Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Mark R. Macbeth"'
Autor:
Keegan Jackson, Rebecca Hoff, Hannah Wright, Ashley Wilkinson, Frances Brewer, Amari Williams, Ben Whiteside, Mark R. Macbeth, Anne M. Wilson
Publikováno v:
Crystals, Vol 14, Iss 7, p 652 (2024)
Microgravity has been shown to be an excellent tool for protein crystal formation. A retrospective analysis of all publicly available crystallization data, including many that have not yet been published, clearly demonstrates the value of the microgr
Externí odkaz:
https://doaj.org/article/48590234b86f41a7aa65fa7b61a4f1a4
Autor:
David H Cho, Zach J Kartje, Luke Edward Severinac, Isobel E Bowles, Mark R. Macbeth, Geoffrey C. Hoops, Emily H Pool, R. Jeremy Johnson, Emily K Lawson, Benjamin S Lancaster, Christopher P. Savas
Publikováno v:
Protein Sci
Mycobacterium tuberculosis virulence is highly metal‐dependent with metal availability modulating the shift from the dormant to active states of M. tuberculosis infection. Rv0045c from M. tuberculosis is a proposed metabolic serine hydrolase whose
Autor:
Elizabeth Ransey, Mark R. Macbeth, Annie Heroux, Sourav K. Dey, Subha R. Das, Eduardo Paredes
Publikováno v:
FEBS Letters. 591:2003-2010
The RNA lariat debranching enzyme, Dbr1, is a metallophosphoesterase that cleaves 2'-5' phosphodiester bonds within intronic lariats. Previous reports have indicated that Dbr1 enzymatic activity is supported by diverse metal ions including Ni2+ , Mn2
Autor:
Carolyn M. Hurdle, Mark R. Macbeth
Publikováno v:
The FASEB Journal. 34:1-1
Autor:
Courtney L. Brown, Mark R. Macbeth
Publikováno v:
The FASEB Journal. 34:1-1
Publikováno v:
RNA. 10:1563-1571
Adenosine deaminases that act on RNA (ADARs) catalyze adenosine to inosine conversion in RNA that is largely double stranded. Human ADAR2 (hADAR2) contains two double-stranded RNA binding motifs (dsRBMs), separated by a 90-amino acid linker, and thes
Autor:
Mark R. Macbeth, Ira G. Wool
Publikováno v:
Journal of Molecular Biology. 285:567-580
The sarcin/ricin domain in 23 S/28 S rRNA is crucial for ribosome function, since it constitutes at least part of the binding site for the elongation factors and hence is essential for binding aminoacyl-tRNA and for translocation. The domain is also
Autor:
Ira G. Wool, Mark R. Macbeth
Publikováno v:
Journal of Molecular Biology. 285:965-975
The sarcin/ricin domain (SRD) in Escherichia coli 23 S rRNA forms a part of the site for the association of the elongation factors with the ribosome and hence is critical for the binding of aminoacyl-tRNA and for translocation. The domain is also the
Publikováno v:
The FASEB Journal. 27
Allosteric regulation of GRASP protein-dependent Golgi membrane tethering by mitotic phosphorylation
Mitotic phosphorylation of the conserved GRASP domain of GRASP65 disrupts its self-association, leading to a loss of Golgi membrane tethering, cisternal unlinking, and Golgi breakdown. Recently, the structural basis of the GRASP self-interaction was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::939a79dd82f466630b228ba7aa6e2660