Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Jonathan D. Dattelbaum"'
Autor:
Alessia Ruggiero, Jonathan D Dattelbaum, Maria Staiano, Rita Berisio, Sabato D'Auria, Luigi Vitagliano
Publikováno v:
PLoS ONE, Vol 9, Iss 5, p e96560 (2014)
The arginine binding protein from Thermatoga maritima (TmArgBP), a substrate binding protein (SBP) involved in the ABC system of solute transport, presents a number of remarkable properties. These include an extraordinary stability to temperature and
Externí odkaz:
https://doaj.org/article/e6d6e3d59dc04e9687f9643a0d3add11
Autor:
Joseph R. Lakowicz, Ignacy Gryczynski, Felix N. Castellano, G Rao, Li Li, Jonathan D. Dattelbaum, Leah Tolosa
Publikováno v:
Acta physica Polonica: A. 95(1)
The technology and applications of fluorescence spectroscopy are rapidly advancing. In this overview presentation we summarize some recent developments from this laboratory. Two and three-photon excitation have been observed for a wide variety of int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59cc5c5f67ee46228c4d76ddb664f0bb
https://pubmed.ncbi.nlm.nih.gov/31660002
https://pubmed.ncbi.nlm.nih.gov/31660002
Autor:
Kristen J. Rubenstein, Jonathan D. Dattelbaum, Michael C. Leopold, Raef H. Lambertson, Margaret A. Schwarzmann, Grace E. Conway, Helene W. Kerins, Michael J. Pannell
Publikováno v:
Journal of Electroanalytical Chemistry. 775:135-145
A layer-by-layer (LbL) strategy of modifying an electrode with a specific combination of polymeric and xerogel materials is used to create an effective first generation biosensor for uric acid (UA) - a clinically relevant molecule implemented in preg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::94987e40ceecb5f708b103c91e94a546
https://doi.org/10.1016/j.jelechem.2016.05.038
https://doi.org/10.1016/j.jelechem.2016.05.038
Autor:
Marilisa Vigorita, Giuseppe Graziano, Luigi Vitagliano, Sabato D'Auria, Jonathan D. Dattelbaum, Giovanni Smaldone, Pompea Del Vecchio, Alessia Ruggiero, Nicole Balasco
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics 1864 (2016): 814–824. doi:10.1016/j.bbapap.2016.04.006
info:cnr-pdr/source/autori:Smaldone, Giovanni; Vigorita, Marilisa; Ruggiero, Alessia; Balasco, Nicole; Dattelbaum, Jonathan D.; D'Auria, Sabato; Del Vecchio, Pompea; Graziano, Giuseppe; Vitagliano, Luigi/titolo:Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein/doi:10.1016%2Fj.bbapap.2016.04.006/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2016/pagina_da:814/pagina_a:824/intervallo_pagine:814–824/volume:1864
info:cnr-pdr/source/autori:Smaldone, Giovanni; Vigorita, Marilisa; Ruggiero, Alessia; Balasco, Nicole; Dattelbaum, Jonathan D.; D'Auria, Sabato; Del Vecchio, Pompea; Graziano, Giuseppe; Vitagliano, Luigi/titolo:Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein/doi:10.1016%2Fj.bbapap.2016.04.006/rivista:Biochimica et biophysica acta. Proteins and proteomics/anno:2016/pagina_da:814/pagina_a:824/intervallo_pagine:814–824/volume:1864
The Arginine Binding Protein isolated from Thermotoga maritima (TmArgBP) is a protein endowed with several peculiar properties. We have previously shown that TmArgBP dimerization is a consequence of the swapping of the C-terminal helix. Here we explo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d60d8b5c402236e6fd3620d6aed4be09
https://doi.org/10.1016/j.bbapap.2016.04.006
https://doi.org/10.1016/j.bbapap.2016.04.006
Autor:
Teraya Donaldson, Sabato D'Auria, Jonathan D. Dattelbaum, Lindsay J. Deacon, Luisa Iozzino, Hilbert Billones, Alessio Ausili
Publikováno v:
Analytical biochemistry
525 (2017): 60–66. doi:10.1016/j.ab.2017.02.021
info:cnr-pdr/source/autori:Donaldson, Teraya; Iozzino, Luisa; Deacon, Lindsay J.; Billones, Hilbert; Ausili, Alessio; D'Auria, Sabato; Dattelbaum, Jonathan D./titolo:Engineering a switch-based biosensor for arginine using a Thermotoga maritima periplasmic binding protein/doi:10.1016%2Fj.ab.2017.02.021/rivista:Analytical biochemistry (Print)/anno:2017/pagina_da:60/pagina_a:66/intervallo_pagine:60–66/volume:525
525 (2017): 60–66. doi:10.1016/j.ab.2017.02.021
info:cnr-pdr/source/autori:Donaldson, Teraya; Iozzino, Luisa; Deacon, Lindsay J.; Billones, Hilbert; Ausili, Alessio; D'Auria, Sabato; Dattelbaum, Jonathan D./titolo:Engineering a switch-based biosensor for arginine using a Thermotoga maritima periplasmic binding protein/doi:10.1016%2Fj.ab.2017.02.021/rivista:Analytical biochemistry (Print)/anno:2017/pagina_da:60/pagina_a:66/intervallo_pagine:60–66/volume:525
The Thermotoga maritima arginine-binding protein (TmArgBP) has been modified to create a reagentless fluorescent protein biosensor. Two design methods for biosensor construction are compared: 1) solvent accessibility of environmentally-sensitive prob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6c9a1aa20ab774936f82c820b3d6649
http://www.cnr.it/prodotto/i/392915
http://www.cnr.it/prodotto/i/392915
Autor:
Jessica J. Field, Jonathan D. Dattelbaum, Peter T. Northcote, John H. Miller, A. Jonathan Singh
Publikováno v:
The Journal of Organic Chemistry. 80:304-312
The NMR-directed isolation and structure elucidation of nine new nitrogenous hamigeran diterpenoids from the New Zealand marine sponge Hamigera tarangaensis are described. Featured in this set are the oxazole-containing hamigeran M (4) and eight comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be69ce08301356356868c6b14dfcaac5
https://doi.org/10.1021/jo502370b
https://doi.org/10.1021/jo502370b
Autor:
Michael C. Leopold, Margot M. Hillyer, Jonathan D. Dattelbaum, Lauren E. Finch, Alisha S. Cerel
Publikováno v:
Chemosphere. 108:205-213
A wide spectrum and large number of children’s toys and toy jewelry items were purchased from both bargain and retail vendors and analyzed for arsenic, cadmium, and lead metal content using multiple analytical techniques, including flame and furnac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34bd629b07e8c442584bdb9241f192c9
https://doi.org/10.1016/j.chemosphere.2014.01.041
https://doi.org/10.1016/j.chemosphere.2014.01.041
Autor:
Sabato D'Auria, Jonathan D. Dattelbaum, Maria Staiano, Alessandro Capo, Antonio Varriale, Alessio Ausili
Publikováno v:
Life, Vol 3, Iss 1, Pp 149-160 (2013)
Life : Open Access Journal
Life : Open Access Journal
Arginine-binding protein from the extremophile Thermotoga maritima is a 27.7 kDa protein possessing the typical two-domain structure of the periplasmic binding proteins family. The protein is characterized by a very high specificity and affinity to b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21257536babeed7ea3a39c40b2a7d3e5
http://www.mdpi.com/2075-1729/3/1/149
http://www.mdpi.com/2075-1729/3/1/149
Publikováno v:
The Open Marine Biology Journal. 4:87-95
Several marine sponges sequester high concentrations of carotenoids in their tissues. The diversity of carotenoid compounds has been described in detail for a handful of species, but to date, little attention has been paid to natural variability in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df3fb7fa34c509d0cafeeb4304d0fb55
https://doi.org/10.2174/1874450801004010087
https://doi.org/10.2174/1874450801004010087
Publikováno v:
Bioconjugate Chemistry. 20:2381-2384
A robust method to immobilize a maltose biosensor is described using an engineered maltose periplasmic binding protein (PBP) covalently coupled to NBDamide, an environmentally sensitive fluorophore. A mesoporous silica sol-gel derived from diglyceryl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8144d6cccda51485ea6a3b21bdfc1be2
https://doi.org/10.1021/bc900341s
https://doi.org/10.1021/bc900341s