Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Joe A. Gaspar"'
Publikováno v:
Molecular Microbiology. 38:262-275
We investigated the involvement of Tol proteins in the surface expression of lipopolysaccharide (LPS). tolQ, -R, -A and -B mutants of Escherichia coli K-12, which do not form a complete LPS-containing O antigen, were transformed with the O7+ cosmid p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fae283b350fb013119e08f42216b178
https://doi.org/10.1046/j.1365-2958.2000.02094.x
https://doi.org/10.1046/j.1365-2958.2000.02094.x
Autor:
Bin Wu, Elizabeth M. Meiering, Adelinda Yee, Gabriela Meglei, Cheryl H. Arrowsmith, Ricardo Stephen, Antonio Pineda-Lucena, Kenrick A. Vassall, Chengsong Liu, Peter B. Stathopulos, Joe A. Gaspar
Publikováno v:
Protein science : a publication of the Protein Society. 14(1)
We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four beta/alpha units, which form a central parallel beta-sheet with strand order 1234. The first three helices pack to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de76df89782a749e3ab094aecae4d0bf
https://pubmed.ncbi.nlm.nih.gov/15608123
https://pubmed.ncbi.nlm.nih.gov/15608123
Based on previous studies of interleukin-1beta (IL-1beta) and both acidic and basic fibroblast growth factors (FGFs), it has been suggested that the folding of beta-trefoil proteins is intrinsically slow and may occur via the formation of essential i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bba1a3b482746980b4bf0df78d62aac
https://europepmc.org/articles/PMC2373481/
https://europepmc.org/articles/PMC2373481/
Autor:
Valérie Wilquet, Elizabeth M. Meiering, Monica van de Lande, Joe A. Gaspar, Mark Van de Casteele, Christianne Legrain, Nicolas Glansdorff
Publikováno v:
Vrije Universiteit Brussel
We have overexpressed the gene for dihydrofolate reductase (DHFR) from Thermotoga maritima in Escherichia coli and characterized the biochemical properties of the recombinant protein. This enzyme is involved in the de novo synthesis of deoxythymidine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cf5c84d0da500ebe639875d24b3b97c
https://biblio.vub.ac.be/vubir/purification-and-characterization-of-recombinant-thermotoga-maritima-dihydrofolate-reductase(7f319abf-eccb-4c0b-8f72-a43b2c91241f).html
https://biblio.vub.ac.be/vubir/purification-and-characterization-of-recombinant-thermotoga-maritima-dihydrofolate-reductase(7f319abf-eccb-4c0b-8f72-a43b2c91241f).html