Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Daniel F. A. R. Dourado"'
Autor:
Daniel F. A. R. Dourado, Balamurali Kannan, Darren Gray, Johann Chan, Michael J. Geier, Aliaksei Pukin, Stefan Mix, Mark E. Scott, Luke D. Humphreys, Xiaotian Wang, Gareth Brown
Publikováno v:
Organic Process Research & Development. 26:849-858
Autor:
Alexandra T. P. Carvalho, Daniel F. A. R. Dourado, Armando J. D. Silvestre, Pedro R. Figueiredo, Andreia F. Sousa, Beatriz C. Almeida
Publikováno v:
ChemCatChem. 12:4845-4852
Autor:
Thomas R Caulfield, Fabienne C Fiesel, Elisabeth L Moussaud-Lamodière, Daniel F A R Dourado, Samuel C Flores, Wolfdieter Springer
Publikováno v:
PLoS Computational Biology, Vol 10, Iss 11, p e1003935 (2014)
Loss-of-function mutations in PINK1 or PARKIN are the most common causes of autosomal recessive Parkinson's disease. Both gene products, the Ser/Thr kinase PINK1 and the E3 Ubiquitin ligase Parkin, functionally cooperate in a mitochondrial quality co
Externí odkaz:
https://doaj.org/article/f7354ae969fb4bd9aa4f52cf1971f172
Autor:
Armando J. D. Silvestre, Stephanie Paul, Derek J. Quinn, Daniel F. A. R. Dourado, Alexandra T. P. Carvalho, Beatriz C. Almeida, Pedro Figueiredo, Andreia F. Sousa, Thomas S. Moody
Reengineered variants of a hyperthermophilic carboxylesterase with improved product yield in the synthesis of poly(ε-caprolactone) and triblock poly(ε-caprolactone)-co-poly(ethylene glycol)Methods: Quantum Mechanics/Molecular Mechanics Molecular Dy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1959d0c8c26828f5b3f470acfce074dc
https://doi.org/10.26434/chemrxiv.14045915
https://doi.org/10.26434/chemrxiv.14045915
Publikováno v:
Chemistry-A European Journal, 2018, vol. 24, núm. 20, p. 5246-5252
Articles publicats (D-Q)
DUGiDocs – Universitat de Girona
instname
Articles publicats (D-Q)
DUGiDocs – Universitat de Girona
instname
A covalently bound flavin cofactor is predominant in the succinate-ubiquinone oxidoreductase (SQR; Complex II), an essential component of aerobic electron transport, and in the menaquinol-fumarate oxidoreductase (QFR), the anaerobic counterpart, alth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0193d98eb864263c70f8dc770d56cb7
https://hdl.handle.net/2072/373074
https://hdl.handle.net/2072/373074
Autor:
Pedro Figueiredo, Daniel F. A. R. Dourado, Beatriz C. Almeida, Andreia F. Sousa, Armando J. D. Silvestre, Alexandra T. P. Carvalho
Plastic pollution is causing an immeasurable damage to marine and land eco-systems. Better alternatives are actively being sought-after, such as biodegradable polyesters obtained by enzymatic synthesis. However, wild type enzymes still pose fundament
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a1d3e4bcc4baac059bb6b6141dbf794
https://doi.org/10.26434/chemrxiv.9638270
https://doi.org/10.26434/chemrxiv.9638270
Autor:
Anders Virtanen, U. Helena Danielson, Mohammad Reza Housaindokht, Olle Nordesjö, Sara Marie Øie Solbak, Daniel F. A. R. Dourado, Ken G. Andersson, Mikael Nissbeck, John Löfblom, Samuel C. Flores, Masoumeh Nosrati
Publikováno v:
Protein Engineering, Design and Selection. 30:593-601
The interaction between the Staphylococcal Protein A (SpA) domain B (the basis of the Affibody) molecule and the Fc of IgG is key to the use of Affibodies in affinity chromatography and in potential therapies against certain inflammatory diseases. De
Autor:
Iain C. Sutcliffe, Meilan Huang, Daniel F. A. R. Dourado, Munir Bilal, Derek J. Quinn, Warispreet Singh, Thomas S. Moody, James McClory
Publikováno v:
Singh, W, Bilal, M, McClory, J, Dourado, D, Quinn, D, Moody, T S, Stucliffe, I & Huang, M 2019, ' Mechanism of Phosphatidylglycerol Activation Catalyzed by Prolipoprotein Diacylglyceryl Transferase ', J. Phys. Chem. B, vol. 123, no. 33, pp. 7092-7102 . https://doi.org/10.1021/acs.jpcb.9b04227
Lipoproteins are essential for bacterial survival. Bacterial lipoprotein biosynthesis is accomplished by sequential modification by three enzymes in the inner membrane, all of which are emerging antimicrobial targets. The X-ray crystal structure of p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c53f8afd5b8309cf5c0e2550d59320ab
Autor:
Carla Cristina Marques de Oliveira, Joana Soares, Maria João Romão, Sara Gomes, Filipa Marcelo, Margarida Bastos, Valentina Barcherini, Lucília Domingues, Helena Ramos, Daniel F. A. R. Dourado, Gilberto Fronza, A. Gomes, Maria M. M. Santos, Benedita A. Pinheiro, Ana Luísa Carvalho, Paola Monti, Lucília Saraiva, Alexandra T. P. Carvalho, Joana B. Loureiro
Publikováno v:
Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
Background Half of human cancers harbour TP53 mutations that render p53 inactive as a tumor suppressor. As such, reactivation of mutant (mut)p53 through restoration of wild-type (wt)-like function represents one of the most promising therapeutic stra
Autor:
Timofey Skvortsov, Miguel de Abreu, Daniel F. A. R. Dourado, Meilan Huang, Alexandra T. P. Carvalho, Lyndsey J. Ferguson, Thomas S. Moody, Derek J. Quinn
Publikováno v:
Physical chemistry chemical physics : PCCP. 20(4)
Phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer–Villiger monooxygenases family, and therefore it is an ideal candidate for the synthesis of industrially relevant ester or lactone compounds. However, its limit