Results 151 to 160 of about 28,629,234 (254)

Conservation in Kansas

open access: yes, 2005
Continues title: Soil conservation in Kansas which was continued by: Conservation in ...
Kansas. State Conservation Commission
core  

Structural and biochemical insights into the thermostable esterase Ta0887 from Thermoplasma acidophilum

open access: yesFEBS Open Bio, EarlyView.
In this study, a novel esterase from the thermoacidophilic archaeon Thermoplasma acidophilum was biochemically and structurally characterized. Our results demonstrate that Ta0887 is a highly thermostable esterase that preferentially hydrolyzes p‐nitrophenyl hexanoate and possesses an α‐helical cap domain that likely contributes to its substrate ...
Alejandro Delgado‐Rey   +4 more
wiley   +1 more source

Language barriers in conservation science citation networks. [PDF]

open access: yesConserv Biol
Hannah K   +4 more
europepmc   +1 more source

Addressing priority questions of conservation science with palaeontological data. [PDF]

open access: yesPhilos Trans R Soc Lond B Biol Sci, 2019
Kiessling W   +4 more
europepmc   +1 more source

Conservation in Kansas

open access: yes, 2001
Continues title: Soil conservation in Kansas which was continued by: Conservation in ...
Kansas. State Conservation Commission
core  

Salmonella enterica serovar typhi limits the potency of typhoid toxin and ADP‐ribosylating toxin AB to establish a persistent infection

open access: yesFEBS Open Bio, EarlyView.
The two catalytic subunits of typhoid toxin dissociate from the holotoxin in the ER of an intoxicated cell, but only CdtB exits the ER to generate immunosuppressive effects. PltA is retained in the ER and sequestered from its cytosolic target, thus allowing the anti‐inflammatory effects of CdtB to promote intestinal colonization.
Maria C. Zabala‐Rodriguez   +4 more
wiley   +1 more source

A minimal cellulosome‐like system in Cellulosilyticum lentocellum

open access: yesFEBS Open Bio, EarlyView.
Cellulose‐degrading bacteria typically use cellulosomes, large multi‐enzyme complexes on a scaffold protein. In Cellulosilyticum lentocellum, we characterise a far smaller arrangement, a single scaffold bound to one cellulase through a single cohesin‐dockerin interaction.
John Allan   +2 more
wiley   +1 more source

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