinase (PNK) that cooperates with the endoribonuclease Las1 to process the preribosomal RNA (rRNA). Aside from being dependent upon Las1 for coordinated kinase and nuclease function, littl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b86376b9d3fb9cc7a2604ecc09311379
https://pubmed.ncbi.nlm.nih.gov/29440475
https://pubmed.ncbi.nlm.nih.gov/29440475