Zobrazeno 1 - 10
of 122
pro vyhledávání: '"Thomas C. Squier"'
Autor:
Karen A. Hecht, Yijia Xiong, Daniel A. Barrack, Nicole R. Ford, Guritno Roesijadi, Thomas C. Squier
Publikováno v:
ACS Omega, Vol 3, Iss 2, Pp 2104-2110 (2018)
Externí odkaz:
https://doaj.org/article/fa2e4ca790e74b06af20ded2b100dc14
Autor:
Nicole R. Ford, Yijia Xiong, Karen A. Hecht, Thomas C. Squier, Gregory L. Rorrer, Guritno Roesijadi
Publikováno v:
Biology, Vol 9, Iss 1, p 14 (2020)
In vivo functionalization of diatom biosilica frustules by genetic manipulation requires careful consideration of the overall structure and function of complex fusion proteins. Although we previously had transformed Thalassiosira pseudonana with cons
Externí odkaz:
https://doaj.org/article/3d52fe080c394166ad55c2ed6d1bb130
Publikováno v:
BioTechniques, Vol 38, Iss 2, Pp 297-299 (2005)
Externí odkaz:
https://doaj.org/article/b9bd36ac822d4605b525efe2180054c1
Autor:
Tammie J. McQuistan, John Mata, James Summerton, Yijia Xiong, Thomas C. Squier, James W. Stanek
Publikováno v:
Analytical Biochemistry. 557:84-90
Here we identify a low-cost diagnostic platform using fluorescently-labeled phosphorodiamidate morpholino oligonucleotide (PMO) probe pairs, which upon binding target oligonucleotides undergo fluorescence resonance energy transfer (FRET). Using a tar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::108ca6b977032166ad1af76c2e42e1e7
https://doi.org/10.1016/j.ab.2018.07.006
https://doi.org/10.1016/j.ab.2018.07.006
Publikováno v:
Bioconjugate Chemistry. 28:2804-2814
Here, we identify the importance of molecular crowding agents in the functional stabilization of scFv antibodies. Antibodies were tethered through an engineered calmodulin (CaM)-binding peptide into a stimulus-responsive hydrogel composed of poly(eth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::623443c5310e62c103f88bf825d26a74
https://doi.org/10.1021/acs.bioconjchem.7b00512
https://doi.org/10.1021/acs.bioconjchem.7b00512
Publikováno v:
Bioconjugate Chemistry. 27:1205-1209
Self-assembly of recombinant proteins within the biosilica of living diatoms represents a means to construct functional materials in a reproducible and scalable manner that will enable applications that harness the inherent specificities of proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c643db8e0cb1552a05ea3fcec1bdf03
https://doi.org/10.1021/acs.bioconjchem.6b00165
https://doi.org/10.1021/acs.bioconjchem.6b00165
Autor:
Galya Orr, Yijia Xiong, Thomas C. Squier, Karen A. Hecht, G. Roesijadi, Dehong Hu, Gregory L. Rorrer, Nicole R. Ford
Publikováno v:
ACS Synthetic Biology. 5:193-199
The diatom Thalassiosira pseudonana was genetically modified to express biosilica-targeted fusion proteins comprising either enhanced green fluorescent protein (EGFP) or single chain antibodies engineered with a tetracysteine tagging sequence. Of int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ea4cbb7ccbe4c00502aaf0af8ee3d87
https://doi.org/10.1021/acssynbio.5b00191
https://doi.org/10.1021/acssynbio.5b00191
Publikováno v:
Phys. Chem. Chem. Phys.. 16:24026-24033
Control of the reactivity of the nickel center of the [NiFe] hydrogenase and other metalloproteins commonly involves outer coordination sphere ligands that act to modify the geometry and physical properties of the active site metal centers. We carrie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59382245d20a738ec18eb88ba8e7f368
https://doi.org/10.1039/c4cp03518f
https://doi.org/10.1039/c4cp03518f
Autor:
Brenda M. Beech, Diana J. Bigelow, Yijia Xiong, Cheryl L. Baird, Thomas C. Squier, Curt B. Boschek, Kathleen McAteer
Publikováno v:
Journal of the American Chemical Society. 136:13134-13137
Stimulus-responsive hydrogel materials that stabilize and control protein dynamics have the potential to enable a range of applications that take advantage of the inherent specificity and catalytic efficiencies of proteins. Here we describe the modul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a989d3affce5a6b8cee62821c95a453
https://doi.org/10.1021/ja506717v
https://doi.org/10.1021/ja506717v
Publikováno v:
Natural Science. :20-24
A putative chromate ion binding site was identified proximal to a rigidly bound FMN from electron densities in the crystal structure of the quinone reductase from Gluconacetobacter hansenii (Gh-ChrR) (3s2y.pdb). To clarify the location of the chromat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c15fccaf3c61900eb07f90049de00456
https://doi.org/10.4236/ns.2013.56a003
https://doi.org/10.4236/ns.2013.56a003