Results 81 to 90 of about 492,895 (317)

Remarkable diversity in the enzymes catalyzing the last step in synthesis of the pimelate moiety of biotin. [PDF]

open access: yesPLoS ONE, 2012
Biotin synthesis in Escherichia coli requires the functions of the bioH and bioC genes to synthesize the precursor pimelate moiety by use of a modified fatty acid biosynthesis pathway.
Madelyn M Shapiro   +2 more
doaj   +1 more source

Cloning and phenotypic expression in Escherichia coli of a Bacillus subtilis gene fragment coding for sucrose hydrolysis

open access: yes, 1986
Friehs K, Schörgendorfer K, Schwab H, Lafferty RM. Cloning and phenotypic expression in Escherichia coli of a Bacillus subtilis gene fragment coding for sucrose hydrolysis. Journal of Biotechnology.
Lafferty, R. M.   +3 more
core   +1 more source

Maternal milk contains antimicrobial factors that protect young rabbits from enteropathogenic Escherichia coli infection [PDF]

open access: yes, 2007
Enteropathogenic Escherichia coli (EPEC) colibacillosis represents a major cause of lethal diarrhea in young children in developing countries. EPEC strains also infect numerous mammal species and represent a major economical problem in rabbit industry ...
Milon, Alain   +13 more
core   +1 more source

C2α‐carbanion‐protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2‐hydroxyacyl‐CoA lyase

open access: yesFEBS Open Bio, EarlyView.
Enzymes of the 2‐hydroxyacyl‐CoA lyase group catalyze the condensation of formyl‐CoA with aldehydes or ketones. Thus, by structural adaptation of active sites, practically any pharmaceutically and industrially important 2‐hydroxyacid could be biotechnologically synthesized. Combining crystal structure analysis, active site mutations and kinetic assays,
Michael Zahn   +4 more
wiley   +1 more source

Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]

open access: yes, 2006
In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
core  

The molecular characterisation of Escherichia coli K1 isolated from neonatal nasogastric feeding tubes [PDF]

open access: yes, 2015
Background: The most common cause of Gram-negative bacterial neonatal meningitis is E. coli K1. It has a mortality rate of 10–15%, and neurological sequelae in 30– 50% of cases.
Rhoma, NR   +17 more
core   +1 more source

Development of human monoclonal antibodies against TARM1 by yeast display

open access: yesFEBS Open Bio, EarlyView.
Human monoclonal antibodies against TARM1 are generated by yeast display‐guided selection. These antibodies bind to soluble and cell‐surface forms of TARM1. Also, these antibodies exhibit agonistic activity in the NFAT‐GFP reporter assay, indicating that TARM1 signaling can be functionally modulated by antibodies and suggesting TARM1 as a potential ...
Rikio Yabe   +5 more
wiley   +1 more source

PhoU homologs from Staphylococcus aureus dimerization and protein interactions

open access: yesMicrobiology Spectrum
PhoU proteins are negative regulators of the phosphate response, regulate virulence, and contribute to antibiotic resistance. Staphylococcus aureus has multiple genes encoding PhoU homologs that regulate persister formation and potentially virulence, but
Clayton T. Matthews   +2 more
doaj   +1 more source

Expression and Purification of Mini G Proteins from Escherichia coli

open access: yesBio-Protocol, 2017
Heterotrimeric G proteins modulate intracellular signalling by transducing information from cell surface G protein-coupled receptors (GPCRs) to cytoplasmic effector proteins.
Byron Carpenter, Christopher Tate
doaj   +1 more source

Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis [PDF]

open access: yes, 2009
Streptomyces coelicolor A3(2) alditol oxidase (AldO) is a soluble monomeric flavoprotein in which the flavin cofactor is covalently linked to the polypeptide chain.
Winter, Remko T.   +11 more
core   +1 more source

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