Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Ramesh B. Iyer"'
Autor:
Maria A. Argiriadi, Lorenzo Benatuil, Ievgeniia Dubrovska, David A. Egan, Lei Gao, Amy Greischar, Jennifer Hardman, John Harlan, Ramesh B. Iyer, Russell A. Judge, Marc Lake, Denise C. Perron, Ramkrishna Sadhukhan, Bernhard Sielaff, Silvino Sousa, Rui Wang, Bradford L. McRae
Publikováno v:
BMC Molecular and Cell Biology, Vol 20, Iss 1, Pp 1-13 (2019)
Abstract Background CD40 is a 48 kDa type I transmembrane protein that is constitutively expressed on hematopoietic cells such as dendritic cells, macrophages, and B cells. Engagement of CD40 by CD40L expressed on T cells results in the production of
Externí odkaz:
https://doaj.org/article/66a26e4226064b91872d1401b83f9517
Publikováno v:
The Protein Journal. 25:17-21
Proteins from thermophilic microorganisms are stabilized by various mechanisms to preserve their native folded states at higher temperatures. A thermostable glucose-6-phosphate dehydrogenase (tG6PDH) from the hyperthermophilic bacterium Aquifex aeoli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::040bef681e978480624aa4ba142490fe
https://doi.org/10.1007/s10930-006-0015-3
https://doi.org/10.1007/s10930-006-0015-3
Autor:
Leonidas G. Bachas, Ramesh B. Iyer
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 28:1-5
A high temperature NADPH recycling system was designed utilizing a thermostable glucose-6-phosphate dehydrogenase (tG6PDH) from Bacillus stearothermophilus with glucose-6-sulfate (G6S) as the substrate. The thermostable alcohol dehydrogenase (tADH) f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::167d725146f309d3735830295fa4335d
https://doi.org/10.1016/j.molcatb.2003.12.007
https://doi.org/10.1016/j.molcatb.2003.12.007
Publikováno v:
Analytical Chemistry. 75:3898-3901
An amperometric enzyme sensor capable of operating at high temperatures was developed by utilizing a "wired" thermostable glucose-6-phosphate dehydrogenase (tG6PDH) from the hyperthermophilic bacterium Aquifex aeolicus. The response of the system was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2ac027e251a0a4bc6252b729ae5e9f1
https://doi.org/10.1021/ac026298o
https://doi.org/10.1021/ac026298o
Publikováno v:
Extremophiles. 6:283-289
The gsdA gene of the extreme thermophilic bacterium Aquifex aeolicus, encoding glucose-6-phosphate dehydrogenase (G6PDH), was cloned into a high-expression vector and overexpressed as a fusion protein in Escherichia coli. Here we report the character
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de6536c875c68cd5bb57a9458e688622
https://doi.org/10.1007/s00792-001-0255-2
https://doi.org/10.1007/s00792-001-0255-2
Publikováno v:
Biochemistry. 45(30)
The methyl-accepting chemotaxis protein, DcrH, from the anaerobic sulfate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), has a hemerythrin-like domain, DcrH-Hr, at its C terminus. DcrH-Hr was previously shown to contain a diiron site tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc71791c37aa0202205ca9fd3d526e58
https://pubmed.ncbi.nlm.nih.gov/16866347
https://pubmed.ncbi.nlm.nih.gov/16866347
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 10:592-592
High-resolution crystal structures of Desulfovibrio vulgaris nigerythrin (DvNgr), a member of the rubrerythrin (Rbr) family, demonstrate an approximately 2-A movement of one iron (Fe1) of the diiron site from a carboxylate to a histidine ligand upon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80d3ebf88b288aefe1d719e0c5ce9cb0
https://doi.org/10.1007/s00775-005-0667-z
https://doi.org/10.1007/s00775-005-0667-z
Autor:
Iyer, Ramesh B.1,2, Silaghi-Dumitrescu, Radu1,2, Kurtz Jr., Donald M.1,2, Lanzilotta, William N.2,3 wlanzilo@bmb.uga.edu
Publikováno v:
Journal of Biological Inorganic Chemistry (JBIC). Sep2005, Vol. 10 Issue 5, p592-592. 1p.
Publikováno v:
Extremophiles; Aug2002, Vol. 6 Issue 4, p283-289, 7p