Zobrazeno 1 - 9
of 9
pro vyhledávání: '"B L, Stoddard"'
Autor:
H. F. Moffett, M. E. Coon, S. Radtke, S. B. Stephan, L. McKnight, A. Lambert, B. L. Stoddard, H. P. Kiem, M. T. Stephan
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-13 (2017)
Current widely used viral and electroporation methods for creating therapeutic cell-based products are complex and expensive. Here, the authors develop targeted mRNA nanocarriers that can transiently program gene expression by simply mixing them with
Externí odkaz:
https://doaj.org/article/980299c002f4470893064c45e6cc2b18
Publikováno v:
Journal of Applied Crystallography. 28:829-834
In order to directly observe the structure of enzyme intermediate complexes that form during turnover, one must ensure the homogeneous and complete accumulation of the intermediate during the collection of diffraction data. In the case of steady-stat
Publikováno v:
Nature structural biology. 8(4)
Homing endonucleases, like restriction enzymes, cleave double-stranded DNA at specific target sites. The cleavage mechanism(s) utilized by LAGLIDADG endonucleases have been difficult to elucidate; their active sites are divergent, and only one low re
Autor:
M L, Liu, B W, Shen, S, Nakaya, K P, Pratt, K, Fujikawa, E W, Davie, B L, Stoddard, A R, Thompson
Publikováno v:
Blood. 96(3)
Factor VIII C domains contain key binding sites for von Willebrand factor (vWF) and phospholipid membranes. Hemophilic patients were screened for factor VIII C-domain mutations to provide a well-characterized series. Mutated residues were localized t
Publikováno v:
Nature structural biology. 6(12)
A novel mechanism of DNA endonucleolytic cleavage has been visualized for the homing endonuclease I-PpoI by trapping the uncleaved enzyme-substrate complex and comparing it to the previously visualized product complex. This enzyme employs a unique si
Publikováno v:
Bioorganicmedicinal chemistry letters. 9(8)
A library of 109 1,3-dioxane-4,6-dione-5-carboxamides was prepared by solution-phase methods as potential inhibitors of human group IIa phospholipase A2. Tight binding inhibitors were found by an interfacial affinity selection method. The crystal str
Publikováno v:
Proteins. 28(1)
Group I intron endonuclease I-CreI is encoded by an open reading frame contained within a self-splicing intron in the Chlamydomonas reinhardtii chloroplast 23S rRNA gene. I-CreI initiates the lateral transfer or homing of this intron by specifically
Publikováno v:
Proteins. 27(2)
A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10-methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, puri
Publikováno v:
Proteins. 27(2)
The monofunctional enzyme 10-formyltetrahydrofolate synthetase (THFS), which is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways, has been subcloned, purified, and c